Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
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D9I2G1 | NL1A4_RAT | MGESQSKQESNTRVAQHGSQQDVDPTFQTKRALERERSSPQVEQSFLGQLQSLLGWSSTSKDVPLSQLIREMDHESRRHSHQSKKKLDRSEHISEGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVPTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQPHRVEVLGFSEFERKDYFYKYFAKERNTIIDFNLIGSIPVLLTLCEVPWVCWLLCTCLEKQMQQGEVLSLTSQTTTALCLKYLSLTIPGQHLSTQLRTLCSLAAEGICQRRTLFSKSDLCKQGLAEDAIATFLKIGVLQRQPSSLSYSFAHLCLQEFFAAMSYILEDSEEAHGDMGNDRTVETLVERYGRQNLFEAPTVRFLLGLLNTREMREMENIFACKFPWETKLKLLRSIIGEPFCQPCHLGLFHCLYENQEEELLTETMLCFPLTASGPNHMEATVFQTNVKRLVIQTDMELMVVTFCITFSHVRSLRLKGKGQQEYKLTAPAMVLYRWTPISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGDNGVRQLCEGLRNPACNLSILRLDQASLSEQVITELRALETKNPKLFISSTWMSHMTMPTENTDGEESLTSSKQQQQQSGDKHMEPLGTDDDFWGPSGPVSTEVVDRERNLYRVRLPMAGSYHCPSTGLHFVVTRAVTIEIGFCAWSQFLHETPLQHSHMVAGPLFDIKAEHGAVTAVCLPHFVSLQEGKVDSSLFHVAHFQDHGMVLETPARVEPHFAVLENPSFSPMGVLLRMIPAVGHFIPITSITLIYYRLYLEDITFHLYLVPNDCTIRKAIDEEELKFQFVRINKPPPVDALYVGSRYIVSSSKEVEILPKELELCYRSPRESQLFSEIYVGNIGSGINLQLTDKKYMNLIWEALLKPGDLRPALPRMASAPKDAPALLHFVDQHREQLVARVTSVDPLLDKLHGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIMDLLEKSGGVSVRL | 3.4.-.- | null | antiviral innate immune response [GO:0140374]; cellular response to UV-B [GO:0071493]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; negative regulation of cellular defense response [GO:0051245]; neuron apoptotic process [GO:0051402]; NLRP1 inflammasome complex assembly [GO:1904784]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of pyroptosis [GO:0140639]; programmed necrotic cell death [GO:0097300]; protein homooligomerization [GO:0051260]; pyroptosis [GO:0070269]; regulation of apoptotic process [GO:0042981]; response to muramyl dipeptide [GO:0032495]; self proteolysis [GO:0097264]; stress-activated protein kinase signaling cascade [GO:0031098] | canonical inflammasome complex [GO:0061702]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; NLRP1 inflammasome complex [GO:0072558]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activator activity [GO:0140608]; double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; enzyme binding [GO:0019899]; molecular condensate scaffold activity [GO:0140693]; pattern recognition receptor activity [GO:0038187]; peptidase activity [GO:0008233]; protein domain specific binding [GO:0019904]; protein self-association [GO:0043621]; scaffold protein binding [GO:0097110]; signaling adaptor activity [GO:0035591] | PF00619;PF13553;PF13516;PF05729;PF17776;PF17779; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: [NACHT, LRR and PYD domains-containing protein 1a allele 4]: Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal parts remain associated non-covalently. {ECO:0000250|UniProtKB:Q9C000}.; PTM: [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: Ubiquitinated in response to pathogen-associated signals, leading to its degradation by the proteasome and subsequent release of the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes and forms the Nlrp1a inflammasome. {ECO:0000250|UniProtKB:Q9C000}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Nucleus {ECO:0000250|UniProtKB:Q9C000}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Inflammasome {ECO:0000250|UniProtKB:Q9C000}. | null | null | null | null | null | FUNCTION: Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (By similarity). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex (PubMed:31383852). In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (By similarity). In the absence of GSDMD expression, the Nlrp1a inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (By similarity). {ECO:0000250|UniProtKB:Q2LKU9, ECO:0000250|UniProtKB:Q2LKW6, ECO:0000250|UniProtKB:Q9C000, ECO:0000269|PubMed:31383852}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a allele 4]: Constitutes the precursor of the Nlrp1a inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals. {ECO:0000250|UniProtKB:Q9C000}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: Regulatory part that prevents formation of the Nlrp1a inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, this part is ubiquitinated by the N-end rule pathway and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the Nlrp1a inflammasome. {ECO:0000250|UniProtKB:Q9C000}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Constitutes the active part of the Nlrp1a inflammasome. In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, N-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing this form, which polymerizes to form the Nlrp1a inflammasome complex: the Nlrp1a inflammasome complex then directly recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, leading to gasdermin-D (GSDMD) cleavage and subsequent pyroptosis. {ECO:0000250|UniProtKB:Q9C000}. | Rattus norvegicus (Rat) |
D9I2G3 | NL1A2_RAT | MEESQSKQESNTRVAQHGSQQDVDPTFQTKRALEKERSKPRPRPLPRVQLQSLPGWSSTSKDVPLSQLIREMDHESRRCIHRSKKKLDRSEHISQGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVPTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQPHRVEVLGFSEFERKDYFYKYFAKERNTIIDFNLIGSIPVLLTLCEVPWVCWLLCTCLEKQMQQGEVLSLTSQTTTALCLKYLSLTIPGQHLSTQLRTLCSLAAEGICQRRTLFSKSDLCKQGLAEDAIATFLKIGVLQRQPSSLSYSFAHLCLQEFFAAMSYILEDSEEAHGDMGNDRTVETLVERYGRQNLFEAPTVRFLLGLLNTREMREMENIFACKFPWETKLKLLQSIIGEPFCQPCHLGLFHCLYENQEEELLTETMLCFPLTASGPNHMEATVFQTNVKRLVIQTDMELMVVTFCITFSHVRSLRLKGKGQQEYKLTAPAMVLYRWTPISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGDNGVRQLCEGLRNPACNLSILRLDQASLSEQVITELRALETKNPKLFISSTWMSHMTMPTENTDGEESLTSSKQQQQQSGDKHMEPLGTDDDFWGPSGPVSTEVVDRERNLYRVRLPMAGSYHCPSTGLHFVVTRAVTIEIGFCAWSQFLHETPLQHSHMVAGPLFDIKAEHGAVTAVCLPHFVSLQEGKVDSSLFHVAHFQDHGMVLETPARVEPHFAVLENPSFSPMGVLLRMIPAVGHFIPITSITLIYYRLYLEDITFHLYLVPNDCTIRKAIDEEELKFQFVRINKPPPVDALYVGSRYIVSSSKEVEILPKELELCYRSPRESQLFSEIYVGNIGSGINLQLTDKKYMNLIWEALLKPGDLRPALPRMASAPKDAPALLHFVDQHREQLVARVTSVDPLLDKLHGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIMDLLEKSGGVSVRL | 3.4.-.- | null | antiviral innate immune response [GO:0140374]; cellular response to UV-B [GO:0071493]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; negative regulation of cellular defense response [GO:0051245]; neuron apoptotic process [GO:0051402]; NLRP1 inflammasome complex assembly [GO:1904784]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of pyroptosis [GO:0140639]; programmed necrotic cell death [GO:0097300]; protein homooligomerization [GO:0051260]; pyroptosis [GO:0070269]; regulation of apoptotic process [GO:0042981]; response to muramyl dipeptide [GO:0032495]; self proteolysis [GO:0097264]; stress-activated protein kinase signaling cascade [GO:0031098] | canonical inflammasome complex [GO:0061702]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; NLRP1 inflammasome complex [GO:0072558]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activator activity [GO:0140608]; double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; enzyme binding [GO:0019899]; molecular condensate scaffold activity [GO:0140693]; pattern recognition receptor activity [GO:0038187]; peptidase activity [GO:0008233]; protein domain specific binding [GO:0019904]; protein self-association [GO:0043621]; scaffold protein binding [GO:0097110]; signaling adaptor activity [GO:0035591] | PF00619;PF13553;PF13516;PF05729;PF17776;PF17779; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: [NACHT, LRR and PYD domains-containing protein 1 allele 2]: Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal parts remain associated non-covalently. {ECO:0000250|UniProtKB:Q9C000}.; PTM: [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: (Microbial infection) Cleavage by B.anthracis lethal toxin (LT) endopeptidase promotes ubiquitination and degradation of the N-terminal part, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes and forms the Nlrp1a inflammasome. {ECO:0000305|PubMed:20502689}.; PTM: [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: Ubiquitinated in response to pathogen-associated signals, leading to its degradation by the proteasome and subsequent release of the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes and forms the Nlrp1a inflammasome. {ECO:0000250|UniProtKB:Q9C000}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Nucleus {ECO:0000250|UniProtKB:Q9C000}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Inflammasome {ECO:0000250|UniProtKB:Q9C000}. | null | null | null | null | null | FUNCTION: Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (By similarity). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as B.anthracis lethal toxin (LT) or Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex (PubMed:20502689, PubMed:31383852). In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (By similarity). In the absence of GSDMD expression, the Nlrp1a inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (By similarity). {ECO:0000250|UniProtKB:Q2LKU9, ECO:0000250|UniProtKB:Q2LKW6, ECO:0000250|UniProtKB:Q9C000, ECO:0000269|PubMed:20502689, ECO:0000269|PubMed:31383852}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1 allele 2]: Constitutes the precursor of the Nlrp1a inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals. {ECO:0000250|UniProtKB:Q9C000}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: Regulatory part that prevents formation of the Nlrp1a inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, this part is ubiquitinated by the N-end rule pathway and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the Nlrp1a inflammasome. {ECO:0000250|UniProtKB:Q9C000}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Constitutes the active part of the Nlrp1a inflammasome. In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, N-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing this form, which polymerizes to form the Nlrp1a inflammasome complex: the Nlrp1a inflammasome complex then directly recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, leading to gasdermin-D (GSDMD) cleavage and subsequent pyroptosis. {ECO:0000250|UniProtKB:Q9C000}. | Rattus norvegicus (Rat) |
D9I2G4 | NL1A5_RAT | MGESQSKQESNTRVAQHGSQQDVDPTFQTKRALERERSSPQVEQSFLGQLQSLLGWSSTSKDVPLSQLIREMDHESRRHSHQSKKKLDRSEHISEGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWEEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVLTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLIPSLGQPHRVEVLGFSEFERKDYFYKYFAKERNTIIDFNLIGSIPVLLTLCEVPWVCWLLCTCLEKQMQQGEVLSLTSQTTTALCLKYLSLTIPGQHLSTQLRTLCSLAAEGICQRRTLFSKSDLCKQGLAEDAIATFLKIGVLQRQPSSLSYSFAHLCLQEFFAAMSYILEDSEEARGDMGNDRTVETLVERYGRQNLFEAPTVRFLLGLLNTREMREMENIFACKFPWKTKLKLLRSIVGEPFCQPCHLGLFHCLYENQEEELLTETMLCFPLTASGPNHMEATVFQTNVKRLVIQTDMELMVVTFCITFSHVRSLRLKGKGQQEYKLTAPAMVLYRWTPISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGDNGVRQLCEGLRNPACNLSILRLDQASLSEQVITELRALETKNPKLFISSTWMSHMTMPTENTDGEESLTSSKQQQQQSGDKHMEPLGTDDDFWGPSGPVSTEVVDRERNLYRVRLPMAGSYHCPSTGLHFVVTRAVTIEIGFCAWSQFLHETPLQHSHMVAGPLFDIKAEHGAVTAVCLPHFVSLQEGKVDSSLFHVAHFQDHGMVLETPARVEPHFAVLENPSFSPMGVLLRMIPAVGHFIPITSITLIYYRLYLEDITFHLYLVPNDCTIRKAIDEEELKFQFVRINKPPPVDALYVGSRYIVSSSKEVEILPKELELCYRSPRESQLFSEIYVGNIGSGINLQLTDKKYMNLIWEALLKPGDLRPALPRMASAPKDAPALLHFVDQHREQLVARVTSVDPLLDKLHGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIMDLLEKSGGVSVRL | 3.4.-.- | null | antiviral innate immune response [GO:0140374]; cellular response to UV-B [GO:0071493]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; negative regulation of cellular defense response [GO:0051245]; neuron apoptotic process [GO:0051402]; NLRP1 inflammasome complex assembly [GO:1904784]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of pyroptosis [GO:0140639]; programmed necrotic cell death [GO:0097300]; protein homooligomerization [GO:0051260]; pyroptosis [GO:0070269]; regulation of apoptotic process [GO:0042981]; response to muramyl dipeptide [GO:0032495]; self proteolysis [GO:0097264]; stress-activated protein kinase signaling cascade [GO:0031098] | canonical inflammasome complex [GO:0061702]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; NLRP1 inflammasome complex [GO:0072558]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activator activity [GO:0140608]; double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; enzyme binding [GO:0019899]; molecular condensate scaffold activity [GO:0140693]; pattern recognition receptor activity [GO:0038187]; peptidase activity [GO:0008233]; protein domain specific binding [GO:0019904]; protein self-association [GO:0043621]; scaffold protein binding [GO:0097110]; signaling adaptor activity [GO:0035591] | PF00619;PF13553;PF13516;PF05729;PF17776;PF17779; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: [NACHT, LRR and PYD domains-containing protein 1a allele 5]: Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal parts remain associated non-covalently. {ECO:0000250|UniProtKB:Q9C000}.; PTM: [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: Ubiquitinated in response to pathogen-associated signals, leading to its degradation by the proteasome and subsequent release of the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes and forms the Nlrp1a inflammasome. {ECO:0000250|UniProtKB:Q9C000}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Nucleus {ECO:0000250|UniProtKB:Q9C000}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Inflammasome {ECO:0000250|UniProtKB:Q9C000}. | null | null | null | null | null | FUNCTION: Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (By similarity). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex (PubMed:31383852). In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (By similarity). In the absence of GSDMD expression, the Nlrp1a inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (By similarity). {ECO:0000250|UniProtKB:Q2LKU9, ECO:0000250|UniProtKB:Q2LKW6, ECO:0000250|UniProtKB:Q9C000, ECO:0000269|PubMed:31383852}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a allele 5]: Constitutes the precursor of the Nlrp1a inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals. {ECO:0000250|UniProtKB:Q9C000}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: Regulatory part that prevents formation of the Nlrp1a inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, this part is ubiquitinated by the N-end rule pathway and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the Nlrp1a inflammasome. {ECO:0000250|UniProtKB:Q9C000}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Constitutes the active part of the Nlrp1a inflammasome. In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, N-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing this form, which polymerizes to form the Nlrp1a inflammasome complex: the Nlrp1a inflammasome complex then directly recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, leading to gasdermin-D (GSDMD) cleavage and subsequent pyroptosis. {ECO:0000250|UniProtKB:Q9C000}. | Rattus norvegicus (Rat) |
D9I2H0 | NL1A3_RAT | MGESQSKQESNTRVAQHGSQQDVDPTFQTKRALERERSSPQVEQSFLGQLQSLLGWSSTSKDVPLSQLIREMDHESRRHSHQSKKKLDRSEHISEGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWDEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVPTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLVPSLGQPHRVEVLGFSEFERKDYFYKYFAKERNTIIDFNLIGSIPVLLTLCEVPWVCWLLCTCLEKQMQQGEVLSLTSQTTTALCLKYLSLTIPGQHLSTQLRTLCSLAAEGICQRRTLFSKSDLCKQGLAEDAIATFLKIGVLQRQPSSLSYSFAHLCLQEFFAAMSYILEDSEEAHGDMGNDRTVETLVERYGRQNLFEAPTVRFLLGLLNTREMREMENIFACKFPWETKLKLLQSIIGEPFCQPCHLGLFHCLYENQEEELLTETMLCFPLTASGPNHMEATVFQTNVKRLVIQTDMELMVVTFCITFSHVRSLRLKGKGQQEYKLTAPAMVLYRWTPISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGDNGVRQLCEGLRNPACNLSILRLDQASLSEQVITELRALETKNPKLFISSTWMSHMTMPTENTDGEESLTSSKQQQQQSGDKHMEPLGTDDDFWGPSGPVSTEVVDRERNLYRVRLPMAGSYHCPSTGLHFVVTRAVTIEIGFCAWSQFLHETPLQHSHMVAGPLFDIKAEHGAVTAVCLPHFVSLQEGKVDSSLFHVAHFQDHGMVLETPARVEPHFAVLENPSFSPMGVLLRMIPAVGHFIPITSITLIYYRLYLEDITFHLYLVPNDCTIRKAIDEEELKFQFVRINKPPPVDALYVGSRYIVSSSKEVEILPKELELCYRSPRESQLFSEIYVGNIGSGINLQLTDKKYMNLIWEALLKPGDLRPALPRMASAPKDAPALLHFVDQHREQLVARVTSVDPLLDKLHGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIMDLLEKSGGVSVRL | 3.4.-.- | null | antiviral innate immune response [GO:0140374]; cellular response to UV-B [GO:0071493]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; negative regulation of cellular defense response [GO:0051245]; neuron apoptotic process [GO:0051402]; NLRP1 inflammasome complex assembly [GO:1904784]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of pyroptosis [GO:0140639]; programmed necrotic cell death [GO:0097300]; protein homooligomerization [GO:0051260]; pyroptosis [GO:0070269]; regulation of apoptotic process [GO:0042981]; response to muramyl dipeptide [GO:0032495]; self proteolysis [GO:0097264]; stress-activated protein kinase signaling cascade [GO:0031098] | canonical inflammasome complex [GO:0061702]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; NLRP1 inflammasome complex [GO:0072558]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activator activity [GO:0140608]; double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; enzyme binding [GO:0019899]; molecular condensate scaffold activity [GO:0140693]; pattern recognition receptor activity [GO:0038187]; peptidase activity [GO:0008233]; protein domain specific binding [GO:0019904]; protein self-association [GO:0043621]; scaffold protein binding [GO:0097110]; signaling adaptor activity [GO:0035591] | PF00619;PF13553;PF13516;PF05729;PF17776;PF17779; | 1.10.533.10;3.40.50.300;3.80.10.10; | NLRP family | PTM: [NACHT, LRR and PYD domains-containing protein 1a allele 3]: Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal parts remain associated non-covalently. {ECO:0000250|UniProtKB:Q9C000}.; PTM: [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: Ubiquitinated in response to pathogen-associated signals, leading to its degradation by the proteasome and subsequent release of the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes and forms the Nlrp1a inflammasome. {ECO:0000250|UniProtKB:Q9C000}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Nucleus {ECO:0000250|UniProtKB:Q9C000}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Inflammasome {ECO:0000250|UniProtKB:Q9C000}. | null | null | null | null | null | FUNCTION: Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (By similarity). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex (PubMed:31383852). In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (By similarity). In the absence of GSDMD expression, the Nlrp1a inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (By similarity). {ECO:0000250|UniProtKB:Q2LKU9, ECO:0000250|UniProtKB:Q2LKW6, ECO:0000250|UniProtKB:Q9C000, ECO:0000269|PubMed:31383852}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a allele 3]: Constitutes the precursor of the Nlrp1a inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals. {ECO:0000250|UniProtKB:Q9C000}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a, N-terminus]: Regulatory part that prevents formation of the Nlrp1a inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, this part is ubiquitinated by the N-end rule pathway and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the Nlrp1a inflammasome. {ECO:0000250|UniProtKB:Q9C000}.; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Constitutes the active part of the Nlrp1a inflammasome. In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of Nlrp1a (NACHT, LRR and PYD domains-containing protein 1a, N-terminus), preventing activation of the Nlrp1a inflammasome. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing this form, which polymerizes to form the Nlrp1a inflammasome complex: the Nlrp1a inflammasome complex then directly recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, leading to gasdermin-D (GSDMD) cleavage and subsequent pyroptosis. {ECO:0000250|UniProtKB:Q9C000}. | Rattus norvegicus (Rat) |
D9IA43 | CCON1_STUST | MNTATSTAYSYKVVRQFAIMTVVWGIVGMGLGVFIAAQLAWPFLNFDLPWTSFGRLRPLHTNAVIFAFGGCALFATSYYSVQRTCQTTLFAPKLAAFTFWGWQLVILLAAISLPLGFTSSKEYAELEWPIDILITIVWVAYAVVFFGTLAKRKVKHIYVGNWFFGAFILTVAILHVVNNLEIPVTAMKSYSLYAGATDAMVQWWYGHNAVGFFLTAGFLGIMYYFVPKQAERPVYSYRLSIVHFWALITVYIWAGPHHLHYTALPDWAQSLGMVMSLILLAPSWGGMINGMMTLSGAWHKLRSDPILRFLVVSLAFYGMSTFEGPMMAIKTVNALSHYTDWTIGHVHAGALGWVAMVSIGALYHLVPKVFGREQMHSIGLINTHFWLATIGTVLYIASMWVNGIAQGLMWRAINDDGTLTYSFVESLEASHPGFVVRMIGGAIFFAGMLVMAYNTWRTVQAAKPAEYDAAAQIA | 7.1.1.9 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:20576851}; Note=Binds 1 copper ion per subunit, denoted as copper B. {ECO:0000269|PubMed:20576851}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:20576851}; Note=Binds 2 heme b groups per subunit, denoted as high- and low-spin. {ECO:0000269|PubMed:20576851}; | aerobic electron transport chain [GO:0019646]; aerobic respiration, using ferrous ions as electron donor [GO:0019411]; electron transport coupled proton transport [GO:0015990]; oxidative phosphorylation [GO:0006119]; proton transmembrane transport [GO:1902600] | cytochrome complex [GO:0070069]; plasma membrane [GO:0005886]; plasma membrane respirasome [GO:0070470]; plasma membrane respiratory chain complex IV [GO:0045278] | copper ion binding [GO:0005507]; cytochrome-c oxidase activity [GO:0004129]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; oxygen binding [GO:0019825]; ubiquinol-cytochrome-c reductase activity [GO:0008121] | PF00115; | 1.20.210.10; | Heme-copper respiratory oxidase family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250|UniProtKB:P0ABI8}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; Evidence={ECO:0000305}; | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000305}. | null | null | FUNCTION: Cbb3-type cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits CcoN and CcoO form the functional core of the enzyme complex. Subunits CcoP and CcoQ may optionally bind to the core. CcoN is the catalytic subunit of the enzyme. Electrons originating in cytochrome c or a quinol are transferred to the bimetallic center formed by a high-spin heme and copper B. The complex also functions as a proton pump. {ECO:0000305}. | Stutzerimonas stutzeri (Pseudomonas stutzeri) |
D9IVE5 | ANM2_XENLA | MESSSECSSISDFQDSTEGDDANTLPENLCMREYVVICDYVATDNTQLSLCSGDKVLLLNAVSQDWWWVNHNGTCGYVPASHLHDALNEQEDTEVNDPWQDEEYYGSYKTLKLHLEMLSDVPRTMTYQNVILKNSSSLCGKHILDLGCGTGIISFFCAKFAQPEAVYAVEASKIAEQTCRLVEQNGISSLVHVIRQQAEELDLPTKVDVLVSEWMGTCLLFEFMLESVLQARDRWLKEDGVMWPSTACIHLVPCSAYKEYSNKVLFWDNPYQLDFSLLKPPATKEFFAKPQPDYILQPEDCLSEPCTLFHLNLKTLQVAELERMNCDFTFLVHTNGLLHGFTAWFSVQFENLEEQGHLELNTGPFSPLTHWKHTLFMLDEPLQVQKRDKISGSVVFERNSVWRRHMSVTLSWVISRELKMQKVGCKVFPIWR | 2.1.1.319 | null | developmental cell growth [GO:0048588]; methylation [GO:0032259]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; positive regulation of apoptotic process [GO:0043065]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of androgen receptor signaling pathway [GO:0060765] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | histone H3R8 methyltransferase activity [GO:0140592]; nuclear estrogen receptor binding [GO:0030331]; protein-arginine omega-N asymmetric methyltransferase activity [GO:0035242] | PF13649;PF07653; | 2.70.160.11;2.30.30.40;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Protein arginine N-methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319; Evidence={ECO:0000250|UniProtKB:P55345}; | null | null | null | null | FUNCTION: Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as histones. Involved in growth regulation (By similarity). Involved in embryonic dorsal development. {ECO:0000250, ECO:0000269|PubMed:20708585}. | Xenopus laevis (African clawed frog) |
D9J041 | MERA_LYSSH | MNKFKVNISGMTCTGCEKHVESALEKIGAKNIESSYRRGEAVFELPDDIEVESAIKAIDEANYQAGEIEEVSSLENVALINEDNYDLLIIGSGAAAFSSAIKAIEYGAKVGMIERGTVGGTCVNIGCVPSKTLLRAGEIIHLSKDNPFIGLQTSAGEVDLASLITQKDKLVSELRNQKYMDLIDEYNFDLIKGEAKFVDASTVEVNGAKLSAKRFLIATGASPSLPQISGLEKMDYLTSTTLLELKKIPKRLTVIGSGYIGMELGQLFHHLGSEITLMQRSERLLKEYDPEISESVEKALIEQGINLVKGATFERVEQSGEIKRVYVTVNGSREVIESDQLLVATGRKPNTDSLNLSAAGVETGKNNEILINDFGQTSNEKIYAAGDVTLGPQFVYVAAYEGGIITDNAIGGLNKKIDLSVVPAVTFTNPTVATVGLTEEQAKEKGYDVKTSVLPLDAVPRAIVNRETTGVFKLVADAETLKVLGVHIVSENAGDVIYAASLAVKFGLTVEDLTETLAPYLTMAEGLKLAALTFDKDIWKLSCCAG | 1.16.1.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|PIRNR:PIRNR000350, ECO:0000255|PIRSR:PIRSR000350-3, ECO:0000255|RuleBase:RU361223, ECO:0000269|PubMed:28894951}; Note=Binds 1 FAD per subunit. {ECO:0000255|PIRNR:PIRNR000350, ECO:0000255|PIRSR:PIRSR000350-3, ECO:0000255|RuleBase:RU361223}; | detoxification of mercury ion [GO:0050787] | null | flavin adenine dinucleotide binding [GO:0050660]; mercury (II) reductase activity [GO:0016152]; mercury ion binding [GO:0045340]; NADP binding [GO:0050661]; oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor [GO:0016668] | PF00403;PF07992;PF02852; | 3.30.390.30;3.30.70.100;3.50.50.60; | Class-I pyridine nucleotide-disulfide oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + Hg + NADP(+) = Hg(2+) + NADPH; Xref=Rhea:RHEA:23856, ChEBI:CHEBI:15378, ChEBI:CHEBI:16170, ChEBI:CHEBI:16793, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.1; Evidence={ECO:0000255|PIRNR:PIRNR000350, ECO:0000255|RuleBase:RU361223, ECO:0000269|PubMed:28894951}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=231 uM for NADPH {ECO:0000269|PubMed:28894951}; Vmax=18 umol/min/mg enzyme {ECO:0000269|PubMed:28894951}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-7.5. {ECO:0000269|PubMed:28894951}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25-50 degrees Celsius. Activity is inhibited only slightly at 60 degrees Celsius, but at temperatures of 70 degrees Celsius and above, the activity is reduced to about 14% of normal activity. {ECO:0000269|PubMed:28894951}; | FUNCTION: Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase (By similarity) (PubMed:28894951). MerA protein is responsible for volatilizing mercury as Hg(0) (By similarity) (PubMed:28894951). Catalyzes reduction of Hg(2+) to elemental Hg, which is volatile and can diffuse out of cells passively (PubMed:28894951). Plays a pivotal role in mercury resistance and cell protection (PubMed:28894951). {ECO:0000255|PIRNR:PIRNR000350, ECO:0000269|PubMed:28894951}. | Lysinibacillus sphaericus (Bacillus sphaericus) |
D9N129 | WDR20_CAEEL | MHQHMLGPSTSLGGTNNSALQSSVLSEGVLLSHSQPTREEIKKNFETREGVYRSVPSAEFSRPRPLPQYHMPPGIASAAASQIAAAGSTVRVSFLNGAEKSVESPEAVAPTSSTYEHHKNEPNGARIDMVDEAQADKICFNVGKELYVFSYRGTQTETDLSRPIDKRVYKGTSPTYHAFNQESAKNGSCQLLIGFTLGQLQIIDPLEKSSSSPFSRLYNEDRYIEKTSVTCIRWLPGDSNIFLASYVSGNLYVYDQRISAASSNNNGSSQPPPWTIHKEGDKFAIHTWKGKVQRNPVTRWQIGEGSIHQFSFSGSDGKMMATVSHDGFLRIFNYHAQELLAVMKSYFGGLLTLSWSPDAKLIATGGEDDLLTVYSVAEKRVVCRGQAHKSWVSQVKFDPYLCTTEEDLENNGIAMTSTFDDVAKDFSIRSGPVPSTSADLNSGVMNATSTFSRCSLASFNTINGAPAGNSVRYRIGSVGHDTFLCLWDITEDMLNQGNIRRHRNSTIIAPMTTLEVQTNSLVGRLEDLQEVSPGGAGVNASSDSQSITNNHTTPRPEKQKKKKFTKRLGFSKFTSGSSSATSNPVGGHKIGTLMNGASVNSESSKKQNPGLISQISCCNETRMLGSKFCPGIRDVPMIEPLMCKKVSHDRLTVLEFREDCVVTACQEGYICTWGRPGRYQPKRDCINSPGTASPESGQKPSGSTSAMTSSYGYGSDALNGVPPSRSSSTYSNSEQQLRSPNITSPSYRVSAASTSVYHRPTYAWQNAN | null | null | carbon catabolite repression of transcription [GO:0045013]; positive regulation of gene expression [GO:0010628]; positive regulation of locomotion involved in locomotory behavior [GO:0090326]; positive regulation of protein deubiquitination [GO:1903003]; positive regulation of protein localization to cell surface [GO:2000010] | cell division site [GO:0032153]; cell tip [GO:0051286]; nucleus [GO:0005634] | null | PF00400; | 2.130.10.10; | null | null | null | null | null | null | null | null | FUNCTION: Together with wdr-48, binds to and stimulates the activity of the deubiquitinating enzyme usp-46, leading to deubiquitination and stabilization of the glr-1 glutamate receptor. {ECO:0000269|PubMed:24356955}. | Caenorhabditis elegans |
D9N164 | IRK10_PARME | MTGGMKPPARKPRILNSDGSSNITRLGLEKRGWLDDHYHDLLTVSWPVFITLITGLYLVTNALFALAYLACGDVIENARPGSFTDAFFFSVQTMATIGYGKLIPIGPLANTLVTLEALCGMLGLAVAASLIYARFTRPTAGVLFSSRMVISDFEGKPTLMMRLANLRIEQIIEADVHLVLVRSEISQEGMVFRRFHDLTLTRSRSPIFSLSWTVMHPIDHHSPIYGETDETLRNSHSEFLVLFTGHHEAFAQNVHARHAYSCDEIIWGGHFVDVFTTLPDGRRALDLGKFHEIAQ | null | null | potassium ion import across plasma membrane [GO:1990573]; regulation of monoatomic ion transmembrane transport [GO:0034765] | monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; inward rectifier potassium channel activity [GO:0005242] | PF07885;PF17655; | 1.10.287.70;2.60.40.1400; | Inward rectifier-type potassium channel (TC 1.A.2.1) family, KCNJ11 subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16216578, ECO:0000269|PubMed:20564790, ECO:0000269|PubMed:20876570, ECO:0000269|PubMed:22231399}; Multi-pass membrane protein {ECO:0000269|PubMed:16216578, ECO:0000269|PubMed:20564790, ECO:0000269|PubMed:20876570, ECO:0000269|PubMed:22231399}. | null | null | null | null | null | FUNCTION: Inward rectifier potassium channel that mediates potassium uptake into the cell. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. The inward rectification may be achieved by the blockage of outward current by cytoplasmic divalent metal ions and polyamines. Complements an E.coli mutant that is defective in K(+) uptake. {ECO:0000269|PubMed:20564790, ECO:0000269|PubMed:20876570, ECO:0000269|PubMed:22231399}. | Paramagnetospirillum magnetotacticum (Aquaspirillum magnetotacticum) |
D9PTN5 | MYRF2_CAEEL | MGDLNPAETPEPKKNPVAKIASNLYSTQIVKPVPSVSNSTNLSPCQNPNMTNLFYITLLQNKLNKYTQQLLKKNEEGLNDPLANVEQFNIIQFLQNDVDFNLPIEAFEQGNMDQNIRIDPILQRQQMANQPMLMPQHMLQQLHQQQIYEQQLASMPMTPAITDLTRHGSSSSPSTTNSDPPYSPEGLNNFGLGTQRPNHGVIPNDISNVPQHINRQFNPRMGPNTSPNPPSFPQFLNSNHPTPGSYVQSISPDSNGQGFAQSNLYNALNVSSDESINGSDDIPNRKRPRMDQNMDPSFIMHAPVSGKLGAEVTEEGGQPNIRFFKYQEEQWCPMYDANGEELGRLQVHVLADKGFNYSTNDNCFVNQKKNHFQVTVKIEAIDPSPPQCFKINGVCKPIENFQLSFVGAKSESQNSEIPIRQSTTERKPILHTPVLFKIVERRMTIVTVPRLHFSETTLNNQRKNLRPNPDQKYFNLVVRLYATATDGTTVLMQAFASERVIVRATNPGSFEPPEMVDASWNKNGGILSTNGPVVIGKSEPRAQLTVDGDIYSSGRVMYPSDIRLKDNITEKGAKDALENLQKLRIVDYFYKPEVASKWGLTEDQRKRTGVIAQELAAVLPDAVKDLGDYLTVNESRVFYETVLATQELCRLTGDLDQKIDDKVAEISQRLTQYAQKKKMLNSMASGLNSEGRSLNASRTSLDSSASALTLTNTKKNRRSSRKDKKDAPKSKMTHGTVIGLVGVMAFCLLAMSALYILDWHNRNFGYHHFTPSATTSGPKEGPGNVVIPLDHYVPLRQPDAPPLVPFCPMETCRGYCCMEYDKDHAELEITEYDPNTATDNDFGFKADTRSDFTLKGFGNNVKISLPELGMQIDERYCIEKSCVKKRKVYSLFIPMTRYLPNVPLEVQIDVPSSKVVNNCGYIQEFDNRKCDETGSSSTETDAPRSIQLFDNTFQVSAGQWTQSAYRFRVGYSTELCSIDDTHFGGFYEEYNLIFYRACNRTNSTAINVV | 3.4.-.- | null | cell differentiation [GO:0030154]; positive regulation of DNA-templated transcription [GO:0045893]; protein autoprocessing [GO:0016540]; regulation of neuron remodeling [GO:1904799]; regulation of synapse assembly [GO:0051963] | apical plasma membrane [GO:0016324]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity [GO:0003700]; peptidase activity [GO:0008233]; sequence-specific DNA binding [GO:0043565] | PF13888;PF13887;PF05224;PF13884; | 2.60.40.1390; | MRF family | PTM: Myelin regulatory factor: Follows autocatalytic cleavage via the peptidase S74 domain. Autoprocessing is apparently constitutive and is essential for transcriptional activity. {ECO:0000250|UniProtKB:G5EFI7}. | SUBCELLULAR LOCATION: [Myelin regulatory factor homolog 2]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28441531}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:33950834}. Apical cell membrane {ECO:0000269|PubMed:33950834}; Single-pass membrane protein {ECO:0000255}. Note=In early L1 larvae, localizes to the cell membrane, but then localizes to the nucleus in late L1 larvae (PubMed:33950834). Cell membrane localization is promoted by pan-1 (PubMed:33950834). {ECO:0000269|PubMed:33950834}.; SUBCELLULAR LOCATION: [Myelin regulatory factor homolog 2, N-terminal]: Nucleus {ECO:0000269|PubMed:28441531}. Cytoplasm {ECO:0000269|PubMed:28441531}. Note=Translocates from the cytoplasm to the nucleus upon autocatalytic cleavage. {ECO:0000269|PubMed:28441531}.; SUBCELLULAR LOCATION: [Myelin regulatory factor homolog 2, C-terminal]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28441531}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: [Myelin regulatory factor homolog 2]: Constitutes a precursor of the transcription factor (PubMed:28441531). Mediates the autocatalytic cleavage that releases the Myelin regulatory factor homolog 2, N-terminal component that specifically activates transcription of genes involved in synaptic rewiring during nervous system maturation (PubMed:28441531). {ECO:0000269|PubMed:28441531}.; FUNCTION: [Myelin regulatory factor homolog 2, C-terminal]: Membrane-bound part that has no transcription factor activity and remains attached to the endoplasmic reticulum membrane following cleavage. {ECO:0000250|UniProtKB:Q9Y2G1}.; FUNCTION: [Myelin regulatory factor homolog 2, N-terminal]: Transcription factor that specifically activates expression of genes involved in synaptic rewiring during nervous system maturation (PubMed:28441531). Specifically required for dorsal D (DD) GABAergic motor neurons synaptic rewiring (PubMed:28441531). Acts in complex with myrf-1 paralog (PubMed:28441531). {ECO:0000269|PubMed:28441531}. | Caenorhabditis elegans |
D9PUX5 | TFRB_METTM | MINVKVLRFEPGVDEKPHLESYDIPSKEKMKVLDALQLINKMYNANIAFRSSCRAGQCGSCAVKMNGEVVLACRAEVEDGAVIEPVDLPVIKDLMVDRSEIEDKVRAMGLYLQSEARGIQRIKPEDYQDTKKLRGCIECFSCISSCPVIKESTEYAGPYFMRYISKFAFDPRDEAERAAGGVEEGLYCCTTCGKCAEVCPKELNVPGDAIEKLRAMACREGAGPLDAHRKIKKLISETGRSVDHIGKGFIESVGQNPGSRIGFFTGCLVDYRMPDVGMALLRVLREHGFEVDVPDGQVCCGSPMIRTGQLDIVEDLVERNRRALEGYDTIITVCAGCGATLKKDYPRYGVELNVLDISEFLADRIDDIKMKPVNMRVTYHDPCHLLRGQGVKLEPRKILNSIPGLEFVEMEKQGQCCGSGGGVKSGKPEIAESLGKKKAEMIRKLNVDAVITICPFCQLHIKDSLEKEGLGDVKVMNILELLDMAYSDD | 1.3.4.1 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:9578488}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000269|PubMed:9578488}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:9578488}; Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000269|PubMed:9578488}; | fumarate metabolic process [GO:0006106]; tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737] | 2 iron, 2 sulfur cluster binding [GO:0051537]; 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on the CH-CH group of donors [GO:0016627] | PF02754;PF13085;PF13183; | 3.10.20.30;1.10.1060.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000303|PubMed:2499256}. | CATALYTIC ACTIVITY: Reaction=coenzyme B + coenzyme M + fumarate = coenzyme M-coenzyme B heterodisulfide + succinate; Xref=Rhea:RHEA:40235, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:58319, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=1.3.4.1; Evidence={ECO:0000269|PubMed:9578488}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for fumarate {ECO:0000269|PubMed:2499256}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is7.0. {ECO:0000269|PubMed:2499256}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 75 degrees Celsius. {ECO:0000269|PubMed:2499256}; | FUNCTION: Catalyzes the reduction of fumarate with reduced coenzyme M (CoM-S-H) and coenzyme B (CoB-S-H). In vitro, is able to reduces fumarate with reduced benzyl viologen, oxidize CoM-S-H and CoB-S-H to CoM-S-S-CoB with methylene blue, and reduce CoM-S-S-CoB with reduced benzyl viologen. The enzyme has specificity for the two thiol compounds as the CoB--CoM heterodisulfide reductase. The enzyme is very sensitive to oxygen. {ECO:0000269|PubMed:9578488}. | Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) |
D9PVP5 | FNO_METTM | MKIAVLGGTGDQGLGLALRLALAGEEVIIGSRDAEKAVSAAQKVLEIAERDDLKVKGATNAEAAEEAEVAILTVPLQAQMATLGSVKEAIKGKVLIDATVPIDSCLGGSAVRYIDLWDGSAAERAARFLEDQGTRVAAAFNNISASALLDITGPVDCDCLIASDHRDALDLASELAEKIDGVRAIDCGGLENARVIEKITPLLINLNIKNRIRNAGIRITNLPE | 1.5.1.40 | null | copper ion import [GO:0015677]; NADPH regeneration [GO:0006740] | plasma membrane [GO:0005886] | 8-hydroxy-5-deazaflavin:NADPH oxidoreductase activity [GO:0102261]; coenzyme F420 binding [GO:0070967]; cupric reductase activity [GO:0008823]; ferric-chelate reductase (NADPH) activity [GO:0052851]; NADP binding [GO:0050661]; oxidoreductase activity, acting on NAD(P)H [GO:0016651]; reduced coenzyme F420:NADP+ oxidoreductase activity [GO:0052808] | PF03807; | 3.40.50.720; | F420-dependent NADP reductase family | null | null | CATALYTIC ACTIVITY: Reaction=NADP(+) + reduced coenzyme F420-(gamma-L-Glu)(n) = 2 H(+) + NADPH + oxidized coenzyme F420-(gamma-L-Glu)(n); Xref=Rhea:RHEA:31363, Rhea:RHEA-COMP:12939, Rhea:RHEA-COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133980, ChEBI:CHEBI:139511; EC=1.5.1.40; Evidence={ECO:0000269|PubMed:9821972}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.3 mM for F420 (at pH 6.0) {ECO:0000269|PubMed:9821972}; KM=50 uM for NADPH (at pH 6.0) {ECO:0000269|PubMed:9821972}; KM=0.15 mM for F420H(2) (at pH 8.0) {ECO:0000269|PubMed:9821972}; KM=70 uM for NADP(+) (at pH 8.0) {ECO:0000269|PubMed:9821972}; Vmax=1500 umol/min/mg enzyme for F420 reduction with NADPH (at pH 6.0) {ECO:0000269|PubMed:9821972}; Vmax=1100 umol/min/mg enzyme for NADP(+) reduction with F420H(2) (at pH 8.0) {ECO:0000269|PubMed:9821972}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.5 for F420 reduction with NADPH, and 8.0 for NADP(+) reduction with F420H(2). {ECO:0000269|PubMed:9821972}; | null | FUNCTION: Catalyzes the reduction of NADP(+) with F420H(2) via hydride transfer, and the reverse reaction, i.e. the reduction of F420 with NADPH. Probably functions in the regeneration of NADPH required in biosynthetic reactions. {ECO:0000269|PubMed:9821972}. | Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) |
D9TT09 | SUCPP_THETC | MALKNKVQLITYPDSLGGNLKTLNDVLEKYFSDVFGGVHILPPFPSSGDRGFAPITYSEIEPKFGTWYDIKKMAENFDILLDLMVNHVSRRSIYFQDFLKKGRKSEYADMFITLDKLWKDGKPVKGDIEKMFLRRTLPYSTFKIEETGEEEKVWTTFGKTDPSEQIDLDVNSHLVREFLLEVFKTFSNFGVKIVRLDAVGYVIKKIGTSCFFVEPEIYEFLDWAKGQAASYGIELLLEVHSQFEVQYKLAERGFLIYDFILPFTVLYTLINKSNEMLYHYLKNRPINQFTMLDCHDGIPVKPDLDGLIDTKKAKEVVDICVQRGANLSLIYGDKYKSEDGFDVHQINCTYYSALNCDDDAYLAARAIQFFTPGIPQVYYVGLLAGVNDFEAVKKTKEGREINRHNYGLKEIEESVQKNVVQRLLKLIRFRNEYEAFNGEFFIEDCRKDEIRLTWKKDDKRCSLFIDLKTYKTTIDYINENGEEVKYLV | 2.4.1.329 | null | carbohydrate metabolic process [GO:0005975] | null | 1,4-alpha-oligoglucan phosphorylase activity [GO:0004645]; hexosyltransferase activity [GO:0016758] | PF00128; | 3.20.20.80; | Glycosyl hydrolase 13 family, Sucrose phosphorylase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=phosphate + sucrose 6(F)-phosphate = alpha-D-glucose 1-phosphate + beta-D-fructose 6-phosphate; Xref=Rhea:RHEA:38863, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:57723, ChEBI:CHEBI:58601; EC=2.4.1.329; Evidence={ECO:0000269|PubMed:24599311}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38864; Evidence={ECO:0000305|PubMed:24599311}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.9 mM for phosphate (at 55 degrees Celsius and pH 6.5) {ECO:0000269|PubMed:24599311}; KM=12.7 mM for sucrose 6(F)-phosphate (at 55 degrees Celsius and pH 6.5) {ECO:0000269|PubMed:24599311}; KM=76.5 mM for sucrose (at 55 degrees Celsius and pH 6.5) {ECO:0000269|PubMed:24599311}; KM=15.1 mM for D-fructose 6-phosphate (at 55 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24599311}; KM=15.6 mM for alpha-D-glucose 1-phosphate (at 55 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24599311}; KM=41.6 mM for D-fructose (at 55 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24599311}; Note=kcat is 82.6 sec(-1) for the phosphorolysis of sucrose 6(F)-phosphate (at 55 degrees Celsius and pH 6.5). kcat is 66.2 sec(-1) for the phosphorolysis of sucrose (at 55 degrees Celsius and pH 6.5). kcat is 24.2 sec(-1) for the synthetic direction with alpha-D-glucose 1-phosphate and D-fructose 6-phosphate as substrates (at 55 degrees Celsius and pH 6.0). kcat is 14.4 sec(-1) for the synthetic direction with alpha-D-glucose 1-phosphate and D-fructose as substrates (at 55 degrees Celsius and pH 6.0). {ECO:0000269|PubMed:24599311}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 and 6.5 for the synthetic and phosphorolytic reaction, respectively. Thermostable. Has a half-life of 60 hours at 60 degrees Celsius. {ECO:0000269|PubMed:24599311}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:24599311}; | FUNCTION: Catalyzes the reversible phosphorolysis of sucrose 6(F)-phosphate into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose 6-phosphate. May be involved in a new pathway for the degradation of sucrose, which could become phosphorylated on its fructose moiety during uptake via a PTS system. To a lesser extent, can also reversibly act on sucrose in vitro (PubMed:24599311). Is also able to catalyze transglycosylation reactions in vitro (PubMed:26074151). {ECO:0000269|PubMed:24599311, ECO:0000269|PubMed:26074151}. | Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) (Clostridium thermosaccharolyticum) |
D9X0I3 | ACNA_STRVT | MSANSFDARSTLQVGDESYEIFRLDKVEGSARLPYSLKVLLENLLRTEDGANITADHIRALGGWDSQAQPSQEIQFTPARVIMQDFTGVPCVVDLATMREAVKELGGDPAKINPLAPAELVIDHSVIADKFGTNDAFKQNVELEYGRNKERYQFLRWGQTAFDEFKVVPPGTGIVHQVNIEHLARTVMVRGGQAYPDTLVGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPVSMLIPRVVGFKLTGELKPGTTATDLVLTITEMLRGHGVVGKFVEFYGEGVAATSLANRATIGNMSPEFGSTAAIFPIDDETLNYLRLTGRSEQQVALVESYAKEQGLWLDPAAEPDFSEKLELDLSTVVPSIAGPKRPQDRIVLAEAAQQFAKDVLNYVEAPAAQPAASASPVDEASAESFPASDAPAYGSQENGAGAPQHADGTGAAVPSNPVTVTAPDGTSYEIDHGAVTVAAITSCTNTSNPYVMVAAALVAKKAVEKGLTRKPWVKTTLAPGSKVVTDYFEKSGLTPYLDKVGFNLVGYGCTTCIGNSGPLPEEVSKAVNDHDLAVTSVLSGNRNFEGRINPDVKMNYLASPPLVVAYALAGSMKVDITKDALGTDQDGNPVYLKDIWPSEAEVNDVVANAIGEDMFSKSYSDVFAGDAQWQALPIPTGNTFEWDPESTYVRKPPYFEGMEMEPAPVEDIAGARVLAKLGDSVTTDHISPAGAIKADTPAGKYLTEHGVERRDFNSYGSRRGNHEVMIRGTFANIRLRNQIAPGTEGGYTRDFTKDDAPVSFIYDASRNYIEQGIPLVVLAGKEYGSGSSRDWAAKGTALLGVKAVIAESYERIHRSNLIGMGVLPLQFPEGQSAATLGLTGEETFSFSGVTELNNGTTPRTVKVTTDTGVEFDAVVRIDTPGEADYYRNGGIMQYVLRSLIRK | 4.2.1.3 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P36683}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250|UniProtKB:P36683}; | citrate metabolic process [GO:0006101]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829] | 2-methylisocitrate dehydratase activity [GO:0047456]; 4 iron, 4 sulfur cluster binding [GO:0051539]; aconitate hydratase activity [GO:0003994]; iron-responsive element binding [GO:0030350]; metal ion binding [GO:0046872] | PF00330;PF00694; | 6.10.190.10;3.30.499.10;3.20.19.10; | Aconitase/IPM isomerase family | null | null | CATALYTIC ACTIVITY: Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336, ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3; Evidence={ECO:0000269|PubMed:23116164, ECO:0000305|PubMed:10559181}; CATALYTIC ACTIVITY: Reaction=citrate = cis-aconitate + H2O; Xref=Rhea:RHEA:10228, ChEBI:CHEBI:15377, ChEBI:CHEBI:16383, ChEBI:CHEBI:16947; Evidence={ECO:0000269|PubMed:23116164}; CATALYTIC ACTIVITY: Reaction=cis-aconitate + H2O = D-threo-isocitrate; Xref=Rhea:RHEA:22144, ChEBI:CHEBI:15377, ChEBI:CHEBI:15562, ChEBI:CHEBI:16383; Evidence={ECO:0000269|PubMed:23116164}; | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. {ECO:0000305|PubMed:10559181}. | null | null | FUNCTION: Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid (TCA) cycle (PubMed:10559181, PubMed:23116164). Aconitase activity is important for the initiation of morphological and physiological differentiation of S.viridochromogenes (PubMed:10559181, PubMed:23116164). In addition, the apo form of AcnA (lacking the [4Fe-4S] cluster) functions as a RNA-binding regulatory protein, which binds to iron responsive elements (IREs) located on the untranslated region of certain mRNAs, including recA and ftsZ (PubMed:23116164). Binding to IRE-like structures probably alters the target mRNA stability and regulates the protein amount (PubMed:23116164). The apo form plays a regulatory role in oxidative stress response (PubMed:23116164, PubMed:24498397). {ECO:0000269|PubMed:10559181, ECO:0000269|PubMed:23116164, ECO:0000269|PubMed:24498397}. | Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494) |
E0CJS3 | EOBII_PETHY | MDKKPCNSQDAEVRKGPWTMEEDLILINYIANHGEGVWNSLAKSAGLKRTGKSCRLRWLNYLRPDVRRGNITPEEQLLIMELHAKWGNRWSKIAKHLPGRTDNEIKNYWRTRIQKHIKQAETMNGQAASSEQNDHQEACTSQMSNGPNDNTIDQTYSPTSYSGNVDTFQAGPNFLTEANDNMWSMEDIWSMQLLNGD | null | null | circadian rhythm [GO:0007623]; floral organ senescence [GO:0080187]; green leaf volatile biosynthetic process [GO:0010597]; regulation of cell wall organization or biogenesis [GO:1903338]; regulation of DNA-templated transcription [GO:0006355]; regulation of flower development [GO:0009909]; regulation of gene expression [GO:0010468]; regulation of phenylpropanoid metabolic process [GO:2000762] | nucleus [GO:0005634]; plant-type cell wall [GO:0009505] | DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976] | PF00249; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:20543029}. | null | null | null | null | null | FUNCTION: MYB-type transcription factor controlling the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) by regulating the expression of ODO1 and EOBI, key regulators of the shikimate pathway, and of several biosynthetic floral scent-related genes including IGS, PAL2 and CFAT (PubMed:20543029, PubMed:21585571, PubMed:23275577). This scent, mostly produced in the evening and night by the petals, attracts the pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta) (PubMed:20543029, PubMed:21585571). Binds to and activates the ODO1 and EOBI promoters via MYB binding sites (MBS) 5'-AAACCTAAT-3' and 5'-CTAACT-3' (PubMed:20543029, PubMed:21585571, PubMed:22499185, PubMed:23275577). Regulates the promoters of IGS1, CFAT and PAL2 (PubMed:20543029). Controls flowers petal opening by modulating a global transcriptomic switch (PubMed:21464473). {ECO:0000269|PubMed:20543029, ECO:0000269|PubMed:21464473, ECO:0000269|PubMed:21585571, ECO:0000269|PubMed:22499185, ECO:0000269|PubMed:23275577}. | Petunia hybrida (Petunia) |
E0CX11 | STMP1_HUMAN | MLQFLLGFTLGNVVGMYLAQNYDIPNLAKKLEEIKKDLDAKKKPPSA | null | null | innate immune response [GO:0045087]; mitochondrial cytochrome c oxidase assembly [GO:0033617]; mitochondrial respirasome assembly [GO:0097250]; mitochondrial respiratory chain complex III assembly [GO:0034551]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227] | mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial outer membrane [GO:0005741]; mitochondrial respirasome [GO:0005746] | null | PF15054; | null | STMP1 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:35450818}; Single-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P0DP99}; Single-pass membrane protein {ECO:0000255}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P0DP99}. | null | null | null | null | null | FUNCTION: Microprotein involved in mitochondrial respiratory chain complex III (ubiquinol-cytochrome c oxidoreductase) and complex IV (mitochondrial cytochrome c oxidase complex) assembly (PubMed:35450818). Required for the formation of mitochondrial supercomplexes (SCs) (PubMed:35450818). Also required for the activation of the NLRP3 inflammasome (By similarity). {ECO:0000250|UniProtKB:P0DP99, ECO:0000269|PubMed:35450818}. | Homo sapiens (Human) |
E0CZ16 | KLHL3_MOUSE | MEGESVKPSPQPTAQAEDEEKNRRTVTVNAAHMGKAFKVMNELRSKRLLCDVMIVAEDVEVEAHRVVLAACSPYFCAMFTGDMSESKAKKIEIKDVDGQTLSKLIDYIYTAEIEVTEENVQVLLPAASLLQLMDVRQNCCDFLQSQLHPTNCLGIRAFADVHTCTDLLQQANAYAEQHFPEVMLGEEFLSLSLDQVCSLISSDKLTVSSEEKVFEAVISWINYEKETRLDHMAKLMEHVRLPLLPRDYLVQTVEEEALIKNNNTCKDFLIEAMKYHLLPLDQRLLIKNPRTKPRTPVSLPKVMIVVGGQAPKAIRSVECYDFEEGRWDQIAELPSRRCRAGVVFMAGHVYAVGGFNGSLRVRTVDVYDGVKDQWTSIASMQERRSTLGAAVLNDLLYAVGGFDGSTGLASVEAYSYKTNEWFFVAPMNTRRSSVGVGVVEGKLYAVGGYDGASRQCLSTVEQYNPATNEWIYVADMSTRRSGAGVGVLSGQLYATGGHDGPLVRKSVEVYDPGTNTWKQVADMNMCRRNAGVCAVNGLLYVVGGDDGSCNLASVEYYNPVTDKWTLLPTNMSTGRSYAGVAVIHKSL | null | null | distal tubule morphogenesis [GO:0072156]; gene expression [GO:0010467]; monoatomic ion homeostasis [GO:0050801]; potassium ion homeostasis [GO:0055075]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein catabolic process [GO:0030163]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; renal absorption [GO:0070293]; renal sodium ion absorption [GO:0070294]; ubiquitin-dependent protein catabolic process [GO:0006511] | Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoskeleton [GO:0005856]; cytosol [GO:0005829] | actin binding [GO:0003779]; cullin family protein binding [GO:0097602]; ubiquitin ligase-substrate adaptor activity [GO:1990756] | PF07707;PF00651;PF01344; | 1.25.40.420;2.120.10.80; | KLHL3 family | PTM: Phosphorylation at Ser-433 by PKA or PKC decreases the interaction with WNK1 and WNK4, leading to inhibit their degradation by the BCR(KLHL3) complex (By similarity). Phosphorylated at Ser-433 by PKC in response to angiotensin II signaling, decreasing ability to promote degradation of WNK1 and WNK4, leading to activation of Na-Cl cotransporter SLC12A3/NCC (PubMed:25313067). Phosphorylation at Ser-433 is increased by insulin (By similarity). Dephosphorylated at Ser-433 by calcineurin PPP3CA, promoting degradation of WNK1 and WNK4 (By similarity). {ECO:0000250|UniProtKB:Q9UH77, ECO:0000269|PubMed:25313067}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9UH77}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UH77}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9UH77}. | null | null | FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of ion transport in the distal nephron (PubMed:24821705, PubMed:25831548, PubMed:28052936, PubMed:35621709). The BCR(KLHL3) complex acts by mediating ubiquitination and degradation of WNK1 and WNK4, two activators of Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney, thereby regulating NaCl reabsorption (PubMed:24821705, PubMed:28052936, PubMed:35621709). The BCR(KLHL3) complex also mediates ubiquitination of CLDN8, a tight-junction protein required for paracellular chloride transport in the kidney, leading to its degradation (PubMed:25831548). {ECO:0000269|PubMed:24821705, ECO:0000269|PubMed:25831548, ECO:0000269|PubMed:28052936, ECO:0000269|PubMed:35621709}. | Mus musculus (Mouse) |
E0D877 | APY_AEDAL | MAGKPGIQLFVIFLLLSSFAAVVWAMDNMPADKDVSKLFPLTLIHINDLHARFDETNMKSNACTAKDQCIAGIARVYQKIQDLLKEYKSKNAIYLNAGDNFQGTLWYNLLRWQVTADFITKLKPTAMTLGNHEFDHTPKGLAPYLAELDKAGIPTLVANLVMNDDPDLKSSKIQKSIKVTVGGKTIGIIGVLYDKTHEIAQTGKVTLSNAVETVKREAAALKKDKVDIIVVLSHCSYDEDKKIAKEAGQDIDVIVGAHSHSFLYSKESNKPYDQKDKIEGPYPTIVESNNKRKIPIVQAKSFGKYVGRLTLYFDNEGEVKHWEGYPEFIDNKVKQDPKILEALIPWRKKVQEIGSTKVGETTIELDRDSCRDKECTLGVLYADAFADHYTNSSFRPFAIIQAGNFRNPIKVGKITNGDIIEAAPFGSTADLIRLKGDNLWAVAEHSLALDDENRTNCLQVSGLRIVIDPSKSVGSRVVKIDVMDNRNPKSEDLKPLDRNAEYFIALPSYLADGKDGFSAMKEATARWTGPLDSDVFKSYVEKIKKVDKLKLDRVIVCKAGSPCT | 3.6.1.5 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:P50635}; | AMP catabolic process [GO:0006196] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | 5'-nucleotidase activity [GO:0008253]; apyrase activity [GO:0004050]; ATP binding [GO:0005524]; metal ion binding [GO:0046872] | PF02872;PF00149; | 3.60.21.10;3.90.780.10; | 5'-nucleotidase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P50635}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5; Evidence={ECO:0000269|PubMed:21842387}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36796; Evidence={ECO:0000305}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.6 uM for ATP {ECO:0000269|PubMed:21842387}; Vmax=1.02 nmol/sec/ug enzyme toward ATP {ECO:0000269|PubMed:21842387}; | null | null | null | FUNCTION: Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation in the host (PubMed:21842387). Cleaves adenosine triphosphate (ATP) and adenosine diphosphate (ADP) to adenosine monophosphate (AMP) and inorganic phosphate (PubMed:21842387). May reduce probing time by facilitating the speed of locating blood. {ECO:0000269|PubMed:21842387}. | Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) |
E0SRA9 | ILVC_IGNAA | MAKIYKDEDISLEPIKNKTIAILGYGSQGRAWALNLRDSGLNVVVGLERQGDSWRRAIDDGFKPMYTKDAVAIADIIVFLVPDMVQKSLWLNSVKDFMKKGADLVFAHGFNIHFKIIEPPKDSDVYMIAPKSPGPIVRRSYEMGGGVPALVAVYQNVSGEALQKALAIAKGIGCARAGVIESTFKEETETDLFGEQVILVGGIMELIKASFETLVEEGYQPEVAYFETVNELKLIVDLIYEKGLTGMLRAVSDTAKYGGITVGKFIIDKSVRDKMKIVLERIRSGEFAREWIKEYERGMPTVFKELSELEGSTIETVGRKLREMMFRGMKQISSH | 1.1.1.383 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:25849365}; Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00435}; | amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099] | cytosol [GO:0005829] | ketol-acid reductoisomerase activity [GO:0004455]; magnesium ion binding [GO:0000287]; NADP binding [GO:0050661] | PF01450;PF07991; | 6.10.240.10;3.40.50.720; | Ketol-acid reductoisomerase family | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NAD(+) = (2S)-2-acetolactate + H(+) + NADH; Xref=Rhea:RHEA:30627, ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58476; EC=1.1.1.383; Evidence={ECO:0000269|PubMed:25172159, ECO:0000269|PubMed:26644020}; CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.383; Evidence={ECO:0000269|PubMed:25172159, ECO:0000269|PubMed:26644020}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.1 mM for S2AL (at pH 7 and 85 degrees Celsius) {ECO:0000269|PubMed:26644020}; Note=kcat is 3.3 sec(-1) for reductoisomerase activity with NADPH (at pH 7 and 85 degrees Celsius with S2AL as substrate) (PubMed:26644020). kcat is 0.03 sec(-1) for reductoisomerase activity with NADPH (at pH 7 with S2AL as substrate) (PubMed:25172159). kcat is 0.02 sec(-1) for reductoisomerase activity with NADH (at pH 7 with S2AL as substrate) (PubMed:25172159). {ECO:0000269|PubMed:25172159, ECO:0000269|PubMed:26644020}; | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}. | null | null | FUNCTION: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH or NADH to yield (R)-2,3-dihydroxy-isovalerate. {ECO:0000269|PubMed:25172159, ECO:0000269|PubMed:26644020}. | Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1) |
E0VIU9 | PRKN_PEDHC | MSILEWFWNILCGMAQYLTFSKNLTNDNLVNIYVKSNVGGTISVNLDPKSDIKNVKELVAPKLGLEPDDVKIIFAGKELLDSTVIEVLDFFSDILHAVKVNKKIKNVIPDKPLCETLEELHQLNDQKNVESIEESNLKNEGKNKAHFFIYCANPCKKINTGKLRVCCSECKHGAFTVDTDPQSWADVLDKNKITGVCNNVGCEGLYAKFYFKCASHPSQGENDTAVPLNLIKRNHKKIPCLACTDICDPVLVFSCDNRHVTCLECFKNYCGSRLKDRQFLSHPDFGYTLPCPAGCSNSFIEEVHHFRLLTDAQYEQYHRFATEEFILQAGGVLCPQPGCGQGILIDQNCNRVQCSCGYVFCGKCLEGFHLGECLNPTDVPFLSQNCDYPLDPEKLEKARWDEASSTVIKVLTKPCPKCRTSTERAGGCMHMICTRANCGFHWCWVCQGPWERDCMASHWFG | 2.3.2.31 | null | autophagy [GO:0006914]; negative regulation of protein phosphorylation [GO:0001933]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein polyubiquitination [GO:0000209]; regulation of apoptotic process [GO:0042981]; regulation of cellular response to oxidative stress [GO:1900407]; regulation of mitochondrion organization [GO:0010821]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; ubiquitin ligase complex [GO:0000151] | ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF00240;PF17976;PF17978; | 1.20.120.1750;2.20.25.20; | RBR family, Parkin subfamily | PTM: Auto-ubiquitinates in an E2-dependent manner leading to its own degradation. {ECO:0000250|UniProtKB:Q7KTX7}.; PTM: Phosphorylated (By similarity). Activation requires phosphorylation at Ser-92 by Pink1 and binding to Pink1-phosphorylated polyubiquitin chains (By similarity). Phosphorylation at Thr-176 by Pink1 is also important for mitochondrial localization (By similarity). {ECO:0000250|UniProtKB:Q7KTX7}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q7KTX7}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q7KTX7}. Note=Translocates from the cytosol to dysfunctional mitochondria that have lost their mitochondrial membrane potential; recruitment to mitochondria is Pink1-dependent. {ECO:0000250|UniProtKB:Q7KTX7}. | CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000269|PubMed:26161729}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:26161729}. | null | null | FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as Marf, Opa1, Sep1, Tom20 and porin (By similarity). Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates, depending on the context (PubMed:26161729). Protects against mitochondrial dysfunction during cellular stress, by acting downstream of Pink1, to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components (By similarity). Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy (By similarity). Appears to be particularly important in maintaining the physiology and function of cells with high energy demands that are undergoing stress or altered metabolic environment, including spermatids, muscle cells and neurons such as the dopaminergic (DA) neurons (By similarity). Activation and recruitment onto the outer membrane of damaged/dysfunctional mitochondria (OMM) requires Pink1-mediated phosphorylation of both park and ubiquitin (By similarity). In depolarized mitochondria, mediates the decision between mitophagy or preventing apoptosis by inducing either the poly- or monoubiquitination of porin/VDAC; polyubiquitination of porin promotes mitophagy, while monoubiquitination of porin decreases mitochondrial calcium influx which ultimately inhibits apoptosis (By similarity). When cellular stress results in irreversible mitochondrial damage, promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins (By similarity). Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains following mitochondrial damage, leading to mitophagy (By similarity). In developing tissues, inhibits JNK-mediated apoptosis by negatively regulating bsk transcription (By similarity). The Pink1-park pathway also promotes fission and/or inhibits fusion of damaged mitochondria by mediating the ubiquitination and subsequent degradation of proteins involved in mitochondrial fusion/fission such as Marf and Opa1 (By similarity). This prevents the refusion of unhealthy mitochondria with the healthy mitochondrial network and/or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (By similarity). Regulates motility of damaged mitochondria by phosphorylating Miro which likely promotes its park-dependent degradation by the proteasome; in motor neurons, this inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria being eliminated in the soma (By similarity). The Pink1-park pathway is also involved in mitochondrial regeneration processes such as promoting mitochondrial biogenesis, activating localized mitochondrial repair, promoting selective turnover of mitochondrial proteins and initiating the mitochondrial import of endogenous proteins (By similarity). Involved in mitochondrial biogenesis via the ubiquitination of transcriptional repressor Paris which leads to its subsequent proteasomal degradation and allows activation of the transcription factor srl (By similarity). Promotes localized mitochondrial repair by activating the translation of specific nuclear-encoded mitochondrial RNAs (nc-mtRNAs) on the mitochondrial surface, including several key electron transport chain component nc-mtRNAs (By similarity). {ECO:0000250|UniProtKB:Q7KTX7, ECO:0000269|PubMed:26161729}. | Pediculus humanus subsp. corporis (Body louse) |
E0W1I1 | PINK1_PEDHC | MSLLAYTNLLLQNGRIFRYYKKANIKKFIKKIIKLDLKSTPSEASVSRQTFLSTGLNSVKNAVQLQARKLLINNVLERVTPTLNSDLKKKAAKRLFYGDSAPFFALVGVSLASGSGLLTKDDELEGICWEIREAVSKGKWNDSESENVEQLQAANLDELDLGEPIAKGCNAVVYSAKLKNVQSNKLAHQLAVKMMFNYDVESNSTAILKAMYRETVPAMSYFFNQNLFNIENISDFKIRLPPHPNIVRMYSVFADRIPDLQCNKQLYPEALPPRINPEGSGRNMSLFLVMKRYDCTLKEYLRDKTPNMRSSILLLSQLLEAVAHMNIHNISHRDLKSDNILVDLSEGDAYPTIVITDFGCCLCDKQNGLVIPYRSEDQDKGGNRALMAPEIANAKPGTFSWLNYKKSDLWAVGAIAYEIFNIDNPFYDKTMKLLSKSYKEEDLPELPDTIPFIIRNLVSNMLSRSTNKRLDCDVAATVAQLYLWAPSSWLKENYTLPNSNEIIQWLLCLSSKVLCERDITARNKTNTMSESVSKAQYKGRRSLPEYELIASFLRRVRLHLVRKGLKWIQELHIYN | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22645651, ECO:0000269|PubMed:29160309}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:D6WMX4}; | autophagy [GO:0006914]; phosphorylation [GO:0016310]; positive regulation of mitochondrial fission [GO:0090141]; regulation of apoptotic process [GO:0042981] | cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Proteolytically cleaved. In healthy cells, the precursor is continuously imported into mitochondria where it is proteolytically cleaved into its short form by the mitochondrial rhomboid protease rho-7 (8231301). The short form is then released into the cytosol where it rapidly undergoes proteasome-dependent degradation. In unhealthy cells, when cellular stress conditions lead to the loss of mitochondrial membrane potential, mitochondrial import is impaired leading to the precursor accumulating on the outer mitochondrial membrane (OMM). {ECO:0000250|UniProtKB:Q0KHV6}.; PTM: Autophosphorylated (PubMed:22645651, PubMed:29160309). Autophosphorylated on Ser-202, which activates kinase activity (PubMed:29160309). Loss of mitochondrial membrane potential results in the precursor accumulating on the outer mitochondrial membrane (OMM) where it is activated by autophosphorylation at Ser-202 (By similarity). Autophosphorylation is sufficient and essential for selective recruitment of park to depolarized mitochondria, likely via Pink1-dependent phosphorylation of polyubiquitin chains (By similarity). Also autophosphorylated at Ser-204 and Thr-305 (PubMed:29160309). {ECO:0000250|UniProtKB:Q0KHV6, ECO:0000269|PubMed:22645651, ECO:0000269|PubMed:29160309}. | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q0KHV6}; Single-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q0KHV6}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q0KHV6}. Note=Localizes mostly in mitochondrion, and the smaller proteolytic processed fragment localizes in the cytosol as well (By similarity). When mitochondria are damaged, defective and/or enriched with deleterious mtDNA mutations, Pink1 import is arrested which induces its accumulation on the outer mitochondrial membrane where it acquires kinase activity (By similarity). {ECO:0000250|UniProtKB:Q0KHV6}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:22645651, ECO:0000269|PubMed:29160309}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:22645651, ECO:0000269|PubMed:29160309}; | null | null | null | null | FUNCTION: Acts as a serine/threonine-protein kinase (PubMed:22645651, PubMed:26161729, PubMed:29160309). Exhibits a substrate preference for proline at position P+1 and a general preference at several residues for basic residues such as arginine (By similarity). Also exhibits moderate preferences for a phosphotyrosine at position P-3 and a tryptophan at P-5 (By similarity). Critical to mitochondrial homeostasis it mediates several pathways that maintain mitochondrial health and function (By similarity) Protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins such as park and likely Drp1, to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components (PubMed:26161729). Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy (By similarity). Appears to be particularly important in maintaining the physiology and function of cells with high energy demands that are undergoing stress or altered metabolic environment, including spermatids, muscle cells and neurons such as the dopaminergic (DA) neurons (By similarity). Mediates the translocation and activation of park at the outer membrane (OMM) of dysfunctional/depolarized mitochondria (PubMed:26161729). At the OMM of damaged mitochondria, phosphorylates pre-existing polyubiquitin chains, the Pink1-phosphorylated polyubiquitin then recruits park from the cytosol to the OMM where park is fully activated by phosphorylation at 'Ser-94' by Pink1 (By similarity). When cellular stress results in irreversible mitochondrial damage, functions with park to promote the clearance of dysfunctional and/or depolarized mitochondria by selective autophagy (mitophagy) (By similarity). The Pink1-park pathway also promotes fission and/or inhibits fusion of damaged mitochondria, by phosphorylating and thus promoting the park-dependent degradation of proteins involved in mitochondrial fusion/fission such as Marf, Opa1 and fzo (By similarity). This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (By similarity). Also likely to promote mitochondrial fission independently of park and Atg7-mediated mitophagy, via the phosphorylation and activation of Drp1 (By similarity). Regulates motility of damaged mitochondria by phosphorylating Miro which likely promotes its park-dependent degradation by the proteasome; in motor neurons, this inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria being eliminated in the soma (By similarity). The Pink1-park pathway is also involved in mitochondrial regeneration processes such as promoting mitochondrial biogenesis, activating localized mitochondrial repair, promoting selective turnover of mitochondrial proteins and initiating the mitochondrial import of endogenous proteins (By similarity). Involved in mitochondrial biogenesis by promoting the park-dependent ubiquitination of transcriptional repressor Paris which leads to its subsequent proteasomal degradation and allows activation of the transcription factor srl (By similarity). Functions with park to promote localized mitochondrial repair by activating the translation of specific nuclear-encoded mitochondrial RNAs (nc-mtRNAs) on the mitochondrial surface, including several key electron transport chain component nc-mtRNAs (By similarity). During oogenesis, phosphorylates and inactivates larp on the membrane of defective mitochondria, thus impairing local translation and mtDNA replication and consequently, reducing transmission of deleterious mtDNA mutations to the mature oocyte (By similarity). Phosphorylates the mitochondrial acyl-CoA dehydrogenase Mcad, and appears to be important for maintaining fatty acid and amino acid metabolism via a mechanism that is independent of it's role in maintaining production of ATP (By similarity). {ECO:0000250|UniProtKB:D6WMX4, ECO:0000250|UniProtKB:Q0KHV6, ECO:0000269|PubMed:22645651, ECO:0000269|PubMed:26161729, ECO:0000269|PubMed:29160309}. | Pediculus humanus subsp. corporis (Body louse) |
E0W4V5 | PSR2_PHYSO | MRLQCVVLFAALTLVAATHAPPNVKTVLSAEQHDIPVKRLLRPGNPAGKEDEERGINFSSVPGFEKLANLLKPKPGLKKLLKWADAKKPPETVFTRLRLDKTGTQLFDNTDFPVWAAYTRSVAQTDSEASAVMLKTLVSRYSDEVLSGMIAAAKKSSKTESIATKLETEQMRTWLAAKKTPDDMFLVFKLNKAGDDILSSPLLSAWTNYMKLSNKENPKAQTTLIATMTKHYGDSGVSQILAAARKSPATQSTAKRLEAEQVQLWLKKGRTPDDTFTLLSLDRAGDDLLASPQFNTWMKYINYYNKENPDEKTTVLAKLMTHFDDEELTPILVVARKVPSTESTAAKLQAEQFKNWLSADKSPEEAFTLLQLDKAGDDLLTNPQLTNWLKYTENFNLNKEINEQVTAIQVFRAQYVDDSRIANMVIAAEKVPNTQAIAKRVEDELFKGWTVVLNKPDDVFINLKLETVGENVFESPLWSFYTKFLEKYNTANPGKEQTMISGLARGYNDVTLTNMLLKAKEAPSTKTLATKLEDELVQYWLADKKLPDKLFGYLELKESVDGILTNPVFNVWLKYLNAFNDKAPVKKALMIDTLKSAFGDVAVSNMLFAAKKDPGTAKVAATLQTALLSKWVLEKKTPGQVSAILKEGAGADVSAKLLATYSAKFKVRWG | null | null | null | extracellular region [GO:0005576]; host cell [GO:0043657] | null | null | null | RxLR effector family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23377181}. Host cell {ECO:0000305|PubMed:23377181}. | null | null | null | null | null | FUNCTION: Secreted effector that possesses RNA silencing suppression activity by inhibiting the biogenesis of small RNAs in the host plant to promote enhanced susceptibility of host to the pathogen during infection (PubMed:23377181, PubMed:25387135, PubMed:30595554). Interferes with secondary siRNA production by associating with host dsRNA-binding protein DRB4 (PubMed:30595554). Inhibits the host salicylic acid pathway during infection (PubMed:25387135). {ECO:0000269|PubMed:23377181, ECO:0000269|PubMed:25387135, ECO:0000269|PubMed:30595554}. | Phytophthora sojae (Soybean stem and root rot agent) (Phytophthora megasperma f. sp. glycines) |
E0W544 | AVH23_PHYSO | MRLTYFLTVIVVATLHAGGTALATAEAPNHAAIVNVASADNVHSLDTTAEIGGRMLRKVKEDTVSKKDHEERGPGAILERQTAFVKKLFSRQNAIVNRAQGAFQRQNAFVNRDQGAFQRQNAFVKRAIQRQNHFKLSDNA | null | null | null | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | null | PF16810; | null | RxLR effector family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28318979}. Host nucleus {ECO:0000269|PubMed:28318979}. Host cytoplasm {ECO:0000269|PubMed:28318979}. Note=Location into the host nucleus is required for virulence. {ECO:0000269|PubMed:28318979}. | null | null | null | null | null | FUNCTION: Effector that suppresses plant defense responses during the early stages of pathogen infection. Suppresses cell death induced by effectors and PAMPs in plant hosts (PubMed:21653195). Acts as a modulator of histone acetyltransferase (HAT) in plants. Avh23 binds to the ADA2 subunit of the HAT complex SAGA and disrupts its assembly by interfering with the association of ADA2 with the catalytic subunit GCN5. As such, Avh23 suppresses H3K9 acetylation mediated by the ADA2/GCN5 module and increases plant susceptibility (PubMed:28318979). {ECO:0000269|PubMed:21653195, ECO:0000269|PubMed:28318979}. | Phytophthora sojae (Soybean stem and root rot agent) (Phytophthora megasperma f. sp. glycines) |
E0WN94 | ODC_NICGL | MAGQTIIVSGLNPAAILQSTIGGGASPTAAAAAENGTRKVIPLSRDALQDFMLSIITQKLQDEKQPFYVLDLGEVVSLMDQWKSALPNIRPFYAVKCNPEPSFLSILSAMGSNFDCASRAEIEYVLALGISPDRIVFANPCKPESDIIFAAKVGVNLTTYDSEDEVYKIRKHHPKSELLLRIKPMFDGNARCPMGPKYGALPEEVEPLLRAAQAARLTVSGVSFHIGSGDADSNAYLGAIAAAKEVFETAAKLGMSKMTVLDVGGGFTSGHQFTAAAVAVKSALKQRFDDEPELTIIAEPGRFFAETAFTLATTIIGKRVRGELREYWINDGLYGSMNCVLYDHATVNATPLAVQSNRSNVTCGGSKTFPTTVFGPTCDALDTVLRDYQLPELQVNDWLVFPNMGAYTKAAGSNFNGFNTSAIVTHLAYAYPS | 4.1.1.17 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P11926}; | alkaloid metabolic process [GO:0009820]; nicotine biosynthetic process [GO:0042179]; putrescine biosynthetic process from ornithine [GO:0033387]; response to jasmonic acid [GO:0009753]; response to wounding [GO:0009611] | chloroplast [GO:0009507] | ornithine decarboxylase activity [GO:0004586] | PF02784;PF00278; | 3.20.20.10; | Orn/Lys/Arg decarboxylase class-II family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911, ChEBI:CHEBI:326268; EC=4.1.1.17; Evidence={ECO:0000250|UniProtKB:P11926}; | null | PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:21232776}.; PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1. {ECO:0000250|UniProtKB:O22616}. | null | null | FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (PubMed:21232776). Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine (By similarity). Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis (By similarity). {ECO:0000250|UniProtKB:P11926, ECO:0000269|PubMed:21232776}. | Nicotiana glauca (Glaucous tobacco) (Tree tobacco) |
E0X9C7 | TODS_PSEPT | MSSLDRKKPQNRSKNNYYNICLKEKGSEELTCEEHARIIFDGLYEFVGLLDAHGNVLEVNQVALEGAGITLEEIRGKPFWKARWWQISKKTEATQKRLVETASSGEFVRCDVEILGKSGGREVIAVDFSLLPICNEEGSIVYLLAEGRNITDKKKAEAMLALKNQELEQSVERIRKLDNAKSDFFAKVSHELRTPLSLILGPLEAVMAAEAGRESPYWKQFEVIQRNAMTLLKQVNTLLDLAKMDARQMGLSYRRANLSQLTRTISSNFEGIAQQKSITFDTKLPVQMVAEVDCEKYERIILNLLSNAFKFTPDGGLIRCCLSLSRPNYALVTVSDSGPGIPPALRKEIFERFHQLSQEGQQATRGTGLGLSIVKEFVELHRGTISVSDAPGGGALFQVKLPLNAPEGAYVASNTAPRRDNPQVVDTDEYLLLAPNAENEAEVLPFQSDQPRVLIVEDNPDMRGFIKDCLSSDYQVYVAPDGAKALELMSNMPPDLLITDLMMPVMSGDMLVHQVRKKNELSHIPIMVLSAKSDAELRVKLLSESVQDFLLKPFSAHELRARVSNLVSMKVAGDALRKELSDQGDDIAILTHRLIKSRHRLQQSNIALSASEARWKAVYENSAAGIVLTDPENRILNANPAFQRITGYGEKDLEGLSMEQLTPSDESPQIKQRLANLLQGGGAEYSVERSYLCKNGSTIWANASVSLMPQRVGESPVILQIIDDITEKKQAQENLNQLQQQLVYVSRSATMGEFAAYIAHEINQPLSAIMTNANAGTRWLGNEPSNIPEAKEALARIIRDSDRAAEIIRMVRSFLKRQETVLKPIDLKALVTDTSLILKAPSQNNSVNLDVVADDELPEIWGDGVQIQQLIINLAMNAIEAISQADCETRQLTLSFSGNDTGDALVISVKDTGPGISERQMAQLFNAFYTTKKEGLGMGLAICLTITEVHNGKIWVECPPAGGACFLVSIPARQGSGT | 2.7.13.3 | null | null | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; phosphorelay sensor kinase activity [GO:0000155] | PF02518;PF00512;PF08448;PF13426;PF00072; | 1.10.287.130;3.40.50.2300;3.30.565.10;3.30.450.20; | null | PTM: Autophosphorylated. Activation requires a sequential transfer of a phosphate group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22212183}. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:16702539, ECO:0000269|PubMed:19240030}; | null | null | null | null | FUNCTION: Member of the two-component regulatory system TodS/TodT involved in the regulation of toluene degradation. Phosphorylates TodT via a four-step phosphorelay in response to toluene. Can also be induced by benzene and ethylbenzene. {ECO:0000269|PubMed:16702539, ECO:0000269|PubMed:19240030, ECO:0000269|PubMed:22212183}. | Pseudomonas putida (strain DOT-T1E) |
E0Y3X1 | NOTF_ASPSM | MTAPELRVDTFRAPEDAPKEPSAQQPRLPSSPSPAQALASYHHFPTNDQERWWEETGSLFSRFLEAGQYGLPQQYQFMFFFMHHLIPALGPYPQKWRSTISRSGLPIEFSLNFQKGSHRLLRIGFEPVSFLSGSSQDPFNRIPITDLLNRLSKLQLSNFDTPFFQHLLSKFQLSLSEVRQLQKQGSGPDAHPLKSQAAFGFDFNPDGAILVKGYVFPYLKAKAADVPVGTLIAEAVRTIDVERNQFTHAFGLINDYMQESTGYNEYTFLSCDFVETSEQRLKIYGAHTEVTWAKIAEMWTLGGRLIEEPEIIAGLARLKQIWSLLQIGEGSRAFKGGFDYDKSSATDQIASPIIWNYEIHPGSRFPVPKFYLPVHGENDLHVARALAQFWDSLGWPEHACAYPDTLQQLYPDQDISQTTRLQSWISYSYTAKRGVYMSVYYHSQSTYLWEED | 2.5.1.109 | null | alkaloid metabolic process [GO:0009820] | null | prenyltransferase activity [GO:0004659] | PF11991; | null | Tryptophan dimethylallyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=brevianamide F + dimethylallyl diphosphate = deoxybrevianamide E + diphosphate; Xref=Rhea:RHEA:35943, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:64530, ChEBI:CHEBI:72948; EC=2.5.1.109; Evidence={ECO:0000269|PubMed:20722388}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35944; Evidence={ECO:0000269|PubMed:20722388}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.33 uM for brevianamide F {ECO:0000269|PubMed:20722388}; KM=1.31 uM for dimethylallyl diphosphate (DMAPP) {ECO:0000269|PubMed:20722388}; Vmax=0.89 uM/min/mg enzyme toward brevianamide F {ECO:0000269|PubMed:20722388}; Vmax=1.18 uM/min/mg enzyme toward dimethylallyl diphosphate (DMAPP) {ECO:0000269|PubMed:20722388}; | PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:20722388}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-9. {ECO:0000269|PubMed:20722388}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 4 to 42 degrees Celsius. {ECO:0000269|PubMed:20722388}; | FUNCTION: Deoxybrevianamide E synthase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core (PubMed:20722388). The first step of notoamide biosynthesis involves coupling of L-proline and L-tryptophan by the bimodular NRPS notE, to produce cyclo-L-tryptophan-L-proline called brevianamide F (PubMed:20722388). The reverse prenyltransferase notF then acts as a deoxybrevianamide E synthase and converts brevianamide F to deoxybrevianamide E via reverse prenylation at C-2 of the indole ring leading to the bicyclo[2.2.2]diazaoctane core (PubMed:20722388). Deoxybrevianamide E is further hydroxylated at C-6 of the indole ring, likely catalyzed by the cytochrome P450 monooxygenase notG, to yield 6-hydroxy-deoxybrevianamide E (Probable). 6-hydroxy-deoxybrevianamide E is a specific substrate of the prenyltransferase notC for normal prenylation at C-7 to produce 6-hydroxy-7-prenyl-deoxybrevianamide, also called notoamide S (PubMed:20722388). As the proposed pivotal branching point in notoamide biosynthesis, notoamide S can be diverted to notoamide E through an oxidative pyran ring closure putatively catalyzed by either notH cytochrome P450 monooxygenase or the notD FAD-linked oxidoreductase (Probable). This step would be followed by an indole 2,3-epoxidation-initiated pinacol-like rearrangement catalyzed by the notB FAD-dependent monooxygenase leading to the formation of notoamide C and notoamide D (PubMed:22188465). On the other hand notoamide S is converted to notoamide T by notH (or notD), a bifunctional oxidase that also functions as the intramolecular Diels-Alderase responsible for generation of (+)-notoamide T (Probable). To generate antipodal (-)-notoaminide T, notH' (or notD') in Aspergillus versicolor is expected to catalyze a Diels-Alder reaction leading to the opposite stereochemistry (Probable). The remaining oxidoreductase notD (or notH) likely catalyzes the oxidative pyran ring formation to yield (+)-stephacidin A (Probable). The FAD-dependent monooxygenase notI is highly similar to notB and is predicted to catalyze a similar conversion from (+)-stephacidin A to (-)-notoamide B via the 2,3-epoxidation of (+)-stephacidin A followed by a pinacol-type rearrangement (Probable). Finally, it remains unclear which enzyme could be responsible for the final hydroxylation steps leading to notoamide A and sclerotiamide (Probable). {ECO:0000269|PubMed:20722388, ECO:0000269|PubMed:22188465, ECO:0000305|PubMed:23213353}. | Aspergillus sp. (strain MF297-2) |
E0Y419 | VSPBF_MACLB | MVLIRVLANLLLLQLSHAQKSSELVVGGDECNINEHRSLVFLYNSSFGCGGTLINQEWVLSAAHCDMENMRIYLGWHNFSLPNMNQKRRVAKEKFFCLSSKNYTEWDKDIMLIKMNRPVTYSTHVAPLSLPSSPPSVGSVCRIMGWGAITSPNETYPDVPHCANINILNYTVCRAAHPWLPAQSRTLCAGILQGGIDTCKGDSGGPLICNGQIQGIVSWGDNPCAQPLKPGHYTNVFDYTDWIQSIIAGNTTATCPP | 3.4.21.- | null | proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | PTM: Glycosylated. Contains 23.0% of hexoses, 8.3% of hexosamines and 1.0% of sialic acids. {ECO:0000269|PubMed:11602278}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=77 uM for N-alpha-benzoyl-L-arginine ethyl ester (BAEE) (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:2028469}; KM=0.36 mM for Tosyl-L-arginine methyl ester (TAME) (at pH 8.5 and 25 degrees Celsius) {ECO:0000269|PubMed:2028469}; KM=0.18 mM for BAPNA (at pH 8.3 and 25 degrees Celsius) {ECO:0000269|PubMed:2028469}; | null | null | null | FUNCTION: Snake venom serine protease that has fibrinogenolytic activities by hydrolyzing the beta chain of fibrinogen (FGB). Typical arginine esterase which hydrolyzes esters and amides of arginine. {ECO:0000269|PubMed:11910177, ECO:0000269|PubMed:2028469}. | Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
E0Y421 | VSPY_MACLB | MVLIRVLANLLLLQLSYAQKSSELVVGGDECNINEHRSLVFLYNSSFGCGGTLINQQWVLSAAHCDMENVQIYLGLHNLRLRNQDEQIRVAEEKFFCLSNKSYTKWDKDIMLIRLNSSVTYNTHIAPLSLPSSPPRVGSVCRIMGWGAITSPNETFPNVPHCANINILRYSVCRAAYRGLPAQSRTLCAGILQGGIGSCMGDSGGPLICNGEIQGIVSWGDDICAQPHKPVHYTKVFDYSDWIQSIIAGNTTATCPL | 3.4.21.- | null | proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | PTM: Partial deglycosylation has not effect on enzyme activity. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom serine protease with tyrosine-specific chymotrypsin-like activity. Hydrolyzes the N-acetyl-L-tyrosine ethyl ester (ATEE). Has weak fibrinogenolytic activity. Weakly hydrolyzes azocasein, Aalpha-chain (FGA) and more slowly Bbeta-chain (FGB) of fibrinogen. Optimal substrates are angiotensins I and II (AGT). {ECO:0000269|PubMed:20950666}. | Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
E1AZ71 | CNGB1_MOUSE | MLGWVQRVLPQPPGTPQKTVETAGPQPETESKPEANPQPEPEPQQEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPVPEEAPPEVQALPPEEPMEGEGEAEAGPSLQETQVADPAQPTSQAQVAVAKVNRPSSWMLSWFWRGMQKVVPQPVCSNGGQNLAAGERDPDQGGAQIPEPCGTGDPGSAEASGTQDTEPSLWLLRWLEQNLEKVLPQPPPPSLAWKVEPEAAVLDPDPPGTPMQMEPTESPSQPNPGPLEPEEEPAAEPQPGFQSSSLPPPGDPVRLIEWLLHRLEMALPQPVLHGKAAEQEPGCPGMCDVQTISILPVEQVEHDLVLEEVDSCWEDAQQEDGASPQETEVAPAHEEESEAIVEIPRELTKIQEEREDEQEEDEEEKEEEKKKGEEEKEKEEEEKEKEKEKEEEKEEEEKEEEEEEEKEEEEEEKEEEEKEEEEKEEEEEEEEEEEEPIVLLDSCLVVQADVDECQLERTPSELASIQELPEEKEEKEEEKEEEKEEEEEKKEEEVEKKEEGEATNSTVPATKEHPELQVEDTDADSGPLIPEETLPPPERPPPSPVKSDTLTVPGAAAAGHRKKLPSQDDEAEELKALSPAESPVVAWSDPTTPQEADGQDRAASTASQNSAIINDRLQELVKMFKERTEKVKEKLIDPDVTSDEESPKPSPAKKAPEPDPAQKPAEAEVAEEEHYCDMLCCKFKRRPLKMYRFPQSIDPLTNLMYILWLFFVVLAWNWNCWLIPVRWAFPYQRADNIHFWLLMDYLCDFIYLLDITVFQMRLQFVKGGDIITDKKEMRNNYLKSRRFKMDLLCLLPLDFLYLKLGINPLLRLPRCLKYMAFFEFNNRLEAILSKAYVYRVIRTTAYLLYSLHLNSCLYYWASAFQGIGSTHWVYDGVGNSYIRCYYWAVKTLITIGGLPDPQTLFEIVFQLLNYFTGVFAFSVMIGQMRDVVGAATAGQTYYRSCMDSTVKYMNFYKIPRSVQNRVKTWYEYTWHSQGMLDESELMVQLPDKMRLDLAIDVNYSIVSKVALFQGCDRQMIFDMLKRLRSVVYLPNDYVCKKGEIGREMYIIQAGQVQVLGGPDGKAVLVTLKAGSVFGEISLLAVGGGNRRTANVVAHGFTNLFILDKKDLNEILVHYPESQKLLRKKARRMLRNNNKPKEEKSVLILPPRAGTPKLFNAALAAAGKMGPRGAKGGKLAHLRARLKELAALEAAARQQQLLEQAKSSQEAGGEEGSGATDQPAPQEPPEPKDPPKPPGPPEPSAQSSPPPASAKPEESTGEAAGPPEPSVRIRVSPGPDPGEQTLSVEVLEEKKEGAE | null | null | detection of chemical stimulus involved in sensory perception of smell [GO:0050911]; detection of light stimulus involved in visual perception [GO:0050908]; ion channel modulating, G protein-coupled receptor signaling pathway [GO:0099105]; membrane depolarization [GO:0051899]; monoatomic cation transmembrane transport [GO:0098655]; olfactory nerve maturation [GO:0021630]; photoreceptor cell maintenance [GO:0045494]; photoreceptor cell outer segment organization [GO:0035845]; phototransduction [GO:0007602]; positive regulation of gene expression [GO:0010628]; protein localization to organelle [GO:0033365]; regulation of cytosolic calcium ion concentration [GO:0051480]; response to odorant [GO:1990834]; retina homeostasis [GO:0001895]; sensory perception of smell [GO:0007608] | intracellular cyclic nucleotide activated cation channel complex [GO:0017071]; membrane [GO:0016020]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]; terminal bouton [GO:0043195] | cAMP binding [GO:0030552]; cGMP binding [GO:0030553]; cyclic nucleotide-activated monoatomic ion channel activity [GO:0043855]; intracellularly cAMP-activated cation channel activity [GO:0005222]; intracellularly cGMP-activated cation channel activity [GO:0005223]; protein-containing complex binding [GO:0044877] | PF00027; | 1.10.287.70;1.10.287.630;2.60.120.10; | Cyclic nucleotide-gated cation channel (TC 1.A.1.5) family, CNGB1 subfamily | null | SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:16980309}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q28181, ECO:0000305|PubMed:16980309}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q28181}; CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:A0A8I5ZN27, ECO:0000250|UniProtKB:Q9NQW8}; CATALYTIC ACTIVITY: Reaction=NH4(+)(in) = NH4(+)(out); Xref=Rhea:RHEA:28747, ChEBI:CHEBI:28938; Evidence={ECO:0000250|UniProtKB:Q28181}; CATALYTIC ACTIVITY: Reaction=Rb(+)(in) = Rb(+)(out); Xref=Rhea:RHEA:78547, ChEBI:CHEBI:49847; Evidence={ECO:0000250|UniProtKB:Q9NQW8}; CATALYTIC ACTIVITY: Reaction=Li(+)(in) = Li(+)(out); Xref=Rhea:RHEA:78551, ChEBI:CHEBI:49713; Evidence={ECO:0000250|UniProtKB:Q9NQW8}; CATALYTIC ACTIVITY: Reaction=Cs(+)(in) = Cs(+)(out); Xref=Rhea:RHEA:78555, ChEBI:CHEBI:49547; Evidence={ECO:0000250|UniProtKB:Q28181}; | null | null | null | null | FUNCTION: Pore-forming subunit of the rod cyclic nucleotide-gated channel. Mediates rod photoresponses at dim light converting transient changes in intracellular cGMP levels into electrical signals. In the dark, cGMP levels are high and keep the channel open enabling a steady inward current carried by Na(+) and Ca(2+) ions that leads to membrane depolarization and neurotransmitter release from synaptic terminals. Upon photon absorption cGMP levels decline leading to channel closure and membrane hyperpolarization that ultimately slows neurotransmitter release and signals the presence of light, the end point of the phototransduction cascade (By similarity) (PubMed:22802073). Pore-forming subunit of the olfactory cyclic nucleotide-gated channel. Operates in the cilia of olfactory sensory neurons where chemical stimulation of the odorant is converted to an electrical signal. Mediates odorant-induced cAMP-dependent Ca(2+) influx triggering neuron depolarization. The rise of intracellular Ca(2+) levels potentiates the olfactory response by activating Ca(2+)-dependent Cl(-) channels, but it also serves as a negative feedback signal to desensitize the channel for rapid adaptation to odorants (By similarity) (PubMed:16980309). Conducts cGMP- and cAMP-gated ion currents, with permeability for monovalent and divalent cations. The selectivity for Ca(2+) over Na(+) increases with cGMP concentrations, whereas the selectivity among monovalent ions is independent of the cGMP levels (By similarity). {ECO:0000250|UniProtKB:A0A8I5ZN27, ECO:0000250|UniProtKB:Q28181, ECO:0000250|UniProtKB:Q9NQW8, ECO:0000269|PubMed:16980309, ECO:0000269|PubMed:22802073}. | Mus musculus (Mouse) |
E1B328 | WR52N_ARATH | MTNCEKDEEFVCISCVEEVRYSFVSHLSEALRRKGINNVVVDVDIDDLLFKESQAKIEKAGVSVMVLPGNCDPSEVWLDKFAKVLECQRNNKDQAVVSVLYGDSLLRDQWLSELDFRGLSRIHQSRKECSDSILVEEIVRDVYETHFYVGRIGIYSKLLEIENMVNKQPIGIRCVGIWGMPGIGKTTLAKAVFDQMSSAFDASCFIEDYDKSIHEKGLYCLLEEQLLPGNDATIMKLSSLRDRLNSKRVLVVLDDVCNALVAESFLEGFDWLGPGSLIIITSRDKQVFRLCGINQIYEVQGLNEKEARQLFLLSASIMEDMGEQNLHELSVRVISYANGNPLAISVYGRELKGKKKLSEMETAFLKLKRRPPFKIVDAFKSSYDTLSDNEKNIFLDIACFFQGENVNYVIQLLEGCGFFPHVEIDVLVDKCLVTISENRVWLHKLTQDIGREIINGETVQIERRRRLWEPWSIKYLLEYNEHKANGEPKTTFKRAQGSEEIEGLFLDTSNLRFDLQPSAFKNMLNLRLLKIYCSNPEVHPVINFPTGSLHSLPNELRLLHWENYPLKSLPQNFDPRHLVEINMPYSQLQKLWGGTKNLEMLRTIRLCHSQHLVDIDDLLKAENLEVIDLQGCTRLQNFPAAGRLLRLRVVNLSGCIKIKSVLEIPPNIEKLHLQGTGILALPVSTVKPNHRELVNFLTEIPGLSEASKLERLTSLLESNSSCQDLGKLICLELKDCSCLQSLPNMANLDLNVLDLSGCSSLNSIQGFPRFLKQLYLGGTAIREVPQLPQSLEILNAHGSCLRSLPNMANLEFLKVLDLSGCSELETIQGFPRNLKELYFAGTTLREVPQLPLSLEVLNAHGSDSEKLPMHYKFNNFFDLSQQVVNDFFLKALTYVKHIPRGYTQELINKAPTFSFSAPSHTNQNATFDLQPGSSVMTRLNHSWRNTLVGFGMLVEVAFPEDYCDATDVGISCVCRWSNKEGRSCRIERNFHCWAPGKVVPKVRKDHTFVFSDVNMRPSTGEGNDPDIWAGLVVFEFFPINQQTKCLNDRFTVTRCGVRVINVATGNTSLENISLVLSLDPVEVSGYEVLRVSYDDLQEMDKVLFLYIASLFNDEDVDFVAPLIAGIDLDVSSGLKVLADVSLISVSSNGEIVMHSLQRQMGKEILHGQSMLLSDCESSMTENLSDVPKKEKKHRESKVKKVVSIPAIDEGDLWTWRKYGQKDILGSRFPRGYYRCAYKFTHGCKATKQVQRSETDSNMLAITYLSEHNHPRPTKRKALADSTRSTSSSICSAITTSASSRVFQNKDEPNQPHLPSSSTPPRNAAVLFKMTDMEEFQDNMEVDNDVVDTRTLALFPEFQHQPEEEDPWSTFFDDYNFYF | null | null | defense response [GO:0006952]; signal transduction [GO:0007165] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565] | PF07725;PF00931;PF03106; | 1.10.8.430;3.40.50.300;3.80.10.10;3.40.50.10140;2.20.25.80; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12788974}. Cytoplasm {ECO:0000305|PubMed:12788974}. Note=The nuclear localization is only detected upon interaction with PopP2. {ECO:0000269|PubMed:12788974}. | null | null | null | null | null | FUNCTION: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Acts also as a disease resistance protein involved in resistance to fungal and bacterial pathogens, including R.solanacearum, P.syringae pv. tomato and C.higginsianum. RRS1 mediated resistance depends on salicylic acid and NDR1 (AC O48915). {ECO:0000250|UniProtKB:P0DKH5, ECO:0000269|PubMed:11842188, ECO:0000305}. | Arabidopsis thaliana (Mouse-ear cress) |
E1BB50 | CDK12_BOVIN | MPNPERHGGKKDGSGGASGTLQPSSGGGSSNSRERHRLGSKHKRHKSKHSKDMGLVTPEAAPLGTVIKPLVEYDDISSDSDTFSDDLAFKVDRRENDERRGTDRSDRLHKHRHHQHRRTRDLLKTKQTEKEKNLEASSKSGSTKDRISGSSKRSNEENDDHGKAQISKSSNKESRSSKLHKEKTRKERELKSGHKDRSKSHRKRETPKSYKTVDSPKRRSRSPHRKWSDSPKQDDSPSGASYGQDYDLSPPRSHTSSNYDSYKKSPGSTSRRQSISPPYKEPSAYQSSTRSPSPYSRRQRSVSPYSRRRSSSYERSGSYSGRSPSPYGRRRSSSPFLSKRSLSRSPLPSRKSMKSRSRSPAYSRHSSSHSKKKRSGSRSRHSSISPVRLPLNSSLGAELSRKKKERAAAAAAAKMDGKESKGSPIFLPKKENSSVEAKDSGLEPKKLPRGVKLEKSAPDTELVNVTHLNTEVKNSLDTGKVKLDENSEKHPVLKDTKVQGTKDSKPVALKEEIVTPKETETSEKETLPPLPTVTSPPPLPTTTPPPQTPPLPPLPPLPAIPQQPPLPPPQPTFSQVLSSSTSTLPPSVHPRTSTLSSQANSQPSVQVSVKTQVSVTAAIPHLKTSTLPPLPLPPLLLGDDDMDSPKETLPSKPVKKEKEQRPRHLLTDLPLPPELPGGDPSPPDSPEPKAITPPQQPYKKRPKICCPRYGERRQTESDWGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLIHRSVVNMKEIVTDKQDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSGQIKLADFGLARLYNSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPYFNTMKPKKQYRRRLREEFSFFFLPWGALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSKMDPPDLPHWQDCHELWSKKRRRQRQSGVLVEEPPPPKASRKETISGTSAEPVKNSSPAPPQPAPGKVEPGAGDAIGLGDITQQLNQSELAVLLNLLQSQTDLSIPQMAQLLNIHSNPEMQQQLEALNQSISALTAATSQQQDSEPTAPEESLKEIAPAPAVQPSAEQTTPEASSTPADMQNMLAVLLSQLMKTQEPAGNLEENNSDKNSGPQGPRRTPTMPQEEAAGKQTGHESH | 2.7.11.22; 2.7.11.23 | null | mRNA processing [GO:0006397]; phosphorylation [GO:0016310]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; regulation of MAP kinase activity [GO:0043405]; RNA splicing [GO:0008380] | cyclin/CDK positive transcription elongation factor complex [GO:0008024]; nuclear cyclin-dependent protein kinase holoenzyme complex [GO:0019908]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353] | PF12330;PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | PTM: Phosphorylation at Thr-893 increases kinase activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Colocalized with nuclear speckles throughout interphase. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; | null | null | null | null | FUNCTION: Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors (By similarity). {ECO:0000250}. | Bos taurus (Bovine) |
E1BB52 | CDK13_BOVIN | MPSSSDTALGGGGGLSWAEKKLEERRKRRRFLSPQQPPLLLPLLQPQLLQPPPPPPPLLFLAAPGTAAAAAAAAAASSSCFSPGPPLEVKRLARGKRRAGGRQKRRRGPRAGQEAEKRRVFSLPQPQQDGGGGASSGGGVTPLVEYEDVSSQSEQGLLLGGASAATAATAAGGTGGSGGSPASSSGTQRRGEGSERRPRRDRRSSSGRSKDRHREHRRRDGQRGGGEASKSRSRHGHGGEERAEAGKSGSSSSSGGRRKSASATSSSSSSRKDRDPKAHRSRTKSSKEPPSAYKEPPKAYREDKTEPKAYRRRQRSLSPLGGRDDSPVSHRASQSLRNRKSPSPAGGGSSPYSRRLARSPSPYSRRRSPSYSRHSSYERGGDVSPSPYSSSSWRRSRSPYSPVIRRSAKSRSRSPYSSRHSRSRSRHRLSRSRSRHSSISPSTLTLKSSLAAELNKNKKARAAEAARAAEAAKAAEAAKAAEAAAKAAKAASTSTPTKGNTETGASASQTNHVKDVKKLKTEHAPSPSSGGTLKNDKAKTKPPLQVTKVDNNLIVDKATKKAVVVGKESKSAATKEEPVSLKEKTKPLTPSIGAKEKEQHVALVTSTLPPLPLPPMLPEDKDADSLRGNISVKAVKKEVEKKLRCLLADLPLPPELPGGDDLSKSPEEKKTATQLHNKRRPKICGPRFGEIKEKDIDWGKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIKLPYFNTMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVEPSKMPPPDLPLWQDCHELWSKKRRRQKQMGMTDDVSTVKAPRKDLSLGMDDSRTSTPQSVLPSSQLKPQGNSNAAPVKTGPGQQLNHSELAILLNLLQSKTSVNMADFVQVLNIKVNSETQQQLNKINLPAGILATGEKQTDPSTPQQESSKPLGGIQPSQNMQPKVEPDAAQAAVQSAFAVLLTQLIKAQQSKQKDVLLEERENGSGHEAPLQLRPPPEPATPASGQDDLIQHQDMRLLELTPEPDRPRILPPDQRPPEPPEPPPVTEEDLDYRTENQHVPTTSSSLTDPHAGVKAALLQLLAQHQPQDDPKRESGIDYQAGDTYVPSSDYKDNFGSSSFSSAPYVSNDGLGSASAPPLERRSFMGNSDIQSLDNYSTTSSHSGGPPQPSAFSESFPSSVAGYGDIYLNTGPMLFSGDKDHRFEYSHGPIAVLANSSDPSTGPESTHPLPAKMHNYNYGGSLQETPGGHGLMHGQTWTSPAQGPGYSQGYRGHISTSAGRGRGRGLPY | 2.7.11.22; 2.7.11.23 | null | alternative mRNA splicing, via spliceosome [GO:0000380]; hemopoiesis [GO:0030097]; phosphorylation [GO:0016310]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968] | cyclin/CDK positive transcription elongation factor complex [GO:0008024]; nuclear cyclin-dependent protein kinase holoenzyme complex [GO:0019908]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353] | PF12330;PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | null | SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; | null | null | null | null | FUNCTION: Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis (By similarity). {ECO:0000250}. | Bos taurus (Bovine) |
E1BBQ2 | MGLYR_BOVIN | MGVMAYPFLFCLLLVHFGLGAIGASREAPSRPDPPRERTLRAKQHAQQPARASASDPSAPWSRSTDGTILAQKLAEEVPMDVASYLYTGDSHKLKRANCSSRYELAGLPGKSPALASSHPSLHGALDTLTHATNFLNMMLQSNKSREQNLQDDLEWYQALVRSLLEGEPSISRAAITFSTESLSAPAPQVFLQATREESRILLQDLSSSAHHLANATLETEWFHGLRRKWRTHLHRRGSNQGPRGLGHSWRRRDGLSGDKSHVKWSPPYLECENGSYKPGWLVTLSAAFYGLQPNLVPEFRGVMKVDINLQKVDIDQCSSDGWFSGTHKCHLNNSECMPIKGLGFVLGAYQCICKAGFYHPRDFSFNNFQRRGPDHHFVESAKDVSEEVHVCLPCSEGCPYCADDSPCFVQEDKYLRLAIISFQALCMLLDFLSMLVVYRFRKAKSIRASGLILLETILFGSLLLYFPVVILYFEPSTFRCILLRWVRLLGFATVYGTVTLKLHRVLKVFLSRTAQRIPYMTGGRVMRMLAVILLVVFWFLVGWTSSVCQNLERHISLIGQGRTSDHLIFSMCLVERWDYMTAAAEFLFLLWGVYLCYAVRTVPSAFHEPRYMAVAVHNELIISAIFHTIRFVLASRLQSDWMLMLYFAHTHLTVTVTIGLLLIPKFSHSSNNPRDDIATEAYEDELDMGRSGSYLNSSINSAWSEHSLDPEDIRDELKKLYAQLEIYKRKKMITNNPHLQKKRCSKKGLGRSIMRRITEIPETVSRQCSKEDKDGGEHGSAKGSSAGRKNPQETAGGSGKPKEESLRSRVFSLKKSHSTYEHVREQPGGPGSPPAQSREEEEATDNSVLGSPVGANRPRPLQEDSQAVSTESVPLVCKSASAHNLSSEKKPGPTRTSVLQKSLSVIASAKEKTLGLAGKTQAACVEERAKAQKALPRERETNRKYSNSDNAETQDSAPPNSSHSEEPRKPQKLGIMKQQRANPTTANSDLSPGATHMKDNFDIGEVCPWEIYDLAPGPGPLESKVQKHVSIAASEMERNPTFSLKEKSHPKPKAADLCQQSNPKSVDKAEVCPWESQGQSLFEEEKYLMSKTQVPLGRAQGENSGQHCATGVCAGQCEELPPKAVASKVENENLNQLGEQEKKTSSSERNVPDSHNSSNNFQPPLMSRAEVCPWEFETPDKPNAERSVAFPASSALSANKIAGPRNEEVRLARKV | null | null | cognition [GO:0050890]; G protein-coupled receptor signaling pathway [GO:0007186]; protein localization to plasma membrane [GO:0072659]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; regulation of synapse organization [GO:0050807] | cell projection [GO:0042995]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734] | enzyme activator activity [GO:0008047]; G protein-coupled glycine receptor activity [GO:0160079]; transmembrane signaling receptor activity [GO:0004888] | PF00003; | 3.30.450.20; | G-protein coupled receptor 3 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5T848}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5T848}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q8C419}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5T848}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q8C419}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5T848}. Nucleus {ECO:0000250|UniProtKB:Q5T848}. Note=Mainly localizes to the postsynaptic membrane, with a small portion to the presynaptic membrane (By similarity). Trafficks between the nucleus and the cell membrane; it is unclear how a multi-pass membrane protein can traffick between the nucleus and the cell membrane (By similarity). {ECO:0000250|UniProtKB:Q5T848, ECO:0000250|UniProtKB:Q8C419}. | null | null | null | null | null | FUNCTION: Metabotropic receptor for glycine that controls synapse formation and function in the brain. Acts as an atypical G-protein coupled receptor that recruits and regulates the RGS7-GNB5 complex instead of activating G proteins. In absence of glycine ligand, promotes the GTPase activator activity of RGS7, increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Glycine-binding changes the conformation of the intracellular surface, inhibiting the GTPase activator activity of the RGS7-GNB5 complex, promoting G protein alpha subunits into their active GTP-bound form and regulating cAMP levels. Also able to bind taurine, a compound closely related to glycine, but with a two-fold lower affinity. Glycine receptor-dependent regulation of cAMP controls key ion channels, kinases and neurotrophic factors involved in neuronal excitability and synaptic transmission (By similarity). Plays a pivotal role in regulating mood and cognition via its ability to regulate neuronal excitability in L2/L3 pyramidal neurons of the prefrontal cortex. Also involved in spatial learning by regulating hippocampal CA1 neuronal excitability. Acts as a synaptic organizer in the hippocampus, required for proper mossy fiber-CA3 neurocircuitry establishment, structure and function: induces presynaptic differentiation in contacting axons via its interaction with GPC4. In addition to glycine, may also act as a receptor for osteocalcin (BGLAP) hormone: osteocalcin-binding initiates a signaling response that prevents neuronal apoptosis in the hippocampus and regulates the synthesis of neurotransmitters (By similarity). {ECO:0000250|UniProtKB:Q5T848, ECO:0000250|UniProtKB:Q8C419}. | Bos taurus (Bovine) |
E1BE10 | PLD6_BOVIN | MRPLRWQVAVVAAAGLALALETLPAVLRWLWVRRRRPRREVLFFPSQVTCTEALLRSPGATPSGCPCSLPHGESSLSRLLSALLAARVSLELCLFAFSSPQLGRAVQLLHQRGVRVRVVTDCDYMALNGSQIGLLRKAGIQVRHDQDLGYMHHKFAIVDRKVLITGSLNWTTQAIQNNRENVLIVEDEEYVRLFLEEFERIWEEFNPTRFSFFPQKERAR | 3.1.4.- | null | lipid catabolic process [GO:0016042]; meiotic cell cycle [GO:0051321]; mitochondrial fusion [GO:0008053]; P granule organization [GO:0030719]; piRNA processing [GO:0034587]; spermatid development [GO:0007286] | Golgi apparatus [GO:0005794]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886] | cardiolipin hydrolase activity [GO:0035755]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; RNA endonuclease activity, producing 5'-phosphomonoesters [GO:0016891] | PF13091; | 3.30.870.10; | Phospholipase D family, MitoPLD/Zucchini subfamily | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q5SWZ9}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q5SWZ9}. Nucleus membrane {ECO:0000250|UniProtKB:Q5SWZ9}. Cell membrane {ECO:0000250|UniProtKB:Q5SWZ9}. Golgi apparatus {ECO:0000250|UniProtKB:Q5SWZ9}. Note=Localization in the mitochondrial outer membrane is found in different cell types where phospholipase was the predominant activity, however, in pachytene spermatocytes and spermatids of mouse testes where nuclease activity is predominant, localization is restricted to the Golgi, suggesting this enzyme is localized in different subcellular compartments depending on the role (phospholipase or nuclease) it needs to play in each cell type and developmental stage. {ECO:0000250|UniProtKB:Q5SWZ9}. | CATALYTIC ACTIVITY: Reaction=a cardiolipin + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a 1,2-diacyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:44884, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58608, ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; Evidence={ECO:0000250|UniProtKB:Q8N2A8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44885; Evidence={ECO:0000250|UniProtKB:Q8N2A8}; | null | null | null | null | FUNCTION: Presents phospholipase and nuclease activities, depending on the different physiological conditions. Interaction with Mitoguardin (MIGA1 or MIGA2) affects the dimer conformation, facilitating the lipase activity over the nuclease activity. Plays a key role in mitochondrial fusion and fission via its phospholipase activity. In its phospholipase role, it uses the mitochondrial lipid cardiolipin as substrate to generate phosphatidate (PA or 1,2-diacyl-sn-glycero-3-phosphate), a second messenger signaling lipid. Production of PA facilitates Mitofusin-mediated fusion, whereas the cleavage of PA by the Lipin family of phosphatases produces diacylgycerol (DAG) which promotes mitochondrial fission. Both Lipin and DAG regulate mitochondrial dynamics and membrane fusion/fission, important processes for adapting mitochondrial metabolism to changes in cell physiology. Mitochondrial fusion enables cells to cope with the increased nucleotide demand during DNA synthesis (By similarity). Mitochondrial function and dynamics are closely associated with biological processes such as cell growth, proliferation, and differentiation. Mediator of MYC activity, promotes mitochondrial fusion and activates AMPK which in turn inhibits YAP/TAZ, thereby inducing cell growth and proliferation. The endonuclease activity plays a critical role in PIWI-interacting RNA (piRNA) biogenesis during spermatogenesis. Implicated in spermatogenesis and sperm fertility in testicular germ cells, its single strand-specific nuclease activity is critical for the biogenesis/maturation of PIWI-interacting RNA (piRNA). MOV10L1 selectively binds to piRNA precursors and funnels them to the endonuclease that catalyzes the first cleavage step of piRNA processing to generate piRNA intermediate fragments that are subsequently loaded to Piwi proteins. Cleaves either DNA or RNA substrates with similar affinity, producing a 5' phosphate end, in this way it participates in the processing of primary piRNA transcripts. piRNAs provide essential protection against the activity of mobile genetic elements. piRNA-mediated transposon silencing is thus critical for maintaining genome stability, in particular in germline cells when transposons are mobilized as a consequence of wide-spread genomic demethylation. PA may act as signaling molecule in the recognition/transport of the precursor RNAs of primary piRNAs. Interacts with tesmin in testes, suggesting a role in spermatogenesis via association with its interacting partner (By similarity). {ECO:0000250|UniProtKB:Q5SWZ9, ECO:0000250|UniProtKB:Q8N2A8}. | Bos taurus (Bovine) |
E1BF86 | BEST2_BOVIN | MTVTYTARVAKARFGGFSKLLLLWRGSIYKLLWRELLCFLGLFMALSAAYRFVLTEEQKRYFEKLVLYCDRYASLIPVSFVLGFYVTLVVHRWWNQYLSMPLTDALMCVVVGTVHGHDERGRLYRRTLMRYAGLSGVLILRSVSTAVFKRFPTIDHVVEAGFMTREERKKFENLNSSYNKYWVPCVWFCNLAAQARREGRIRDNGAFKLLLEELNVFRSKCGMLFHYDWISVPLVYTQVVTIAVYSYFLACLIGRQFLDPAQGYKDHDLDLCVPIFTLLQFFFYAGWLKVAEQLINPFGEDDDDFETNFLIDRCFQVSMLAVDEMYDDLAMLEKDLYWDAAEARAPYTAATAFLMQQPSFQGSTFDITLAKEDMQFQRQDGLEAPLNEAHGDFLQRLLPVGTGMGTGGLLGRRVPLLRRKNSHVSEESMAASCACAGAPDGAVPECGCEGPLVDLGQPEPESEPITGPESPALVPAPRAPSEPLTVVPLSGTRGPAPPWLPSPIGEEEESLA | null | null | bicarbonate transport [GO:0015701] | basolateral plasma membrane [GO:0016323]; chloride channel complex [GO:0034707]; plasma membrane [GO:0005886] | bicarbonate channel activity [GO:0160133]; chloride channel activity [GO:0005254]; intracellularly ligand-gated monoatomic ion channel activity [GO:0005217]; ligand-gated monoatomic anion channel activity [GO:0099095]; ligand-gated monoatomic cation channel activity [GO:0099094] | PF01062; | null | Anion channel-forming bestrophin (TC 1.A.46) family, Calcium-sensitive chloride channel subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32251414}; Multi-pass membrane protein {ECO:0000305|PubMed:32251414, ECO:0000305|PubMed:35789156, ECO:0000305|PubMed:36289327}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8NFU1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NFU1}. | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:32251414, ECO:0000269|PubMed:36289327}; CATALYTIC ACTIVITY: Reaction=iodide(out) = iodide(in); Xref=Rhea:RHEA:66324, ChEBI:CHEBI:16382; Evidence={ECO:0000269|PubMed:32251414}; CATALYTIC ACTIVITY: Reaction=hydrogencarbonate(in) = hydrogencarbonate(out); Xref=Rhea:RHEA:28695, ChEBI:CHEBI:17544; Evidence={ECO:0000250|UniProtKB:Q8NFU1}; CATALYTIC ACTIVITY: Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336, ChEBI:CHEBI:29985; Evidence={ECO:0000250|UniProtKB:Q8NFU1}; CATALYTIC ACTIVITY: Reaction=L-glutamine(out) = L-glutamine(in); Xref=Rhea:RHEA:73419, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q8NFU1}; | null | null | null | null | FUNCTION: Ligand-gated anion channel that allows the movement of anions across cell membranes when activated by calcium (Ca2+) (PubMed:32251414, PubMed:36289327). Transports a large specter of anions, namely mediates the movement of chloride, L-glutamate and iodide (PubMed:32251414, PubMed:36289327). Calcium-binding triggers the dilation of the aperture, but calcium-dependent gating is only effective when the size of the passing anion is bigger than the closed aperture (PubMed:32251414). Mediates the calcium-activated hydrogencarbonate movement and participates in colonic hydrogencarbonate secretion concomitant with mucin secretion (By similarity). In non-pigmented epithelium (NPE), mediates the efflux of intracellular L-glutamate; binding of intracellular L-glutamate activates and open both the neck and the aperture of the channel, leading to L-glutamate exit promoting chloride influx movement from the extracellular side in trans (By similarity). Also exhibits a directional permeability for intracellular glutamine, in a similar manner as for L-glutamate (By similarity). {ECO:0000250|UniProtKB:Q8BGM5, ECO:0000250|UniProtKB:Q8NFU1, ECO:0000269|PubMed:32251414, ECO:0000269|PubMed:36289327}. | Bos taurus (Bovine) |
E1BFR5 | GWL_BOVIN | MEPTMGGEMESGGGAATGECVNRIPVPRPPSIEEFTIVKPISRGAFGKVYLGQKGNRLYAVKVVKKADMINKNMTHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRDIDINMMDILTTPSMAKPRQDYSRTPGQVLSLISSLGFHTPVAEGNHDTANVLSTQVSETSPLSQGLTCPMSVDQKDTTPYSSKLLKSCPEMVASHPRMPVKCLTSHLLQSRKRLATSSTSSPSHTFISSMESECHSSPRWEKDCQESDDAAGSTMMSWNTVEKPLCTKSVDAMETKSFNERDLELALSPIHNSSVVPATGNSYVNLAKKCSSGEVSWEARELDVNNINMTADTSQYCFHESNQRAVDSGGMTEEHLGKRSCKRIFELVDSSPRQGIIPNKKSCFEYECSNEMRDCYATQRTGFAFEVQDLKLLVYRDQQNDCVNKENVGSSFTDKHQTPEKSPVPMIEKNLMCELDDDCDKNSKKDYLSSSFLCSDGDRTPKSIHMDSDSSFPGISIMESPLGGQSLDPDKNIKESSLEESNIEDLLPVSPSCQESTLPKGVECPTIQDSNQKMLAPSSEVLKPLTSKRNAVAFRSFNSHINASNSSEPSKMSITSLDMMDVSCAYSGSYPTAITPTQRERSDMPYQQTPNQVKSETPYRTPKSVRRGAAPVDDGRILGTPDYLAPELLLARAHGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILKRDIPWPEGEEKLSDNAQSAVDILLTIDDTKRAGMKELKHHPLFSGVDWENLQHQKMPFIPQPDDETDTSYFEARNNAQHLTVSGFSL | 2.7.11.1 | null | cell division [GO:0051301]; DNA damage response [GO:0006974]; G2/M transition of mitotic cell cycle [GO:0000086]; intracellular signal transduction [GO:0035556]; mitotic cell cycle [GO:0000278]; negative regulation of phosphoprotein phosphatase activity [GO:0032515]; phosphorylation [GO:0016310] | centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein phosphatase 2A binding [GO:0051721]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family | PTM: Phosphorylation at Thr-745 by CDK1 during M phase activates its kinase activity. Maximum phosphorylation occurs in prometaphase (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus. Note=During interphase is mainly nuclear, upon nuclear envelope breakdown localizes at the cytoplasm and during mitosis at the centrosomes. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | null | null | null | null | FUNCTION: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser-62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited (By similarity). {ECO:0000250}. | Bos taurus (Bovine) |
E1BGN7 | CGAS_BOVIN | MAPPRRKATRKASETASGVSAPCVEGGLSAEPSEPAAVPEAPRPGARRCGAAGASGSRREKSRLDPREKPQVRARAARAEDQAEGPAAPTADAEPPAAPGHSLPRASTRSRGTASSARARRPQSGPPEGPGLGPRAPSPHLGRREEAPGAWKPRAVLEKLKLSRQEISVAAEVVNRLGDHLLRRLNSRESEFKGVDLLRTGSYYERVKISAPNEFDLMFTLEVPRIQLEEYCNSSAHYFVKFKRNPKGSPLDQFLEGGILSASKMLFKFRKIIKEEIKHIEDTDVIMERKKRGSPAVTLLIRKPREISVDIILALESKSSWPASTQKGLPISNWLGTKVKDNLKRQPFYLVPKHAKEGSLFQEETWRLSFSHIEKAILTNHGQTKTCCETEGVKCCRKECLKLMKYLLEQLKKKFGKQRGLDKFCSYHVKTAFLHVCTQNPHDSWWLYKDLELCFDNCVTYFLQCLKTEHLEHYFIPDVLSKQIEYEQNNGFPVFDEF | 2.7.7.86 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8C6L5}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8C6L5}; Note=Binds 1 Mg(2+) per subunit. Is also active with Mn(2+). Mn(2+)-activated enzyme forms an inverted pppGp(2'-5')A intermediate, suggesting a non-canonical but accelerated 2',3'-cGAMP cyclization without substrate flip-over. Mn(2+) ions are coordinated by triphosphate moiety of the inverted substrate, independent of the catalytic triad residues. {ECO:0000250|UniProtKB:Q8C6L5}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8C6L5}; Note=Undergoes a liquid-like phase transition after binding to DNA, which is dependent on zinc. {ECO:0000250|UniProtKB:Q8N884}; | activation of innate immune response [GO:0002218]; cAMP-mediated signaling [GO:0019933]; cellular response to exogenous dsRNA [GO:0071360]; defense response to virus [GO:0051607]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; innate immune response [GO:0045087]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]; paracrine signaling [GO:0038001]; positive regulation of cellular senescence [GO:2000774]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of type I interferon production [GO:0032481] | cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; site of double-strand break [GO:0035861] | 2',3'-cyclic GMP-AMP synthase activity [GO:0061501]; ATP binding [GO:0005524]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; molecular condensate scaffold activity [GO:0140693]; nucleosome binding [GO:0031491]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; poly-ADP-D-ribose modification-dependent protein binding [GO:0160004]; protein homodimerization activity [GO:0042803] | PF03281;PF20266; | 1.10.1410.40;3.30.460.90; | Mab-21 family | PTM: The N-terminal disordered part (1-146) is phosphorylated by AURKB during the G2-M transition, blocking CGAS liquid phase separation and preventing activation. Phosphorylation at Tyr-204 by BLK promotes cytosolic retention. Localizes into the nucleus following dephosphorylation at Tyr-204 (By similarity). Phosphorylation at Ser-426 activates the nucleotidyltransferase activity. Dephosphorylation at Ser-426 by PPP6C impairs its ability to bind GTP, thereby inactivating it (By similarity). Phosphorylation at Ser-202 by PRKDC inhibits its cyclic GMP-AMP synthase activity by impairing homodimerization and activation (By similarity). Phosphorylation at Ser-294 by AKT (AKT1, AKT2 or AKT3) suppresses the nucleotidyltransferase activity. Phosphorylation at Ser-294 by CDK1 during mitosis leads to its inhibition, thereby preventing CGAS activation by self-DNA during mitosis. Dephosphorylated at Ser-294 by protein phosphatase PP1 upon mitotic exit (By similarity). {ECO:0000250|UniProtKB:Q8C6L5, ECO:0000250|UniProtKB:Q8N884}.; PTM: Ubiquitinated at Lys-405 via 'Lys-48'-linked polyubiquitin chains, leading to its SQSTM1-mediated autophagic degradation. Interaction with TRIM14 promotes recruitment of USP14, leading to deubiquitinate Lys-405 and stabilize CGAS. Ubiquitinated at Lys-375 by RNF185 via 'Lys-27'-linked polyubiquitination, promoting CGAS cyclic GMP-AMP synthase activity (By similarity). Monoubiquitination at Lys-338 by TRIM56 promotes oligomerization and subsequent activation (By similarity). Monoubiquitination by TRIM41 promotes CGAS activation (By similarity). Ubiquitination at Lys-274 via 'Lys-48'-linked polyubiquitination promotes its degradation. Deubiquitination at Lys-274 by USP29 promotes its stabilization. Deubiquitinated by USP27X, promoting its stabilization (By similarity). Ubiquitinated at Lys-402 via 'Lys-63'-linked polyubiquitin chains by MARCHF8, leading to the inhibition of its DNA binding ability (By similarity). {ECO:0000250|UniProtKB:Q8C6L5, ECO:0000250|UniProtKB:Q8N884}.; PTM: Sumoylated by TRIM38 in uninfected cells and during the early phase of viral infection, promoting its stability by preventing ubiquitination at Lys-274, and subsequent degradation. Desumoylated by SENP2 during the late phase of viral infection. Sumoylation at Lys-338, Lys-375 and Lys-385 prevents DNA-binding, oligomerization and nucleotidyltransferase activity. Desumoylation at Lys-338, Lys-375 and Lys-385 by SENP7 relieves inhibition and activates CGAS. {ECO:0000250|UniProtKB:Q8C6L5}.; PTM: Polyglutamylated by TTLL6 at Glu-275, leading to impair DNA-binding activity. Deglutamylated by AGBL5/CCP5 and AGBL6/CCP6. {ECO:0000250|UniProtKB:Q8C6L5}.; PTM: Acetylation at Lys-375, Lys-385 and Lys-405 inhibits the cyclic GMP-AMP synthase activity. Deacetylated upon cytosolic DNA challenge such as viral infections. Acetylation by KAT5 increases the cyclic GMP-AMP synthase activity by promoting DNA-binding and subsequent activation. {ECO:0000250|UniProtKB:Q8N884}.; PTM: Proteolytically cleaved by apoptotic caspases during apoptosis, leading to its inactivation. The damage of the nucleus and the mitochondria during apoptosis leads to leakage of nuclear and mitochondrial DNA, which activate CGAS: cleavage and inactivation during apoptosis in required to prevent cytokine overproduction. Cleaved by CASP7 and CASP3 during virus-induced apoptosis, thereby inactivating it and preventing cytokine overproduction. Cleaved by CASP1 upon DNA virus infection; the cleavage impairs cGAMP production. Also cleaved by the pyroptotic CASP4 during non-canonical inflammasome activation; does not cut at the same sites than CASP1. {ECO:0000250|UniProtKB:Q8C6L5}.; PTM: Degraded via selective autophagy following interaction with IRGM. IRGM promotes CGAS recruitment to autophagosome membranes, promoting its SQSTM1/p62-dependent autophagic degradation. {ECO:0000250|UniProtKB:Q8N884}.; PTM: Poly-ADP-ribosylation at Asp-179 by PARP1 impairs DNA-binding, thereby preventing the cyclic GMP-AMP synthase activity. {ECO:0000250|UniProtKB:Q8N884}.; PTM: Palmitoylation at Cys-465 by ZDHHC18 impairs DNA-binding, thereby preventing the cyclic GMP-AMP synthase activity (By similarity). Palmitoylation at Cys-395 and Cys-396 by ZDHHC9 promotes homodimerization and cyclic GMP-AMP synthase activity (By similarity). Depalmitoylation at Cys-395 and Cys-396 by LYPLAL1 impairs homodimerization and cyclic GMP-AMP synthase activity (By similarity). {ECO:0000250|UniProtKB:Q8N884}.; PTM: Monomethylated at Lys-482 by SETD7 (By similarity). Monomethylation promotes interaction with SGF29, preventing interaction between PARP1 nad SGF29. Demethylation by RIOX1 promotes interaction with PARP1, followed by PARP1 inactivation (By similarity). {ECO:0000250|UniProtKB:Q8C6L5}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8C6L5}. Chromosome {ECO:0000250|UniProtKB:Q8C6L5}. Cell membrane {ECO:0000250|UniProtKB:Q8C6L5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8C6L5}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8C6L5}. Note=Mainly localizes in the nucleus, and at low level in the cytosol (By similarity). On chromosomes, enriched on centromeric satellite and LINE DNA repeat elements. Exported from the nucleus to the cytosol in a XPO1/CRM1 via the nuclear export signal in response to DNA stimulation (By similarity). Outside the nucleus, localizes at the cell membrane as a peripheral membrane protein in resting conditions: association to the cell membrane is mediated via binding to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) (By similarity). Localization at the cell membrane is required to limit the recognition of self-DNA. Following detection of double-stranded DNA (dsDNA), released from the cell membrane into the cytosol in order to signal. Upon transfection with dsDNA forms punctate structures that co-localize with DNA and Beclin-1 (BECN1). Phosphorylation at Tyr-204 promotes cytosolic retention. In response to translation stress, translocates to the cytosol and associates with collided ribosomes (By similarity). {ECO:0000250|UniProtKB:Q8C6L5, ECO:0000250|UniProtKB:Q8N884}. | CATALYTIC ACTIVITY: Reaction=ATP + GTP = 2',3'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:42064, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:143093; EC=2.7.7.86; Evidence={ECO:0000250|UniProtKB:Q8C6L5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42065; Evidence={ECO:0000250|UniProtKB:Q8C6L5}; | null | null | null | null | FUNCTION: Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Catalysis involves both the formation of a 2',5' phosphodiester linkage at the GpA step and the formation of a 3',5' phosphodiester linkage at the ApG step, producing c[G(2',5')pA(3',5')p]. Acts as a key DNA sensor: directly binds double-stranded DNA (dsDNA), inducing the formation of liquid-like droplets in which CGAS is activated, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates STING1, thereby triggering type-I interferon production. Preferentially binds long dsDNA (around 45 bp) and forms ladder-like networks that function cooperatively to stabilize individual cGAS-dsDNA complexes. Acts as a key foreign DNA sensor, the presence of double-stranded DNA (dsDNA) in the cytoplasm being a danger signal that triggers the immune responses. Has antiviral activity by sensing the presence of dsDNA from DNA viruses in the cytoplasm. Also acts as an innate immune sensor of infection by retroviruses by detecting the presence of reverse-transcribed DNA in the cytosol (By similarity). Detection of retroviral reverse-transcribed DNA in the cytosol may be indirect and be mediated via interaction with PQBP1, which directly binds reverse-transcribed retroviral DNA. Also detects the presence of DNA from bacteria (By similarity). 2',3'-cGAMP can be transferred from producing cells to neighboring cells through gap junctions, leading to promote STING1 activation and convey immune response to connecting cells. 2',3'-cGAMP can also be transferred between cells by virtue of packaging within viral particles contributing to IFN-induction in newly infected cells in a cGAS-independent but STING1-dependent manner. Also senses the presence of neutrophil extracellular traps (NETs) that are translocated to the cytosol following phagocytosis, leading to synthesis of 2',3'-cGAMP (By similarity). In addition to foreign DNA, can also be activated by endogenous nuclear or mitochondrial DNA (By similarity). When self-DNA leaks into the cytosol during cellular stress (such as mitochondrial stress, DNA damage, mitotic arrest or senescence), or is present in form of cytosolic micronuclei, CGAS is activated leading to a state of sterile inflammation. Acts as a regulator of cellular senescence by binding to cytosolic chromatin fragments that are present in senescent cells, leading to trigger type-I interferon production via STING1 and promote cellular senescence. Also involved in the inflammatory response to genome instability and double-stranded DNA breaks: acts by localizing to micronuclei arising from genome instability. Micronuclei, which as frequently found in cancer cells, consist of chromatin surrounded by its own nuclear membrane: following breakdown of the micronuclear envelope, a process associated with chromothripsis, CGAS binds self-DNA exposed to the cytosol, leading to 2',3'-cGAMP synthesis and subsequent activation of STING1 and type-I interferon production (By similarity). In a healthy cell, CGAS is however kept inactive even in cellular events that directly expose it to self-DNA, such as mitosis, when cGAS associates with chromatin directly after nuclear envelope breakdown or remains in the form of postmitotic persistent nuclear cGAS pools bound to chromatin (By similarity). Nuclear CGAS is inactivated by chromatin via direct interaction with nucleosomes, which block CGAS from DNA binding and thus prevent CGAS-induced autoimmunity. Also acts as a suppressor of DNA repair in response to DNA damage: inhibits homologous recombination repair by interacting with PARP1, the CGAS-PARP1 interaction leading to impede the formation of the PARP1-TIMELESS complex (By similarity). In addition to DNA, also sense translation stress: in response to translation stress, translocates to the cytosol and associates with collided ribosomes, promoting its activation and triggering type-I interferon production (By similarity). {ECO:0000250|UniProtKB:Q8C6L5, ECO:0000250|UniProtKB:Q8N884}. | Bos taurus (Bovine) |
E1BH29 | ALKB5_BOVIN | MAAASGYTDLREKLKSMTSRDNYKAGSREAAAAAAAAVAAAAAAAAAAEPYAAPGVKRKYPEDSDPERSDFEEQQLQKEEEARKVKSGIRQMRLFSQDECAKIEARIDEVVSRAEKGLYNEHTVDRAPLRNKYFFGEGYTYGAQLQKRGPGQERLYPPGDVDEIPEWVHQLVIQKLVEHRVIPEGFVNSAVINDYQPGGCIVSHVDPIHIFERPIVSVSFFSDSALCFGCKFQFKPIRVSEPVLSLPVRRGSVTVLSGYAADEITHCIRPQDIKERRAVIILRKTRLDAPRLETKSLSSSVLPPSYASDRLSGNNRDPALKPKRSHRKADPDAAHRPRILEMDKEENRRSVLLPAHRRAGRFSSENYRRKSYEPGEDCSEAAGSPARKVKMRRH | 1.14.11.53 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q6P6C2}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6P6C2}; | cell differentiation [GO:0030154]; mRNA destabilization [GO:0061157]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; non-membrane-bounded organelle assembly [GO:0140694]; oxidative single-stranded RNA demethylation [GO:0035553]; regulation of translation [GO:0006417]; response to hypoxia [GO:0001666]; spermatogenesis [GO:0007283] | nuclear speck [GO:0016607]; nucleus [GO:0005634]; paraspeckles [GO:0042382] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; metal ion binding [GO:0046872]; molecular condensate scaffold activity [GO:0140693]; mRNA N6-methyladenosine dioxygenase activity [GO:1990931]; oxidative RNA demethylase activity [GO:0035515] | PF13532; | 2.60.120.590; | AlkB family | PTM: Phosphorylated at Ser-87 and Ser-325 in response to reactive oxygen species (ROS), promoting sumoylation and inactivation. {ECO:0000250|UniProtKB:Q6P6C2}.; PTM: Acetylated by KAT8 at Lys-235, promoting interaction with PSPC1, thereby facilitating recognition of N(6)-methyladenosine (m6A) mRNA by ALKBH5. Deacetylated at Lys-235 by HDAC7. {ECO:0000250|UniProtKB:Q6P6C2}.; PTM: Sumoylated at Lys-86 and Lys-321 by PIAS4 following phosphorylation at Ser-87 and Ser-325 in response to reactive oxygen species (ROS), inhibiting the RNA demethylase activity. Desumoylated by SENP1; relieving RNA demethylase inhibition, leading to N(6)-methyladenosine-containing mRNAs demethylation. {ECO:0000250|UniProtKB:Q6P6C2}.; PTM: Ubiquitinated at Lys-57 via 'Lys-48'-linked polyubiquitin chain, leading to its degradation by the proteasome. Deubiquitinated at Lys-57 by USP9X, promoting its stabilizazion. {ECO:0000250|UniProtKB:Q6P6C2}. | SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q6P6C2}. Note=Promotes formation and localizes to paraspeckles, a nuclear membraneless organelle. {ECO:0000250|UniProtKB:Q6P6C2}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + an N(6)-methyladenosine in mRNA + O2 = an adenosine in mRNA + CO2 + formaldehyde + succinate; Xref=Rhea:RHEA:49520, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12417, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=1.14.11.53; Evidence={ECO:0000250|UniProtKB:Q6P6C2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49521; Evidence={ECO:0000250|UniProtKB:Q6P6C2}; | null | null | null | null | FUNCTION: Dioxygenase that specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Demethylates RNA by oxidative demethylation, which requires molecular oxygen, alpha-ketoglutarate and iron. Demethylation of m6A mRNA affects mRNA processing, translation and export. Can also demethylate N(6)-methyladenosine in single-stranded DNA (in vitro) (By similarity). Required for the late meiotic and haploid phases of spermatogenesis by mediating m6A demethylation in spermatocytes and round spermatids: m6A demethylation of target transcripts is required for correct splicing and the production of longer 3'-UTR mRNAs in male germ cells (By similarity). Involved in paraspeckle assembly, a nuclear membraneless organelle, by undergoing liquid-liquid phase separation. Paraspeckle assembly is coupled with m6A demethylation of RNAs, such as NEAT1 non-coding RNA (By similarity). Also acts as a negative regulator of T-cell development: inhibits gamma-delta T-cell proliferation via demethylation of JAG1 and NOTCH2 transcripts. Inhibits regulatory T-cell (Treg) recruitment by mediating demethylation and destabilization of CCL28 mRNAs (By similarity). {ECO:0000250|UniProtKB:Q3TSG4, ECO:0000250|UniProtKB:Q6P6C2}. | Bos taurus (Bovine) |
E1BJS7 | LIN41_BOVIN | MASFPETDFQICLLCKEMCGSPAPLSSNSSASSSSSQTSTSSGGGGGGPGAAARRLHVLPCLAFCRPCLEAHRGGAPGEPLKLRCPVCDQKVVLAEAAGMDARPSSAFLLSNLLDAVVATADEPPPKNGRAGAAAGAGGHGSNHRHHAHHAHPRAAASAPPPPLPPAPPPPAPPRSAPGGPAGSPSALLLRRPHGCSSCDEGNAASSRCLDCQEHLCDNCVRAHQRVRLTKDHYIERGPPGPAAAAAAAAAQQLGLGPPFPGAPFSLLSVFPERLGFCQHHDDEVLHLYCDTCSVPICRECTVGRHGGHSFVYLQEALQDSRALTIQLLADAQQGRQAIQLSIEQAQTVAEQVEMKAKVVQSEVKAVTARHKKALEERECELLWKVEKIRQVKAKSLYLQVEKLRQNLNKLESTISAVQQVLEEGRALDILLARDRMLAQVQELKTVRSLLQPQEDDRVMFTPPDQALYLAIKSFGFVSSGAFAPLTKATGDGLKRALQGKVASFTVIGYDHDGEPRLSGGDLMSAVVLGPDGNLFGAEVSDQQNGTYVVSYRPQLEGEHLVSVTLCNQHIENSPFKVVVKSGRSYVGIGLPGLSFGSEGDSDGKLCRPWGVSVDKEGYIVVADRSNNRIQVFKPCGAFHHKFGTLGSRPGQFDRPAGVACDASRRIVVADKDNHRIQIFTFEGQFLLKFGEKGTKNGQFNYPWDVAVNSEGKILVSDTRNHRIQLFGPDGVFLNKYGFEGALWKHFDSPRGVAFNHEGHLVVTDFNNHRLLVIHPDCQSARFLGSEGTGNGQFLRPQGVAVDQEGRIIVADSRNHRVQMFESNGSFLCKFGAQGSGFGQMDRPSGIAVTPDGMIVVVDFGNNRILIF | 2.3.2.27 | null | fibroblast growth factor receptor signaling pathway [GO:0008543]; G1/S transition of mitotic cell cycle [GO:0000082]; miRNA processing [GO:0035196]; miRNA-mediated gene silencing by inhibition of translation [GO:0035278]; neural tube development [GO:0021915]; post-transcriptional regulation of gene expression [GO:0010608]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein polyubiquitination [GO:0000209]; regulation of neural precursor cell proliferation [GO:2000177]; stem cell proliferation [GO:0072089] | P-body [GO:0000932] | miRNA binding [GO:0035198]; translation repressor activity [GO:0030371]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF00630;PF01436;PF00643; | 4.10.830.40;3.30.160.60;2.60.40.10;2.120.10.30; | TRIM/RBCC family | PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q1PSW8}. | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q2Q1W2}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance (By similarity). Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A (By similarity). In addition, participates in post-transcriptional mRNA repression in a miRNA independent mechanism (By similarity). Facilitates the G1-S transition to promote rapid embryonic stem cell self-renewal by repressing CDKN1A expression. Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development: positively regulates FGF signaling by controlling the stability of SHCBP1 (By similarity). Specific regulator of miRNA biogenesis. Binds to miRNA MIR29A hairpin and postranscriptionally modulates MIR29A levels, which indirectly regulates TET proteins expression (By similarity). {ECO:0000250|UniProtKB:Q1PSW8, ECO:0000250|UniProtKB:Q2Q1W2}. | Bos taurus (Bovine) |
E1BMF7 | UBP13_BOVIN | MQRRGALFGMPGGSGSRKMAAGDIGELLVPHMPTIRVPRSGDRVYKNECAFSYDSPNSEGGLYVCMNTFLAFGREHVERHFRKTGQSVYMHLKRHVREKVRGASGGALPKRRNSKMFLDLDTDDDLNSDDYEYEDEAKLVIFPDHYEIALPNIEELPALVTIACDAVLSSKSPYRKQDPDTWENELPVSKYANNLTQLDNGVRIPPSGWKCARCDLRENLWLNLTDGSVLCGKWFFDSSGGNGHALEHYRDTGYPLAVKLGTITPDGADVYSFQEEEAVLDPHLAKHLAHFGIDMLHMHGTENGLQDNDIKPRVSEWEVIQETGTKLKPMYGPGYTGLKNLGNSCYLSSVMQAIFSIPEFQRAYVGNLPRIFDYSPLDPTQDFNTQMTKLGHGLLSGQYSKPPVKSELIEQVMKEEHKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVERNRIGSENPSDVFRFLVEERIQCCQTRKVRYTERVDYLMQLPVAMEAATNKDELIAYELTRREAESNRRPLPELVRAKIPFSACLQAFSEPENVDDFWSSALQAKSAGVKTSRFASFPEYLVVQIKKFTFGLDWVPKKFDVSVDMPDLLDINHLRARGLQPGEEELPDISPPIVIPDDSKDRLMTQLIDPSDIDESSVMQLAEMGFPLEACRKAVYFTGNMGAEVAFNWIVVHMEEPDFAEPLTMPGYGGAASAGASVFGATGLDNQPPEETVAIITSMGFHRNQAIQALRATNSNLERALDWIFSHPEFEEDSDFVIEMENNANANIVSEAKPEGPRVKDGSGMYELFAFISHMGTSTMSGHYVCHIKKEGRWVIYNDHKVCASERPPKDLGYMYFYRRIPS | 3.4.19.12 | null | autophagy [GO:0006914]; cell population proliferation [GO:0008283]; protein K63-linked deubiquitination [GO:0070536]; protein stabilization [GO:0050821]; proteolysis [GO:0006508]; regulation of autophagy [GO:0010506]; regulation of DNA-templated transcription [GO:0006355] | cytosol [GO:0005829]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; ubiquitin binding [GO:0043130]; zinc ion binding [GO:0008270] | PF00627;PF00443;PF02148;PF17807; | 3.90.70.10;1.10.8.10;3.30.40.10; | Peptidase C19 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92995}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q92995}; | null | null | null | null | FUNCTION: Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy, endoplasmic reticulum-associated degradation (ERAD), cell cycle progression or DNA damage response. Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Alternatively, forms with NEDD4 a deubiquitination complex, which subsequently stabilizes VPS34 to promote autophagy. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Also regulates ERAD through the deubiquitination of UBL4A a component of the BAG6/BAT3 complex. Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Regulates the cell cycle progression by stabilizing cell cycle proteins such as SKP2 and AURKB. In addition, plays an important role in maintaining genomic stability and in DNA replication checkpoint activation via regulation of RAP80 and TOPBP1. Deubiquitinates the multifunctional protein HMGB1 and subsequently drives its nucleocytoplasmic localization and its secretion. Positively regulates type I and type II interferon signalings by deubiquitinating STAT1 but negatively regulates antiviral response by deubiquitinating STING1. {ECO:0000250|UniProtKB:Q92995}. | Bos taurus (Bovine) |
E1BMN8 | NLK_BOVIN | MPNVFQNLVSCKRVFRELKMAAYNGGTSAAAAGHHHHHHHHLPHLPPPHLHHHHHPQHHLHPGSAAAVHPVQQHTSSAAAAAAAAAAAAAMLNPGQQQPYFPSPAPGQAPGPAAAAPAQVQAAAAATVKAHHHQHSHHPQQQLDIEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIDYFEEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESRHMTQEVVTQYYRAPEILMGSRHYSNAIDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPSLEAMRTACEGAKAHILRGPHKQPSLPVLYTLSSQATHEAVHLLCRMLVFDPSKRISAKDALAHPYLDEGRLRYHTCMCKCCFSTSTGRVYTSDFEPVTNPKFDDTFEKNLSSVRQVKEIIHQFILEQQKGNRVPLCINPQSAAFKSFISSTVAQPSEMPPSPLVWE | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O54949}; | intracellular signal transduction [GO:0035556]; negative regulation of TORC1 signaling [GO:1904262]; phosphorylation [GO:0016310]; protein stabilization [GO:0050821]; Wnt signaling pathway [GO:0016055] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Phosphorylated on Thr-305. Intermolecular autophosphorylation on Thr-305 activates the enzyme. {ECO:0000250|UniProtKB:O54949}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O54949}. Cytoplasm {ECO:0000250|UniProtKB:O54949}. Note=Predominantly nuclear. A smaller fraction is cytoplasmic. {ECO:0000250|UniProtKB:O54949}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000250|UniProtKB:O54949}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000250|UniProtKB:O54949}; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination. Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Negative regulator of the canonical Wnt/beta-catenin signaling pathway. Binds to and phosphorylates TCF7L2/TCF4 and LEF1, promoting the dissociation of the TCF7L2/LEF1/beta-catenin complex from DNA, as well as the ubiquitination and subsequent proteolysis of LEF1. Together these effects inhibit the transcriptional activation of canonical Wnt/beta-catenin target genes. Negative regulator of the Notch signaling pathway. Binds to and phosphorylates NOTCH1, thereby preventing the formation of a transcriptionally active ternary complex of NOTCH1, RBPJ/RBPSUH and MAML1. Negative regulator of the MYB family of transcription factors. Phosphorylation of MYB leads to its subsequent proteolysis while phosphorylation of MYBL1 and MYBL2 inhibits their interaction with the coactivator CREBBP. Other transcription factors may also be inhibited by direct phosphorylation of CREBBP itself. Acts downstream of IL6 and MAP3K7/TAK1 to phosphorylate STAT3, which is in turn required for activation of NLK by MAP3K7/TAK1. Upon IL1B stimulus, cooperates with ATF5 to activate the transactivation activity of C/EBP subfamily members. Phosphorylates ATF5 but also stabilizes ATF5 protein levels in a kinase-independent manner. Acts as an inhibitor of the mTORC1 complex in response to osmotic stress by mediating phosphorylation of RPTOR, thereby preventing recruitment of the mTORC1 complex to lysosomes. {ECO:0000250|UniProtKB:Q9UBE8}. | Bos taurus (Bovine) |
E1BPK6 | MYO6_BOVIN | MEDGRPVWAPHPTEGFQMGNIVDIGPDSLTIEPLGQKGKTFLALINQVFPAEEDSKKDVEDNCSLMYLNEATLLHNIKVRYSKDRIYTYVANILIAVNPYFDIPKIYSSDSIKSYQGKSLGTMPPHVFAIADKAFRDMKVLKMSQSIIVSGESGAGKTENTKFVLRYLTESYGSGQDIDDRIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGKEERNYHIFYRLCAGASEDIRERLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKTPEHLKAGSLKDPLLDDHGDFVRMCTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCNLKNKSTQSLEYCAELLGLDQDDLRVSLTTRVMLTTAGGTKGTVIKVPLKVEQANNARDALAKTVYSHLFDHVVNRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKLQQFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEAKLMGILDILDEENRLPQPSDQHFTSAVHQKHKDHFRLSIPRKSKLAVHRNIRDDEGFIVRHFAGAVCYETTQFVEKNNDALHMSLESLICESRDKFIRELFESSTNNNKDTKQKAGKLSFISVGNKFKTQLNLLLDKLRSTGASFIRCIKPNLKMTSHDFEGAQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKKYMPDKLARLDPRLFCKALFKALGLNEVDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAQLVKRVNHWLICSRWKKVQWCSLSVIKLKNKIKYRAEACIKMQKTIRMWLCKRRHKPRIDGLVKVGTLKKRLDKFNEVVSALKDGKAEMNKQVKDLEISIDALMAKIKSTMMTREQIQKEYDALVKSSEVLLSALQKKKQQEEEAERLRRIQEEMEKERKRREEDEQRRRKEEEERRMKLEMEAKRKQEEEERKKREDDEKRIQAEVEAQLARQREEESQQQAVLEQERRDRELALRIARSEAELIIDEAQADPAALRSLDFHPVTSKINGTRRTMTPEQMAKEMSEILSRGPAVQATKAAAGTKKHDLSKWKYAELRDTINTSCDIELLAACREEFHRRLKVYHAWKSKNKKRNTETEQRAPKSVTDYDFAPFLNNSPQQNPAAQLPARQQEIEMNRQQRFFRIPFIRPADQYKDPQNKKKGWWYAHFDGPWIARQMELHPDKPPILLVAGKDDMEMCELNLEETGLTRKRGAEILPRQFEEIWERCGGIQYLQSAIESRQARPTYATAMLQNLLK | null | null | actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; endocytosis [GO:0006897]; inner ear auditory receptor cell differentiation [GO:0042491]; inner ear morphogenesis [GO:0042472]; protein localization [GO:0008104]; protein transport [GO:0015031]; regulation of secretion [GO:0051046]; sensory perception of sound [GO:0007605]; vesicle transport along actin filament [GO:0030050] | actin cytoskeleton [GO:0015629]; clathrin-coated endocytic vesicle [GO:0045334]; clathrin-coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endocytic vesicle [GO:0030139]; filamentous actin [GO:0031941]; filopodium [GO:0030175]; Golgi apparatus [GO:0005794]; microvillus [GO:0005902]; myosin complex [GO:0016459]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; ruffle membrane [GO:0032587] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146] | PF21521;PF16521;PF00063; | 1.10.10.820;1.20.58.530;3.30.70.1590;6.10.220.10;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | PTM: Phosphorylation in the motor domain, induced by EGF, results in translocation of MYO6 from the cell surface to membrane ruffles and affects F-actin dynamics. Phosphorylated in vitro by p21-activated kinase (PAK). {ECO:0000250|UniProtKB:Q29122}. | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9UM54}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UM54}. Golgi apparatus {ECO:0000250|UniProtKB:Q9UM54}. Nucleus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UM54}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9UM54}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9UM54}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q29122}. Cell projection, microvillus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q29122}. Note=Also present in endocytic vesicles (By similarity). Translocates from membrane ruffles, endocytic vesicles and cytoplasm to Golgi apparatus, perinuclear membrane and nucleus through induction by p53 and p53-induced DNA damage. Recruited into membrane ruffles from cell surface by EGF-stimulation. Colocalizes with DAB2 in clathrin-coated pits/vesicles (By similarity). Colocalizes with OPTN at the Golgi complex and in vesicular structures close to the plasma membrane (By similarity). {ECO:0000250|UniProtKB:Q29122, ECO:0000250|UniProtKB:Q9I8D1, ECO:0000250|UniProtKB:Q9UM54}. | null | null | null | null | null | FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements (By similarity). Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments (By similarity). Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration (By similarity). Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells (By similarity). Together with TOM1, mediates delivery of endocytic cargo to autophagosomes thereby promoting autophagosome maturation and driving fusion with lysosomes (By similarity). Links TOM1 with autophagy receptors, such as TAX1BP1; CALCOCO2/NDP52 and OPTN (By similarity). May act as a regulator of F-actin dynamics (By similarity). As part of the DISP complex, may regulate the association of septins with actin and thereby regulate the actin cytoskeleton (By similarity). May play a role in transporting DAB2 from the plasma membrane to specific cellular targets (By similarity). May play a role in the extension and network organization of neurites (By similarity). Required for structural integrity of inner ear hair cells (By similarity). Required for the correct localization of CLIC5 and RDX at the stereocilium base (By similarity). Modulates RNA polymerase II-dependent transcription (By similarity). {ECO:0000250|UniProtKB:Q29122, ECO:0000250|UniProtKB:Q64331, ECO:0000250|UniProtKB:Q9UM54}. | Bos taurus (Bovine) |
E1BPQ1 | FOXO1_BOVIN | MAEAPQVVEIDPDFEPLPRPRSCTWPLPRPEFSQSNSATSSPAPSGGAAANPDGAAGLPSASAAAVNADFMSNLSLLEESGDFQQAPGSVAAAAPLSQHPPVPPAAAAAAAGGQLAGQPRKSSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRGRAAKKKASLQSGQEGAGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGDGDVHSMVYPPSAAKMASTLPSLSEISNPENMENLLDNLNLLSSPTSLTVSTQSSPGTMMQQTPCYSFAPPNTSLNSPTPNYQKYTYGQSSMSPLPQMPMQTLQDNKSSYGGMSQYCAPGLLKELLTSDSPPHNDIMTPVDPGVAQANSRVLGQSVLMGPNSVMPAYGGQASHNKMMTPSSHTHPGHAQSTSAVNGRALPHAVNTMPHTSGMNRLAPVKTALQVPLAHPMQMSALGGYSSVSSCNGYGRMGVLHQEKLPSDLDGMFIERLDCDMESIIRNDLMDGDTLDFNFDNVLPNQSFPHSVKTTTHSWVSG | null | null | apoptotic process [GO:0006915]; autophagy [GO:0006914]; cell differentiation [GO:0030154]; cellular response to hyperoxia [GO:0071455]; cellular response to insulin stimulus [GO:0032869]; cellular response to nitric oxide [GO:0071732]; cellular response to oxidative stress [GO:0034599]; cellular response to starvation [GO:0009267]; DNA damage response [GO:0006974]; insulin receptor signaling pathway [GO:0008286]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of insulin secretion [GO:0046676]; positive regulation of apoptotic process [GO:0043065]; positive regulation of autophagy [GO:0010508]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of smooth muscle cell apoptotic process [GO:0034393]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of transcription initiation by RNA polymerase II [GO:0060260]; response to fatty acid [GO:0070542] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein phosphatase 2A binding [GO:0051721]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF00250;PF16676;PF16675; | 1.10.10.10; | null | PTM: Phosphorylation by NLK promotes nuclear export and inhibits the transcriptional activity. In response to growth factors, phosphorylation on Thr-24, Ser-226 and Ser-292 by PKB/AKT1 promotes nuclear export and inactivation of transactivational activity. Phosphorylation on Thr-24 is required for binding 14-3-3 proteins. Phosphorylation of Ser-226 decreases DNA-binding activity and promotes the phosphorylation of Thr-24 and Ser-289, permitting phosphorylation of Ser-292 and Ser-295, probably by CDK1, leading to nuclear exclusion and loss of function. Stress signals, such as response to oxygen or nitric oxide, attenuate the PKB/AKT1-mediated phosphorylation leading to nuclear retention. Phosphorylation of Ser-299 is independent of IGF1 and leads to reduced function. Dephosphorylated on Thr-24 and Ser-226 by PP2A in beta-cells under oxidative stress leading to nuclear retention. Phosphorylation of Ser-219 by CDK1 disrupts binding of 14-3-3 proteins leading to nuclear accumulation and has no effect on DNA binding nor transcriptional activity. Phosphorylation by STK4/MST1 on Ser-182, upon oxidative stress, inhibits binding to 14-3-3 proteins and nuclear export (By similarity). PPIA/CYPA promotes its dephosphorylation on Ser-226 (By similarity). {ECO:0000250|UniProtKB:Q12778, ECO:0000250|UniProtKB:Q9R1E0}.; PTM: Ubiquitinated by SKP2 (By similarity). Ubiquitination leads to proteasomal degradation (By similarity). Ubiquitinated by STUB1/CHIP; when Ser-226 is phosphorylated (By similarity). {ECO:0000250|UniProtKB:Q12778, ECO:0000250|UniProtKB:Q9R1E0}.; PTM: Methylation inhibits AKT1-mediated phosphorylation at Ser-226 and is increased by oxidative stress. {ECO:0000250|UniProtKB:Q9R1E0}.; PTM: Acetylated. Acetylation at Lys-232 and Lys-244 are necessary for autophagic cell death induction. Deacetylated by SIRT2 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1-mediated autophagic cell death. Once in the nucleus, acetylated by CREBBP/EP300. Acetylation diminishes the interaction with target DNA and attenuates the transcriptional activity. It increases the phosphorylation at Ser-226. Deacetylation by SIRT1 results in reactivation of the transcriptional activity. Oxidative stress by hydrogen peroxide treatment appears to promote deacetylation and uncoupling of insulin-induced phosphorylation. By contrast, resveratrol acts independently of acetylation. Acetylated at Lys-393, promoting its localization to the nucleus and transcription factor activity. Deacetylation at Lys-393 by SIRT6, promotes its translocation into the cytoplasm, preventing its transcription factor activity. Deacetylation and subsequent inhibition by SIRT6 has different effects depending on cell types: it inhibits gluconeogenesis in hepatocytes, promotes glucose sensing in pancreatic beta-cells and regulates lipid catabolism in brown adipocytes. {ECO:0000250|UniProtKB:Q12778}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9R1E0}. Nucleus {ECO:0000250|UniProtKB:Q9R1E0}. Note=Shuttles between the cytoplasm and nucleus (By similarity). Largely nuclear in unstimulated cells (By similarity). In osteoblasts, colocalizes with ATF4 and RUNX2 in the nucleus. Serum deprivation increases localization to the nucleus, leading to activate expression of SOX9 and subsequent chondrogenesis (By similarity). Insulin-induced phosphorylation at Ser-253 by PKB/AKT1 leads, via stimulation of Thr-24 phosphorylation, to binding of 14-3-3 proteins and nuclear export to the cytoplasm where it is degraded by the ubiquitin-proteasomal pathway (By similarity). Phosphorylation at Ser-249 by CDK1 disrupts binding of 14-3-3 proteins and promotes nuclear accumulation (By similarity). Phosphorylation by NLK results in nuclear export (By similarity). Translocates to the nucleus upon oxidative stress-induced phosphorylation at Ser-212 by STK4/MST1 (By similarity). SGK1-mediated phosphorylation also results in nuclear translocation. Retained in the nucleus under stress stimuli including oxidative stress, nutrient deprivation or nitric oxide. Methylated form is nuclear (By similarity). PPIA/CYPA stimulates its nuclear accumulation (By similarity). Deacetylation by SIRT6, promotes its translocation into the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q12778, ECO:0000250|UniProtKB:Q9R1E0}. | null | null | null | null | null | FUNCTION: Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3'. Activity suppressed by insulin. Main regulator of redox balance and osteoblast numbers and controls bone mass. Orchestrates the endocrine function of the skeleton in regulating glucose metabolism. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation. Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity. Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP. Acts as an inhibitor of glucose sensing in pancreatic beta cells by acting as a transcription repressor and suppressing expression of PDX1. In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC1 and PCK1 (By similarity). Also promotes gluconeogenesis by directly promoting expression of PPARGC1A and G6PC1 (By similarity). Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1 (By similarity). Promotes neural cell death (By similarity). Mediates insulin action on adipose tissue (By similarity). Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake (By similarity). Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells (By similarity). Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner (By similarity). Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (By similarity). Positive regulator of apoptosis in cardiac smooth muscle cells as a result of its transcriptional activation of pro-apoptotic genes (By similarity). Regulates endothelial cell (EC) viability and apoptosis in a PPIA/CYPA-dependent manner via transcription of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (By similarity). {ECO:0000250|UniProtKB:A4L7N3, ECO:0000250|UniProtKB:G3V7R4, ECO:0000250|UniProtKB:Q12778, ECO:0000250|UniProtKB:Q9R1E0}. | Bos taurus (Bovine) |
E1BPW0 | ENTP5_BOVIN | MALYQGAAFFMLVASCVCSTVFHREQQTWFEGVFLSSMCPVNVSAGTLYGIMFDAGSTGTRIHVYTFVQKVPDNTGQLPVLEGEIFDSVKPGLSAFVDQPKQGAETVQELLEVAKDSIPPSHWKRTPVVLKATAGLRLLPEEKAEALLFEVKEIFKKSPFLVPDDSVSIMDGSYEGILAWVTVNFLTGQLHGHNQETVGTLDLGGASTQITFLPQFEKTLEQTPRDYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETAGIDGYTFRSACLPRWLEAEWIFGGVKYQYGGNQEAGEVGFEPCYAEVLRVVQGKLHQPDEVQRGSFYAFSYYYDRAVDTDMIDYEKGGVLKVEDFERKAREVCDNLENFTSGSPFLCMDLSYITALLKDGFGFASSTVLQLTKKVNNIETGWALGATFHLLQSLGISH | 3.6.1.6 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:O75356}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O75356}; | 'de novo' post-translational protein folding [GO:0051084]; nucleoside diphosphate catabolic process [GO:0009134]; protein N-linked glycosylation [GO:0006487]; UDP catabolic process [GO:0006256]; UDP-glucose metabolic process [GO:0006011] | endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; membrane [GO:0016020] | ADP phosphatase activity [GO:0043262]; CDP phosphatase activity [GO:0036384]; GDP phosphatase activity [GO:0004382]; IDP phosphatase activity [GO:1990003]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; UDP phosphatase activity [GO:0045134] | PF01150; | 3.30.420.40;3.30.420.150; | GDA1/CD39 NTPase family | PTM: N-glycosylated; high-mannose type. {ECO:0000250|UniProtKB:Q9WUZ9}. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9WUZ9}. Secreted {ECO:0000250|UniProtKB:O75356}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800; Evidence={ECO:0000250|UniProtKB:O75356}; CATALYTIC ACTIVITY: Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157; Evidence={ECO:0000250|UniProtKB:O75356}; CATALYTIC ACTIVITY: Reaction=H2O + UDP = H(+) + phosphate + UMP; Xref=Rhea:RHEA:64876, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877; Evidence={ECO:0000250|UniProtKB:O75356}; CATALYTIC ACTIVITY: Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208; Evidence={ECO:0000250|UniProtKB:O75356}; CATALYTIC ACTIVITY: Reaction=CDP + H2O = CMP + H(+) + phosphate; Xref=Rhea:RHEA:64880, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64881; Evidence={ECO:0000250|UniProtKB:O75356}; CATALYTIC ACTIVITY: Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437; Evidence={ECO:0000250|UniProtKB:O75356}; | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q9WUZ9}. | null | null | FUNCTION: Hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP (By similarity). In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases. UMP can be transported back by an UDP-sugar antiporter to the cytosol where it is consumed to regenerate UDP-glucose. Therefore, it positively regulates protein reglucosylation by clearing UDP from the ER lumen and by promoting the regeneration of UDP-glucose. Protein reglucosylation is essential to proper glycoprotein folding and quality control in the ER (By similarity). {ECO:0000250|UniProtKB:O75356, ECO:0000250|UniProtKB:Q9WUZ9}. | Bos taurus (Bovine) |
E1BPX4 | MCM8_BOVIN | MNGKYRGRGFGQGRFQSWKSGRGGRGFSGKWREREHRPDLNKATGKHPEQTPQSLLLQSTLDHFIPYKGWKLYFSEVYSDSIPFIEKIEAFESFFTERIELYDKDEIERKGSILVDFKELINDDEIIKLIPNIANELRDTPEKTLACMGLAIHQVLTKDLERHAAELQAQEGLSRNGETVVNVPHIHARVYNYEPLTQLKNVRANYYGKYIALRGTVVRVSNTKPLCTKMAFLCAACGEIQSLSLPDGKYNLPTKCPVPACRGKSFTALRSSPLTVTMDWQSIKIQELMSDDQREAGRIPRTIECELVHDLVDSCVPGDTVTITGVVKVSNAEEANSVSNNKGQKTKASEDGCKHGALMEFSLKDLYAIQEIQSEENLFKLIVNSLCPVIFGHELVKAGLALALFGGSQKYADDKNRIPIRGDPHVLVVGDPGLGKSQMLQAVCSVAPRGVYVCGNTTTTSGLTVTLSKDSSSGDFALEAGALVLGDQGICGIDEFDKMGNQHQALLEAMEQQSISLAKAGMVCSLPARTSIIAAANPVGGHYNKAKTVSENLKMGSALLSRFDLVFILLDTPNEDHDHLLSEHVIAIRAGKQRAVSSATVARMNSQDSNTSILEVVSDKPLSERLKVVPGETIDPIPHQLLRKYIGYSRQYVYPRLSTEAAQILQNFYLELRKQSQRLSSSPITTRQLESLIRLTEARARLELREEATKEDAEDIVEIMKYSMLGTYSDEFGNLDFERSQHGSGMSNRSAAKRFISALNKIAERTYNNLFQFHQLQQIAKELNIQVADFENFIGSLNDQGYLLKKGPKVYQLQTM | 3.6.4.12 | null | cell cycle [GO:0007049]; DNA damage response [GO:0006974]; DNA replication [GO:0006260]; double-strand break repair via homologous recombination [GO:0000724]; female gamete generation [GO:0007292]; male gamete generation [GO:0048232]; protein localization to chromatin [GO:0071168]; protein stabilization [GO:0050821]; recombinational interstrand cross-link repair [GO:0036298] | chromosome [GO:0005694]; MCM complex [GO:0042555]; MCM8-MCM9 complex [GO:0097362]; nucleus [GO:0005634]; organelle membrane [GO:0031090] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; enzyme binding [GO:0019899]; MutLbeta complex binding [GO:0032406]; MutSalpha complex binding [GO:0032407]; MutSbeta complex binding [GO:0032408]; single-stranded DNA binding [GO:0003697]; single-stranded DNA helicase activity [GO:0017116] | PF00493;PF17855;PF17207; | 2.20.28.10;2.40.50.140;3.40.50.300; | MCM family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UJA3}. Chromosome {ECO:0000250|UniProtKB:Q9UJA3}. Note=Localizes to nuclear foci. Localizes to double-stranded DNA breaks. Binds chromatin throughout the cell cycle. {ECO:0000250|UniProtKB:Q9UJA3}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:Q9UJA3}; | null | null | null | null | FUNCTION: Component of the MCM8-MCM9 complex, a complex involved in the repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-links (ICLs) by homologous recombination (HR). Required for DNA resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex by recruiting the MRN complex to the repair site and by promoting the complex nuclease activity. Probably by regulating the localization of the MNR complex, indirectly regulates the recruitment of downstream effector RAD51 to DNA damage sites including DBSs and ICLs. The MCM8-MCM9 complex is dispensable for DNA replication and S phase progression. However, may play a non-essential for DNA replication: may be involved in the activation of the prereplicative complex (pre-RC) during G(1) phase by recruiting CDC6 to the origin recognition complex (ORC). Probably by regulating HR, plays a key role during gametogenesis. Stabilizes MCM9 protein. {ECO:0000250|UniProtKB:Q9CWV1, ECO:0000250|UniProtKB:Q9UJA3}. | Bos taurus (Bovine) |
E1BSI0 | PARP3_CHICK | MAPKRRAPPASQPADGGKKAKGGQEEEEDAWSSALNALKTAPREKPPATIDGQCPLSAGPDAKVYEDYDCTLNQTNISANNNKFYIIQLIEHGGTYSTWNRWGRVGEVGQSKLLPFTSLEAAKKDFEKKFWEKTKNRWAARDNFVAQPGKYTLIEVQPGAGQEVALRVDGAGDEKVSKRRVLPCALDETTQKLVALIFSSDMFRHAMQAMNIDVKKMPLGKLSKQQIARGFEALEELEAALGEQPRSMSRLEELSSRFYTIVPHNFGRARPPPIDSPELLRAKKDMLLVLADIEVAQSLQAQKVEEEEVVAHPLDRDYALLCCQLTLLEDTSQEYEMILNYVAQTGGQVYVLNVWRVAREGEDKLFQAHDHLEHRRLLWHGTNVAVVAAILKNGLRIMPHSGGRVGKGIYFASENSKSACYVGCTSKRVGLMFLTEVALGKPYCITRDEPTLQQPPNGYDSVQACGRTEPDPAQDVEVTLDGKKVLVCQGKPIPMPAYKDSSFFQSEYLIYQESQCRIRYLVQLHF | 2.4.2.- | null | double-strand break repair [GO:0006302] | centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; site of double-strand break [GO:0035861] | NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD+- protein-lysine ADP-ribosyltransferase activity [GO:0140804]; NAD+-protein ADP-ribosyltransferase activity [GO:1990404]; nucleotidyltransferase activity [GO:0016779] | PF00644;PF02877;PF05406; | 3.90.228.10;1.20.142.10;2.20.140.10; | ARTD/PARP family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y6F1}. Chromosome {ECO:0000269|PubMed:27530147}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y6F1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9Y6F1}. Note=Almost exclusively localized in the nucleus and appears in numerous small foci and a small number of larger foci whereas a centrosomal location has not been detected (By similarity). In response to DNA damage, localizes to sites of double-strand break (By similarity). Also localizes to single-strand breaks (PubMed:27530147). Preferentially localized to the daughter centriole (By similarity). {ECO:0000250|UniProtKB:Q9Y6F1, ECO:0000269|PubMed:27530147}. | CATALYTIC ACTIVITY: Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154, ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102; Evidence={ECO:0000250|UniProtKB:Q9Y6F1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425; Evidence={ECO:0000250|UniProtKB:Q9Y6F1}; CATALYTIC ACTIVITY: Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154, ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540; Evidence={ECO:0000250|UniProtKB:Q9Y6F1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225; Evidence={ECO:0000250|UniProtKB:Q9Y6F1}; CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + NAD(+) = H(+) + N(6)-(ADP-D-ribosyl)-L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58220, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15088, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:142515; Evidence={ECO:0000250|UniProtKB:Q9Y6F1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58221; Evidence={ECO:0000250|UniProtKB:Q9Y6F1}; | null | null | null | null | FUNCTION: Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins and plays a key role in the response to DNA damage (PubMed:27530147). Mediates mono-ADP-ribosylation of glutamate, aspartate or lysine residues on target proteins (By similarity). In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (By similarity). Involved in DNA repair by mediating mono-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism, such as histone H2B, XRCC5 and XRCC6 (By similarity). ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks (By similarity). Involved in single-strand break repair by catalyzing mono-ADP-ribosylation of histone H2B on 'Glu-2' (H2BE2ADPr) of nucleosomes containing nicked DNA (PubMed:27530147). Cooperates with the XRCC5-XRCC6 (Ku80-Ku70) heterodimer to limit end-resection thereby promoting accurate NHEJ (By similarity). Associates with a number of DNA repair factors and is involved in the response to exogenous and endogenous DNA strand breaks (By similarity). Together with APLF, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ) (By similarity). In addition to proteins, also able to ADP-ribosylate DNA: mediates DNA mono-ADP-ribosylation of DNA strand break termini via covalent addition of a single ADP-ribose moiety to a 5'- or 3'-terminal phosphate residues in DNA containing multiple strand breaks (By similarity). {ECO:0000250|UniProtKB:Q9Y6F1, ECO:0000269|PubMed:27530147}. | Gallus gallus (Chicken) |
E1BSW7 | CENPS_CHICK | MEAAGGEQRELLIQRLRAAVHYTTGCLCQDVAEDKGVLFSKQTVAAISEITFRQCENFARDLEMFARHAKRSTITSEDVKLLARRSNSLLKYITQKSDELASSNMEQKEKKKKKSSAAKGRKTEENETPVTESEDSNMA | null | null | cell division [GO:0051301]; DNA repair [GO:0006281]; replication fork processing [GO:0031297]; resolution of meiotic recombination intermediates [GO:0000712] | FANCM-MHF complex [GO:0071821]; Fanconi anaemia nuclear complex [GO:0043240]; kinetochore [GO:0000776] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982] | PF15630; | 1.10.20.10; | TAF9 family, CENP-S/MHF1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19620631}. Chromosome, centromere {ECO:0000269|PubMed:19620631}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19620631}. Note=Assembly of CENPS and CENPX and its partner subunits CENPT and CENPW at centromeres occurs through a dynamic exchange mechanism. Although exchange is continuous in the cell cycle, de novo assembly starts principally during mid-late S phase and is complete by G2. CENPS is more stably bound at the kinetochore than CENPX. During S phase, rapidly recruited to DNA interstrand cross-links that block replication. Recruited to DNA damage sites about 20 minutes following UV irradiation, reaching a plateau after approximately 40 minutes. {ECO:0000250|UniProtKB:Q8N2Z9}. | null | null | null | null | null | FUNCTION: DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage (PubMed:20347428). In complex with CENPX (MHF heterodimer), crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. Stabilizes FANCM. In complex with CENPX and FANCM (but not other FANC proteins), rapidly recruited to blocked forks and promotes gene conversion at blocked replication forks. In complex with CENPT, CENPW and CENPX (CENP-T-W-S-X heterotetramer), involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression (PubMed:19620631). As a component of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like structure. DNA-binding function is fulfilled in the presence of CENPX, with the following preference for DNA substates: Holliday junction > double-stranded > splay arm > single-stranded. Does not bind DNA on its own (By similarity). {ECO:0000250|UniProtKB:Q8N2Z9, ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:20347428}. | Gallus gallus (Chicken) |
E1BTG2 | LMOD2_CHICK | MSTFGYRRELSKYEDIDEDELLASLTEEELKELERELEDIEPDRNLPVGQRQKSLTEKTPTGTFSREALMAYWERETRKLLEKERLGACEKDSEQEEDNSEDIQEECFTESNSEVSEEAYTEEDDEEEEEEEEEEEDEDDSDDEDEEKQNSAASERPVNCEDGRSSSHVRHKKCSNAKNSENLFNGHDGKDTENLSFKSSAIHPCGNPTVIEDALEKVRSNDPETTEVNLNNIENITSQMLIQFSQALRDNTVVKSFSLANTHADDNVAIAIAGMLKVNQHITSLNIESNFITGKGVLAIMRALQHNKVLTELRFHNQRHIMGSQVEMDIVKLLKENTTLVKLGYHFDLAGPRMSMTSILTRNMDKQRQKRMQEQRQQEYGCDGAINPKTKVLQKGTPRSSPYTSPKSSPWSSPKLPRKSAPAKSQPPAPAPPPPPPPPPPPPPPPPPVIPDKKAPTRNIAEVIKQQESSRKALQNGQKKKKGKKGKKHENSILKEIKDSLKSVSDRKSEEGSRPSTRPSTPQRSLHDNLMEAIRASSIKQLRRVEVPEALR | null | null | actin filament organization [GO:0007015]; actin filament polymerization [GO:0030041]; muscle contraction [GO:0006936]; myofibril assembly [GO:0030239]; pointed-end actin filament capping [GO:0051694] | actin filament [GO:0005884]; cytoskeleton [GO:0005856]; M band [GO:0031430]; myofibril [GO:0030016]; striated muscle thin filament [GO:0005865] | actin binding [GO:0003779]; tropomyosin binding [GO:0005523] | PF03250; | 3.80.10.10; | Tropomodulin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:20736303}. Cytoplasm, myofibril {ECO:0000269|PubMed:20736303}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:20736303}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20736303}. Note=Colocalizes with actin filament pointed ends in sarcomeres. Detected close to the M line. {ECO:0000269|PubMed:20736303}. | null | null | null | null | null | FUNCTION: Mediates nucleation of actin filaments and thereby promotes actin polymerization (By similarity). Plays a role in the regulation of actin filament length (PubMed:20736303). Required for normal sarcomere organization in the heart, and for normal heart function (By similarity). {ECO:0000250|UniProtKB:Q3UHZ5, ECO:0000250|UniProtKB:Q6P5Q4, ECO:0000269|PubMed:20736303}. | Gallus gallus (Chicken) |
E1BY77 | UBP13_CHICK | MQRAALFGGGDAQMAAGDLGELLVPYMPTIRVPKSGDRVYKTECAFSYDSPDSEGGLYVCMNTFLGFGREHIERHYRKTGQCVYLHLKRHVIEKVPGASGGALPKRRNAKLFLDLEANGDLSSDDFEYEDEAKLVIFPDHYEISLPNIEELPALVTIASDALLSAKSPYRKQDPDSWEEELQASKHAKSLVQLDNGVRIPPSGWKCSKCDLRENLWLNLTDGSVLCGKWFFDGSGGNGHAMEHYKETGYPLAVKLGTITPDGADVYSFDEEEPVLDPHIAKHLAHFGIDMLQMQVAENGLRDNDIKPRVSEWEVIQEAGVKLKPMYGPGYTGMKNLGNSCYLNAVMQAIFSIPEFQRAYVGNLPRIFDYSPLDPTQDFNTQMAKLGHGLLSGQYSKPPMKSELIEQVMKEEHKPQQNGISPQMFKAFISKDHTEFSSNRQQDAQEFFLHLINLVERNPVGSENPSDVFRFLVEERTQCCQSRKVRYTERVDYIMQLPVAMEAATNKDELIAYELKRREAEAARRAPPELVRAKIPFSACLQAFSEPTNVEDFWSSALQAKSAGVKTSRFASFPQYLVVQIKKFTFGLDWIPKKLDVSIDMPDFLDISHLRAMGLQPGEEELPDIAPPIIIPEDPKDRMMNNFVESLDIDESSVMQLAEMGFPLEACRKAVYYTGNLGAEVAFNWIIAHMEEPDFAEPLVVPVFGGAASSGVAGLGAVGLDNQPPEEMVSIIISMGFQRSLAIQALKATNNNLERALEWIFSHPELEEEDGEPALNVMDLENHTNANILAEARSEGPRIKDGPGRYELFGFISHMGTSTMSGHYVCHLKKEGRWVIYNDLRVCASERPPKDLGYIYFYHRIPS | 3.4.19.12 | null | autophagy [GO:0006914]; cell population proliferation [GO:0008283]; maintenance of unfolded protein [GO:0036506]; positive regulation of ERAD pathway [GO:1904294]; protein K63-linked deubiquitination [GO:0070536]; protein stabilization [GO:0050821]; proteolysis [GO:0006508]; regulation of autophagy [GO:0010506]; regulation of DNA-templated transcription [GO:0006355] | cytosol [GO:0005829]; nucleus [GO:0005634] | BAT3 complex binding [GO:1904288]; cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; K48-linked deubiquitinase activity [GO:1990380]; proteasome binding [GO:0070628]; protein-folding chaperone binding [GO:0051087]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270] | PF00627;PF00443;PF02148;PF17807; | 3.90.70.10;1.10.8.10;3.30.40.10; | Peptidase C19 family | null | null | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; | null | null | null | null | FUNCTION: Deubiquitinase that mediates deubiquitination of target proteins and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). {ECO:0000250|UniProtKB:Q92995}. | Gallus gallus (Chicken) |
E1C1L6 | ENTP5_CHICK | MTSSRLPVLLALVFSSLSPVLSHSNREMWFQDLFPPNTCPINAKTKTFYGIMFDAGSTGTRIHIYTFVQKSPEILPELEGEIFESVKPGLSAYADQPEKGAESVKRLLDMAIDAVPPHLWKKTPVVLKATAGLRLLSEEKAQALLSEVKEVFEESPFLVPEDSVSIMDGSYEGILAWITVNFLTGQLSGQNQHTVGTLDLGGASTQITFLPRFEETLKESPTDFLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALNTEVADRQMFRSSCLPKQLEAEWHFGGVKYRYGGNKEGETGFKPCYLEVLKVVKGKLHQPDEIRGSSFYAFSYYYDRAADTNLIDYEQGGVLEVRDFERKAKEVCDNMERFSSASPFLCMDLTYITALLKEGFGFRDNTLLQLTKKVNNIETSWTLGATFHLLQSLGITY | 3.6.1.6 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:O75356}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O75356}; | 'de novo' post-translational protein folding [GO:0051084]; nucleoside diphosphate catabolic process [GO:0009134]; protein N-linked glycosylation [GO:0006487]; UDP catabolic process [GO:0006256]; UDP-glucose metabolic process [GO:0006011] | endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; membrane [GO:0016020] | ADP phosphatase activity [GO:0043262]; CDP phosphatase activity [GO:0036384]; GDP phosphatase activity [GO:0004382]; IDP phosphatase activity [GO:1990003]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; UDP phosphatase activity [GO:0045134] | PF01150; | 3.30.420.40;3.30.420.150; | GDA1/CD39 NTPase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9WUZ9}. Secreted {ECO:0000250|UniProtKB:O75356}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800; Evidence={ECO:0000250|UniProtKB:O75356}; CATALYTIC ACTIVITY: Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157; Evidence={ECO:0000250|UniProtKB:O75356}; CATALYTIC ACTIVITY: Reaction=H2O + UDP = H(+) + phosphate + UMP; Xref=Rhea:RHEA:64876, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877; Evidence={ECO:0000250|UniProtKB:O75356}; CATALYTIC ACTIVITY: Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208; Evidence={ECO:0000250|UniProtKB:O75356}; CATALYTIC ACTIVITY: Reaction=CDP + H2O = CMP + H(+) + phosphate; Xref=Rhea:RHEA:64880, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64881; Evidence={ECO:0000250|UniProtKB:O75356}; CATALYTIC ACTIVITY: Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437; Evidence={ECO:0000250|UniProtKB:O75356}; | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q9WUZ9}. | null | null | FUNCTION: Hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP (By similarity). In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases. UMP can be transported back by an UDP-sugar antiporter to the cytosol where it is consumed to regenerate UDP-glucose. Therefore, it positively regulates protein reglucosylation by clearing UDP from the ER lumen and by promoting the regeneration of UDP-glucose. Protein reglucosylation is essential to proper glycoprotein folding and quality control in the ER (By similarity). {ECO:0000250|UniProtKB:O75356, ECO:0000250|UniProtKB:Q9WUZ9}. | Gallus gallus (Chicken) |
E1C2I2 | GWL_CHICK | MSTVEPLSDEGVAAGPRRIEVPRPPSIEEFTIVKPISRGAFGKVYLGRKAGRLYAVKVMKKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEAALALDYLHRHGIIHRDLKPDNMLISNQGHIKLTDFGLSRVTLNREINMIDILTTPSMAKPKHDYSRTPGQLLSLISSLGFYTPVGMKMPINPNSGGASDSLHEVISPLSMIEKENTPLSTKLFKTGLDTSPLTPVMPVRSLTPALLQSRERFGASTASSQSCMYLSSMESECCSSPRLEKDVKQTEDEMCSTGTSNSRPPLPSSREVLNSKDPKVLKKELESAISPISSNDCGSRQKLGTERSEITDTPVTTLDTKGIVRKCLSENKIWEEKLVARREMTNEMLETASSQQSPLFLKDPVQPVKEEEIFEKPGVKRSFELVDTSPCQELNYVKKTNAEYKRGCWISELSASKSTGLTTEIQSLMLSGEICESKEIMRCIDRQQTEKPLVPTVAKNLLCDLDADHEKDKEYMNSSLLCADDEKPLGALSADSDLSFPETSVSESHLEKQLVDLDKGVKDLSFEEPKAEDLLTMSPNCQEASRNGVEADVVQNCTMLCCEQDNHQKHTEETDTISSPSEKMTETVHLFRKNNVVFRSYNSPINVSNVSDPCSMASLDIMDLSPACSGSYPTAITPLQKTPRQGDAGTPYRTPKSVRRGAAPVEGERILGTPDYLAPELLLTKPHGSAVDWWALGVCLFEFLTGIPPFNDETPAQVFQNILKRDIPWPEGEEKLSDNAQNAIDILLTFDSTKRAGLKELKHHPLFHGVDWDNLQNQPMPFIPQPDDETDTSYFEARNNAQHLTVSGFSL | 2.7.11.1 | null | cell division [GO:0051301]; DNA damage response [GO:0006974]; G2/M transition of mitotic cell cycle [GO:0000086]; intracellular signal transduction [GO:0035556]; mitotic cell cycle [GO:0000278]; negative regulation of phosphoprotein phosphatase activity [GO:0032515]; phosphorylation [GO:0016310] | centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein phosphatase 2A binding [GO:0051721]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family | PTM: Phosphorylation at Thr-743 by CDK1 during M phase activates its kinase activity. Maximum phosphorylation occurs in prometaphase (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus. Note=During interphase is mainly nuclear, upon nuclear envelope breakdown localizes at the cytoplasm and during mitosis at the centrosomes. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | null | null | null | null | FUNCTION: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser-62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited (By similarity). {ECO:0000250}. | Gallus gallus (Chicken) |
E1C3P4 | CBPC1_CHICK | MKVKKNLTCSVSTSSRTMSLLSQLEKINLDSVLGEADNARYVTAKILHLVQSQEKTKKEMTSKGSSAIEVILSTLENTRDPQTILNILSILIELVSVGGGRRASVLVTKGGTQILLQLLLNASKESPPNEELMVLLHTLLAKIGPKDKKIGMKARINGALNISLNLVKQNLQNHRLILPCLQVLRVYSTNSVNAVSLGKNGVVELMFKIIGPFSKKNTSLMKVALDTLAALLKSKTNARRAVDRGYVHMLLTIYVDWHRHDSRHRYMLIRKGVLQCIKSVTNIKLGRKAFIDANGMKILYNTSQECLAVRTLDPLVNTSSLIMRKCFPKNRLPLPTIKSAFHFQLPVIPASGPVAQMYNLPPDVDDVVDESDDNDDAETESEIETEDDKDQNFKNDDIETDINKLKPRQELGRPLEELKMYEQFFPELTENFQECDLVSKEPKPFVSNANLGGPIVVPTAGEEFSAETNPSVIGISLKEGNPLLTEEYNRRPAFLGLPKKDSIKASSLLQQNVQRNLLPSCQCLSQEIVTGLDRISLQNTSENDQYYATGCVIKKDNKTSLTPLACSKTCEHVSPCGSSLFEGSSVHLGKFCCTGVESEEEDSKSSSSGEQVVLEVSDVSPVHDCDLYIEMVKTTKSIPEYSEVAYPDYFGHIPPPFKEPILERPYGVQRTKISQDIERLIHQNDIIDRVVYDLDNSICSAPEEVDVLKFNSKFESGNLRKVIQIRKNEYDLILNSDINSNHYHQWFYFEVSGMKTGIGYRFNIINCEKSNSQFNYGMQPLMYSVQEALNSRPSWTRVGTDICYYKNHFSRSSIAAGGQKGKSYYTITFTVTFQHKDDVCYFAYHYPYTYSTLKMHLQKLESMHNPQQIYFRQDALCETLGGNICPIVTITAMPESNYYEHICQFRNRPYIFLSARVHPGETNASWVMKGTLEYLMSSNPSAQSLRESYIFKIIPMLNPDGVINGNHRCSLSGEDLNRQWQNPNPDLHPTIYHAKGLLQYLAAIKRLPLVYCDYHGHSRKKNVFMYGCSIKETMWHTNVNTASCDLMEDPGYRVLPKILSQTAPAFCMGSCSFVVEKSKESTARVVVWREIGVQRSYTMESTLCGCDQGKYKGLQIGTKELEEMGAKFCVGLLRLKRMASPLEYNLPSGLLDIENELIESSCKVTSPTTYVLDEDEPRFLEEVDYSAESNDDQDAELADNVGDYEANNQEDGLSDSDSTRILLS | 3.4.17.-; 3.4.17.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | C-terminal protein deglutamylation [GO:0035609]; cerebellar Purkinje cell differentiation [GO:0021702]; eye photoreceptor cell differentiation [GO:0001754]; mitochondrion organization [GO:0007005]; neuromuscular process [GO:0050905]; olfactory bulb development [GO:0021772]; protein side chain deglutamylation [GO:0035610]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | metallocarboxypeptidase activity [GO:0004181]; tubulin binding [GO:0015631]; zinc ion binding [GO:0008270] | PF18027;PF00246; | 2.60.40.3120;1.25.10.10;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPW5}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q641K1}. Nucleus {ECO:0000250|UniProtKB:Q641K1}. Mitochondrion {ECO:0000250|UniProtKB:Q641K1}. | CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + H2O = (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-glutamate; Xref=Rhea:RHEA:60004, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:143623; Evidence={ECO:0000250|UniProtKB:Q641K1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000250|UniProtKB:Q641K1}; CATALYTIC ACTIVITY: Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + L-glutamate; Xref=Rhea:RHEA:63792, Rhea:RHEA-COMP:16435, Rhea:RHEA-COMP:16436, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:149555, ChEBI:CHEBI:149556; EC=3.4.17.24; Evidence={ECO:0000250|UniProtKB:Q641K1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793; Evidence={ECO:0000250|UniProtKB:Q641K1}; | null | null | null | null | FUNCTION: Metallocarboxypeptidase that mediates protein deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of alpha-tubulin as well as non-tubulin proteins. {ECO:0000250|UniProtKB:Q641K1}. | Gallus gallus (Chicken) |
E1C3U7 | LOXL2_CHICK | MEGFLGFNHNHCFIVLFFVSLSLAQYEHWPYLPGYPEPPPQVYQPPRRPADVPKIQLRLAGQKRKHNEGRVEVFYNGEWGTVCDDDFSIHAAHVICRELGYVEAVSWLPSSKYGKGEGKIWMDNVHCNGKEATLAACTSNGWGVTDCKHTEDVGVVCSEKRIPGFKFDNSLLNQIENMNIQVEDIRIRPILATYRKRVPVTEGYVEVKDEGTWKQICDKHWTMKNSRVVCGMFGFPSERKYNTKVYKMFASRRKQHYWAYSMDCTGNEAHISSCKLGNHLNVDTEKNATCDNGMPAVASCVPGRAFAPSSHSGFRKAFRQEQPLVRLKGGANTGEGRVEVLKNGEWGTVCDDNWNLVSASVVCRELGFGSAKEAITGARLGQGMGPIHLNEIDCTGFEKSLTDCKFNMESQGCNHEEDAAVRCNVPAMGFQNQLRLVGGRNPYEGRVEVLAERNGTLRWGTVCSQGWSTVEAMVVCRQLGLGFASHAFQETWYWHGDVSADSVVMSGVKCSGTEMSLAHCRHDGADVSCPRGGGRFGAGVSCSETAPDLVLNAELVEQTAYLEDRPMFMLQCAQEENCLASSAVNTSVTSGYRRLLRFSSQIHNNGQSDFRPKNGRHAWVWHDCHRHYHSMEVFTHYDLLNLNGTKVAEGHKASFCLEDTECEADVQKQYECANFGEQGITVGCWDVYRHDIDCQWIDITDVPPGDYLFQVVINPNYEVAESDYSNNVMKCRSRYDGQRIWMYNSVHNGANQDGDTEERFSAYWKLGNSILFSR | 1.4.3.13 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; COFACTOR: Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072, ECO:0000250|UniProtKB:Q9Y4K0}; | collagen fibril organization [GO:0030199]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; epithelial to mesenchymal transition [GO:0001837]; heterochromatin organization [GO:0070828]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of stem cell population maintenance [GO:1902455]; negative regulation of transcription by RNA polymerase II [GO:0000122]; peptidyl-lysine oxidation [GO:0018057]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; response to hypoxia [GO:0001666]; sprouting angiogenesis [GO:0002040] | basement membrane [GO:0005604]; chromatin [GO:0000785]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634] | calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; protein-lysine 6-oxidase activity [GO:0004720] | PF01186;PF00530; | 3.10.250.10; | Lysyl oxidase family | PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:Q9Y4K0}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q9Y4K0}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K0}. Chromosome {ECO:0000250|UniProtKB:Q9Y4K0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y4K0}. Note=Associated with chromatin. It is unclear how LOXL2 is nuclear as it contains a signal sequence and has been shown to be secreted. However, a number of reports confirm its intracellular location and its key role in transcription regulation. {ECO:0000250|UniProtKB:Q9Y4K0}. | CATALYTIC ACTIVITY: Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803; EC=1.4.3.13; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; | null | null | null | null | FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription. LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency including POU5F1/OCT4, NANOG, KLF4 and SOX2. Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin CDH1, probably by mediating deamination of histone H3. During EMT, involved with SNAI1 in negatively regulating pericentromeric heterochromatin transcription. SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits. Interacts with the endoplasmic reticulum protein HSPA5 which activates the IRE1-XBP1 pathway of the unfolded protein response, leading to expression of several transcription factors involved in EMT and subsequent EMT induction. When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation. {ECO:0000250|UniProtKB:P58022, ECO:0000250|UniProtKB:Q9Y4K0}. | Gallus gallus (Chicken) |
E1C656 | HACE1_CHICK | MERAMEQLNRLTRSLRRARTVELPDDNETAVYTLMPMVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSNVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLMRGAKYLPDKNGITPLDLCVQGGYGETCEVLIQYHPRLFQTIIQMTQNEDLRENMLRQVLEHLSQQSESQYLKILTSLAEVATTNGHKLLSLSSNYEAQMKSLLRIVRIFCHVFRIGPSSPSNGNDMGYNGNKTPRSQVFKVRKVYDVVRKIDVKEMNFTKHAFINQTSHEQEPLELLWHSLDEWLVLIATELMKNKRDSANITSILLKQKGPDHQDATPTPSFAAAGTESRKELSTDTGDSKTYEVAGKQEAYADCQDVISMTANRLSAVIQAFYMCCSCQMPQGMTSPRFIEFVCKHDDVLKCFVNRNPKIIFDHFHFLLECPELMSRFMHIIKAQPFKDRCEWFYEHLHSGQPDSDMVHRPVNENDILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMGQGVVREWFDILSSEIVNPDYALFTQSADGTTFQPNSNSSVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVETDVFGAMEEVPLKPGGASILVTQENKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVNDWLKNTEYTSGYERGDQVIQWFWDVVEELTQEERVLLLQFVTGSSRVPHGGFAHIMGGSGLQNFTIAAVPYTANLLPTSSTCINMLKLPEYPSKEILKDRLLVALHCGSYGYTMA | 2.3.2.26 | null | cell cycle [GO:0007049]; Golgi organization [GO:0007030]; membrane fusion [GO:0061025]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; regulation of cell migration [GO:0030334]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; nucleus [GO:0005634] | small GTPase binding [GO:0031267]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF12796;PF13857;PF00632; | 1.25.40.20;3.30.2160.10;3.30.2410.10;3.90.1750.10; | null | null | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase involved in Golgi membrane fusion and regulation of small GTPases. Acts as a regulator of Golgi membrane dynamics during the cell cycle: recruited to Golgi membrane by Rab proteins and regulates postmitotic Golgi membrane fusion. Acts by mediating ubiquitination during mitotic Golgi disassembly, ubiquitination serving as a signal for Golgi reassembly later, after cell division. {ECO:0000250|UniProtKB:Q8IYU2}. | Gallus gallus (Chicken) |
E1C7U0 | STING_CHICK | MPQDPSTRSSPARLLIPEPRAGRARHAACVLLAVCFVVLFLSGEPLAPIIRSVCTQLAALQLGVLLKGCCCLAEEIFHLHSRHHGSLWQVLCSCFPPRWYLALLLVGGSAYLDPPEDNGHSPRLALTLSCLCQLLVLALGLQKLSAVEVSELTESSKKNVAHGLAWSYYIGYLKVVLPRLKECMEELSRTNPMLRAHRDTWKLHILVPLGCDIWDDLEKADSNIQYLADLPETILTRAGIKRRVYKHSLYVIRDKDNKLRPCVLEFASPLQTLCAMSQDDCAAFSREQRLEQARLFYRSLRDILGSSKECAGLYRLIAYEEPAEPESHFLSGLILWHLQQQQREEYMVQEELPLGTSSVELSLQVSSSDLPQPLRSDCP | null | null | activation of innate immune response [GO:0002218]; autophagosome assembly [GO:0000045]; cGAS/STING signaling pathway [GO:0140896]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of macroautophagy [GO:0016239]; positive regulation of type I interferon production [GO:0032481]; protein complex oligomerization [GO:0051259]; reticulophagy [GO:0061709] | autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi membrane [GO:0000139]; perinuclear region of cytoplasm [GO:0048471] | 2',3'-cyclic GMP-AMP binding [GO:0061507]; cyclic-di-GMP binding [GO:0035438]; protein homodimerization activity [GO:0042803]; proton channel activity [GO:0015252] | PF15009; | 1.20.5.5200;3.40.50.12100; | STING family | PTM: Phosphorylation by TBK1 leads to activation and production of IFN-beta (Probable). Following cyclic nucleotide (c-di-GMP or cGAMP)-binding, activation and translocation from the endoplasmic reticulum, STING1 is phosphorylated by TBK1 at Ser-366 in the pLxIS motif (Probable). The phosphorylated pLxIS motif constitutes an IRF3-binding motif, leading to recruitment of the transcription factor IRF3 to induce type-I interferons and other cytokines (Probable). {ECO:0000305|PubMed:30842653}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q86WV6}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q86WV6}; Multi-pass membrane protein {ECO:0000255}. Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post-Golgi vesicles, where the kinase TBK1 is recruited. Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis. {ECO:0000250|UniProtKB:Q86WV6}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q86WV6}; | null | null | null | null | FUNCTION: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (By similarity). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (PubMed:30842659). Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes and is able to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state (PubMed:30842659). Exhibits 2',3' phosphodiester linkage-specific ligand recognition: can bind both 2'-3' linked cGAMP and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (By similarity). In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). Promotes autophagy by acting as a proton channel that directs proton efflux from the Golgi to facilitate LC3 lipidation (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q86WV6, ECO:0000269|PubMed:30842659}. | Gallus gallus (Chicken) |
E1C8P7 | DSCL1_CHICK | MWLVTFFLLYSLRKAHTEDVGTSLYFVNDSIQQVTFSSTVGVVIPCPAAGSPSAVLRWYLATGDDIYDVPHIRHVHANGTLQLYPFSPSAFNSFIHDNDYFCTAENSAGKIRSPNIRVKAVFREPYTVRVEDQRSMRGNVAVFKCLIPSSVQEYVSVVSWEKDTVSIIPENRFFITSYGGLYISDVQKEDALSTYRCITKHKYSGETRQSNGARLSVSDADPAESIPTMLDSFQSREVRAGRLVELPCIASGYPNPAIRWLKDGRPLPADGRWAKRITGLSIADLRVEDSGTYICEVTNTFGSAEVTGTLTVIDPLRVTLTPKKLKTGIGSTVILSCALSGSPEYVIRWYRNTDLVVVDDFISIRGISNETLLITAAQKSHSGAYQCFATRKSQTAQDFSIITLEDGTPRIVSSFSEKVVNPGEQFSLMCAAKGAPPPTVTWALDDEPIPRDNGHRTNQYTMSDGTTVSHMNVTSPQIKDGGVYRCTARNSVGSAEYQARINVRGPPSIRAMKNITAVAGRDTFINCRVIGYPYYSIKWYKDSLLLPDNHRQVVFENGTLKLMDVQKGMDEGEYLCSVLIQPQLSISQSVHVTVKVPPLIQPFEFPPASIGQLLYIPCVVSSGDMPIHITWRKDGHVILSGSGVTIESKEFMSSLQISSVSLKHNGNYTCIASNAAATVSRERQLIVRVPPRFVVQPNNQDGIYGKAGVLNCSVDGYPPPKVMWKHAKGSGNPQQYHPIPLTGRIQILPNSSLLIRHVLEEDIGYYLCQASNGVGTDISKSMFLTVKIPAMITSHPNTTIAIKGQSKELNCTARGERPIIIRWEKGDTVIDPDRNMRYAIATKDNGDEVISTLKLKPADRGDSVFFSCHAINSYGEDRGLIQLTVQEPPDPPELEIREVKARSMNLRWTQRFDGNSIITGFDIEYKNKSDSWDFKQSTRNISPTINQANIVDLHPASVYSIRMYSFNKIGRSEPSKELTISTEEAAPDGPPMDVTLQPMTSQSIQVTWKAPKKELQNGVIRGYQIGYRENSPGSNGQYSIVEMKATGDSEVYTLDNLKKFAQYGVVVQAFNRAGTGPSSSEINATTLEDVPSQPPENVRAISITSDVAVISWSEPPRSTLNGVLKGYRVIFWSLYMDGEWGEMQNITTTRERVELRGMEKFTNYSVQVLAYTQAGDGVRSSVLYIQTKEDIPGPPAGIKAVPSSASSVVVSWLPPAKPNGIIRKYTIFCSSPGSGQPAPSEYETSPDQLFYRIAHLNRGQQYMLWVAAVTSAGRGNISEKVTIEPAGKAPAKIISFGGTVTTPWMKDVRLPCNSVGEPVPAIKWTKDSEDSAIPVTVDGHRLIQANGTLVLRSVKAEDSGYYTCTATNTWGFDTIIINLLVQVPPDQPRLTVSKTSASSITLAWIPGDNGGSSIRGFVLQYSVDNSEEWKDVFISSSERSFKLESLKCGTWYKVKLAAKNSVGAGRISEIIEAKTHGREPSFSKDQHLFTHINSTHARLNLQGWSSGGCPITAIVLEYRPKGNWGWQSLRTNSSGEVFLTELREATWYELRMKACNSAGCGNESTQFATLDYDGSTIPPIKSAQGEGDDVKKLFTIACPIILATLGVALLFIIRKKRKEKRLKRLRDAKSLAEMLISKNNRSFDTPVKGPPQGPRLHIDIPRVQLLIEDKEGIKQLGDDKATIPVTDTEFSQAVNPQSFCTGVSLHHPALIQNTGPLIDMSDIRPGTNPVSRKSVKSAHSTRNRYSSQWTLTKCQASTPARTLTSDWRTVGSQHGITVTESDSYSASLSQDTDKGRNSMVSTESASSTYEELARAYEHAKLEEQLQHAKFEITECFISDSSSDQMTTGTTDNADSMTSMSTPSEPGICRFTASPPKPQDSERGKSVAVPIPHRASKSDYCNLPLYVKSDAFFRKPDSHEPCPVVPPREASIRSLARGYHPPARHLTLDPAAKPPGLPPPSSSSSSTTLPQRTLPMPTAASTAPAPAPAPAAPAEPPANTTTTTTTHSKVGGSRDSLLEMSTSGAGRAQKQGAGAYSKSYTLV | null | null | axon guidance [GO:0007411]; camera-type eye photoreceptor cell differentiation [GO:0060219]; dendrite self-avoidance [GO:0070593]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; retina layer formation [GO:0010842]; synapse assembly [GO:0007416] | axon [GO:0030424]; plasma membrane [GO:0005886]; synapse [GO:0045202] | cell-cell adhesion mediator activity [GO:0098632] | PF00041;PF07679;PF13927; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q4VA61}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q4VA61}. Synapse {ECO:0000269|PubMed:18216854}. | null | null | null | null | null | FUNCTION: Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells (By similarity). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (PubMed:18216854). {ECO:0000250|UniProtKB:Q4VA61, ECO:0000269|PubMed:18216854}. | Gallus gallus (Chicken) |
E1CG36 | CAP15_STRSQ | MNELEFHPHADRRTGSHTMEYQHLGVVPVVSAQANSTPLGGCTLSDGVIRAMGDAARFHVDMEQLWQAAGSFLAEATGSEDACPVTGAAAGMAIAVAACVAGTDGLRVQRLPDPGDQPNEIVLQKGHSISYGGAPLAQMIALGGGRAVEVGAVNETPRSHVASAVTRRTAALVYVTSRTHAVHRKGVPLDELVAIGREHGVPVIVDAAGEGGLRRWVASGADLVIYSGPKMLGAPTSGFICGRGDLVAACRAQYSGIARPMKVGKENLLGLLQAVREYTAVPEEQRAAEQLERMTKLAARLDKIPGLSARTAQDDSGRTIYRVLLTVDPAAAGRSAATLAEEMRAGIPSIYLRDFKLHLGQLEVDPRALSPDGEESVVRRLEELLLDHGGAPTGMEDAR | 1.-.-.- | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:29343643, ECO:0000269|PubMed:37556254}; Note=Requires pyridoxal phosphate as an oxygenase cofactor. {ECO:0000269|PubMed:29343643}; | antibiotic biosynthetic process [GO:0017000] | null | L-seryl-tRNA(Sec) selenium transferase activity [GO:0004125]; monooxygenase activity [GO:0004497] | PF03841; | 3.40.640.10; | SelA family | null | null | CATALYTIC ACTIVITY: Reaction=(5'S,6'R)-C-glycyluridine + O2 = CO2 + H2O + uridine-5'-carboxamide; Xref=Rhea:RHEA:77179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:195553, ChEBI:CHEBI:195554; Evidence={ECO:0000269|PubMed:29343643}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77180; Evidence={ECO:0000269|PubMed:29343643}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=560 uM for (5'S,6'R)-C-glycyluridine {ECO:0000269|PubMed:29343643}; Note=kcat is 0.93 min(-1) with (5'S,6'R)-C-glycyluridine as substrate. {ECO:0000269|PubMed:29343643}; | PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:29343643}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:29343643}; | null | FUNCTION: Monooxygenase-decarboxylase involved in the biosynthesis of the capuramycin-type nucleoside antibiotic A-503083 (PubMed:29343643). Catalyzes the oxidative decarboxylation of 5'-C-glycyluridine (GlyU) to uridine-5'-carboxamide (CarU) (PubMed:29343643). Is stereospecific for the (5'S,6'R)-diastereomer of GlyU (PubMed:29343643). Directly incorporates a single oxygen atom from O(2) into the product CarU (PubMed:29343643). {ECO:0000269|PubMed:29343643}. | Streptomyces sp |
E1JIB2 | IYD_DROME | MDVDELISSSKLLKHWPSLFITLALIWIVKRLFFKGNRVLKTYNLDEQVEEEVEHFADLGDELQPALEDKPHVPFVPGQNLNPNGAKRLYELMRGRRSIRSFNSHPKPDLSVIEDCIRAAGTAPSGAHTEPWTYCVVQEPELKRSIREIVEQEELVNYSQRMHPQWVTDLRPLQTNHVKEYLTEAPYLILIFKQTYGLSENGKRMRRHYYNEISTSIAAGILLCALQAAGLASLVTTPLNCGPALRNLLGRPVNEKLLILLPVGYPKDGCTVPDLARKNLSNIMVTF | 1.21.1.1 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:27643701}; | positive regulation of fertilization [GO:1905516]; thyroid hormone metabolic process [GO:0042403]; tyrosine metabolic process [GO:0006570] | plasma membrane [GO:0005886] | FMN binding [GO:0010181]; iodide peroxidase activity [GO:0004447]; iodotyrosine deiodinase activity [GO:0140616] | PF00881; | 3.40.109.10; | Nitroreductase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH; Xref=Rhea:RHEA:32479, ChEBI:CHEBI:15378, ChEBI:CHEBI:16382, ChEBI:CHEBI:57506, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349; EC=1.21.1.1; Evidence={ECO:0000269|PubMed:27643701}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:32481; Evidence={ECO:0000269|PubMed:27643701}; CATALYTIC ACTIVITY: Reaction=iodide + L-tyrosine + NADP(+) = 3-iodo-L-tyrosine + NADPH; Xref=Rhea:RHEA:27453, ChEBI:CHEBI:16382, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:59898; Evidence={ECO:0000269|PubMed:27643701}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27455; Evidence={ECO:0000269|PubMed:27643701}; CATALYTIC ACTIVITY: Reaction=3-iodo-L-tyrosine + iodide + NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + NADPH; Xref=Rhea:RHEA:27457, ChEBI:CHEBI:15378, ChEBI:CHEBI:16382, ChEBI:CHEBI:57506, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59898; Evidence={ECO:0000269|PubMed:27643701}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27459; Evidence={ECO:0000269|PubMed:27643701}; CATALYTIC ACTIVITY: Reaction=chloride + L-tyrosine + NADP(+) = 3-chloro-L-tyrosine + NADPH; Xref=Rhea:RHEA:70343, ChEBI:CHEBI:17996, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:189422; Evidence={ECO:0000269|PubMed:27643701}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70345; Evidence={ECO:0000269|PubMed:27643701}; CATALYTIC ACTIVITY: Reaction=bromide + L-tyrosine + NADP(+) = 3-bromo-L-tyrosine + NADPH; Xref=Rhea:RHEA:70347, ChEBI:CHEBI:15858, ChEBI:CHEBI:57783, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:189423; Evidence={ECO:0000269|PubMed:27643701}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70349; Evidence={ECO:0000269|PubMed:27643701}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14 uM for 3-iodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:27643701}; KM=8 uM for 3-bromo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:27643701}; KM=21 uM for 3-chloro-L-tyrosine (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:27643701}; KM=11 uM for 3,5-diiodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:27643701}; Note=kcat is 12 sec(-1) for the dehalogenation of 3-iodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) (PubMed:27643701). kcat is 6.9 sec(-1) for the dehalogenation of 3-bromo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) (PubMed:27643701). kcat is 5.0 sec(-1) for the dehalogenation of 3-chloro-L-tyrosine (at pH 7.4 and 25 degrees Celsius) (PubMed:27643701). kcat is 10.8 sec(-1) for the dehalogenation of 3,5-diiodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) (PubMed:27643701). {ECO:0000269|PubMed:27643701}; | null | null | null | FUNCTION: Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine (PubMed:27643701). Activity towards 3-fluoro-L-tyrosine is weak (PubMed:27643701). Important for male and female fertility (PubMed:29764939). May be involved in maintaining the viability of sperm, both during development in the testes and storage in the female spermatheca (PubMed:29764939). {ECO:0000269|PubMed:27643701, ECO:0000269|PubMed:29764939}. | Drosophila melanogaster (Fruit fly) |
E1JIT7 | PSD_DROME | MSEELKVVLRRSEQHSGFGFSLLGTTGPPHVIYDIVENSPAADCGAVEAGDVILKVNGTDVHRYTTKEVLKCLRLSEQLVTLELKRDPKLKARIKEQLANTQSPHYVDIESPNIYDYHSSSTNSSPNHRPNAGGKGAATTPSQTGLRYKSPTHLPSLRQNSSPLLASGSTTTTTTATHTHSHSRNSSASSTKIKVVETSITTSTTNVVGLTSPTGSVGGGVGGEATSPTFRPSRIPQALTKCAVPKPVPVLHSPQNKRPRPSQIPTKAANGNGNGHTAHLPPQSLQHSNSYSGSPVTRQRFADREPEREPEPNSAPPQPAKAPRFEAYMMTGDLILNLSRTPQTSNPLPAQAKKIDSLRDSPSRLVNPRINGALAPRASGESSPTSSSSVDSPTNTSSDSVKREAKLLQKQQQQQQQTYQQQQQRDSINNSYNRKDSLTNDTLLMCEELEPDEEGEYVLEEDNKQQRQRQQQQRYRQQQNQQRYEYYQNEDELEEQEEVEEEREEDQTHYDITNIETYQSGVGRGDDDDSDRQCLVDDDDDDDAYDDEENDAGDEDYSTNSLGSGSAKQRLRALKQRTATRQQQRNRDAVDCAGRSGSGSSSTTVKSEAGGLGLDETSFSVPTSPISLSTPLIDKETANSVPTSPEPSSLVPESSSGAGAGAVVVRRHNGHVVRKCDAAGFRTSKSEDHLQQIQREGIAAVIPIDIDEDVNSSLNTLLDTRQDSEDSQSMATVIVNNSSLASNNNEGEQTDNRSSSSSSNSSDNNNCSSNTGEPATSETATATATIITATSTRTMNCSSKLNYILCKKASDRDRIVWTYNAPLQPHQLAALQRQQQQQEQQFQQQQQQLHQQHLQQQQQLQQQHQQQQQQQQQQQQQQLYGQQSHSNSHSSSISSSPQHSAVGSPASPTSVSSSVMSSSGSKGALGLGSSSNGPMAAVQQQQLREREQGGQVAQPPSGIPGLLSCPGGGCGNNGGGGGIGGGGNNDQSVSEAISNISSPDYQDDDNLLSSRDILGGMVLSDPSDSDSTILVSDAAAHQRQQLKQQLRAQQQQQRERERDRDRDREQSEHKVVIQVRGLDSNSSGGNGTNGRSEEDVVTLTDEPLGTMTVGMRDASPPVSDDGSDVESLHSYHYSPKAVDMPSAIRLAKRLHSLDGFKKSDVSRHLSKNNDFSRAVADEYLKHFTFEKKSLDQALREFLQQFSLSGETQERERVLVHFSKRFLDCNPGTFNSQDAVHTLTCAIMLLNTDLHGQNINRKMSCAEFVDNLADLNDGENFPKDVLKSLYQAIKTKPLEWALDEEAGDLQQQRANNSALGNVGLNPFLDPPELATAVEYKKGYVMRKCCYDSSFKKTPFGKRSWKMFYCTLRDLVLYLHKDEHGFRKSQMSDNLHNAIRIHHALATKANDYTKKQHVFRLQTADQAEYLFQTSDSKELQSWVETINYVCAAISAPPLEGGVGSQKRFQRPLLPSKQSKLMLKEQLDSHEVQLAQLDQELNEHKKGPIPSKGLALQNYKEKESYLQYELRRYRTYVSILSAKMLADQQQLELQAQQPSPASHEEEADTFPVGTTACTPPTPQSINQKDQQKEQQQQQPTNRKEKKKK | null | null | axoneme assembly [GO:0035082]; compound eye morphogenesis [GO:0001745]; negative regulation of microtubule polymerization [GO:0031115]; positive regulation of ARF protein signal transduction [GO:0032014]; response to alcohol [GO:0097305] | axon [GO:0030424]; cell body [GO:0044297]; cell cortex [GO:0005938]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886] | guanyl-nucleotide exchange factor activity [GO:0005085]; microtubule binding [GO:0008017]; phospholipid binding [GO:0005543] | PF17820;PF15410;PF01369; | 2.30.42.10;1.10.1000.11;2.30.29.30; | PSD family | null | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:31718774}. Cytoplasm {ECO:0000269|PubMed:31718774}. Cell membrane {ECO:0000269|PubMed:31718774}; Peripheral membrane protein {ECO:0000269|PubMed:31718774}. Cytoplasm, cell cortex {ECO:0000269|PubMed:31718774}. | null | null | null | null | null | FUNCTION: Guanine nucleotide exchange factor for Arf6 (PubMed:28607459). Regulates axon growth and branching by inhibiting microtubule polymerisation at the cortex (PubMed:31718774). Together with shot, promotes axonal microtubule bundle integrity (PubMed:31718774). Required for normal ethanol-induced tolerance and preference (PubMed:28607459). Probably by activating Arf6, counteracts ethanol-induced sedation (PubMed:28607459). {ECO:0000269|PubMed:28607459, ECO:0000269|PubMed:31718774}. | Drosophila melanogaster (Fruit fly) |
E1U8D0 | MTCL2_MOUSE | METPAGESSARGYGPPPAPAPAAERKKSHRAPSPARPKDVAGWSLAKGRRGTGPGSATACGTASSARPDKKGRAVAPGTRGTGPRVAGVRTGVRAKGRPRPGTGPRPPPPPPSLTDSSSEVSDCASEEARQLGLELALSSDAESAAGGPAGTRTGQPPQPAQSGQQPPRPPASPDEPSVAASSVGSSRLPLSASLAFSDLTEEMLDCGPGGLVRELEELRSENDYLKDEIEELRAEMLEMRDVYMEEDVYQLQELRQQLDQASKTCRILQYRLRKAERRSLRAAQTGQVDGELIRGLEQDVKVSKDISMRLHKELEVVEKKRMRLEEENEGLRQRLIETELAKQVLQTELDRPREHSLKKRGTRSLGKTDKKPTAQEDSADLKCQLHFAKEESALMCKKLTKLAKENDSMKEELLKYRSLYGDLDAALSAEELADAPHSRETELKVHLKLVEEEANLLSRRIVELEVENRGLRAEMDDMKDHGGGGGPEARLAFSSLGGECGESLAELRRHLQFVEEEAELLRRSSAELEDQNKLLLNELAKYRSEHELDVTLSEDSCSVLSEPSQEELAAAKLQIGELSGKVKKLQYENRVLLSNLQRCDLASCQSTRPMLETDAEAGDSAQCVPAPLGETLEPHAARLCRAREAEALPGLREQAALVSKAIDVLVADANGFSVGLRLCLDNECADLRLHEAPDNSEGPRDAKLIHAILVRLSVLQQELNAFTRKADVALGSSGKEQPEPFPALPALGSQGPAKEIMLSKDLGSDFQPPDFRDLLEWEPRIREAFRTGDLESKPDPSRNFRPYRAEDNDSYASEIKDLQLVLAEAHDSLRGLQEQLSQERQLRKEEADSFNQKMVQLKEDQQRALLRREFELQSLSLQRRLEQKFWSQEKNILVQESQQFKHNFLLLFMKLRWFLKRWRQGKVLPSEEDDFLEVNSMKELYLLMEEEEMNAQHSDNKACTGESWTQNTPNECIKTLADMKVTLKELCWLLQDERRGLTELQQQFAKAKATWETERAELKGHASQMELKAGKGASERPGPDWKAALQREREEQQHLLAESYSAVMELTRQLQLSERHWSQEKLQLVERLQGEKQQVEQQVKELQNRLSQLQKAAEPWVLKHSDMEKQDNSWKEARSEKTHDKEGVSEAELGGTGLKRTKSVSSMSEFESLLDCSPYLAGGDARNKKLPNGPAFAFVSTEPVEPEKDAKEKAGLSTRDCSHIGSLACQEPAGRQMQRSYTAPDKTGIRVYYSPPVARRLGVPVVHDKEGKILIEPGFLFTTAKPKESAEADGLAESSYSRWLCNFSRQRLDGGSGASTSGSGPAFPALHDFEMSGNMSDDMKEITNCVRQAMRSGSLERKVKNTSSQTVGVATVGTQTIRTVSVGLQTDPPRSSLHSKSWSPRSSSLVSVRSKQISSSLDKVHSRIERPCCSPKYGSPKLQRRSVSKLDSTKDRSLWNLHQGKQNGSAWARSTTTRDSPVLRNINDGLSSLFSVVEHSGSTESVWKLGMSEARTKPEPPKYGIVQEFFRNVCGRAPSPTTAAGEESCKKPEPLSPASYHQPEGVSRILNKKAAKAGGSEEVRPTMLSQVGKDGILRDGDGSLILPSEDAVCDCSAQSLASCFIRPSRNTIRHSPSKCRLHPSESGWGGEERAAPQ | null | null | cell division [GO:0051301]; chromosome segregation [GO:0007059]; insulin receptor signaling pathway [GO:0008286]; negative regulation of gluconeogenesis [GO:0045721]; regulation of autophagy [GO:0010506] | extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; microtubule [GO:0005874]; midbody [GO:0030496] | null | PF14818;PF11365; | null | MTCL family | PTM: Proteolytically cleaved into a C-terminal SOGA 25 kDa form that is detected in plasma (By similarity). Proteolytically cleaved in primary hepatocytes into a C-terminal SOGA 80 kDa form. {ECO:0000250|UniProtKB:O94964, ECO:0000269|PubMed:20813965}.; PTM: Phosphorylated during mitosis in a CDK1-dependent manner. {ECO:0000250|UniProtKB:O94964}. | SUBCELLULAR LOCATION: [C-terminal 80 kDa form]: Secreted {ECO:0000269|PubMed:20813965}. Note=Secreted in primary hepatocyte-conditioned media. {ECO:0000269|PubMed:20813965}.; SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28550165, ECO:0000269|PubMed:35543016}. Golgi apparatus membrane {ECO:0000269|PubMed:35543016}. Midbody {ECO:0000250|UniProtKB:O94964}. Note=Co-localizes with CLASP2 in microtubules. {ECO:0000269|PubMed:28550165}. | null | null | null | null | null | FUNCTION: Microtubule-associated factor that enables integration of the centrosomal and Golgi-associated microtubules on the Golgi membrane, supporting directional migration. Preferentially acts on the perinuclear microtubules accumulated around the Golgi. Associates with the Golgi membrane through the N-terminal coiled-coil region and directly binds microtubules through the C-terminal domain (PubMed:35543016). Required for faithful chromosome segregation during mitosis (By similarity). Regulates autophagy by playing a role in the reduction of glucose production in an adiponectin- and insulin-dependent manner (PubMed:20813965). {ECO:0000250|UniProtKB:O94964, ECO:0000269|PubMed:20813965, ECO:0000269|PubMed:35543016}. | Mus musculus (Mouse) |
E1WAC8 | SCTB1_SALTS | MLISNVGINPAAYLNNHSVENSSQTASQSVSAKDILNSIGISSSKVSDLGLSPTLSAPAPGVLTQTPGTITSFLKASIQNTDMNQDLNALANNVTTKANEVVQTQLREQQAEVGKFFDISGMSSSAVALLAAANTLMLTLNQADSKLSGKLSLVSFDAAKTTASSMMREGMNALSGSISQSALQLGITGVGAKLEYKGLQNERGALKHNAAKIDKLTTESHSIKNVLNGQNSVKLGAEGVDSLKSLNMKKTGTDATKNLNDATLKSNAGTSATESLGIKDSNKQISPEHQAILSKRLESVESDIRLEQNTMDMTRIDARKMQMTGDLIMKNSVTVGGIAGASGQYAATQERSEQQISQVNNRVASTASDEARESSRKSTSLIQEMLKTMESINQSKASALAAIAGNIRA | null | null | actin filament organization [GO:0007015]; protein localization to Golgi apparatus [GO:0034067]; regulation of entry of bacterium into host cell [GO:2000535]; regulation of protein localization [GO:0032880] | extracellular region [GO:0005576]; host cell membrane [GO:0033644]; membrane [GO:0016020]; phagocytic vesicle [GO:0045335] | identical protein binding [GO:0042802]; syntaxin binding [GO:0019905] | PF09599; | null | SctB/SipC family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7608068}. Host membrane {ECO:0000250|UniProtKB:P0CL47}; Single-pass membrane protein {ECO:0000255}. Note=Secreted via the type III secretion system 1 (SPI-1 T3SS). {ECO:0000269|PubMed:7608068}. | null | null | null | null | null | FUNCTION: Component of the type III secretion system 1 (SPI-1 T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (By similarity). SipB/SctE1 and SipC/SctB1 are inserted into the host membrane where they form a pore and allow the translocation of effector proteins into the cytosol of target cells (By similarity). Plays a role in promoting human PERP translocation to the host apical epithelial cell surface via promotion of exocytic translocation (PubMed:27078059). {ECO:0000250|UniProtKB:P0CL47, ECO:0000269|PubMed:27078059}. | Salmonella typhimurium (strain SL1344) |
E1WKT5 | SOTC_BACF6 | MKKFTCVQDIGDLKSALAESFEIKKDRFKYVELGRNKTLLMIFFNSSLRTRLSTQKAALNLGMNVIVLDINQGAWKLETERGVIMDGDKPEHLLEAIPVMGCYCDIIGVRSFARFENREYDYNEVIINQFIQHSGRPVFSMEAATRHPLQSFADLITIEEYKKTARPKVVMTWAPHPRPLPQAVPNSFAEWMNATDYEFVITHPEGYELDPKFVGNARVEYDQMKAFEGADFIYAKNWAAYTGDNYGQILSTDRNWTVGDRQMAVTNNAYFMHCLPVRRNMIVTDDVIESPQSIVIPEAANREISATVVLKRLLENLP | 2.1.3.11 | null | arginine biosynthetic process via ornithine [GO:0042450]; citrulline biosynthetic process [GO:0019240] | null | amino acid binding [GO:0016597]; ornithine carbamoyltransferase activity [GO:0004585] | PF00185;PF02729; | 3.40.50.1370; | Aspartate/ornithine carbamoyltransferase superfamily, SOTCase family | null | null | CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + N(2)-succinyl-L-ornithine = H(+) + N(2)-succinyl-L-citrulline + phosphate; Xref=Rhea:RHEA:25884, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58514, ChEBI:CHEBI:58862; EC=2.1.3.11; Evidence={ECO:0000269|PubMed:16704984}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25885; Evidence={ECO:0000269|PubMed:16704984}; | null | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis. {ECO:0000269|PubMed:12095263, ECO:0000269|PubMed:16704984}. | null | null | FUNCTION: Catalyzes the transfer of the carbamoyl group from carbamoyl phosphate to the delta-amino group of N(2)-succinyl-L-ornithine to produce N(2)-succinyl-L-citrulline (PubMed:16704984). Is essential for arginine biosynthesis (PubMed:12095263, PubMed:16704984). Has no activity with either L-ornithine or L-aspartate as substrate (PubMed:12095263, PubMed:16704984). Has also no detectable AOTCase activity, being unable to convert N(2)-acetyl-L-ornithine to N(2)-acetyl-L-citrulline (PubMed:16585758, PubMed:16704984). {ECO:0000269|PubMed:12095263, ECO:0000269|PubMed:16585758, ECO:0000269|PubMed:16704984, ECO:0000303|PubMed:12095263}. | Bacteroides fragilis (strain 638R) |
E1XUJ2 | LDI_CASD6 | MRFTLKTTAIVSAAALLAGFGPPPRAAELPPGRLATTEDYFAQQAKQAVTPDVMAQLAYMNYIDFISPFYSRGCSFEAWELKHTPQRVIKYSIAFYAYGLASVALIDPKLRALAGHDLDIAVSKMKCKRVWGDWEEDGFGTDPIEKENIMYKGHLNLMYGLYQLVTGSRRYEAEHAHLTRIIHDEIAANPFAGIVCEPDNYFVQCNSVAYLSLWVYDRLHGTDYRAATRAWLDFIQKDLIDPERGAFYLSYHPESGAVKPWISAYTTAWTLAMVHGMDPAFSERYYPRFKQTFVEVYDEGRKARVRETAGTDDADGGVGLASAFTLLLAREMGDQQLFDQLLNHLEPPAKPSIVSASLRYEHPGSLLFDELLFLAKVHAGFGALLRMPPPAAKLAGK | 4.2.1.127; 5.4.4.4 | null | cellular response to organic substance [GO:0071310]; monoterpene catabolic process [GO:0043694]; monoterpenoid metabolic process [GO:0016098]; protein tetramerization [GO:0051262] | periplasmic space [GO:0042597] | hydro-lyase activity [GO:0016836]; intramolecular hydroxytransferase activity [GO:0050486] | PF18566; | null | null | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:20663876}. | CATALYTIC ACTIVITY: Reaction=(S)-linalool = beta-myrcene + H2O; Xref=Rhea:RHEA:30711, ChEBI:CHEBI:98, ChEBI:CHEBI:15377, ChEBI:CHEBI:17221; EC=4.2.1.127; Evidence={ECO:0000269|PubMed:20663876, ECO:0000269|PubMed:21950166, ECO:0000269|PubMed:27062179, ECO:0000269|PubMed:28068311, ECO:0000269|Ref.8}; CATALYTIC ACTIVITY: Reaction=(2E)-geraniol = (S)-linalool; Xref=Rhea:RHEA:30715, ChEBI:CHEBI:98, ChEBI:CHEBI:17447; EC=5.4.4.4; Evidence={ECO:0000269|PubMed:20663876, ECO:0000269|PubMed:21950166, ECO:0000269|PubMed:27062179, ECO:0000269|PubMed:28068311, ECO:0000269|Ref.8}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=750 uM for linalool {ECO:0000269|PubMed:20663876}; KM=800 uM for linalool (for linalool dehydration) {ECO:0000269|Ref.8}; KM=500 uM for geraniol {ECO:0000269|PubMed:20663876, ECO:0000269|Ref.8}; KM=200 uM for beta-myrcene {ECO:0000269|Ref.8}; Vmax=140 nmol/sec/mg enzyme for the linalool dehydration reaction {ECO:0000269|PubMed:20663876}; Vmax=410 nmol/sec/mg enzyme for the geraniol isomerization reaction {ECO:0000269|PubMed:20663876}; Note=kcat is 4.37 min(-1) for linalool dehydration. kcat is 9.0 min(-1) for beta-myrcene hydration. kcat is 1.66 min(-1) for geraniol isomerization. {ECO:0000269|Ref.8}; | PATHWAY: Terpene metabolism; monoterpene degradation. {ECO:0000269|PubMed:20663876, ECO:0000269|PubMed:22286981}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 for the linalool dehydratase activity. {ECO:0000269|PubMed:20663876}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius for the linalool dehydratase activity. {ECO:0000269|PubMed:20663876}; | FUNCTION: Anaerobically catalyzes the stereospecific hydration of beta-myrcene to (3S)-linalool and the isomerization of (3S)-linalool to geraniol (PubMed:20663876, PubMed:28068311, Ref.8). Is thus involved in the initial steps of the anaerobic degradation of the monoterpene beta-myrcene (PubMed:20663876). Also catalyzes the reverse reactions, i.e. the isomerization of geraniol to linalool and the dehydration of linalool to myrcene (PubMed:20663876, PubMed:28068311, Ref.8). In this direction, the formation of myrcene from geraniol may be seen as a detoxification process for the monoterpene alcohol (PubMed:20663876). Shows a relatively broad substrate specificity and can use various geraniol and linalool derivatives (PubMed:28068311). Substrates required a specific alpha-methylallyl alcohol signature motif (PubMed:28068311). Neither the monoterpenes alpha- and beta-ocimene nor the monoterpenoids citronellol and nerol can be used as substrates (PubMed:20663876). {ECO:0000269|PubMed:20663876, ECO:0000269|PubMed:28068311, ECO:0000269|Ref.8}. | Castellaniella defragrans (strain DSM 12143 / CCUG 39792 / 65Phen) (Alcaligenes defragrans) |
E2AXC7 | BRCC3_CAMFO | MDDSSLQKVELQTDVYMVCLQHALSTENFEVMGLLIGNFACGIAKISAVIILRRLDKKKDRVEISSEQLLKAAAEAERLTVELNRPMRVLGWYHSHPHITVCPSHVDVRTQATYQTMDHSFVGLIFSVFSEGKESKEHEIFLNCFQSDNGEATEIPLEIVHTPDISDRCLRTMTDLSKILVQEEEDMAEACKDHPDVLASIHNNAVRTRALIHITDIITKPLVQTFEKRIALNKLRATHLQRQLQELQKMCNG | 3.4.19.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:26344097}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:26344097}; | cell cycle [GO:0007049]; cell division [GO:0051301]; double-strand break repair [GO:0006302]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227]; proteolysis [GO:0006508] | BRCA1-A complex [GO:0070531]; BRISC complex [GO:0070552]; cytoplasm [GO:0005737]; spindle pole [GO:0000922] | cysteine-type deubiquitinase activity [GO:0004843]; metal ion binding [GO:0046872]; metal-dependent deubiquitinase activity [GO:0140492]; polyubiquitin modification-dependent protein binding [GO:0031593] | PF18110;PF01398; | 3.40.140.10; | Peptidase M67A family, BRCC36 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46736}. Nucleus {ECO:0000250|UniProtKB:P46736}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q15018}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q15018}. Note=A minor proportion is detected in the nucleus. Translocates into the nucleus in response to DNA damage. Directly binds to microtubules and is detected at the minus end of K-fibers. {ECO:0000250|UniProtKB:Q15018}. | null | null | null | null | null | FUNCTION: Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains, leaving the last ubiquitin chain attached to its substrates. Catalytic subunit of the BRISC complex; does not have activity by itself, but needs to be associated into a heterotetramer with ABRAXAS2 for minimal in vitro activity (PubMed:26344097). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (By similarity). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating spindle assembly factors (By similarity). {ECO:0000250|UniProtKB:Q15018, ECO:0000250|UniProtKB:Q3TCJ1, ECO:0000269|PubMed:26344097}. | Camponotus floridanus (Florida carpenter ant) |
E2BJ30 | ORCO_HARSA | MMKMKQQGLVADLLPNIRVMKFFGHFVFNYYDDNSSKYLHKIFCCVNLFLLLLQFALCAVNLIIESADVDDLTANTITLLFFTHSIVKIIYFAVRSKYFYRTWAIWNNPNSHPLFAESNARYHAIALKKMRLLLFLVGATTVLSAIAWTVLTFFEHPIRKLVDPVTNETTIIELPQLLLRSYYPFDASKGIMHVIVLIYQFYWVLFMLIDANSLDVLFCSWLLFACEQLQHLKQIMKPLMELSATLDTVVPNSSELFKAGSAEHLRESENQPPPPVPPQGDSMLDLDLRNIYSNRQDFTATFRPTAGMTFNGGVGPNGLTKKQEMLVRSAIKYWVERHKHIVRLVTAVGDAYGFALLLHMLTTTITLTLLAYQATKVNGVNVYAASTIGYIIYTFGQVFLFCIFGNRLIEESTSVMEAAYSCHWYDGSEEAKTFVQIVCQQCQKAMSISGAKFFTVSLDLFASVLGAVVTYFMVLVQLK | null | null | antennal development [GO:0007469]; detection of chemical stimulus involved in sensory perception of smell [GO:0050911]; detection of pheromone [GO:0043695]; mating behavior [GO:0007617]; olfactory behavior [GO:0042048]; response to pheromone [GO:0019236]; signal transduction [GO:0007165]; social behavior [GO:0035176] | plasma membrane [GO:0005886] | odorant binding [GO:0005549]; olfactory receptor activity [GO:0004984] | PF02949; | null | Insect chemoreceptor superfamily, Heteromeric odorant receptor channel (TC 1.A.69) family, Orco subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Odorant coreceptor which complexes with conventional odorant receptors (ORs) to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity). Obligate coreceptor of all odorant receptors (By similarity). Orco is a universal and integral part of the functional odorant receptor, involved in the dendritic localization of other olfactory receptors. Can form functional ion channels in the absence of an odor-binding odorant receptor (By similarity). Plays a central role in the perception of olfactory stimuli in ants and is essential for ant social organization (PubMed:28802043). Required for pheromone sensing and mating behavior (PubMed:28802043). Also required for the development and maintenance of odorant receptor neurons (ORNs) and of antennal lobe glomeruli (PubMed:28802043). {ECO:0000250|UniProtKB:Q7QCC7, ECO:0000269|PubMed:28802043}. | Harpegnathos saltator (Jerdon's jumping ant) |
E2DWQ7 | A3AKI_PHYIN | MRLAIMLSATAVAINFATCSAIDQTKVLVYGTPAHYIHDSAGRRLLRKNEENEETSEERAPNFNLANLNEEMFNVAALTKRADAKKLAKQLMGNDKLADAAYIWWQHNRVTLDQIDTFLKLASRKTQGAKYNQIYNSYMMHLGLTGY | null | null | null | extracellular region [GO:0005576]; host cell endosome [GO:0044174] | null | PF16810; | 1.10.10.2460; | RxLR effector family | PTM: Proteolytically cleaved. The cleavage site directly after the RxLR sequence and the high conservation among other effector proteins suggest that the RxLR motif might play a crucial role in the intracellular processing before secretion. {ECO:0000269|PubMed:28522546}.; PTM: glycosylated. {ECO:0000269|PubMed:28522546}.; PTM: N-acetylated at Lys-48 after cleavage. {ECO:0000269|PubMed:28522546}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15894622, ECO:0000269|PubMed:16965554, ECO:0000269|PubMed:17914356, ECO:0000269|PubMed:29312401}. Host cytoplasm {ECO:0000269|PubMed:15894622, ECO:0000269|PubMed:16965554, ECO:0000269|PubMed:17914356, ECO:0000269|PubMed:29312401}. Host endosome {ECO:0000269|PubMed:23243124}. Note=Avr3A(KI), but not Avr3A(EM), is relocalized to endosomes in the presence of R3a. {ECO:0000269|PubMed:23243124}. | null | null | null | null | null | FUNCTION: Multifunctional effector that can suppress host BAK1/SERK3-mediated immunity through at least two different pathways (PubMed:19794118, PubMed:20457921, PubMed:21348873, PubMed:26348328). Manipulates plant immunity by targeting and stabilizing host E3 ligase CMPG1. Preventing the normal 26S proteasome-dependent degradation of potato CMPG1, and thus potentially of its protein substrates in the host cell, further abolishes host cell death during the biotrophic phase of infection (PubMed:19794118, PubMed:20457921, PubMed:21348873). Associates also with the dynamin-related protein 2 (DRP2), a plant GTPase involved in immune receptor-mediated endocytosis (PubMed:26348328). The Avr3A(KI) form is recognized by R3a which triggers R3a-mediated hypersensitivity and suppresses INF1-induced cell death (PubMed:15894622, PubMed:16965554, PubMed:19245321). {ECO:0000269|PubMed:15894622, ECO:0000269|PubMed:16965554, ECO:0000269|PubMed:19245321, ECO:0000269|PubMed:19794118, ECO:0000269|PubMed:20457921, ECO:0000269|PubMed:21348873, ECO:0000269|PubMed:26348328}. | Phytophthora infestans (Potato late blight agent) (Botrytis infestans) |
E2E2N7 | BCGS_ORIVU | MEIYSPVVPAVKDVKRLDEIRKSAKFHPSIWGDFFLSYNSDNTQISEAEEEEVAKQKEAVRELLAQVPEGSTYKMELIDLIQRLGVNYHFEKEIHDSLNYIHENSQHNDDEVRTTALRFRLLRQQGYRVPCDVFRKFTDGEGNFATALTNDVEGLLELYEASHLATRGEEILDRAMEFSSSHLQALLNQHLVGSVSLSKRVDEALKMPIRKTLTRLGARKFISLYQEDESRNELLLNFAKLDFNMVQKMHQRELSDATRWWKKLEVAKRMPYARDRVVECFFWIVGVYFEPCYATARRILSKAINMASIVDDTYEYATLDELQILTDAIQRWDVNETLEDSPPHVQMCYKALIQAYAEIEDEVVENFGGEELYRVQYAIEHVKQSAVAFFEEAKWIYNNSIPTVEEYMKVAFVTCGYMMLSTTSLVGVGSDRVSKADFDWIVNEPLIVRASCVICRLMDDLVGDEYEEKPSSVLCYMKQYVVSKDEARARLEQQVKDAWKDMNEECIEPRPASMQILTRVLNLGRVIHLLYREGDSYTDPNRSKEWVKMVFVDPI | 3.1.7.11; 4.2.3.-; 4.2.3.100; 4.2.3.113; 4.2.3.20 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:20419468}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20419468}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:E2E2P0}; | diterpenoid biosynthetic process [GO:0016102] | null | (R)-limonene synthase activity [GO:0034002]; hydrolase activity [GO:0016787]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; sesquiterpene synthase activity [GO:0010334] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = bicyclogermacrene + diphosphate; Xref=Rhea:RHEA:31999, ChEBI:CHEBI:33019, ChEBI:CHEBI:63709, ChEBI:CHEBI:175763; EC=4.2.3.100; Evidence={ECO:0000269|PubMed:20419468}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32000; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene; Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.113; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (4R)-limonene + diphosphate; Xref=Rhea:RHEA:10940, ChEBI:CHEBI:15382, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.20; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10941; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = (2E)-geraniol + diphosphate; Xref=Rhea:RHEA:32679, ChEBI:CHEBI:15377, ChEBI:CHEBI:17447, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=3.1.7.11; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32680; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = allo-aromadendrene + diphosphate; Xref=Rhea:RHEA:67400, ChEBI:CHEBI:33019, ChEBI:CHEBI:166670, ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67401; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}. | null | null | FUNCTION: Involved in the biosynthesis of phenolic sesquiterpenes natural products (Ref.2). Sesquiterpene synthase converting (2E,6E)-farnesyl diphosphate (FPP) to alloaromadendrene and bicyclo-germacrene. The product formation is dependent on the metal ions present and in presence of manganese, bicyclo-germacrene is greatly favored while both alloaromadendrene and bicyclo-germacrene are produced in equivalent amounts in the presence of magnesium. Can also convert geranyl diphosphate (GPP) to terpinolene, limonene and geraniol, and this conversion is not affected by the presence of magnesium or manganese. {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}. | Origanum vulgare (Wild marjoram) |
E2E2P0 | GTPS_ORIVU | MATLSMQVSILSKEVKNVNNIGMRASKPMVARRVSTTRLRPICSASLQVEEETRRSGNYQASIWNNDYVQSFNTNQYKDEKHLKKKEELIAQVKILLNTKMEAVKQLELIEDLRNLGLTYYFQDEVKKILTSIYNDHKCFKNEQVGDLYFTSLGFRLLRLHGFDVSEEVFDFFKNEDGSDFKASLGENIKDVLQLYEASFLIREGEVILEQARVFSTKHLEKKVDEGINDEKLLAWIRHSLALPLHWRIQRLEARWFLDAYRARKDMIPLIFELGKIDFHIIQETQLEELQEVSKWWTNSNLAEKLPFVRDRIVECYFWALGLFEPHEYGYQRKMAAIIITFVTIIDDVYDVYGTLDELQLFTDAIRKWDFQSISTLPYYMQVCYLALYTYASELAYDILKDQGFNSIAYLQRSWLSLVEGFFQEAKWYYAGYTPTLAEYLENAKVSISSPTIISQVYFTLPNSTERTVVENVFGYHNILYLSGMILRLADDLGTTQFELKRGDVQKAIQCYMKDNNATEKEGAEHVKYLLREAWKEMNTAMADPECPLSEDLVDAAANLGRASQFIYLEGDGHGVQHSEIHNQMGGLIFEPYV | 4.2.3.114; 4.2.3.115 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; Note=Manganese > magnesium. {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; | defense response to insect [GO:0002213]; diterpenoid biosynthetic process [GO:0016102]; geranyl diphosphate metabolic process [GO:0033383]; response to insect [GO:0009625]; response to water deprivation [GO:0009414] | chloroplast [GO:0009507] | gamma-terpinene synthase activity [GO:0102903]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; terpene synthase activity [GO:0010333] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + gamma-terpinene; Xref=Rhea:RHEA:32559, ChEBI:CHEBI:10577, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.114; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32560; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = alpha-terpinene + diphosphate; Xref=Rhea:RHEA:32563, ChEBI:CHEBI:10334, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.115; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32564; Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.71 uM for geranyl diphosphate (in the presence of 0.5 mM manganese) {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; KM=0.7 mM for manganese (in the presence of 10 uM geranyl diphosphate) {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; KM=3.41 mM for magnesium (in the presence of 10 uM geranyl diphosphate) {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; Vmax=6.18 umol/min/g enzyme with geranyl diphosphate as substrate {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8. {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 28 degrees Celsius. {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}; | FUNCTION: Involved in the biosynthesis of phenolic monoterpenes natural products thymol and carvacrol which have a broad range of biological activities acting as antimicrobial compounds, insecticides, antioxidants and pharmaceutical agents (PubMed:20419468, PubMed:26156773, PubMed:30231481, Ref.2). Monoterpene synthase which catalyzes the conversion of geranyl diphosphate (GPP) to gamma-terpinene and the minor products alpha-thujene, alpha-terpinene, myrcene, sabinene, (+)-R-limonene, alpha-pinene and alpha-phellandrene (PubMed:20419468, Ref.2). {ECO:0000269|PubMed:20419468, ECO:0000269|PubMed:26156773, ECO:0000269|PubMed:30231481, ECO:0000269|Ref.2}. | Origanum vulgare (Wild marjoram) |
E2JF22 | PIEZ1_MOUSE | MEPHVLGAGLYWLLLPCTLLAASLLRFNALSLVYLLFLLLLPWLPGPSRHSIPGHTGRLLRALLCLSLLFLVAHLAFQICLHTVPHLDQFLGQNGSLWVKVSQHIGVTRLDLKDIFNTTRLVAPDLGVLLASSLCLGLCGRLTRKAGQSRRTQELQDDDDDDDDDDEDIDAAPAVGLKGAPALATKRRLWLASRFRVTAHWLLMTSGRTLVIVLLALAGIAHPSAFSSIYLVVFLAICTWWSCHFPLSPLGFNTLCVMVSCFGAGHLICLYCYQTPFIQDMLPPGNIWARLFGLKNFVDLPNYSSPNALVLNTKHAWPIYVSPGILLLLYYTATSLLKLHKSCPSELRKETPREDEEHELELDHLEPEPQARDATQGEMPMTTEPDLDNCTVHVLTSQSPVRQRPVRPRLAELKEMSPLHGLGHLIMDQSYVCALIAMMVWSIMYHSWLTFVLLLWACLIWTVRSRHQLAMLCSPCILLYGLTLCCLRYVWAMELPELPTTLGPVSLHQLGLEHTRYPCLDLGAMLLYLLTFWLLLRQFVKEKLLKKQKVPAALLEVTVADTEPTQTQTLLRSLGELVTGIYVKYWIYVCAGMFIVVSFAGRLVVYKIVYMFLFLLCLTLFQVYYTLWRKLLRVFWWLVVAYTMLVLIAVYTFQFQDFPTYWRNLTGFTDEQLGDLGLEQFSVSELFSSILIPGFFLLACILQLHYFHRPFMQLTDLEHVPPPGTRHPRWAHRQDAVSEAPLLEHQEEEEVFREDGQSMDGPHQATQVPEGTASKWGLVADRLLDLAASFSAVLTRIQVFVRRLLELHVFKLVALYTVWVALKEVSVMNLLLVVLWAFALPYPRFRPMASCLSTVWTCIIIVCKMLYQLKIVNPHEYSSNCTEPFPNNTNLQPLEINQSLLYRGPVDPANWFGVRKGYPNLGYIQNHLQILLLLVFEAVVYRRQEHYRRQHQQAPLPAQAVCADGTRQRLDQDLLSCLKYFINFFFYKFGLEICFLMAVNVIGQRMNFMVILHGCWLVAILTRRRREAIARLWPNYCLFLTLFLLYQYLLCLGMPPALCIDYPWRWSKAIPMNSALIKWLYLPDFFRAPNSTNLISDFLLLLCASQQWQVFSAERTEEWQRMAGINTDHLEPLRGEPNPIPNFIHCRSYLDMLKVAVFRYLFWLVLVVVFVAGATRISIFGLGYLLACFYLLLFGTTLLQKDTRAQLVLWDCLILYNVTVIISKNMLSLLSCVFVEQMQSNFCWVIQLFSLVCTVKGYYDPKEMMTRDRDCLLPVEEAGIIWDSICFFFLLLQRRIFLSHYFLHVSADLKATALQASRGFALYNAANLKSINFHRQIEEKSLAQLKRQMKRIRAKQEKYRQSQASRGQLQSKDPQDPSQEPGPDSPGGSSPPRRQWWRPWLDHATVIHSGDYFLFESDSEEEEEALPEDPRPAAQSAFQMAYQAWVTNAQTVLRQRRERARQERAEQLASGGDLNPDVEPVDVPEDEMAGRSHMMQRVLSTMQFLWVLGQATVDGLTRWLRAFTKHHRTMSDVLCAERYLLTQELLRVGEVRRGVLDQLYVGEDEATLSGPVETRDGPSTASSGLGAEEPLSSMTDDTSSPLSTGYNTRSGSEEIVTDAGDLQAGTSLHGSQELLANARTRMRTASELLLDRRLHIPELEEAERFEAQQGRTLRLLRAGYQCVAAHSELLCYFIIILNHMVTASAASLVLPVLVFLWAMLTIPRPSKRFWMTAIVFTEVMVVTKYLFQFGFFPWNSYVVLRRYENKPYFPPRILGLEKTDSYIKYDLVQLMALFFHRSQLLCYGLWDHEEDRYPKDHCRSSVKDREAKEEPEAKLESQSETGTGHPKEPVLAGTPRDHIQGKGSIRSKDVIQDPPEDLKPRHTRHISIRFRRRKETPGPKGTAVMETEHEEGEGKETTERKRPRHTQEKSKFRERMKAAGRRLQSFCVSLAQSFYQPLQRFFHDILHTKYRAATDVYALMFLADIVDIIIIIFGFWAFGKHSAATDIASSLSDDQVPQAFLFMLLVQFGTMVIDRALYLRKTVLGKLAFQVVLVVAIHIWMFFILPAVTERMFSQNAVAQLWYFVKCIYFALSAYQIRCGYPTRILGNFLTKKYNHLNLFLFQGFRLVPFLVELRAVMDWVWTDTTLSLSNWMCVEDIYANIFIIKCSRETEKKYPQPKGQKKKKIVKYGMGGLIILFLIAIIWFPLLFMSLIRSVVGVVNQPIDVTVTLKLGGYEPLFTMSAQQPSIVPFTPQAYEELSQQFDPYPLAMQFISQYSPEDIVTAQIEGSSGALWRISPPSRAQMKQELYNGTADITLRFTWNFQRDLAKGGTVEYTNEKHTLELAPNSTARRQLAQLLEGRPDQSVVIPHLFPKYIRAPNGPEANPVKQLQPDEEEDYLGVRIQLRREQVGTGASGEQAGTKASDFLEWWVIELQDCKADCNLLPMVIFSDKVSPPSLGFLAGYGIVGLYVSIVLVVGKFVRGFFSEISHSIMFEELPCVDRILKLCQDIFLVRETRELELEEELYAKLIFLYRSPETMIKWTRERE | null | null | cellular response to mechanical stimulus [GO:0071260]; detection of mechanical stimulus [GO:0050982]; monoatomic cation transport [GO:0006812]; positive regulation of cell-cell adhesion mediated by integrin [GO:0033634]; positive regulation of integrin activation [GO:0033625]; positive regulation of myotube differentiation [GO:0010831]; regulation of membrane potential [GO:0042391] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; lamellipodium membrane [GO:0031258]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; mechanosensitive monoatomic cation channel activity [GO:0140135]; mechanosensitive monoatomic ion channel activity [GO:0008381]; monoatomic cation channel activity [GO:0005261] | PF15917;PF12166; | null | PIEZO (TC 1.A.75) family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92508}; Multi-pass membrane protein {ECO:0000269|PubMed:29261642, ECO:0007744|PDB:6BPZ}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q0KL00}. Cell membrane {ECO:0000269|PubMed:20813920, ECO:0000269|PubMed:26390154, ECO:0000269|PubMed:29261642, ECO:0000269|PubMed:36515266, ECO:0007744|PDB:6BPZ}; Multi-pass membrane protein {ECO:0000269|PubMed:26390154, ECO:0000269|PubMed:29261642, ECO:0007744|PDB:6BPZ}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q92508}. Note=In erythrocytes, located in the plasma membrane (PubMed:23479567). Accumulates at the leading apical lamellipodia of endothelial cells in response to shear stress (By similarity). Colocalizes with F-actin and MYH9 at the actomyosin cortex in myoblasts. Non-uniform distribution of Piezo1 in the red blood cell membrane with an enrichment at the dimple (PubMed:36515266). {ECO:0000250|UniProtKB:Q92508, ECO:0000269|PubMed:23479567, ECO:0000269|PubMed:29799007, ECO:0000269|PubMed:36515266}. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:20813920}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:20813920}; CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:20813920}; CATALYTIC ACTIVITY: Reaction=Mg(2+)(in) = Mg(2+)(out); Xref=Rhea:RHEA:29827, ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20813920}; | null | null | null | null | FUNCTION: Pore-forming subunit of a mechanosensitive non-specific cation channel. Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium (PubMed:20813920, PubMed:22343900). Conductance to monovalent alkali ions is highest for K(+), intermediate for Na(+) and lowest for Li(+). Divalent ions except for Mn(2+) permeate the channel but more slowly than the monovalent ions and they also reduce K(+) currents (By similarity). Plays a key role in epithelial cell adhesion by maintaining integrin activation through R-Ras recruitment to the ER, most probably in its activated state, and subsequent stimulation of calpain signaling. In the kidney, may contribute to the detection of intraluminal pressure changes and to urine flow sensing (PubMed:24157948). Acts as a shear-stress sensor that promotes endothelial cell organization and alignment in the direction of blood flow through calpain activation. Plays a key role in blood vessel formation and vascular structure in both development and adult physiology (PubMed:24958852, PubMed:25119035, PubMed:36515266). Acts as a sensor of phosphatidylserine (PS) flipping at the plasma membrane and governs morphogenesis of muscle cells. In myoblasts, flippase-mediated PS enrichment at the inner leaflet of plasma membrane triggers channel activation and Ca2+ influx followed by Rho GTPases signal transduction, leading to assembly of cortical actomyosin fibers and myotube formation (PubMed:29799007). {ECO:0000250|UniProtKB:Q92508, ECO:0000269|PubMed:20813920, ECO:0000269|PubMed:22343900, ECO:0000269|PubMed:24157948, ECO:0000269|PubMed:24958852, ECO:0000269|PubMed:25119035, ECO:0000269|PubMed:29799007, ECO:0000269|PubMed:36515266}. | Mus musculus (Mouse) |
E2QWQ2 | NLK_CANLF | MSLCGARANAKMMAAYNGGTSAAAAGHHHHHHHHLPHLPPPHLHHHHHPQHHLHPGSAAAVHPVQQHTSSAAAAAAAAAAAAAMLNPGQQQPYFPSPAPGQAPGPAAAAPAQVQAAAAATVKAHHHQHSHHPQQQLDIEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIDYFEEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESRHMTQEVVTQYYRAPEILMGSRHYSNAIDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPSLEAMRTACEGAKAHILRGPHKQPSLPVLYTLSSQATHEAVHLLCRMLVFDPSKRISAKDALAHPYLDEGRLRYHTCMCKCCFSTSTGRVYTSDFEPITNPKFDDTFEKNLSSVRQVKEIIHQFILEQQKGNRVPLCINPQSAAFKSFISSTVAQPSEMPPSPLVWE | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O54949}; | cellular response to osmotic stress [GO:0071470]; intracellular signal transduction [GO:0035556]; negative regulation of TORC1 signaling [GO:1904262]; negative regulation of Wnt signaling pathway [GO:0030178]; phosphorylation [GO:0016310]; protein stabilization [GO:0050821]; regulation of DNA-templated transcription [GO:0006355]; transforming growth factor beta receptor signaling pathway [GO:0007179]; Wnt signaling pathway [GO:0016055] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; magnesium ion binding [GO:0000287]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; SH2 domain binding [GO:0042169]; ubiquitin protein ligase binding [GO:0031625] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Phosphorylated on Thr-298. Intermolecular autophosphorylation on Thr-298 activates the enzyme. {ECO:0000250|UniProtKB:O54949}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O54949}. Cytoplasm {ECO:0000250|UniProtKB:O54949}. Note=Predominantly nuclear. A smaller fraction is cytoplasmic. {ECO:0000250|UniProtKB:O54949}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000250|UniProtKB:O54949}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000250|UniProtKB:O54949}; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination. Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Negative regulator of the canonical Wnt/beta-catenin signaling pathway. Binds to and phosphorylates TCF7L2/TCF4 and LEF1, promoting the dissociation of the TCF7L2/LEF1/beta-catenin complex from DNA, as well as the ubiquitination and subsequent proteolysis of LEF1. Together these effects inhibit the transcriptional activation of canonical Wnt/beta-catenin target genes. Negative regulator of the Notch signaling pathway. Binds to and phosphorylates NOTCH1, thereby preventing the formation of a transcriptionally active ternary complex of NOTCH1, RBPJ/RBPSUH and MAML1. Negative regulator of the MYB family of transcription factors. Phosphorylation of MYB leads to its subsequent proteolysis while phosphorylation of MYBL1 and MYBL2 inhibits their interaction with the coactivator CREBBP. Other transcription factors may also be inhibited by direct phosphorylation of CREBBP itself. Acts downstream of IL6 and MAP3K7/TAK1 to phosphorylate STAT3, which is in turn required for activation of NLK by MAP3K7/TAK1. Upon IL1B stimulus, cooperates with ATF5 to activate the transactivation activity of C/EBP subfamily members. Phosphorylates ATF5 but also stabilizes ATF5 protein levels in a kinase-independent manner. Acts as an inhibitor of the mTORC1 complex in response to osmotic stress by mediating phosphorylation of RPTOR, thereby preventing recruitment of the mTORC1 complex to lysosomes. {ECO:0000250|UniProtKB:Q9UBE8}. | Canis lupus familiaris (Dog) (Canis familiaris) |
E2QY99 | PALS1_CANLF | MTTSHMNGHVTEESDNEVKNVDLASPEEHQKHREMAVDCPGDLGTRMMPVRRSAQLERIRQQQEDMRRRREEEGKKQELDLNSSMRLKKLAQIPPKTGIDNPIFDTEEGIVLESPHYAVKILEVEDLFSSLKHIQHTLVDSQSQEDISLLLQLVQNKDFQNAFKIHNAVTVHMNKASPPFPLISNAQDLAQEVQTVLKPVHHKEGQELTALLSAPHVQALLLAHDKVAEQEMQLEPFTDERVYESIGQYGGETVKIVRIEKARDIPLGATVRNEMDSVIISRIVKGGAAEKSGLLHEGDEVLEINGIEIRGKDVNEVFDLLSDMHGTLTFVLIPSQQIKPPPAKETVIHVKAHFDYDPSDDPYVPCRELGLSFQKGDILHIISQEDPNWWQAYREGDEDNQPLAGLVPGKSFQQQREAMKQTIEEDKEPEKSGKLWCAKKNKKKRKKVLYNANKNDDYDNEEILTYEEMSLYHQPANRKRPIILIGPQNCGQNELRQRLMNKEKDRFASAVPHTTRSRRDHEVAGRDYHFVSRQAFEADIAAGKFIEHGEFEKNLYGTSIDSVRQVINSGKICLLSLRTQSLKTLRNSDLKPYIIFIAPPSQERLRALLAKEGKNPKPEELREIIEKTREMEQNNGHYFDTAIVNSDLDKAYQELLRLINKLDTEPQWVPSSWLR | null | null | central nervous system neuron development [GO:0021954]; cerebral cortex development [GO:0021987]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; establishment or maintenance of polarity of embryonic epithelium [GO:0016332]; generation of neurons [GO:0048699]; morphogenesis of an epithelial sheet [GO:0002011]; protein localization to plasma membrane [GO:0072659]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015] | adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; axon [GO:0030424]; bicellular tight junction [GO:0005923]; Golgi apparatus [GO:0005794]; perikaryon [GO:0043204]; plasma membrane [GO:0005886] | ATP binding [GO:0005524] | PF00625;PF02828;PF09060;PF00595;PF07653; | 2.30.42.10;1.10.287.650;3.40.50.300;2.30.30.40; | MAGUK family | null | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q8N3R9}. Cell membrane {ECO:0000250|UniProtKB:Q9JLB2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JLB2}. Endomembrane system {ECO:0000250|UniProtKB:Q9JLB2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JLB2}. Cell junction, tight junction {ECO:0000269|PubMed:17182851}. Cell junction, adherens junction {ECO:0000269|PubMed:17182851}. Cell projection, axon {ECO:0000250|UniProtKB:Q9JLB2}. Perikaryon {ECO:0000250|UniProtKB:Q9JLB2}. Apical cell membrane {ECO:0000250|UniProtKB:Q8N3R9}. Note=Localized to the tight junctions of epithelial cells (By similarity). Localized to the Golgi apparatus in T lymphocytes (By similarity). Localized to a subset of intracellular vesicles (By similarity). Localized to the Purkinje cell body and axon (By similarity). Localized to intercellular junctions in vascular endothelial cells (By similarity). Localized to Schmidt-Lanterman incisures, the adaxonal domain, and the inner part of paranodal loops in myelinating Schwann cells of the sciatic nerve (By similarity). Localized to apical membrane domains of the outer limiting membrane (OLM) junctions in the retina (By similarity). Colocalizes with CRB1 at the OLM, apical to the adherens junction (By similarity). Colocalizes with MPP1 in the retina at the OLM (By similarity). Colocalizes with MPP3 to the subapical region of adherens junctions in the retina OLM (By similarity). {ECO:0000250|UniProtKB:Q8N3R9, ECO:0000250|UniProtKB:Q9JLB2}. | null | null | null | null | null | FUNCTION: Plays a role in tight junction biogenesis and in the establishment of cell polarity in epithelial cells (PubMed:17182851). Also involved in adherens junction biogenesis by ensuring correct localization of the exocyst complex protein EXOC4/SEC8 which allows trafficking of adherens junction structural component CDH1 to the cell surface (PubMed:17182851). Plays a role through its interaction with CDH5 in vascular lumen formation and endothelial membrane polarity (By similarity). Required during embryonic and postnatal retinal development (By similarity). Required for the maintenance of cerebellar progenitor cells in an undifferentiated proliferative state, preventing premature differentiation, and is required for cerebellar histogenesis, fissure formation, cerebellar layer organization and cortical development (By similarity). Plays a role in neuronal progenitor cell survival, potentially via promotion of mTOR signaling (By similarity). Plays a role in the radial and longitudinal extension of the myelin sheath in Schwann cells (By similarity). May modulate SC6A1/GAT1-mediated GABA uptake by stabilizing the transporter (By similarity). May play a role in the T-cell receptor-mediated activation of NF-kappa-B (By similarity). Required for localization of EZR to the apical membrane of parietal cells and may play a role in the dynamic remodeling of the apical cytoskeleton (By similarity). Required for the normal polarized localization of the vesicular marker STX4 (By similarity). Required for the correct trafficking of the myelin proteins PMP22 and MAG (By similarity). Involved in promoting phosphorylation and cytoplasmic retention of transcriptional coactivators YAP1 and WWTR1/TAZ which leads to suppression of TGFB1-dependent transcription of target genes such as CCN2/CTGF, SERPINE1/PAI1, SNAI1/SNAIL1 and SMAD7 (By similarity). {ECO:0000250|UniProtKB:B4F7E7, ECO:0000250|UniProtKB:Q8N3R9, ECO:0000250|UniProtKB:Q9JLB2, ECO:0000269|PubMed:17182851}. | Canis lupus familiaris (Dog) (Canis familiaris) |
E2QYC9 | INADL_CANLF | MPENPAPDKLQVLQVLDRLKMKLQEKGDTSQNEKLSLFYETLQSPLFNQILTLQQSIKQLKGQLSHIPSDCSTNFDFSRKGLLVFTDSAITNGNAQRPSNNLTVSGLFPWTPKSGNEDFNSVIQQMAQGRQIEYIDIERPSTGGLGFSVVALRSQNLGEVDIFVKEVQPGSIADRDQRLRENDQILAINHTPLDQNISHQQAIALLQQTTGSLHLVVAREPVHTKSRTSINLTDTTMPETVHWGHIEDVELINDGSGLGFGIVGGKSSGVVVRTIVPGGLADRDGRLQTGDHILKIGDTDVQGMTSEQVAQVLRNCGNSVRMLVARDPVGETSVTPPTPAALPVALPAVANRSPSTDSSLYETYGVELIKKDGQSLGIRIVGYIGTAHTGEASGIYVKSIIPGSAAYHNGQIQVNDKIVAVDGVNIQGFTNQDVVEVLRNAGQVVHLTLVRRKMCSSTSPLERSSDRGTVVEPSGTPARYVTGAVETETNLDGGDEETEERMDNLKNDNIQALEKLERVPDSPENELKSRWENLLGPDYEVMVATLDTQIADDAELQKYSKLLPIHTLRLGMEVDSFDGHHYISSIAPGGPVDALNLLQPEDELLEVNGVQLYGKSRREAVSFLKEVPPPFTLVCCRRLFDDEASVDEPRTTETLLPEMEADHNVDINTEEEEEEELALWSPEVKIVELVKDHKGLGFSILDYQDPLDPTRSVIVIRSLVANGVAEKGGELLPGDRLVSVNEYCLENTTLAEAVEVLKAVPPGIVHLGVCKPLVDNDKEEESHYILHSNNNEDETELSETIHDINSSLILEAPKGFRDEPYYKEELVDEPFLDLGKAFQSQQKEIDNSKEAWEMQEFLPPRLQEMGEEREMLVDEECDLYQDHFQSMDLYPSSHLQEAAPVSSVKELHFGTQWLHDSEPPELQEARSMMNMYSQETQQYGYSTENMIKENFGIDSLPSISSSEGNSQQGRFDDLENLNSLTKSSLDLGMMIPNDVQGPGMLVELPAVAQRREQEDLPLYQLPRTRVVSKASAYTGASSSRYTAGACELPEREEGEGEETPNFSHWGPPRIVEIFREPNVSLGISIVGGQTVIKRLKNGEELKGIFIKQVLEDSPAGKTNALKTGDKILEVSGVDLQNASHREAVEAIKNAGNPVVFVVQSLSSTPRVIPSVHNKANKIANNQDQNTEEKKEKRQGTPPPPMKLPPPYKAPSDDSDENEEEYAFTNKKIRQRYADLPGELHIIELEKDKNGLGLSLAGNKDRSRMSIFVVGINPEGPAATDGRMRIGDELLEINNQILYGRSHQNASAVIKTAPSKVKLVFIRNEDAVNQMAVAPFPVPSSSPSSLEDQSGTEPVSSEEDGSLEVGIKQLPENESSKLEDISQVAGQGMVAGQQKALDCPTDNAVSQMKPQKYSTKVSFSSQEIPLAPAPSYHSTDVDFTSYGGFQAPLSVDPATCPIVPGQEMIIEISKGRSGLGLSIVGGRDTPLDAIVIHEVYEEGAAARDGRLWAGDQILEVNGIDLRSASHEEAITALRQTPQKVRLVVYRDEAHYRDEENLEIFPVDLQKKAGRGLGLSIVGKRNGSGVFISDIVKGGAADLDRRLIQGDQILSVNGEDMRNASQETVATVLKCAQGLVQLEIGRLRAGSWTSSRKTSQNSQGSQHSTHSSFHPSLAPVITSLQNLVGTKRATDPSLKSSGMDMGPRTVEIIRELSDALGISIAGGKGSPLGDIPIFIAMIQASGVAARTQKLKVGDRIVSINGQPLDGLSHADVVNLLKNAYGRIILQVVADTNISAIATQLENMSTGYHLGSPTAEHHPEDTEEPLQMTAG | null | null | establishment of apical/basal cell polarity [GO:0035089]; microtubule organizing center organization [GO:0031023]; positive regulation of epithelial cell migration [GO:0010634]; regulation of microtubule cytoskeleton organization [GO:0070507]; regulation of protein localization [GO:0032880]; tight junction assembly [GO:0120192] | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; tight junction [GO:0070160] | null | PF09045;PF00595; | 1.20.1440.360;2.30.42.10; | null | null | SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:12527193, ECO:0000269|PubMed:12771187, ECO:0000269|PubMed:15738264}. Apical cell membrane {ECO:0000269|PubMed:15738264}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NI35}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63ZW7}. Note=Localizes to the apical region at the start of epithelial cell polarization then locates to tight junctions as polarization is completed (PubMed:15738264). Localized in the paranodal region of myelinating Schwann cells (By similarity). Localized to the leading edge of the actin cortex of migrating epithelia cells (PubMed:17235357). {ECO:0000250|UniProtKB:Q63ZW7, ECO:0000269|PubMed:15738264, ECO:0000269|PubMed:17235357}. | null | null | null | null | null | FUNCTION: Scaffolding protein that facilitates the localization of proteins to the cell membrane (PubMed:17235357). Required for the correct formation of tight junctions and epithelial apico-basal polarity (PubMed:15738264). Positively regulates epithelial cell microtubule elongation and cell migration, possibly via facilitating localization of PRKCI/aPKC and PAR3D/PAR3 at the leading edge of migrating cells (PubMed:17235357). Plays a role in the correct reorientation of the microtubule-organizing center during epithelial migration (PubMed:17235357). May regulate the surface expression and/or function of ASIC3 in sensory neurons (By similarity). May recruit ARHGEF18 to apical cell-cell boundaries (By similarity). {ECO:0000250|UniProtKB:Q63ZW7, ECO:0000250|UniProtKB:Q8NI35, ECO:0000269|PubMed:15738264, ECO:0000269|PubMed:17235357}. | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RAK7 | APOA2_CANLF | MKLLAVTVLLLVICSLEGAFVRRQAEEPNLQSLVSQYFQTVTDYGKDLMEKAKGPELQAQAKAYFEKTQEQLTPLVKKAGTDLLNFLSNFMDLKTQPATQ | null | null | cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle remodeling [GO:0034375]; lipoprotein metabolic process [GO:0042157]; low-density lipoprotein particle remodeling [GO:0034374]; positive regulation of phagocytosis [GO:0050766]; protein stabilization [GO:0050821]; triglyceride-rich lipoprotein particle remodeling [GO:0034370] | blood microparticle [GO:0072562]; chylomicron [GO:0042627]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361] | apolipoprotein receptor binding [GO:0034190]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; high-density lipoprotein particle binding [GO:0008035]; high-density lipoprotein particle receptor binding [GO:0070653]; lipase inhibitor activity [GO:0055102]; phosphatidylcholine binding [GO:0031210] | PF04711; | 6.10.250.100; | Apolipoprotein A2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02652}. | null | null | null | null | null | FUNCTION: May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism. | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RD63 | PLD6_CANLF | MERFRWQVAAVAAVGLALALEALPSVLCWLRAGRRQQQRPPRRQVLFFPSQVTCTEALLQAPGEAPSGPPAGCRCSLPHGESSLSRLLRALLAARASLELCLFAFSSPQLGRAVQLLHQRGVRVRVITDCDYMALNGSQIGLLRKAGIQVRHDQDLGYMHHKFAIVDKKVLITGSLNWTTQAIQNNRENVLIMEDEEYVRLFLEEFERIWEEFNPTKYTFFPQKKTGTSLPPQVSCFGQLVSCHSKCSHHLSQV | 3.1.4.- | null | lipid catabolic process [GO:0016042]; meiotic cell cycle [GO:0051321]; mitochondrial fusion [GO:0008053]; P granule organization [GO:0030719]; piRNA processing [GO:0034587]; spermatid development [GO:0007286] | Golgi apparatus [GO:0005794]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886] | cardiolipin hydrolase activity [GO:0035755]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; RNA endonuclease activity, producing 5'-phosphomonoesters [GO:0016891] | PF13091; | 3.30.870.10; | Phospholipase D family, MitoPLD/Zucchini subfamily | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q5SWZ9}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q5SWZ9}. Nucleus membrane {ECO:0000250|UniProtKB:Q5SWZ9}. Cell membrane {ECO:0000250|UniProtKB:Q5SWZ9}. Golgi apparatus {ECO:0000250|UniProtKB:Q5SWZ9}. Note=Localization in the mitochondrial outer membrane is found in different cell types where phospholipase was the predominant activity, however, in pachytene spermatocytes and spermatids of mouse testes where nuclease activity is predominant, localization is restricted to the Golgi, suggesting this enzyme is localized in different subcellular compartments depending on the role (phospholipase or nuclease) it needs to play in each cell type and developmental stage. {ECO:0000250|UniProtKB:Q5SWZ9}. | CATALYTIC ACTIVITY: Reaction=a cardiolipin + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a 1,2-diacyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:44884, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58608, ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; Evidence={ECO:0000250|UniProtKB:Q8N2A8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44885; Evidence={ECO:0000250|UniProtKB:Q8N2A8}; | null | null | null | null | FUNCTION: Presents phospholipase and nuclease activities, depending on the different physiological conditions. Interaction with Mitoguardin (MIGA1 or MIGA2) affects the dimer conformation, facilitating the lipase activity over the nuclease activity. Plays a key role in mitochondrial fusion and fission via its phospholipase activity. In its phospholipase role, it uses the mitochondrial lipid cardiolipin as substrate to generate phosphatidate (PA or 1,2-diacyl-sn-glycero-3-phosphate), a second messenger signaling lipid. Production of PA facilitates Mitofusin-mediated fusion, whereas the cleavage of PA by the Lipin family of phosphatases produces diacylgycerol (DAG) which promotes mitochondrial fission. Both Lipin and DAG regulate mitochondrial dynamics and membrane fusion/fission, important processes for adapting mitochondrial metabolism to changes in cell physiology. Mitochondrial fusion enables cells to cope with the increased nucleotide demand during DNA synthesis (By similarity). Mitochondrial function and dynamics are closely associated with biological processes such as cell growth, proliferation, and differentiation. Mediator of MYC activity, promotes mitochondrial fusion and activates AMPK which in turn inhibits YAP/TAZ, thereby inducing cell growth and proliferation. The endonuclease activity plays a critical role in PIWI-interacting RNA (piRNA) biogenesis during spermatogenesis. Implicated in spermatogenesis and sperm fertility in testicular germ cells, its single strand-specific nuclease activity is critical for the biogenesis/maturation of PIWI-interacting RNA (piRNA). MOV10L1 selectively binds to piRNA precursors and funnels them to the endonuclease that catalyzes the first cleavage step of piRNA processing to generate piRNA intermediate fragments that are subsequently loaded to Piwi proteins. Cleaves either DNA or RNA substrates with similar affinity, producing a 5' phosphate end, in this way it participates in the processing of primary piRNA transcripts. piRNAs provide essential protection against the activity of mobile genetic elements. piRNA-mediated transposon silencing is thus critical for maintaining genome stability, in particular in germline cells when transposons are mobilized as a consequence of wide-spread genomic demethylation. PA may act as signaling molecule in the recognition/transport of the precursor RNAs of primary piRNAs. Interacts with tesmin in testes, suggesting a role in spermatogenesis via association with its interacting partner (By similarity). {ECO:0000250|UniProtKB:Q5SWZ9, ECO:0000250|UniProtKB:Q8N2A8}. | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RDM9 | TSPO2_CANLF | MQPQGAIFVALPHLGPILVSLLTRHRMIRWYDIPKKPPWCPPHKVLLAGWITIYFVMGYASYLVWKDLGGGFGRPLALPLGLYAVQLAVSWAVLIFFFAAHAHGLALLHMLLLYGLVVSTALIWHPINKLAAVLLLPYLAWLTVTASIAYHLWRDSLCPNHHQPLPMGEKRD | null | null | 5-aminolevulinic acid import across plasma membrane [GO:0140484]; enucleate erythrocyte differentiation [GO:0043353]; import across plasma membrane [GO:0098739]; intracellular cholesterol transport [GO:0032367]; lipid droplet organization [GO:0034389] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; mitochondrial outer membrane [GO:0005741]; plasma membrane [GO:0005886] | 5-aminolevulinic acid transmembrane transporter activity [GO:0140485]; cholesterol binding [GO:0015485] | PF03073; | 1.20.1260.100; | TspO/BZRP family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5TGU0}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:32358067}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the plasma membrane and intracellular membranes in developing and mature erythrocytes. {ECO:0000250|UniProtKB:Q5TGU0}. | null | null | null | null | null | FUNCTION: Cholesterol-binding protein involved in the redistribution of cholesterol from lipid droplets to the endoplasmic reticulum (PubMed:32358067). Required to meet cholesterol demands during erythropoietic differentiation (PubMed:32358067). May play a role in transport processes at the plasma membrane of erythrocytes, including regulating VDAC-mediated ATP export, and import of the heme precursors protoporphyrin IX and 5-aminolevulinic acid (By similarity). {ECO:0000250|UniProtKB:Q5TGU0, ECO:0000269|PubMed:32358067}. | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RDP2 | ATG4D_CANLF | MNSVSPAAAQYRSGSPEDARRPEGRRPRGPRVPDPNGPRPSGASGPALGSPAAAPGEPDEVDKFKAKFLTAWNNVKYGWAVKSRTSFSKISSVHLCGRRYRFEGEGDIQRFQRDFVSRLWLTYRRDFPPLAGGCLTSDCGWGCMLRSGQMMLAQGLLLHFLPRDWTWAEGPGLGPSEPAGLASPNRYRGPARWMPPRWAQGTPELEQERRHRQIVSWFADHPQAPFGLHRLVELGQSSGKKAGDWYGPSLVAHILRKAVESCSEITRLVVYVSQDCTVYKADVARLVARPDPTAEWKSVVILVPVRLGGETLNPVYVPCVKELLRSELCLGIMGGKPRHSLYFIGYQDDFLLYLDPHYCQPTVDVSQADFPLESFHCTSPRKMAFAKMDPSCTVGFYAGDQKEFETLCSELTRVLSSSSATERYPMFTLAEGHAQDHSLDDLCSQLSQPTLRLPRTGRLLKAKRPSSEDFVFL | 3.4.22.- | null | aggrephagy [GO:0035973]; apoptotic process [GO:0006915]; autophagosome assembly [GO:0000045]; mitophagy [GO:0000423]; piecemeal microautophagy of the nucleus [GO:0034727]; protein processing [GO:0016485]; protein transport [GO:0015031] | cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759] | cysteine-type endopeptidase activity [GO:0004197]; protein-phosphatidylethanolamide deconjugating activity [GO:0019786] | PF03416; | null | Peptidase C54 family | PTM: Cleaved by CASP3 during apoptosis which leads to increased activity. The cleavage by CASP3 reveals a cryptic mitochondrial targeting sequence immediately downstream of their canonical caspase cleavage sites which leads to mitochondrial import of the protein. {ECO:0000250|UniProtKB:Q86TL0}. | SUBCELLULAR LOCATION: [Cysteine protease ATG4D]: Cytoplasm {ECO:0000250|UniProtKB:Q86TL0}.; SUBCELLULAR LOCATION: [Cysteine protease ATG4D, mitochondrial]: Cytoplasm {ECO:0000250|UniProtKB:Q86TL0}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q86TL0}. Note=Imported into mitochondrial matrix after cleavage by CASP3 during oxidative stress and cell death. {ECO:0000250|UniProtKB:Q86TL0}. | CATALYTIC ACTIVITY: Reaction=[protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:67548, Rhea:RHEA-COMP:17323, Rhea:RHEA-COMP:17324, ChEBI:CHEBI:15377, ChEBI:CHEBI:64612, ChEBI:CHEBI:172940, ChEBI:CHEBI:172941; Evidence={ECO:0000250|UniProtKB:Q86TL0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67549; Evidence={ECO:0000250|UniProtKB:Q86TL0}; CATALYTIC ACTIVITY: Reaction=[protein]-C-terminal L-amino acid-glycyl-phosphatidylserine + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:67576, Rhea:RHEA-COMP:17324, Rhea:RHEA-COMP:17326, ChEBI:CHEBI:15377, ChEBI:CHEBI:57262, ChEBI:CHEBI:172940, ChEBI:CHEBI:172942; Evidence={ECO:0000250|UniProtKB:Q86TL0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67577; Evidence={ECO:0000250|UniProtKB:Q86TL0}; | null | null | null | null | FUNCTION: [Cysteine protease ATG4D]: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine (By similarity). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (By similarity). In addition to the protease activity, also mediates delipidation of ATG8 family proteins. Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy. Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (By similarity). ATG4D plays a role in the autophagy-mediated neuronal homeostasis in the central nervous system (PubMed:25875846). Compared to other members of the family (ATG4A, ATG4B or ATG4C), constitutes the major protein for the delipidation activity, while it promotes weak proteolytic activation of ATG8 proteins (By similarity). Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins: acts by regulating ATG9A trafficking to mitochondria and promoting phagophore-endoplasmic reticulum contacts during the lipid transfer phase of mitophagy (By similarity). {ECO:0000250|UniProtKB:Q86TL0, ECO:0000250|UniProtKB:Q8BGV9, ECO:0000250|UniProtKB:Q9Y4P1, ECO:0000269|PubMed:25875846}.; FUNCTION: [Cysteine protease ATG4D, mitochondrial]: Plays a role as an autophagy regulator that links mitochondrial dysfunction with apoptosis. The mitochondrial import of ATG4D during cellular stress and differentiation may play important roles in the regulation of mitochondrial physiology, ROS, mitophagy and cell viability. {ECO:0000250|UniProtKB:Q86TL0}. | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RE76 | APOA4_CANLF | MFLKAVVLTLSLVAITGARAEVSADQVATVVWDYFSQLSNNAKEAVEHLQQSELTQQLKSVTKGHISALRVIEKGRERNSWEHSRRVGPCEIMGRQVGIFGQPLRVATLPNCDLPVNSVPPNTHLSQAVGPYAEELRTQVNTHAEQLRNQLTSHAQRMQSALRQNVDDLHSSLTPFADELKAKIDQNVEELKGHLTPYTDELKVKIDQNVEELRRSLAPYAQDVQEKLNHQLEGLAFQMKKNAEELKAKISANAEELRQRLAPVAEDVRGKLKDNTAGLHKSLAELSSRLDQQVEEFRRNVGPYGETFNKALLQQVEELRQKLGPYAGDMEDHLSFLEKDLRDKVNSFFSTLQEKESQDTPVALPKQEQEQSAVPLES | null | null | acylglycerol homeostasis [GO:0055090]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; lipoprotein metabolic process [GO:0042157]; phosphatidylcholine metabolic process [GO:0046470]; phospholipid efflux [GO:0033700]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of triglyceride catabolic process [GO:0010898]; regulation of intestinal cholesterol absorption [GO:0030300]; reverse cholesterol transport [GO:0043691]; triglyceride homeostasis [GO:0070328]; very-low-density lipoprotein particle remodeling [GO:0034372] | blood microparticle [GO:0072562]; chylomicron [GO:0042627]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; very-low-density lipoprotein particle [GO:0034361] | cholesterol transfer activity [GO:0120020]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543] | PF01442; | 6.10.250.2890;1.20.120.20; | Apolipoprotein A1/A4/E family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P06727}. | null | null | null | null | null | FUNCTION: May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons. {ECO:0000250|UniProtKB:P06727}. | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RG47 | STT3B_CANLF | MAEPSAPESKHKSSLNSSPWSGLMALGNSRHGHHGPGAQCAHKAAGGVAPPKPAPAGLSGGLSQPAGWQSLLSFTILFLAWLAGFSSRLFAVIRFESIIHEFDPWFNYRSTHHLASHGFYEFLNWFDERAWYPLGRIVGGTVYPGLMITAGLIHWILNTLNITVHIRDVCVFLAPTFSGLTSISTFLLTRELWNQGAGLLAACFIAIVPGYISRSVAGSFDNEGIAIFALQFTYYLWVKSVKTGSVFWTMCCCLSYFYMVSAWGGYVFIINLIPLHVFVLLLMQRYSKRVYIAYSTFYIVGLILSMQIPFVGFQPIRTSEHMAAAGVFALLQAYAFLQYLRDRLTKQEFQTLFFLGVSLAAGAVFLSVIYLTYTGYIAPWSGRFYSLWDTGYAKIHIPIIASVSEHQPTTWVSFFFDLHILVCTFPAGLWFCIKNINDERVFVALYAISAVYFAGVMVRLMLTLTPVVCMLSAIAFSNVFEHYLGDDMKRENPPVEDSSDEDDKRNPGNLYDKAGKVRKHVTEQEKTEEGLGPNIKSIVTMLMLMLLMMFAVHCTWVTSNAYSSPSVVLASYNHDGTRNILDDFREAYFWLRQNTDEHARVMSWWDYGYQIAGMANRTTLVDNNTWNNSHIALVGKAMSSNESAAYKIMRSLDVDYVLVIFGGVIGYSGDDINKFLWMVRIAEGEHPKDIRESDYFTPQGEFRVDKAGSPTLLNCLMYKMSYYRFGEMQLDFRTPPGFDRTRNAEIGNKDIKFKHLEEAFTSEHWLVRIYKVKAPDNRETLDHKPRVTNIFPKQKYLSKKTTKRKRGYIKNKLVFKKGKKISKKTV | 2.4.99.18 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8TCJ2}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:B9KDD4}; | post-translational protein modification [GO:0043687]; protein N-linked glycosylation via asparagine [GO:0018279] | oligosaccharyltransferase I complex [GO:0034998]; oligosaccharyltransferase II complex [GO:0034999] | dolichyl-diphosphooligosaccharide-protein glycotransferase activity [GO:0004579]; metal ion binding [GO:0046872] | PF02516;PF21436; | 3.40.50.12610; | STT3 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:12887896}. Endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P39007}. | CATALYTIC ACTIVITY: Reaction=a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein] = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-asparaginy-[protein]; Xref=Rhea:RHEA:22980, Rhea:RHEA-COMP:9529, Rhea:RHEA-COMP:12635, Rhea:RHEA-COMP:12804, Rhea:RHEA-COMP:12805, ChEBI:CHEBI:15378, ChEBI:CHEBI:50347, ChEBI:CHEBI:57497, ChEBI:CHEBI:57570, ChEBI:CHEBI:132529; EC=2.4.99.18; Evidence={ECO:0000250|UniProtKB:P39007}; | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q8TCJ2}. | null | null | FUNCTION: Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (By similarity). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (By similarity). STT3B is present in a small subset of OST complexes and mediates both cotranslational and post-translational N-glycosylation of target proteins: STT3B-containing complexes are required for efficient post-translational glycosylation and while they are less competent than STT3A-containing complexes for cotranslational glycosylation, they have the ability to mediate glycosylation of some nascent sites that are not accessible for STT3A. STT3B-containing complexes also act post-translationally and mediate modification of skipped glycosylation sites in unfolded proteins. Plays a role in ER-associated degradation (ERAD) pathway that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins by mediating N-glycosylation of unfolded proteins, which are then recognized by the ERAD pathway and targeted for degradation (PubMed:12887896). {ECO:0000250|UniProtKB:P39007, ECO:0000250|UniProtKB:Q8TCJ2, ECO:0000269|PubMed:12887896}. | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RH47 | RS3_CANLF | MAVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQGVLGIKVKIMLPWDPSGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA | 4.2.99.18 | null | apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell division [GO:0051301]; DNA repair [GO:0006281]; positive regulation of apoptotic signaling pathway [GO:2001235]; regulation of translation [GO:0006417]; translation [GO:0006412] | cytosolic small ribosomal subunit [GO:0022627]; mitochondrial inner membrane [GO:0005743]; nucleolus [GO:0005730]; nucleus [GO:0005634]; spindle [GO:0005819] | class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; DNA binding [GO:0003677]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF07650;PF00189; | 3.30.300.20;3.30.1140.32; | Universal ribosomal protein uS3 family | PTM: Methylation by PRMT1 is required for import into the nucleolus and for ribosome assembly. {ECO:0000250|UniProtKB:P23396}.; PTM: Sumoylation by SUMO1 enhances protein stability through increased resistance to proteolysis. Sumoylation occurs at one or more of the three consensus sites, Lys-18, Lys-214 and Lys-230. {ECO:0000250|UniProtKB:P23396}.; PTM: Phosphorylation at Thr-221 by CDK1 occurs mainly in G2/M phase. Phosphorylation by PRKCD occurs on a non-ribosomal-associated form which results in translocation of RPS3 to the nucleus and enhances its endonuclease activity. Phosphorylated on Ser-209 by IKKB in response to activation of the NF-kappa-B p65-p50 complex which enhances the association of RPS3 with importin-alpha and mediates the nuclear translocation of RPS3. Phosphorylation by MAPK is required for translocation to the nucleus following exposure of cells to DNA damaging agents such as hydrogen peroxide. Phosphorylation by PKB/AKT mediates RPS3 nuclear translocation, enhances RPS3 endonuclease activity and suppresses RPS3-induced neuronal apoptosis. {ECO:0000250|UniProtKB:P23396}.; PTM: Ubiquitinated; ubiquitination is prevented by interaction with HSP90 which stabilizes the protein. Monoubiquitinated at Lys-214 by RNF10 and ZNF598 when a ribosome has stalled during translation of poly(A) sequences, leading to preclude synthesis of a long poly-lysine tail and initiate the ribosome quality control (RQC) pathway to degrade the potentially detrimental aberrant nascent polypeptide. Deubiquitinated at Lys-214 by USP10, preventing degradation by the proteasome and promoting 40S ribosome subunit recycling following ribosome dissociation. {ECO:0000250|UniProtKB:P23396}.; PTM: Ufmylated by UFL1. {ECO:0000250|UniProtKB:P62908}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23396}. Nucleus {ECO:0000250|UniProtKB:P23396}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P23396}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P23396}; Peripheral membrane protein {ECO:0000250|UniProtKB:P23396}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P23396}. Note=In normal cells, located mainly in the cytoplasm with small amounts in the nucleus but translocates to the nucleus in cells undergoing apoptosis. Nuclear translocation is induced by DNA damaging agents such as hydrogen peroxide. Accumulates in the mitochondrion in response to increased ROS levels. Localizes to the spindle during mitosis. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P23396, ECO:0000250|UniProtKB:P62908}. | CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000250|UniProtKB:P23396}; | null | null | null | null | FUNCTION: Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Has endonuclease activity and plays a role in repair of damaged DNA. Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA. Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS). Has also been shown to bind with similar affinity to intact and damaged DNA. Stimulates the N-glycosylase activity of the base excision protein OGG1. Enhances the uracil excision activity of UNG1. Also stimulates the cleavage of the phosphodiester backbone by APEX1. When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage. Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide. Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes. Represses its own translation by binding to its cognate mRNA. Binds to and protects TP53/p53 from MDM2-mediated ubiquitination. Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization. Involved in induction of apoptosis through its role in activation of CASP8. Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5. Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation. {ECO:0000250|UniProtKB:P23396}. | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RK30 | PKHD1_CANLF | MIVWLISLMSIEILLLAGPALSFHIEPKEGSLAGGTWITVIFDGLELEQLYPTNGSQLEIHLVNVAVPALPSIPCDVSPVFLDLPVVMCRTRSLLPEVHEGLYYLEAHAGGQVVGSPSPGLQDCCTFKFSREQTPIVYQVTPPSGVPGKMIHVYGWIITGRSETFDFDAEYIDSPLILEAQGDKWVTACSLINRQTGSCYPLQENHGLGTLQCRVEGNYIGSQNVSFSVFNKGKSMVHKNAWLVSAKLDLFLYQTYSEILSVFPETGSLGGKTDIIITGDFFDNPALVTIAGVPCDIRHMSPRKIECTTRAPGKRARLTAPQAGNRGLLFEVGEAVEGLDLTVATPGYRWQIVPNASSPFGFWFKEGQPFRARLSGFFVAPETNNYTFWIQADNQASLYFSQSEDPRMKVKVASIRVGTADWFDAWEQDRNEGVWQRKTPKLELVGGTRYYLEAEHYGRTPSRGMRIGVQIHNTWLNPDVVSTYLREKHQIRVRAQRLPEIQMLTVSGRGSFFLTWDNVTSQPIPENATAHQIQTAIEELLAVKCKLEPLSANILLWLGFEQGPEGSSFEGDLTSGTEPFCGRFSLHQPRRLVLTPPAAQKDYWLDRYTHLCIAYKGRMKNILKVTVFFTTDFQNFIKKNITCDWNLVGTRPNSWQFTCTDLWETCVHHSMYLQPPLVDSPVLVHRIDLFPLSQETSGFYVDEIIIADTNITVSQADSETAHPGGNLVESLCVVGSPPVYNISFWLVGCGQELPLITASIVPTGGEARRSGLVQVTTQRIQKTSPPLGGYFHIQLPTSVIPDVPVHISASHLRKLLQNNADNFTSRYLNSSDLTVMEDLKSCYEHEWTLSWSSQVGDLPNFIRVSDANLTGVNPAATVRVVYDGGVFLGPVFGDMLVTANQHTQVVVRVNDIPAHCSGSCSFQYLEGSTPQIHSAWYSLDGDISLLIYIFGINFSGDPQALEIMVNKTNCKVIFSNQTNVICQTDLLPVGMHRLFMVVRPFGRAINTSGEALFLSVEPRLDAVEPSRAAEIGGLWATIQGSGLEDVSLVLFGSQSCAINITTSNSRRIQCRVPPRGKDGPVVNLTVVSGDHSAVLPMAFTYVSSLNPVITSLSRNRSNIAGGDTLFIRMALLVNYTDLDVEVCIQNTLAPAHVQMPQGLEVVLPPLPAGLYSISVSINGISIRSPGVDLHIQYITEVFSIEPCCGSLLGGTILSISGIGFIRDPTLVWVFVGNRSCDILNSTETVIWCETPPAALLPDSNIPAIPVPMEIWAGNVSFARESLLNLSFTFLYEAAMTPVVTAMRGEIINNSLRFYVEGNNLSNSVILLGVSHCDLETQTLRNNVSLSGCSFPLHSLEAGFYPLQVRQKQMGFANMSAVPQQYVITPWIMAISPTHGSACGGTVLTVRGLALSSRKRSVQVDLLGPFTCVILSLGHQTILCQINKVNDSFPDVSFTLNVTVIVNGLPSECQGNCTLFLQEETTPIVDSLTTNISGSLTMVLIRGRKLGITAVEPMVFVDDHLPCIVTFFNASYVICWISDLTPGLHYVSVFHARNGYACFGNVSRHFYILPQVFHYFPKNFSIHGGSLLTVEGTALRGKNSTLVYVGQQACLTVSISTELIQCIVPAGNGSVGLVIEVDGLSYQMGVIGYSSAFTPRLLSISQTDDVLTFAVAQVSGAENVDIFIGMSPCVGISGNHTVLQCVVSSLPAGEYPVRGYDRMRGWASSVLVFTSTATISGVTENFGCLGGRLVHVFGAGFSPGNVSAAVCGAPCQVLANATVSAFSCLVLPLNVSLAFLCGLKHSEESCEASSSTYVQCDLTVTVGTETLPQSWPYLYICEESPQCLFAPDHWTESTFPWFSGLFISPKVERDEVLIYNSSCNIAMETEAKMECETPNQPITAKITEIRKSRGQSTQGNFSLQFCLRWSRTHSWFPERVPQDGDNVTVENGQLLLLDTNTSILNLLHIKGGKLIFMDPGPIELRAHAILISDGGELRIGSEDKPFQGKAEIKLYGSSHSTPFFPYGVKFLAVRNGTLSLHGLLPEVTFTHLQAAAYAGDTVLALEDAVDWHPGDEAVIISRIGVGGAKPMEEIVIVEAVHNTDLYLRSPLRYSHNFTENWVAGVLHILKVTVVLLSRSITIQGNLTAERMKHLASCQEASDSEGNLQDCLYSKSEKMLGSRDLGARVIVQSFPEEPSRVQLRGVQFRDLGQAFRKHVSALTLVGAMRDSYVQGCTVWSSFNRGLSMSMTLGLKVDSNIFYNILGHALLVGTDMDIKYISWEAAPEKKPDWSEQGNIIRNNVIISISGTEGLSSPEMLTPSGIYILNPTNVVEGNRVYVAGLGYFFHLVTSQTSQAPLLSFTQNIAHSCTRYGLFIYPQFQPPWDDGRGPTLFQNFTVWGSAGGARISRSSNLHLKNFQVYSCRDFGIDILESDANTSVTDSLLLGHFAHKGSLCMSAGIKTPKRWELIISNTTFVNFDLTDCVSIRTCSGCSRGQGGFTVKTNQLKFINSPNLVAFPFPHAAILEDLDGSLSGRNRSHILASMETLSASCLVNLSFSQIVPGSVCGEDVIFHHMSIGLANAPNVSYDLTITDSRNKTTTVNYVRDTLSNLYGWMALLLDQETYSLQFETPWISRSLQYSATFGSFAPGNYLLLVHTVLWPYPDILVRCGSQEGRSLPSLPLPGQDQGCDWFFNTQLRQLIYLVSGEGQVQVTLQVKEGVPPTISASTSAPESALKWSLPEAWTGIEEGWGGHNHTIPGPGDDILILPNRTVLVDTNLPFLKGLYVMGTLEFPVDRSNVLSVACMVIAGGELKVGTLDNPLEKEQKLLILLRASEGIFCDRLNGIHIDPGTIGVYGKVQLHGACPKKSWTRLAADIASGNERIIVEDAVDWRPHDKIVLSSSSYEPHEAEILTVKEVQAHHVKIYERLKYRHIGSVHVMEDGRCIRLAAEVGLLTRNIQIQPDISCRARLLVGSFRNSSSKEFSGVLQLSNVEIQNFGSPLYSSIEFTNASAGSWIISSSLHQSCSGGIRAAASHGIILNDNIVFGTVGHGIDLEGQNFSLSNNLVVLMTQSAWSTVWVAGIKANQAKDINLYGNVVAGSERIGFHIQGHRCSSPEARWSDNVAHSSLHGLHLYKENGLDNCTGISGFLAFKNFDYGAMLHVENSVEIENITLVDNSIGLLATVYVSSVPKSHIENVQIVLRNSVIIATSSSFDCIQDRVKPRSANLTSSDRAPSNPRGGRVGILWPIFTSEPNWWPQEPWHRVRNGHSTSGILKLQDVTFSNFVKSCYSDDLDICILPNVENTGIMHPIMAEGTRMLKIKDKNKFYFPPLQARKGLGILVCPESDCENPRKYLFKDLDGRALGLPPPVSVFPKTEAEWTGSFFNTGTFREEQKCTYRALIQGYICKQSDQAILILDNADATWAMQKLYPVVSVTRGFVDTFSSVNADAPCSTSGSASTFYSILPTREITKICFVDQTPQVLRFFLLGNRSTSKLLLAVFYHELQNPRVFIGESFIPPIMVQSTSSLLDESIGSNYFSILDNLLYVVLQGQEPIEIHSGVSIHLALTVMFSVLEKGWEIIILERLTDFLQVSQDQIRFIHEMPGNEATLKAIADNKAKRKRNCPTVTCASPYRVGQRRPLMTEMSSYRVPSPTIMETASKVIVIEIGDLPTIRSTRLISYLTSNKLQNLAHQIITAQQTGVLENVLNMTIGALLVTQPKGVTDYGNASSFKTGNFIYIRPYALSVLVQPSDGEVGKELTVQPRLVFLDKQNQRIESLGPPSEPWAISVSLEGTSDPVLKGCTQAESQDGYVSFSNLAVLISGSNWHFIFTVTSPPGANFTARSRSFTVLPAAPSEKSSIILAVSLCSVASWLALCCLVCCWFRKSKSRKIKSEDISEFKTNDQKSHIHMSSKHPRSQETKKEDTMMGEDMKIKVIMDKVNQLPHQSLNGVSRRKVSRRAVREEGSSREEDVVPAPRIISITSQGHTCVPGSPDQQIYLQEAGNWKEAQEQLVSYQLAGQDQRLLLCPDLRRERQQLQGQSQLGQEGGSVGLSQEKKASGGATQASCPHLVHPETIQEQL | null | null | branching morphogenesis of an epithelial tube [GO:0048754]; cell-cell junction organization [GO:0045216]; epithelial cell morphogenesis [GO:0003382]; establishment of centrosome localization [GO:0051660]; establishment of mitotic spindle orientation [GO:0000132]; negative regulation of epithelial cell apoptotic process [GO:1904036]; positive regulation of epithelial cell proliferation [GO:0050679]; regulation of cell adhesion [GO:0030155]; regulation of cell-cell adhesion [GO:0022407]; regulation of cell-matrix adhesion [GO:0001952]; regulation of cholangiocyte proliferation [GO:1904054]; regulation of establishment of planar polarity [GO:0090175] | apical plasma membrane [GO:0016324]; chromosome, centromeric region [GO:0000775]; cilium [GO:0005929]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; spindle [GO:0005819] | null | PF10162;PF01833; | 2.60.40.10;2.160.20.10; | null | PTM: Palmitoylated. Palmitoylation facilitates the trafficking to the cilia and membrane targeting. {ECO:0000250|UniProtKB:E9PZ36}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:E9PZ36}.; PTM: Several proteolytic cleavages occur within the extracellular domain, whereas at least one cleavage occurs within the cytoplasmic domain. Cleaved by a probable proprotein convertase which produces an extracellular domain (polyductin extracellular domain, (PECD)) and a C-terminal fragment (polyductin transmembrane fragment (PTM)) which are tethered together by disulfide bonds. This extracellular domain (PECD) is then shed from the primary cilium by activation of a member of the ADAM metalloproteinase disintegrins family, resulting in concomitant release of an intra-cellular C-terminal fragment (ICD) via a gamma-secretase-dependent process. The proteolytic cleavage of the C-terminal intracellular fragment (ICD) is controlled by cytosolic calcium concentration and activation of PKC. {ECO:0000250|UniProtKB:E9PZ36}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08F94}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P08F94}. Apical cell membrane {ECO:0000250|UniProtKB:E9PZ36}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:P08F94}. Cell projection, cilium {ECO:0000250|UniProtKB:E9PZ36}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P08F94}. Chromosome, centromere {ECO:0000250|UniProtKB:P08F94}. Nucleus {ECO:0000250|UniProtKB:E9PZ36}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:E9PZ36}. Secreted {ECO:0000250|UniProtKB:E9PZ36}. Endoplasmic reticulum {ECO:0000250|UniProtKB:E9PZ36}. Golgi apparatus {ECO:0000250|UniProtKB:E9PZ36}. Note=The intra-cellular C-terminal fragment (ICD) translocates to the nucleus and is not detected in primary cilia (By similarity). The extracellular domain (PECD) traffics beyond the mid-Golgi and localizes on exosome like vesicles (ELVs) attached to the primary cilium (By similarity). In the urine, the extracellular domain (PECD) exists as an highly abundant secreted form and a less abundant PECD form that is either tethered to or shed with the C-terminal fragment (PTM) in ELVs (By similarity). The majority of full length PKHD1 protein resides at the endoplasmic reticulum and cannot pass beyond the mid-Golgi apparatus and is not detected in primary cilia (By similarity). The intra-cellular C-terminal fragment of 21-kDa translocates to the nucleus. The extracellular domain traffics beyond the mid-Golgi and localizes on exosome like vesicles (ELVs) attached to the primary cilium (By similarity). {ECO:0000250|UniProtKB:E9PZ36}. | null | null | null | null | null | FUNCTION: Promotes ciliogenesis in renal epithelial cells and therefore participates in the tubules formation and/ or ensures the maintenance of the architecture of the lumen of the kidney (By similarity). Has an impact on cellular symmetry by ensuring correct bipolar cell division through the regulation of centrosome duplication and mitotic spindle assembly and by maintaining oriented cell division (OCD) during tubular elongation through planar cell polarity (PCP) pathway (By similarity). During epithelial cell morphogenesis regulates also cell-cell and cell-matrix adhesion and participates in cell motility (PubMed:31398719, PubMed:32698519). Promotes cell-cell contact through the positive regulation of PTK2 kinase activity leading to either positive regulation of epithelial cell proliferation through the HRAS/RAF1 pathways, or negative regulation of apoptosis through the PDK1/AKT1 pathway (By similarity). May act in collecting-duct and biliary differentiation (By similarity). May participate in the regulation of the cholangiocytes proliferation and the CCN2 production in an CXCL8-dependent manner (By similarity). {ECO:0000250|UniProtKB:E9PZ36, ECO:0000250|UniProtKB:P08F94, ECO:0000269|PubMed:31398719, ECO:0000269|PubMed:32698519}. | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RQ08 | RPN1_CANLF | MEVPTARLLLLLLLGAWAPAPESASPEAPLLVNEDVKRTVDLSSHLAKVTAEVVLAHPGGGSTARAASFLLALEPELEARLAHLGVQVKGEDEEENNLEVRETKIKGKSGRFFTVKLPVALDPGAKVSVVVETVYTHVLQPYPTQITQSEKQFVVFEGNHYFYSPYPTKTQTMRVKLASRNVESYTKLGNPTRSEDLLDYGPFRDIPAYSQDTFKVHYENNSPFLTITSMTRVIEVSHWGNIAVEENVDLKHTGAVLKGPFSRYDYQRQPDSGIASIRSFKTILPAAAQDVYYRDEIGNVSTSHLLILDDSVEMEIRPRFPLFGGWKTHYIVGYNLPSYEYLYNLGDQYALKMRFVDHVFDEQVIDSLTVKIILPEGAKNIQVDSPYEISRAPDELHYTYLDTFGRPVIVAYKKNLVEQHIQDIVVHYTFNKVLMLQEPLLVVAAFYILFFTVIIYVRLDFSITKDPAAEARMKVACITEQVLTLVNKRIGLYRHFDETINRYKQSRDVSTLNSGKKSLETEHKALTSEIASLQSRLKTEGSDLCDKVSEMQKLDAQVKELVLKSAVEAERLVAGKLKKDTYIENEKLISGKRQELVTKIDHILDAL | null | null | protein glycosylation [GO:0006486]; protein N-linked glycosylation via asparagine [GO:0018279] | cytosol [GO:0005829]; oligosaccharyltransferase complex [GO:0008250]; rough endoplasmic reticulum [GO:0005791] | null | PF04597; | null | OST1 family | PTM: Ufmylated by UFL1 in response to endoplasmic reticulum stress, promoting reticulophagy of endoplasmic reticulum sheets. {ECO:0000250|UniProtKB:P04843}. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:12887896}. Endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000269|PubMed:29519914}. | null | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P04843}. | null | null | FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. {ECO:0000269|PubMed:12887896}. | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RSS3 | WEE2_CANLF | MDDSSINKELKQKLNVSYCEEESESEGQKEAPESRETQSQTPDWAEGQESEAKFTPPRTPSSSIHGVGTFEEKDKMSPDQALRTPGPGFHKCPGTPAQPDSRSEVVHCESPYTPKSLLSQSVISSTEKLPSRGSKHLRFTPVPFVDEMTSSALVNINPFTPESYRKQFLRSNGKRKTRGDLEEADPGEGKVEQGLPAKRCVLRETNMASRYEKEFLEVEKIGVGEFGTVYKCIKRLDGCVYAIKRSMKPVAGLSNENLALHEVYAHAVLGHHPHVVRYYSAWAEDDHMIIQNEYCNGGSLQTAISENTKSGNHFPELKLKDILLQISLGLKYIHNSGMVHLDIKPSNIFICHKMQCDSPVVPEEIENEADWFLSANVMYKIAGDLGHVTSISKPKVEEGDSRFLANEILQEDYQHLPKADIFALGLTIAVAAGAESLPANGAKWHHIREGNLPDIPQKLSEEFHNLLKNMIHPDPSERPSAAGLARSRVLRPSLRKAEELQQQLNLEKSKTATLERELREAQQAWSPQEEHSDPGVSGTPTGSRCTKRPVGGKSAKSSSFTCGKSSP | 2.7.10.2 | null | female meiotic nuclear division [GO:0007143]; female pronucleus assembly [GO:0035038]; mitotic cell cycle [GO:0000278]; negative regulation of G2/MI transition of meiotic cell cycle [GO:0110031]; negative regulation of oocyte maturation [GO:1900194]; phosphorylation [GO:0016310]; positive regulation of phosphorylation [GO:0042327]; regulation of fertilization [GO:0080154]; regulation of meiosis I [GO:0060631] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, WEE1 subfamily | PTM: Phosphorylation leads to increase its activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027}; | null | null | null | null | FUNCTION: Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1 and acts as a key regulator of meiosis during both prophase I and metaphase II. Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, by phosphorylating CDK1 at 'Tyr-15', leading to inhibit CDK1 activity and prevent meiotic reentry. Also required for metaphase II exit during egg activation by phosphorylating CDK1 at 'Tyr-15', to ensure exit from meiosis in oocytes and promote pronuclear formation (By similarity). {ECO:0000250}. | Canis lupus familiaris (Dog) (Canis familiaris) |
E2RTQ2 | KIN13_GIAIC | MSDLVYQWLESANLQQYYPAFEQQGITPQRFITITIQDYGALGIQALPDKQKLFRLITTLKSRENILEQQPSAPNTGATPQSVPSSHVSPHVAQGDRFVGDKQKQNDIQQAQDMSLYESYDGGYEPPYVSAQGSGPANGDDYVIPTIPYHPNAPNPPNPRGIPTVNRTVVPPVDLFLNQIQSRIRVVIRKRPINPKELSQNQRDVVTADGWNQVSIHEPKVKVDLTKYTDLHTFKFDHVFNEQSDNQEIYQYAAKPLIRSVFEGKNCTVFAYGQTGSGKSFTMMHKDNGIYVLACFDILEYLRVYNGSQGNNSKFLVPVVSFFEIYGGKLFDLLNNRQRLQALEDGKGNVQITGLTEKQISSVDAMLNLIDSGLTLRAVGATGANADSSRSHAILQIALKYTKSGKEYSRISFIDLAGSERASDVQNSDRQTRMEGAEINKSLLALKECIRAMDKSNDSKSGAHIPFRGSKLTMVLRDSFIGNSQTVMIANISPNDKSCDNTLNTLRYADRVKELQHGKGGIIKFNVLKMGQNAADVILGTARDDENDVYKAGIVGVNAAPSQQARVPPASQAPITARQIQQNLPQPHYNPNYNPPNSKPAFEPRVETTDEDDMVRTHCDLVDSIYEQEDLIVRAHRRQVDSMMQLVKEEVALLHAIENDQVSIDDWLVKLSDILSRKEEAITTLKGNLSAFKQALQKEEELSHSIDLNKARKK | null | null | axonemal microtubule depolymerization [GO:0060404]; cell morphogenesis [GO:0000902]; microtubule depolymerization [GO:0007019]; microtubule-based movement [GO:0007018]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; mitotic spindle microtubule depolymerization [GO:1990755]; plus-end specific microtubule depolymerization [GO:0070462] | 9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; ciliary basal body [GO:0036064]; kinetochore [GO:0000776]; median body [GO:0097568]; microtubule [GO:0005874]; spindle [GO:0005819]; ventral disc [GO:0097597] | ATP binding [GO:0005524]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777] | PF00225;PF00536; | 3.40.850.10;1.10.150.50; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, KIN-13 subfamily | PTM: Phosphorylated by PLK. {ECO:0000250|UniProtKB:Q969B0}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17766466, ECO:0000269|PubMed:31855176}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:17766466, ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000250|UniProtKB:Q969B0}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:17766466, ECO:0000269|PubMed:31855176}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17766466}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:17766466}. Note=Localizes and accumulates in a length-dependent manner to the distal regions of flagellar tips (PubMed:31855176). Amount at the distal flagellar tip increases during de novo assembly possibly as a consequence of its transport along the flagellum (PubMed:31855176). More of it is present in the caudal flagellar tips than in the longer anterior flagellar tips (PubMed:31855176). Amount decreases sharply immediately proximal to the flagellar tip indicating that it does not undergo directed retrograde transport on the axoneme, but likely diffuses from the flagella tip toward the base (PubMed:31855176). During diffusion, it may be recaptured by anterograde intraflagellar transport (IFT) trains to sequester it to the tip region (PubMed:31855176). Localizes to basal bodies in interphase (By similarity). Localizes uniformly to the median body and unevenly at distinct regions of all eight flagella, primarily localizing to the distal flagellar tips, in interphase (PubMed:17766466, PubMed:31855176). Localizes to the cytoplasmic axonemes in interphase (PubMed:17766466, PubMed:31855176). Localizes to the ventral disk in interphase (PubMed:31855176). Localizes to the plus ends of interphase and mitotic microtubules (PubMed:17766466). Localizes to single spots on chromosomes during mitosis (PubMed:17766466). Localizes to the plus ends of microtubules and kinetochores in anaphase spindles (PubMed:17766466). Localizes to the growing flagellar tips of the posterolateral and ventral axonemes during mitotic telophase (PubMed:17766466). Localizes also to kinetochores during flagellar duplication (PubMed:17766466). {ECO:0000250|UniProtKB:Q969B0, ECO:0000269|PubMed:17766466, ECO:0000269|PubMed:31855176}. | null | null | null | null | null | FUNCTION: Involved in cell cycle (PubMed:17766466). Involved in formation of flagella, regulation of flagellar length, and formation of median bodies during interphase (By similarity). Regulates flagellar length in all eight distal flagellar tips by promoting disassembly of the microtubules (PubMed:17766466, PubMed:31855176). Disassembles microtubules at the distal flagellar tips in a length-dependent manner in order to maintain different equilibrium lengths of the four flagellar pairs (PubMed:31855176). Regulates interphase and mitotic microtubule dynamics (PubMed:17766466). Regulates microtubule disassembly dynamics of the dual mitotic spindles and the median body (PubMed:17766466). {ECO:0000250|UniProtKB:Q969B0, ECO:0000269|PubMed:17766466, ECO:0000269|PubMed:31855176}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
E2RTQ7 | AURK_GIAIC | MPQHLVPHTGTGKRTTIEDFEIGRFLGRGKYGLVYLAREQSSKLVVALKVLYKSYIKSERVEGQVRRELDIHLNVRHINIIRLYTWFQDETRVFLVLEVAPYGELYQRLQQFGKFPLPVVSKIIRDVAQAIQYLHRKNIFHRDLKAENILICKGKETKEHTDAHNSDDSISVHEHELVRMAHYTYKIADFGWSVHHPTHGGRRRTQCGTLDYLPPEVMLGQSYDKACDIWSLGALCYELICGTAPFYHDEIKITRQNIANVEYSFTKDFSPASKDFIQRMLIRSPEARISIEDILRHPFLRQTDHRSKVPK | 2.7.11.1 | null | microtubule cytoskeleton organization involved in mitosis [GO:1902850]; mitotic cytokinesis [GO:0000281]; mitotic nuclear division [GO:0140014]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; regulation of cell cycle [GO:0051726]; regulation of cytokinesis [GO:0032465] | centrosome [GO:0005813]; chromosome passenger complex [GO:0032133]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; median body [GO:0097568]; motile cilium [GO:0031514]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; spindle [GO:0005819]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]; spindle pole [GO:0000922]; spindle pole centrosome [GO:0031616]; ventral disc [GO:0097597] | ATP binding [GO:0005524]; cytoskeletal protein binding [GO:0008092]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily | PTM: Phosphorylated in mitosis and cytokinesis (PubMed:17964578). Activated by autophosphorylation at Thr-205 (PubMed:27859890). {ECO:0000269|PubMed:17964578, ECO:0000269|PubMed:27859890}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17964578}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17964578}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17964578, ECO:0000269|PubMed:27859890}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:17964578}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17964578, ECO:0000269|PubMed:27859890}. Nucleus membrane {ECO:0000269|PubMed:27859890}. Note=Non-phosphorylated form is exclusively localized to both nuclei in interphase trophozoites. At the beginning of mitosis, it is mostly in the nuclei and co-localizes with chromatin through telophase. Phosphorylated form co-localizes with centrin to centrosomes from prophase through cytokinesis. Phosphorylated form localizes also to the spindle microtubules surrounding each two nuclei and the spindle poles in metaphase. It is additionally dynamically localized to cytoskeletal structures including the median body, rim of the attachment disk, and anterior and posterior-lateral paraflagellar dense rods during different stages of mitosis. Phosphorylated form remains localized to microtubules of both spindles in anaphase through telophase as the spindles elongate to allow the four nuclei segregate to opposite poles of both spindles. Phosphorylated form localizes only to the gradually unfolding parental ventral attachment disk called pontoon later in telophase and cytokinesis, but not to the two nascent daughter disks dorsal to the disassembling parental disk and spindles. Phosphorylated form localizes to the median body in all stages of mitosis, but it is less prominent after anaphase. Neither non-phosphorylated nor phosphorylated form localizes to endoplasmic reticulum, lysosome-like peripheral vesicles, mitosomes or flagellar axonemes (PubMed:17964578). Colocalizes with EB1 at the nuclear membrane and median bodies in interphase, at the spindle microtubules surrounding the chromosomes in metaphase, at the mitotic spindles in anaphase and telophase, and at the nuclear membranes in cytokinesis (PubMed:27859890). {ECO:0000269|PubMed:17964578, ECO:0000269|PubMed:27859890}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000255|RuleBase:RU367134, ECO:0000269|PubMed:27859890}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000255|RuleBase:RU367134, ECO:0000269|PubMed:27859890}; | null | null | null | null | FUNCTION: Involved in regulation of the cell cycle (PubMed:17964578, PubMed:27859890). Required for mitotic cell division and cytokinesis (PubMed:17964578, PubMed:27859890). Based on its localization to centrosomes and spindle microtubules, as well as to various cytoskeletal components such as the median body, parental attachment disk, and anterior and posterior-lateral paraflagellar dense rods, may coordinate reorganization and segregation of tubulin-containing structures during mitosis and cytokinesis (PubMed:17964578). May regulate microtubule disassembly by phosphorylating cytoskeletal proteins leading to their destabilization (PubMed:17964578). Phosphorylates EB1 at 'Ser-148' in vitro (PubMed:27859890). Phosphorylates histone H3 in vitro (PubMed:27859890). {ECO:0000269|PubMed:17964578, ECO:0000269|PubMed:27859890}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
E2RTZ4 | HMP_GIAIC | MTLSEDTLRAVEATAGLIAAQGIEFTRAFYERMLTKNEELKNIFNLAHQRTLRQPKALLDSLVAYALNIRRINELYELKGKGLPVPPEHWAELQGFFSAAERVANKHTSFGIQPAQYQIVGAHLLATIEDRITKDKDILAEWAKAYQFLADLFIKREEEIYAATEGCKGGWRQTRTFRVEEKTRVNEIICKFRLVPAEEGAGVVEHRPGQYLAIFVRSPEHFQHQQIRQYSIISAPNSAYYEIAVHRDEKGTVSRYLHDYVSTGDLLEVAPPYGDFFLRYLEADEQAPADTQASQEFQMLQSGAINFAAEKTMPIVLISGGIGQTPLLSMLRFLAQKEGKETARPIFWIHAAHNSRVRAFKEEVDAIRETALPSLRVVTFLSEVRATDREGEDYDFAGRINLDRISELTKLEADNANPHYFFVGPTGFMTAVEEQLKTKSVPNSRIHFEMFGPFKASH | 1.14.12.17 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b group.; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD.; | cellular response to nitrosative stress [GO:0071500]; nitric oxide catabolic process [GO:0046210]; response to toxic substance [GO:0009636] | null | FAD binding [GO:0071949]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitric oxide dioxygenase NAD(P)H activity [GO:0008941]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344] | PF00970;PF00042;PF00175; | 1.10.490.10;3.40.50.80;2.40.30.10; | Globin family, Two-domain flavohemoproteins subfamily; Flavoprotein pyridine nucleotide cytochrome reductase family | null | null | CATALYTIC ACTIVITY: Reaction=NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate; Xref=Rhea:RHEA:19465, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.12.17; CATALYTIC ACTIVITY: Reaction=NADH + 2 nitric oxide + 2 O2 = H(+) + NAD(+) + 2 nitrate; Xref=Rhea:RHEA:19469, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.12.17; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=22 uM for O(2) {ECO:0000269|PubMed:20691663}; | null | null | null | FUNCTION: Flavohemoprotein involved in nitric oxide (NO) detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the protozoan parasite from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. May also be involved in O(2) detoxification. {ECO:0000269|PubMed:20655876, ECO:0000269|PubMed:20691663}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
E2RU10 | EB1_GIAIC | MPPVKAPGNVSDCYFVGRVSLLKWISELLNEPVKKVEDLASGHHYCMALNLVYPGQVNMHRVRMNAINEWERSENFKIIQDVLSRNNIDKGIDVNKLVTGKYMDNFEFFQWFKWFFDQNYKGSKSGATESGSANAVTKTSKPGNRSGSTAASMQNPKASSTSGPSIDSKELEDLRRQIAKGQLESQFYFDKLHEIEIYMDQMNELMTQVEIAEPEDSPFYIKSVVKKIEDILYAEYHQ | null | null | cell division [GO:0051301]; protein localization to microtubule [GO:0035372]; regulation of microtubule polymerization or depolymerization [GO:0031110]; spindle assembly [GO:0051225]; thigmotropism [GO:0009652] | cytoplasmic microtubule [GO:0005881]; microtubule organizing center [GO:0005815]; microtubule plus-end [GO:0035371]; motile cilium [GO:0031514]; nuclear membrane [GO:0031965]; spindle midzone [GO:0051233] | microtubule plus-end binding [GO:0051010] | PF00307;PF03271; | 1.20.5.1430;1.10.418.10; | MAPRE family | PTM: Phosphorylated in vitro by aurora kinase. Phosphorylation is important for cell division. {ECO:0000269|PubMed:27859890}. | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:18590831, ECO:0000269|PubMed:19953272, ECO:0000269|PubMed:24828878, ECO:0000269|PubMed:27859890, ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17766466, ECO:0000269|PubMed:18590831, ECO:0000269|PubMed:19953272, ECO:0000269|PubMed:24828878, ECO:0000269|PubMed:27859890, ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17766466, ECO:0000269|PubMed:24828878, ECO:0000269|PubMed:27859890}. Nucleus envelope {ECO:0000269|PubMed:24828878}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:17766466, ECO:0000269|PubMed:18590831, ECO:0000269|PubMed:19953272}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:17766466}. Cytoplasm {ECO:0000269|PubMed:24828878}. Note=Localizes to the plus ends of mitotic and interphase microtubules (PubMed:17766466). Localizes to the eight flagellar tips, the median body and the mitotic spindles (PubMed:17766466). Localizes particularly at the distal tips of axonemes and axonemal exit points (flagellar pores) (PubMed:17766466). Localizes to nuclear membranes and median bodies in trophozoites (PubMed:18590831, PubMed:19953272, PubMed:24828878). Localizes to axonemes between the two nuclei in trophozoites (PubMed:18590831, PubMed:19953272). Localizes to the mitotic spindles of the dividing trophozoites at anaphase (PubMed:24828878). Localizes mainly to the nuclear membranes 24 hours after induction of encystation and to median bodies in some of the encysting cells (PubMed:24828878). Dispersed in a condensed pattern in the cytoplasm of the cysts, but absent from the nuclear membranes, 48 hours after induction of encystation (PubMed:24828878). Colocalizes with aurora kinase at the nuclear membrane and the median bodies in interphase, at the spindle microtubules surrounding the chromosomes in metaphase, at the mitotic spindles in anaphase and telophase, and at the nuclear membranes in cytokinesis (PubMed:27859890). Does not localize to the median body during cell division (PubMed:27859890). Does not localize to ventral disk (PubMed:17766466). {ECO:0000269|PubMed:17766466, ECO:0000269|PubMed:18590831, ECO:0000269|PubMed:19953272, ECO:0000269|PubMed:24828878, ECO:0000269|PubMed:27859890}. | null | null | null | null | null | FUNCTION: Involved in cell division (PubMed:18590831, PubMed:24828878, PubMed:27859890). Involved in mitosis (PubMed:18590831, PubMed:24828878). Regulates dynamics of microtubules (MTs) during mitosis (PubMed:24828878). Required for cytokinesis (PubMed:27859890). Binds polymerized MTs in vitro (PubMed:18590831, PubMed:24828878). Is able to rescue a mitotic division defect, the proper positioning of the nucleus, of the S.cerevisiae BIM1 knockout mutant in a complementation assay (PubMed:18590831, PubMed:24828878). May play a role in spindle positioning and MT distribution (PubMed:18590831). May be involved in MT nucleation for the formation of median bodies and in the biogenesis of flagella (PubMed:30318753). Based on its localization to both the flagellar exit point and the distal flagellar tips, it may mediate the transition from anterograde to retrograde intraflagellar transport (IFT) (PubMed:17766466). {ECO:0000269|PubMed:17766466, ECO:0000269|PubMed:18590831, ECO:0000269|PubMed:24828878, ECO:0000269|PubMed:27859890, ECO:0000269|PubMed:30318753}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
E2RU81 | PFP_GIAIC | MSAFEVYRRKFKPALPRAIQGASYHLHTEEKTHPVADEQDIAALFPKTTHLPLLDIQPDTGAPKLLEPKRVGVIFSGGQAPGGHNVLCGLYDKLQQIAPKSVLLGFQNGPKGLMTNKYVELTEKFLEPFRNMGGFHAIGSGRDKIAKPEDFDAAAKTAKDNNLDIICIIGGDDSNTNACLLAEDFLKRGLKTAVIGVPKTIDRDLYSTKGIECSFGFDSSTKVYAELIGNICYDCLSAKKYWHFIRLMGRSASHITLECGLQTHANICLVGEEILSKKMTSRQLFEYLADCVTKRADSGKNYGVCLVPEGLIEFIPENNELFAYLNNTLLPHWTGELTADAVAAKLPDPLRTTFMAIPASIRTQLLLDRDPHGNIAISQIETEKFLGAGVQQVLRERGSKTKFTPLYHFFGYEGRCAAPSDFDCSLCYSLGAVAAILGCNGKTGYMASLRNLVRPPADWSPIGLPLTCLMNMEMRHGHKTPVIMKQMTDLNGNPYKLLARNRDTWLMNDDYQNPGPIQQIATESAEGTAVCARPTITLIEEARK | 2.7.1.90 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03185}; | fructose 6-phosphate metabolic process [GO:0006002]; photosynthesis [GO:0015979]; response to glucose [GO:0009749] | cytosol [GO:0005829] | 6-phosphofructokinase activity [GO:0003872]; ATP binding [GO:0005524]; diphosphate-fructose-6-phosphate 1-phosphotransferase activity [GO:0047334]; metal ion binding [GO:0046872] | PF00365; | 3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, PPi-dependent PFK group II subfamily, Clade 'Long' sub-subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03185}. | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; Evidence={ECO:0000255|HAMAP-Rule:MF_03185, ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.09 mM for phosphate {ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346}; KM=0.039 mM for diphosphate {ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346}; KM=0.25 mM for fructose 6-phosphate {ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346}; KM=0.072 mM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346}; Vmax=4.62 umol/min/mg enzyme for the forward reaction {ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346}; Vmax=0.15 umol/min/mg enzyme for the reverse reaction {ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346}; | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_03185}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2 for the forward reaction and 7.0 for the reverse reaction. {ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346}; | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. {ECO:0000255|HAMAP-Rule:MF_03185, ECO:0000269|PubMed:7663168, ECO:0000269|PubMed:8577346, ECO:0000269|PubMed:9242987}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
E2RU97 | 1433_GIAIC | MAEAFTREDYVFMAQLNENAERYDEMVETMRKISGMEGELSDKERNLLSVAYKNVIGPRRAAWRIVSSIEAKEKGRQKPNAKRIEQIRVYRQKIEKELSDICNDILKLLQEQFVPRSTNADAKVFYYKMQGDYYRYLAEYSSGEDKEKIAGSALNAYNSAFEISQQLPPTHPIRLGLALNFSVFYYEILASPDRACELARKAFDAAITDLDKLTEESYKDSTLIMQLLRDNLNLWVTDSAGDDNAEEK | null | null | actin cytoskeleton organization [GO:0030036]; activation of protein kinase C activity [GO:1990051]; establishment of cell polarity [GO:0030010]; MAPK cascade [GO:0000165]; positive regulation of cytoskeleton organization [GO:0051495]; protein homotetramerization [GO:0051289]; protein homotrimerization [GO:0070207]; regulation of nucleus size [GO:0097298]; signal transduction [GO:0007165] | axoneme [GO:0005930]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; endoplasmic reticulum [GO:0005783]; motile cilium [GO:0031514]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; spindle [GO:0005819] | actin binding [GO:0003779]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; phosphoprotein binding [GO:0051219]; phosphoserine residue binding [GO:0050815]; protein homodimerization activity [GO:0042803] | PF00244; | 1.20.190.20; | 14-3-3 family | PTM: Phosphorylated constitutively throughout the life cycle. Phosphorylation is very high in trophozoites and encysting cells of 12 hours (PubMed:16368691). Phosphorylated during excystation (PubMed:19861170). Phosphorylation promotes its binding to various target proteins and is critical for encystation process. Phosphorylation modification is not influenced by polyglycylation modification (PubMed:19733174). {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:19861170}.; PTM: Polyglycylated on a glutamate residue, resulting in polyglycine chain on the gamma-carboxyl group (PubMed:16368691, PubMed:19733174, PubMed:21135098, PubMed:24147113, PubMed:24658679). Polyglycylated by the tubulin--tyrosine ligase-like protein GL50803_8456 (gTTLL3). The polyglycine chain is shortened by metallopeptidases of the M20 family, namely dipeptidases GL50803_15832 (gDIP1) and GL50803_8407 (gDIP2) (PubMed:21135098). The length of the polyglycine chain is developmental stage-dependent. In trophozoites, glycine residues range from 10 to 31, with the greatest occurrence of 21 residues. In 12 hour encystation stage, glycine residues range from 6 to 22, with the greatest occurrence of 10 residues. The differential rate of polyglycylation/deglycylation during the encystation process regulates the intracellular localization of this protein. Relocalizes partially from the cytoplasm inside the nuclei following the shortening of the polyglycine chain in encysting cells (PubMed:16368691, PubMed:19733174). Polyglycylation modification is not influenced by phosphorylation modification (PubMed:19733174). Polyglycylation prevents oligomerization in vivo (PubMed:24658679). {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:21135098, ECO:0000269|PubMed:24147113, ECO:0000269|PubMed:24658679}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:19861170, ECO:0000269|PubMed:21135098, ECO:0000269|PubMed:24147113, ECO:0000269|PubMed:24728194, ECO:0000269|PubMed:28932813}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28932813}. Nucleus {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:21135098, ECO:0000269|PubMed:22452640}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:28932813}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:28932813}. Nucleus envelope {ECO:0000269|PubMed:28932813}. Endoplasmic reticulum {ECO:0000269|PubMed:28932813}. Note=In trophozoites and cysts, localizes intensely in the cytoplasm. Not detected in the central area of the cell corresponding to the median body nor in flagella. Detected in the nuclei of the encysting cells. Nuclear localization increases during the transition of cells from the early to the late encysting stage. Does not localize to the encystation-specific vesicles of the encysting cells (PubMed:16368691, PubMed:19733174). In interphase cells, detected throughout the cell with somewhat enriched at the cortex and perinuclear region. Associates with the intracytoplasmic axonemes of all flagella, but it is most apparent in the anterior flagella of interphase cells. Localizes also to the nuclear envelope/endoplasmic reticulum and to the microtubule bare area of the ventral disc during interphase. In mitotic cells, disassociates from the intracytoplasmic axonemes and localizes around the spindle. During cytokinesis, localizes with the ingressing furrow, which does not utilize a contractile ring (PubMed:28932813). Does no colocalize with F-actin (PubMed:24728194, PubMed:28932813). {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:24728194, ECO:0000269|PubMed:28932813}. | null | null | null | null | null | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Binds with varying affinity to various synthetic phosphopeptides having a consensus binding motif RSX(pS/pT)XP, called mode-1, where X is any residue and pS/pT is a phosphorylated serine/threonine, and to synthetic phosphopeptides having a consensus binding motif Xp(S/T)X1-2-COOH, called mode-3, in which the phosphorylated residue occupies the penultimate C-terminal position in the target protein, but does not bind to their unphosphorylated counterparts (PubMed:19733174). Binds to synthetic human RAF1 phosphopeptides, but not to their unphosphorylated forms. Binds to difopein, a polypeptide containing a phosphorylation-independent binding motif (PubMed:16368691, PubMed:19733174). Involved in encystation (PubMed:19733174). Involved in cell proliferation. Required for actin and tubulin cytoskeletal organization. Regulates actin filament formation and nuclear size (PubMed:28932813). {ECO:0000250|UniProtKB:P62261, ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:28932813}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
E3PJ86 | GSPD2_ECOH1 | MFWRDITLSVWRKKTTGLKTKKRLLPLVLAAALCSSPVWAEEATFTANFKDTDLKSFIETVGANLNKTIIMGPGVQGKVSIRTMTPLNERQYYQLFLNLLEAQGYAVVPMENDVLKVVKSSAAKVEPLPLVGEGSDNYAGDEMVTKVVPVRNVSVRELAPILRQMIDSAGSGNVVNYDPSNVIMLTGRASVVERLTEVIQRVDHAGNRTEEVIPLDNASASEIARVLESLTKNSGENQPATLKSQIVADERTNSVIVSGDPATRDKMRRLIRRLDSEMERSGNSQVFYLKYSKAEDLVDVLKQVSGTLTAAKEEAEGTVGSGREIVSIAASKHSNALIVTAPQDIMQSLQSVIEQLDIRRAQVHVEALIVEVAEGSNINFGVQWASKDAGLMQFANGTQIPIGTLGAAISQAKPQKGSTVISENGATTINPDTNGDLSTLAQLLSGFSGTAVGVVKGDWMALVQAVKNDSSSNVLSTPSITTLDNQEAFFMVGQDVPVLTGSTVGSNNSNPFNTVERKKVGIMLKVTPQINEGNAVQMVIEQEVSKVEGQTSLDVVFGERKLKTTVLANDGELIVLGGLMDDQAGESVAKVPLLGDIPLIGNLFKSTADKKEKRNLMVFIRPTILRDGMAADGVSQRKYNYMRAEQIYRDEQGLSLMPHTAQPVLPAQNQALPPEVRAFLNAGRTR | null | null | protein secretion by the type II secretion system [GO:0015628] | cell outer membrane [GO:0009279]; type II protein secretion system complex [GO:0015627] | null | PF00263;PF03958;PF21305; | 3.30.1370.120; | Bacterial secretin family, GSP D subfamily | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:22585966, ECO:0000305|PubMed:29632366}. Note=Some protein is also found in the cell inner membrane, the inner membrane protein does not form multimers and is unstable (PubMed:22585966). Most of the protein is in the periplasm which it traverses to contact proteins of the cell inner membrane (Probable). {ECO:0000269|PubMed:22585966, ECO:0000305|PubMed:29632366}. | null | null | null | null | null | FUNCTION: Part of a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane (Probable). This subunit forms the outer membrane channel (Probable). {ECO:0000305|PubMed:22585966, ECO:0000305|PubMed:23820381, ECO:0000305|PubMed:29632366}. | Escherichia coli O78:H11 (strain H10407 / ETEC) |
E3PQQ8 | CCAP_CONVL | MVSLGHVLFVILLPVLLPVAADDPDDQMLSQISLPSSSRSEYDDNDVSKRVFCNGFTGCGGRHRDRSRRQERYGKRLIPVLAKRPFCNSFGCYNGKRSLSGAGPALSTPVDPSRNNKARTMARMLDAAASARHEQQQQLLQQREQRGLESRDPAASGDLSKRLFCNGYGGCRGGKRTLYSPWLERMNEVADDRSARNALCTRLGWRE | null | null | modulation of heart rate in another organism [GO:0044554]; negative regulation of heart rate in another organism [GO:0044555] | extracellular region [GO:0005576]; host extracellular space [GO:0043655] | toxin activity [GO:0090729] | null | null | null | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: [ConoCAP-a]: In contrast to other members of the CCAP family which are cardio-accelerators, conoCAP-a decreases the heart frequency in Drosophila larvae (26%), rats and zebrafish embryos. It also reduces the blood pressure in rats. It decreases systolic calcium in ventricular cardiac myocytes, indicating that it may act via impairment of intracellular calcium trafficking.; FUNCTION: [ConoCAP-b]: Synthetic conoCAP-b decreases the heart frequency of 23% in Drosophila larvae.; FUNCTION: [ConoCAP-c]: Synthetic conoCAP-c decreases the heart frequency of 12% in Drosophila larvae. | Conus villepinii (Villepin's cone) |
E3PRJ4 | KAME_ACESD | MSSGLYSMEKKEFDKVLDLERVKPYGDTMNDGKVQLSFTLPLKNNERSAEAAKQIALKMGLEEPSVVMQQSLDEEFTFFVVYGNFVQSVNYNEIHVEAVNSEILSMEETDEYIKENIGRKIVVVGASTGTDAHTVGIDAIMNMKGYAGHYGLERYEMIDAYNLGSQVANEDFIKKAVELEADVLLVSQTVTQKNVHIQNMTHLIELLEAEGLRDRFVLLCGGPRINNEIAKELGYDAGFGPGRFADDVATFAVKTLNDRMNS | 5.4.3.3 | COFACTOR: Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; Evidence={ECO:0000269|PubMed:10617592, ECO:0000269|PubMed:11318641}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:11318641, ECO:0000269|PubMed:15514022}; | null | null | cobalamin binding [GO:0031419]; D-lysine 5,6-aminomutase activity [GO:0047826]; metal ion binding [GO:0046872]; protein dimerization activity [GO:0046983] | PF02310;PF16554; | 3.40.50.280;3.30.30.60; | KamE family | null | null | CATALYTIC ACTIVITY: Reaction=(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate; Xref=Rhea:RHEA:21736, ChEBI:CHEBI:57434, ChEBI:CHEBI:57436; EC=5.4.3.3; Evidence={ECO:0000269|PubMed:11318641}; CATALYTIC ACTIVITY: Reaction=D-lysine = (2R,5S)-2,5-diaminohexanoate; Xref=Rhea:RHEA:18241, ChEBI:CHEBI:32557, ChEBI:CHEBI:137487; EC=5.4.3.3; Evidence={ECO:0000269|PubMed:10617592, ECO:0000269|PubMed:11318641}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.6 uM for adenosylcobalamin (for recombinant alpha and beta subunits expressed together in E.coli to overcome presence of corrinoids in native system) {ECO:0000269|PubMed:10617592}; | PATHWAY: Amino-acid metabolism; lysine degradation. {ECO:0000269|PubMed:10617592}. | null | null | FUNCTION: Catalyzes the migration of the L-beta-lysine and D-lysine epsilon amino group to the delta carbon to produce 3,5-diaminohexanoate and 2,5-diaminohexanoate, respectively. {ECO:0000269|PubMed:10617592, ECO:0000269|PubMed:11318641}. | Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF) (Clostridium sticklandii) |
E3PRJ5 | KAMD_ACESD | MISVESKLNLDFNLVEKARAKAKAIAIDTQEFIEKHTTVTVERAVCRLLGIDGVDTDEVPLPNIVVDHIKENNGLNLGAAMYIANAVLNTGKTPQEIAQAISAGELDLTKLPMKDLFEVKTKALSMAKETVEKIKNNRSIRESRFEEYGDKSGPLLYVIVATGNIYEDITQAVAAAKQGADVIAVIRTTGQSLLDYVPYGATTEGFGGTYATQENFRLMREALDKVGAEVGKYIRLCNYCSGLCMPEIAAMGAIERLDVMLNDALYGILFRDINMQRTMIDQNFSRIINGFAGVIINTGEDNYLTTADAFEEAHTVLASQFINEQFALLAGLPEEQMGLGHAFEMDPELKNGFLYELSQAQMAREIFPKAPLKYMPPTKFMTGNIFKGHIQDALFNMVTIMTNQRIHLLGMLTEALHTPFMSDRALSIENAQYIFNNMESISEEIQFKEDGLIQKRAGFVLEKANELLEEIEQLGLFDTLEKGIFGGVKRPKDGGKGLNGVVSKDENYYNPFVELMLNK | 5.4.3.3 | COFACTOR: Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; Evidence={ECO:0000269|PubMed:10617592, ECO:0000269|PubMed:11318641}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:11318641, ECO:0000269|PubMed:15514022}; | null | null | cobalamin binding [GO:0031419]; D-lysine 5,6-aminomutase activity [GO:0047826] | PF09043; | 3.20.20.440; | KamD family | null | null | CATALYTIC ACTIVITY: Reaction=(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate; Xref=Rhea:RHEA:21736, ChEBI:CHEBI:57434, ChEBI:CHEBI:57436; EC=5.4.3.3; Evidence={ECO:0000269|PubMed:11318641}; CATALYTIC ACTIVITY: Reaction=D-lysine = (2R,5S)-2,5-diaminohexanoate; Xref=Rhea:RHEA:18241, ChEBI:CHEBI:32557, ChEBI:CHEBI:137487; EC=5.4.3.3; Evidence={ECO:0000269|PubMed:10617592, ECO:0000269|PubMed:11318641}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.6 uM for adenosylcobalamin (for recombinant alpha and beta subunits expressed together in E.coli to overcome the presence of corrinoids in native system) {ECO:0000269|PubMed:10617592}; | PATHWAY: Amino-acid metabolism; lysine degradation. {ECO:0000269|PubMed:10617592}. | null | null | FUNCTION: Catalyzes the migration of the L-beta-lysine and D-lysine epsilon amino group to the delta carbon to produce 3,5-diaminohexanoate and 2,5-diaminohexanoate, respectively. {ECO:0000269|PubMed:10617592, ECO:0000269|PubMed:11318641}. | Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF) (Clostridium sticklandii) |
E3PY95 | OAME_ACESD | MEKDLQLRVNEKLDVENILKDLDKYTPKRRGWTWRQPAENLQMGPFIYKDASTPLENSVALPSAKYFGDIDPQPLPVITTEIASGRFEDDIRRMRMAAWHGADHIMVIRTAGQSHYDGLIEGTPQGIGGVPITRKQVRAQRKALDLIEEEVGRPINYHSYVSGVAGPDIAVMFAEEGVNGAHQDPQYNVLYRNINMIRSFIDACESKTIMAWADMAQIDGAHNANATAREAWKVMPELMVQHALNSIFSLKVGMKKSNICLSTVPPTAPPAPSMYLDLPYAVALREMFEGYRMRAQMNTKYMEASTREATVTHVLNLLISKLTRADIQSTITPDEGRNVPWHIYNIEACDTAKQALIGMDGLMDMVQLKREGVLGDTVRELKERAVLFMEEIIEAGGYFNAVEQGFFVDSGYYPERNGDGIARQINGGIGAGTVFERDEDYMAPVTAHFGYNNVKQYDEALVSEPSKLIDGCTLEVPEKIVYIDELDENDNVNVRMEETKEFRHSSMIKPEVEWQADGTVLLTMFLPTSKRVAEFAAIEFAKKMNLEEVEVINREVMQEAEGTRIELKGRVPFSIDINSLVIPPEPEILSEDEIREDIEKTPLKIVAATVGEDEHSVGLREVIDIKHGGIEKYGVEVHYLGTSVPVEKLVDAAIELKADAILASTIISHDDIHYKNMKRIHELAVEKGIRDKIMIGCGGTQVTPEVAVKQGVDAGFGRGSKGIHVATFLVKKRREMREGK | 5.4.3.5 | COFACTOR: Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; Evidence={ECO:0000269|PubMed:11577113, ECO:0000269|PubMed:20106986, ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:11577113, ECO:0000269|PubMed:20106986, ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4}; | null | null | cobalamin binding [GO:0031419]; D-ornithine 4,5-aminomutase activity [GO:0047831]; metal ion binding [GO:0046872]; protein dimerization activity [GO:0046983] | PF02310;PF09043;PF16554; | 3.40.50.280;3.20.20.440;3.30.30.60; | null | null | null | CATALYTIC ACTIVITY: Reaction=D-ornithine = (2R,4S)-2,4-diaminopentanoate; Xref=Rhea:RHEA:14893, ChEBI:CHEBI:57668, ChEBI:CHEBI:58697; EC=5.4.3.5; Evidence={ECO:0000269|PubMed:11577113, ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=44.5 uM for D-ornithine {ECO:0000269|PubMed:11577113, ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4}; KM=0.43 uM for adenosylcobalamin {ECO:0000269|PubMed:11577113, ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4}; KM=1.5 uM for pyridoxal phosphate {ECO:0000269|PubMed:11577113, ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4}; Note=kcat is 6.3 sec(-1). Values are measured for recombinant S and E components expressed together in E.coli to overcome the presence of corrinoids in native system.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 or between 8.5-8.7 (with Tris-HCl buffer). Half-maximal activity is observed at pH 7.4 and 9.7. {ECO:0000269|PubMed:11577113, ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius for native enzyme. Displays half-maximal activity at 23 degrees Celsius and 49 degrees Celsius. Rapidly inactivated at temperatures above 45 degrees Celsius. Loses more than 35% and 30% of its activity when stored at -20 degrees Celsius for 1 month and at 4 degrees Celsius for 48 hours, respectively. {ECO:0000269|PubMed:11577113, ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4}; | FUNCTION: Component of a complex that catalyzes the reversible migration of the omega amino group of D-ornithine to C-4 to form (2R,4S)-2,4-diaminopentanoic acid. OraE may be the catalytic subunit. Active only on D-ornithine and 2,4-diaminopentanoic acid but not active on L-ornithine, L-beta-lysine, L-alpha-lysine or D-alpha-lysine. {ECO:0000269|PubMed:11577113, ECO:0000269|PubMed:4711468, ECO:0000269|Ref.4}. | Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF) (Clostridium sticklandii) |
E3PZS2 | STAD2_OPHSP | MELHLALRASPLPAADPGRRPPPPRGNFATNCTAAINSTHISQEKFRSLDSWVEHNMLTFLKPVEKCWQPQDFLPDPSHLSAEELGDAVREIHERAAEIPDEVWVCMVGNMVTEEALPTYQSLISSVLGGTVAGSTPWDRWIRGWSAEENRHGDLLNKYLYLTGRLDMRQVEKTIQYLIGSGMDVGVGNSILCGFIYTCFQEKATFISHGNTARLAKHHGDTTLAKICGLVAADEKRHAVAYTNLMKKLFEVAPNESMLAFAHIMRAHVTMPASRMFDGRDPRLFTHFSAVTQKIGVYTVRDYGEMLDFFLKEWEISAVVDDLSPEGRQAQEYVCGLPEVMGKMAERADDRRKKLVNVGEPRYIPFSWIFNKQVCV | 1.14.19.11; 1.14.19.2 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P22337}; Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:P22337}; | defense response [GO:0006952]; unsaturated fatty acid biosynthetic process [GO:0006636] | chloroplast stroma [GO:0009570]; cytosol [GO:0005829] | acyl-[acyl-carrier-protein] desaturase activity [GO:0045300]; metal ion binding [GO:0046872]; stearoyl-[acp] desaturase activity [GO:0102786]; stearoyl-CoA 9-desaturase activity [GO:0004768] | PF03405; | 1.10.620.20; | Fatty acid desaturase type 2 family | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250|UniProtKB:P22337}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + hexadecanoyl-[ACP] + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = (4Z)-hexadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:38043, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:11488, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:78483, ChEBI:CHEBI:85919; EC=1.14.19.11; Evidence={ECO:0000269|PubMed:21436056}; CATALYTIC ACTIVITY: Reaction=2 H(+) + O2 + octadecanoyl-[ACP] + 2 reduced [2Fe-2S]-[ferredoxin] = (9Z)-octadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:11776, Rhea:RHEA-COMP:9656, Rhea:RHEA-COMP:9924, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:78495, ChEBI:CHEBI:78783; EC=1.14.19.2; Evidence={ECO:0000269|PubMed:21436056}; | null | PATHWAY: Lipid metabolism; fatty acid metabolism. | null | null | FUNCTION: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain. Converts palmitoyl-ACP to (4Z)-hexadec-4-enoyl-ACP by introduction of a cis double bond between carbons 4 and 5 of the acyl chain. Catalyzes the desaturation of saturated fatty acid 18:0 and 16:0 to generate 18:1 (delta-9) and 16:1 (delta-4) intermediates, expected to give rise to 9-alkenes and 12-alkenes, respectively. {ECO:0000269|PubMed:21436056}. | Ophrys sphegodes (Early spider orchid) (Arachnites aranifera) |
E3Q1H1 | GNA1_TRYBB | MTDIVDLELRVLEESDLSSHLELLGHLTEAPPLSGVELANIADMRRRAGIVTKVFCHQPTGRIVGSASLMIQPKFTRGGRAVGHIEDVVVDPSYRGAGLGKALIMDLCEISRSKGCYKVILDSSEKSLPFYEKLGFRAHERQMRLDL | 2.3.1.4 | null | poly-N-acetyllactosamine biosynthetic process [GO:0030311]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; glycosome [GO:0020015]; Golgi apparatus [GO:0005794] | glucosamine 6-phosphate N-acetyltransferase activity [GO:0004343]; identical protein binding [GO:0042802]; monosaccharide binding [GO:0048029]; protein homodimerization activity [GO:0042803] | PF00583; | 3.40.630.30; | Acetyltransferase family, GNA1 subfamily | PTM: Contains poly-N-acetyllactosamines. {ECO:0000269|PubMed:21531872}. | SUBCELLULAR LOCATION: Glycosome {ECO:0000269|PubMed:21531872}. Note=Predominantly located in glycosome microbodies in the bloodstream form of T.brucei. {ECO:0000269|PubMed:21531872}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate; Xref=Rhea:RHEA:10292, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=2.3.1.4; Evidence={ECO:0000255|RuleBase:RU365086, ECO:0000269|PubMed:21531872}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=144 uM for glucosamine 6-phosphate (at pH 7.2 and room temperature) {ECO:0000269|PubMed:21531872}; KM=234 uM for acetyl-CoA (at pH 7.2 and room temperature) {ECO:0000269|PubMed:21531872}; | PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2. {ECO:0000255|RuleBase:RU365086, ECO:0000269|PubMed:21531872}. | null | null | FUNCTION: Involved in the biosynthesis of UDP-N-acetyl-alpha-D-glucosamine. Catalyzes the formation of N-acetyl-D-glucosamine 6-phosphate from acetyl-coenzyme A (acetyl-CoA) and D-glucosamine 6-phosphate. {ECO:0000269|PubMed:21531872}. | Trypanosoma brucei brucei |
E3SCZ8 | BIRC5_CAVPO | MGAPSLPRAWQLYLKEHRVSTFKNWPFVNGCSCTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDNPIEEHKKHSSGCAFLSVKKQFEELTLSEFLKLDKERAKNKIAKETNSKQKEFEETAAKVRQAMEQLAALE | null | null | apoptotic process [GO:0006915]; cell division [GO:0051301]; chromosome segregation [GO:0007059]; meiosis I [GO:0007127]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of apoptotic process [GO:0043066]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]; regulation of mitotic cell cycle [GO:0007346]; regulation of type B pancreatic cell proliferation [GO:0061469]; sensory perception of sound [GO:0007605] | chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; microtubule [GO:0005874]; midbody [GO:0030496]; nucleus [GO:0005634]; spindle midzone [GO:0051233] | cysteine-type endopeptidase inhibitor activity [GO:0004869]; metal ion binding [GO:0046872] | PF00653; | null | IAP family | PTM: Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex, leading to its degradation. Ubiquitination is required for centrosomal targeting. Deubiquitinated by USP35 or USP38; leading to stabilization. {ECO:0000250|UniProtKB:O15392}.; PTM: In vitro phosphorylation at Thr-117 by AURKB prevents interaction with INCENP and localization to mitotic chromosomes. Phosphorylation at Thr-48 by CK2 is critical for its mitotic and anti-apoptotic activities. Phosphorylation at Thr-34 by CDK15 is critical for its anti-apoptotic activity. Phosphorylation at Ser-20 by AURKC is critical for regulation of proper chromosome alignment and segregation, and possibly cytokinesis. {ECO:0000250|UniProtKB:O15392}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954, ECO:0000269|PubMed:21364656}. Nucleus {ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954, ECO:0000269|PubMed:21364656}. Chromosome {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere {ECO:0000269|PubMed:20727954}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:20727954}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O15392}. Midbody {ECO:0000269|PubMed:20727954}. Note=Localizes at the centromeres from prophase to metaphase, at the spindle midzone during anaphase and a the midbody during telophase and cytokinesis. Accumulates in the nucleus upon treatment with leptomycin B (LMB), a XPO1/CRM1 nuclear export inhibitor (PubMed:20727954). Localizes on chromosome arms and inner centromeres from prophase through metaphase. Localizes to kinetochores in metaphase, distributes to the midzone microtubules in anaphase and at telophase, localizes exclusively to the midbody. Colocalizes with AURKB at mitotic chromosomes (By similarity). {ECO:0000250|UniProtKB:O15392, ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954, ECO:0000269|PubMed:21364656}. | null | null | null | null | null | FUNCTION: Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis (PubMed:20627126, PubMed:20727954, PubMed:21364656). Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis (PubMed:20727954). Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules (By similarity). Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis (By similarity). The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules (By similarity). May counteract a default induction of apoptosis in G2/M phase (By similarity). The acetylated form represses STAT3 transactivation of target gene promoters (By similarity). May play a role in neoplasia. Inhibitor of CASP3 and CASP7 (By similarity). Essential for the maintenance of mitochondrial integrity and function (By similarity). {ECO:0000250|UniProtKB:O15392, ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954, ECO:0000269|PubMed:21364656}. | Cavia porcellus (Guinea pig) |
E3VNM4 | TGA10_ARATH | MQGHHQNHHQHLSSSSATSSHGNFMNKDGYDIGEIDPSLFLYLDGQGHHDPPSTAPSPLHHHHTTQNLAMRPPTSTLNIFPSQPMHIEPPPSSTHNTDNTRLVPAAQPSGSTRPASDPSMDLTNHSQFHQPPQGSKSIKKEGNRKGLASSDHDIPKSSDPKTLRRLAQNREAARKSRLRKKAYVQQLESCRIKLTQLEQEIQRARSQGVFFGGSLIGGDQQQGGLPIGPGNISSEAAVFDMEYARWLEEQQRLLNELRVATQEHLSENELRMFVDTCLAHYDHLINLKAMVAKTDVFHLISGAWKTPAERCFLWMGGFRPSEIIKVIVNQIEPLTEQQIVGICGLQQSTQEAEEALSQGLEALNQSLSDSIVSDSLPPASAPLPPHLSNFMSHMSLALNKLSALEGFVLQADNLRHQTIHRLNQLLTTRQEARCLLAVAEYFHRLQALSSLWLARPRQDG | null | null | anther development [GO:0048653]; DNA-templated transcription [GO:0006351]; hydrogen peroxide mediated signaling pathway [GO:0071588]; response to molecule of bacterial origin [GO:0002237] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; protein homodimerization activity [GO:0042803]; transcription cis-regulatory region binding [GO:0000976] | PF00170;PF14144; | 1.20.5.170; | BZIP family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:20805327}. | null | null | null | null | null | FUNCTION: Together with TGA9, basic leucine-zipper transcription factor required for anther development, probably via the activation of SPL expression in anthers and via the regulation of genes with functions in early and middle tapetal development (PubMed:20805327). Required for signaling responses to pathogen-associated molecular patterns (PAMPs) such as flg22 that involves chloroplastic reactive oxygen species (ROS) production and subsequent expression of H(2)O(2)-responsive genes (PubMed:27717447). {ECO:0000269|PubMed:20805327, ECO:0000269|PubMed:27717447}. | Arabidopsis thaliana (Mouse-ear cress) |
E3VWI2 | G3P2_STRAE | MTVRIGINGFGRIGRNVFRAAAARSSELEIVAVNDLGDVPTMAHLLAYDSILGRFPEEVTAEPGAIRVGDRTIKVLAERDPGALPWGDLGVDIVIESTGIFTDAAKARSHVDGGAKKVIIAAPASGEDFTVVLGVNDGDYDPERHTIISNASCTTNCLGVLAKVLHDAVGIDSGMMTTVHAYTQDQNLQDAPHKDLRRARAAALNIVPTSSGAAKAIGLVLPELAGRLDAFALRVPVPTGSVTDLTVTTRRGTSVEEVKEAYAAAASGPYKGLLSYVDAPLVSTDIVGDPASCVFDAGLTRVSGPQVKVVGWYDNEWGYSNRLIDLATLIGSSL | 1.2.1.12 | null | glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096] | cytosol [GO:0005829] | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; NAD binding [GO:0051287]; NADP binding [GO:0050661] | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000269|PubMed:6822480}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=110 uM for NAD (at pH 8 and 26 degrees Celsius) {ECO:0000269|PubMed:6822480}; KM=250 uM for G3P (at pH 8 and 26 degrees Celsius) {ECO:0000269|PubMed:6822480}; | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}. | null | null | FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. {ECO:0000269|PubMed:6822480}. | Streptomyces arenae |
E3W9M2 | AA5GT_DIACA | MNMSCKFEIVLLVSWWLLLVLVFGVESSMFSEFDRLDFPKHFIFGASSCAYQVEGAAFEDGRTLSTFDIAAHSGHLPGNGDITSDEYHKYKEDVELMVETGLDAYRFSISWSRLIPNGRGPVNPKGLEYYNNLVNALLTKGTQPHVTLLHSDLPQALRDEYGGLFISPKFIDDFVAYADVCFREFGDRVLHWTTFNEANFLAFGDENTPASALYLSAHHLLLAHASATRLYRENYQASQRGFIGINVYAYDFIPETNTEVDVIAAKRARDFFIGWFVQPLMNGEYPLTMRKNGGPRLPKFTPNETELLTGSYDFIGLNYYTAKTVKDDPVMLTVEPRNYYTDQGLISSYLGNIDPYQGHPFFNTPWGLHDVLQQFKQVYGNPPVYIHENGEVGDHDADYDKLINDIPRVEYLQGHIRAVLDAVRNGSNVKGYFVWSFLDMYELMYGTKFTFGLYYIDFNDPKLTRHPKLSQKWYSRFLKGEKASTKASIHTPNEAETHTYFY | 2.4.1.299 | null | anthocyanin-containing compound biosynthetic process [GO:0009718]; carbohydrate metabolic process [GO:0005975]; pigmentation [GO:0043473] | plant-type vacuole [GO:0000325] | beta-glucosidase activity [GO:0008422]; cyanidin 3-O-glucoside 5-O glucosyltransferase (vanilloyl-glucose dependent) activity [GO:0102458]; cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose dependent) activity [GO:0102506]; delphinidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose dependent) activity [GO:0102512]; hexosyltransferase activity [GO:0016758]; pelargonidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose dependent) activity [GO:0102510] | PF00232; | 3.20.20.80; | Glycosyl hydrolase 1 family | null | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:20971893}. | CATALYTIC ACTIVITY: Reaction=1-O-(trans-sinapoyl)-beta-D-glucose + cyanidin 3-O-beta-D-glucoside = (E)-sinapate + cyanidin 3,5-di-O-beta-D-glucoside; Xref=Rhea:RHEA:35427, ChEBI:CHEBI:16546, ChEBI:CHEBI:30023, ChEBI:CHEBI:71511, ChEBI:CHEBI:77857; EC=2.4.1.299; Evidence={ECO:0000269|PubMed:20971893}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 mM for cyanidin 3-glucopyranoside (with native enzyme at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:20971893}; KM=46.5 mM for 1-O-beta-D-vanillyl-glucose (with native enzyme at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:20971893}; KM=6.5 mM for cyanidin 3-glucopyranoside (with recombinant enzyme at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:20971893}; KM=51.9 mM for 1-O-beta-D-vanillyl-glucose (with recombinant enzyme at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:20971893}; Note=kcat is 0.06 sec(-1) with cyanidin 3-glucopyranoside (with native enzyme at pH 5.0 and 30 degrees Celsius). kcat is 0.01 sec(-1) with 1-O-beta-D-vanillyl-glucose (with native enzyme at pH 5.0 and 30 degrees Celsius). kcat is 0.07 sec(-1) with cyanidin 3-glucopyranoside (with recombinant enzyme at pH 5.0 and 30 degrees Celsius). kcat is 0.01 sec(-1) with 1-O-beta-D-vanillyl-glucose (with recombinant enzyme at pH 5.0 and 30 degrees Celsius).; | PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis. {ECO:0000269|PubMed:20971893}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-5.0. {ECO:0000269|PubMed:20971893}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 48 degrees Celsius. {ECO:0000269|PubMed:20971893}; | FUNCTION: Beta-glycosidase that catalyzes the transfer of glucose moiety to anthocyanidin 3-glucoside at the 5 position. Anthocyanins are ubiquitous colored pigments that are responsible for variations in petal color. Uses acyl-glucoses, but not UDP-glucose, as the glucose donor. {ECO:0000269|PubMed:20971893}. | Dianthus caryophyllus (Carnation) (Clove pink) |
E3W9M3 | AA7GT_DELGR | MCPSFLVTLLLLQLSSLVVVLVVWAEQLPEFNVRRDDFPSNFVFGAGTSALQVEGAIAEDGKTPNIWDVDSHMGHMPDKSTTDIACDSYHRYKEDVKIMSDIGLEAYRFSIAWTRILPYGRGFINPKGVEYYNNLIDTLLEHGIQPHATIYHIDHPQILEDEYGGWLSPRMIEDFTTYADVCFREFGDRVSHWTTINEPNIISLGAYDSGQIPPHRCTPPGAYNCTAGNSSVEPYKAMHHFLLAHASAVQIYRTKYQAKQKGLIGLNVYGFWCAPQTNSRADIEATKRATAFYTGWAADPLVFGDYPIIMKENVGSRLPSFTKNESELVKGSFDFIGLNHYFVFYIQDDPEEITTPISLRNFDSDMRVKASVKPGDSGDPSGLKNLLRYFKDNYGNPPVYVHENGFGSPQNETLDDDMGRIRYISGYIGSMLEAIKNGSDTRGYFVWSFMDAFEILSGYQTRYGIVHVDFDDKSLKRQLKPSAQWYSNFIKKKNTTEDEISYSSQ | 2.4.1.300 | null | anthocyanin-containing compound biosynthetic process [GO:0009718]; carbohydrate metabolic process [GO:0005975] | plant-type vacuole [GO:0000325] | beta-glucosidase activity [GO:0008422]; cyanidin 3-O-glucoside 7-O-glucosyltransferase (feruloyl-glucose dependent) activity [GO:0102514]; cyanidin 3-O-glucoside 7-O-glucosyltransferase (hydroxybenzoly-glucose dependent) activity [GO:0102507]; cyanidin 3-O-glucoside 7-O-glucosyltransferase (vanilloyl-glucose dependent) activity [GO:0102457]; hexosyltransferase activity [GO:0016758]; pelargonidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose dependent) activity [GO:0102511] | PF00232; | 3.20.20.80; | Glycosyl hydrolase 1 family | null | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:20971893}. | CATALYTIC ACTIVITY: Reaction=1-O-(4-hydroxy-3-methoxybenzoyl)-beta-D-glucose + cyanidin 3-O-beta-D-glucoside = cyanidin 3,7-di-O-beta-D-glucoside + vanillate; Xref=Rhea:RHEA:35431, ChEBI:CHEBI:16632, ChEBI:CHEBI:71512, ChEBI:CHEBI:71513, ChEBI:CHEBI:77857; EC=2.4.1.300; Evidence={ECO:0000269|PubMed:20971893}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=22.9 mM for cyanidin 3-glucopyranoside (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:20971893}; KM=260.8 mM for 1-O-beta-D-vanillyl-glucose (at pH 5.0 and 30 degrees Celsius) {ECO:0000269|PubMed:20971893}; Note=kcat is 0.17 sec(-1) with cyanidin 3-glucopyranoside (at pH 5.0 and 30 degrees Celsius). kcat is 0.10 sec(-1) with 1-O-beta-D-vanillyl-glucose (at pH 5.0 and 30 degrees Celsius).; | PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis. {ECO:0000269|PubMed:20971893}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0.; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:20971893}; | FUNCTION: Beta-glycosidase that catalyzes the transfer of glucose moiety to anthocyanidin 3-glucoside at the 7 position. Anthocyanins are ubiquitous colored pigments that are responsible for variations in petal color. {ECO:0000269|PubMed:20971893}. | Delphinium grandiflorum (Siberian larkspur) (Delphinium sinense) |
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