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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F5HSE3 | NIPLA_DANRE | MNGDMPHVPITTLAGIAGLTDLLNQLPLPSPLPGTTTKSLLYNGRVAEDVGHLLGCRDETLVSQLANSLSQVSTEHIELKDSLGSDELEGDVPVLLQLLMSRNPNIFRNKTAPNTPQYPAQAGISQQSMAPPYKITHGSMQGSPASANYQQASMSHSPSGHFVPGQSGPGGRFLPQQGSPVPSPYAPQSPATGYRQYPHPPAYSQHQHLQQGSVASPMIPGAMRNVHENKDQMRMGFTSHLLQSSPPYTPPCDGTKDLHLGSQDKQRGQKSSEGEQDSPDKATVYDIVGSPAKDHTKLILRPSRARPAEVELGGMYPGSDPEGELVEALAAIERMESEAAMETERSAKEVQDKDKPLKKRKQDSHPQEPGAAGTAGSGSGAPGGGGGANAGHRLAPQEASAAGTSASRPGLQVSLEQAGRVEDDCMGMPIPASEAQRWPQEPQEGVTPKAVKHEHDHDPEHPHYDDKQPDTPRQKHRPEGRHGDGGAQRAAVQSGSKQVELPPYMLGENTGVLKNFTIPKIRKGELGGGDIPEGWKQPCVRLERLEADVDVKKSVKPVVVLQKLSIDEVQRLMRERDSRASKSGKNRLSSGRSGKGGIDPSVLKDLPPELLAEIESTMPLCERVKMNKRKRSTVNERPKYAEDSSEDEEFSSRKRQRKDRDRTWEAEERDRRSSGEHRRGNFDARRGSGSRYDDSDQDSPPPSLNEVARRLKMKQKKRKVYEPKLTPEEMMDSSTFKRFTLSIDNILENLEDVDFTAQDDDEIPQELLLGKQQLNELGSESAKIKAMGITSRIPSDKLVKLLNILEKNILDGASLSTLMNLDNEGEDEERLWRDLIMERVTKSADACLTALNIMTSTHMPKAVYIEDVIERVLQYTKFHLQNTLYPQYDPVYRVNPKGGSMLSSRAKRAKCSTAKQKVIIMLYNKVCDVVSNISELLEIQLMTDTTILQVSSMGITPFFVENVSELQLCAIKLVTAVFSRYEKHRQLILEEIFTSLARLPTSKRSLRNFRLNSSDDEGEPIYIQMVSALVLQLIQCVVHLPADRDSEDDHKKVDDDVFITNSYETARRTAQNFLSVFLKKCGSKQGEEDYRPLFENFVQDLLSTVNKPDWPASELLLSLLGRLLVHQFSNKQTEMALRVASLDYLGTVAARLRKDSVTSRMDQKAIERIIRENTEGDETQRLQKALLDYMDENAETDPALAFARKFYIAQWFRDCTTETEKAMRSQNQKEDDSDGAQHAKELQATGDIMQRAETRKKFLHSVVKSTPNQFTTLRMNSDTVDYDDACLIVRYLASTRPFSQSFDIYLTQILRVLGESAIAVRTKAMKCLSEVVAVDPSILARSDMQRGVHGRLMDNSTSVREAAVELLGRFVLSRPQLTEQYYDMLIERILDTGISVRKRVIKILRDICLEQPNFSKITEMCVKMIRRVNDEEGIKKLVNETFQKLWFTPTPNHDKETMNRKILNITDVVSACKDTGYDWFEQLLQNLLKSEEDSSYKPTRKACVQLVDNLVEHILKYEEALAEHKSVNSTRLVACITTLYLFSKIRAQLMVKHAMTMQPYLTTKCSSQSDFMVICNVAKILELVVPLMDHPSESFLTTIEEDLMKLILKYGMTVVQYCVSCLGAIVNKVTHNYKFVWACFNRYYGALTKLKVQHQEGTNSMALAATKAALLRSLFTAGALCRHFDFDLEQFKGTTKVVIKEKVLELLLYFTNHEDEEVKCKAIIGLGFLFIMHPSQMFVPEVKTLYNGLLSDKRSSITLKIQVLKNLQMYLQEEDTRMQEADREWQKLSKQEDLKEMGDISSGMSSSIMQLYLKQVLESFFHAQSSVRHFALNVIALTLSQGLIHPVQCVPYLIAMGTDAEPTMRNKADQQLVEIDKKYTGFIHMKAVAGMKMSYQVQQAVFGSAGSVIRGFRQDESNSAQCSHLYSMVRANRQHRRAFLISLLNLFDDSSKMEVNMLLFIADNLAYFPYQSQEEPLFIMHHIDITLSVSGSNLLQTFKESLVKIPGRKSRKRRRRRRRPQRQQPPPPPPQQQQQQNGSEEERGAQDEERERHSGDEEYDDDDYEEDEDGHRVRKPKPTEDIRQSESDSDSDLDDVDAVMERLPDDSTSLVDFARASQGILLLLVLKQHLKNLYGFSDGKIQKYSPSESAKVYDKAVNRKTLANFNPQQTIDFLRHHDVHGELTYELKRKIVKQFLDFKLLMEHLDPDEEDEDGDTSANVRNKAITALLGGAAASPRNHHTGDSEEDDERSEGEERTPGASRRGRRTGDSADLLSANMNESVSALDIIAIHCPKYRDRPQIARVIQKNSDGYSIHWMAGSYSSTWAEAKKRDGRKLVPWVDSIKETDIIYKKITLTSGNKLNHKVAQTLRSLYAAKDRNSS | null | null | brain development [GO:0007420]; digestive tract development [GO:0048565]; embryonic pectoral fin morphogenesis [GO:0035118]; embryonic viscerocranium morphogenesis [GO:0048703]; establishment of mitotic sister chromatid cohesion [GO:0034087]; establishment of protein localization to chromatin [GO:0071169]; heart development [GO:0007507]; heart jogging [GO:0003146]; heart morphogenesis [GO:0003007]; mitotic cohesin loading [GO:0061780]; mitotic sister chromatid cohesion [GO:0007064]; regulation of gene expression [GO:0010468]; replication-born double-strand break repair via sister chromatid exchange [GO:1990414] | Scc2-Scc4 cohesin loading complex [GO:0090694] | chromatin binding [GO:0003682]; chromatin loop anchoring activity [GO:0140587] | PF12765;PF12830; | 1.25.10.10; | SCC2/Nipped-B family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6KCD5}. | null | null | null | null | null | FUNCTION: May play a structural role in chromatin. Involved in sister chromatid cohesion, possibly by facilitating the cohesin complex loading. Transcription factor, which may promote cortical neuron migration during brain development by regulating the transcription of crucial genes in this process (By similarity). {ECO:0000250|UniProtKB:Q6KCD5, ECO:0000269|PubMed:22039349}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F6NXI9 | TRNT1_DANRE | MWAKLFLRPSFVNRVHLTWSCRALLTMQLKTKEFESLFTDGLVGLAEIFQKNQFELRIAGGAVRDLLSGKRPEDVDFATTATPEEMKSMFQTAGVRMINNKGEKHGTITARLHEENFEVTTLRVDVQTDGRHAEVEFTTDWQKDAERRDLTINSMFLGLDGTLYDYFQGYEDLKNRKVRFVGSASLRIQEDYLRILRYFRFYGRVAAEPGQHEPETLEAIRENARGLAGISGERIWVELKKMLVGNHAGHLLELVYELGLAQYTGLPADGDVEEMKQVWQRAHVSSPKPMTVLAALFRKQADVENLDQRLKVSREEKNLGLFLVKYRRDLVKGHDEHDTMKPYTDFITDSREPDTQSKVLELLKYQGENKLLDELRRWSIPRFPVSGHDLRKLGYTSGKEIGTILQELRDMWKKSRYQMSKDELLSTLSQS | 2.7.7.72 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O66728}; | eye development [GO:0001654]; mitochondrial tRNA 3'-end processing [GO:1990180]; thigmotaxis [GO:0001966]; tRNA 3'-terminal CCA addition [GO:0001680]; tRNA processing [GO:0008033]; visual behavior [GO:0007632] | mitochondrion [GO:0005739]; nucleus [GO:0005634] | ATP binding [GO:0005524]; CCA tRNA nucleotidyltransferase activity [GO:0004810]; CCACCA tRNA nucleotidyltransferase activity [GO:0160016]; metal ion binding [GO:0046872]; tRNA binding [GO:0000049] | PF01743;PF12627; | 3.30.460.10;1.10.3090.10; | TRNA nucleotidyltransferase/poly(A) polymerase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q96Q11}. Cytoplasm {ECO:0000250|UniProtKB:Q96Q11}. Nucleus {ECO:0000250|UniProtKB:Q96Q11}. | CATALYTIC ACTIVITY: Reaction=a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate; Xref=Rhea:RHEA:14433, Rhea:RHEA-COMP:10465, Rhea:RHEA-COMP:10468, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74896, ChEBI:CHEBI:83071; EC=2.7.7.72; Evidence={ECO:0000250|UniProtKB:Q96Q11}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14434; Evidence={ECO:0000250|UniProtKB:Q96Q11}; CATALYTIC ACTIVITY: Reaction=a tRNA with a 3' CCA end + ATP + 2 CTP = a tRNA with a 3' CCACCA end + 3 diphosphate; Xref=Rhea:RHEA:76235, Rhea:RHEA-COMP:10468, Rhea:RHEA-COMP:18655, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:83071, ChEBI:CHEBI:195187; Evidence={ECO:0000250|UniProtKB:Q96Q11}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76236; Evidence={ECO:0000250|UniProtKB:Q96Q11}; | null | null | null | null | FUNCTION: Nucleotidyltransferase that catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs, which is necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates (PubMed:26494905). tRNA 3'-terminal CCA addition is required both for tRNA processing and repair (By similarity). Promotes tRNA repair and recycling downstream of the ribosome-associated quality control (RQC) pathway by mediating addition of the tRNA 3'-terminal CCA following cleavage by ankzf1 and repair by elac1 (By similarity). Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs and tRNA-like transcripts (By similarity). While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs beginning with GG are marked with CCACCA and rapidly degraded (By similarity). The structural flexibility of RNA controls the choice between CCA versus CCACCA addition: following the first CCA addition cycle, nucleotide-binding to the active site triggers a clockwise screw motion, producing torque on the RNA (By similarity). This ejects stable RNAs, whereas unstable RNAs are refolded while bound to the enzyme and subjected to a second CCA catalytic cycle (By similarity). {ECO:0000250|UniProtKB:Q96Q11, ECO:0000269|PubMed:26494905}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F6Q1T7 | FUT1_BOVIN | MWAPGHHHLCLIFLLTCVFACVFFLLIHQNLFHSGLDLFLPCPDRSRVRSPVAILCLSGTLMNPNATFTCPRHSASVSGTWTIDPKGRFGNQMGQYATLLALAQLNGRQAFIQPSMHAVLAPVFRITLPVLAPEVDRHAPWQELELHDWMSEEYAHLKEPWLKLTGFPCSWTFFHHLRDQIRSEFTLHEHLRQEAQRSLSGLRFPRTGGRPSTFVGVHVRRGDYLQVMPLHWKGVVGDRAYLQQAMDWFRARHKAPIFVVTSNGMKWCRENIDTSRGDVIFAGDGQEGAPNKDFALLTQCNHTIMTIGTFGFWAAYLAGGDTIYLANFTLPDSSFLKIFKPEAAFLPEWVGINADLSPLQ | 2.4.1.344; 2.4.1.69 | null | carbohydrate metabolic process [GO:0005975]; fucosylation [GO:0036065]; lipid metabolic process [GO:0006629]; olfactory bulb development [GO:0021772]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell-matrix adhesion via fibronectin [GO:1904906]; positive regulation of sprouting angiogenesis [GO:1903672]; protein glycosylation [GO:0006486] | Golgi cisterna membrane [GO:0032580] | alpha-(1,2)-fucosyltransferase activity [GO:0031127]; galactoside 2-alpha-L-fucosyltransferase activity [GO:0008107] | PF01531; | null | Glycosyltransferase 11 family | null | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:O09160}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O09160}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250|UniProtKB:O09160}. | CATALYTIC ACTIVITY: Reaction=a ganglioside GM1 + GDP-beta-L-fucose = a ganglioside Fuc-GM1 + GDP + H(+); Xref=Rhea:RHEA:48292, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:82639, ChEBI:CHEBI:90189; Evidence={ECO:0000269|PubMed:10814703}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48293; Evidence={ECO:0000305|PubMed:10814703}; CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:50668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133507, ChEBI:CHEBI:133510; EC=2.4.1.344; Evidence={ECO:0000250|UniProtKB:P19526}; CATALYTIC ACTIVITY: Reaction=a ganglioside GA1 + GDP-beta-L-fucose = a ganglioside Fuc-GA1 + GDP + H(+); Xref=Rhea:RHEA:48320, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:88069, ChEBI:CHEBI:90262; Evidence={ECO:0000250|UniProtKB:O09160}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48321; Evidence={ECO:0000250|UniProtKB:O09160}; CATALYTIC ACTIVITY: Reaction=a beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer(d18:1(4E)) + GDP-beta-L-fucose = alpha-L-fucosyl-(1->2)- beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + GDP + H(+); Xref=Rhea:RHEA:32175, ChEBI:CHEBI:15378, ChEBI:CHEBI:17292, ChEBI:CHEBI:28743, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189; EC=2.4.1.69; Evidence={ECO:0000250|UniProtKB:O09160}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32176; Evidence={ECO:0000250|UniProtKB:O09160}; CATALYTIC ACTIVITY: Reaction=a neolactoside nLc4Cer(d18:1(4E)) + GDP-beta-L-fucose = a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:1(4E)) + GDP + H(+); Xref=Rhea:RHEA:48304, ChEBI:CHEBI:15378, ChEBI:CHEBI:17006, ChEBI:CHEBI:28691, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:O09160}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48305; Evidence={ECO:0000250|UniProtKB:O09160}; CATALYTIC ACTIVITY: Reaction=beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + GDP-beta-L-fucose = alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + GDP + H(+); Xref=Rhea:RHEA:62964, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:84728, ChEBI:CHEBI:546807; Evidence={ECO:0000269|PubMed:10814703}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62965; Evidence={ECO:0000305|PubMed:10814703}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.26 uM for Galacto-N-biose {ECO:0000269|PubMed:10814703}; KM=1.29 uM for ganglioside GM1a {ECO:0000269|PubMed:10814703}; Vmax=48.6 pmol/min/mg enzyme towards Galacto-N-biose {ECO:0000269|PubMed:10814703}; Vmax=58.5 pmol/min/mg enzyme towards ganglioside GM1a {ECO:0000269|PubMed:10814703}; | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P19526}. | null | null | FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose residue of glycoconjugates through an alpha(1,2) linkage leading to H antigen synthesis that is an intermediate substrate in the synthesis of ABO blood group antigens (PubMed:10814703). H antigen is essential for maturation of the glomerular layer of the main olfactory bulb, in cell migration and early cell-cell contacts during tumor associated angiogenesis (By similarity). Preferentially fucosylates soluble lactose and to a lesser extent, fucosylates glycolipids gangliosides GA1 and GM1a (PubMed:10814703). {ECO:0000250|UniProtKB:O09160, ECO:0000269|PubMed:10814703}. | Bos taurus (Bovine) |
F6RG56 | MCLN3_CALJA | MANPEIVISSCSSHEEENRCNFNQHTSPSEELLLEDQMRRKLKFFFMNPCEKFWARGRKPWKLAIQILKIAMVTIQLVLFGLSNQMVVAFKEENTVAFKHLFLKGYIDRMDDTYAVYTQSDVYDQIIFAVNQYLQLYNVSVGNHAYENKGTDQSAMAICQHFYKRGNIYPGNDTFDIDPEIETDCFFVEPDEPFHIGTPAENKLNLTLDFHRLLTVELQFKLKAINLQTVRHQELPDCYDFTLTITFDNKAHSGRIKISLDNDISIRECKDWHVSGSIQKNTHNMMIFDAFVILTCLVSLILCIRSVISGLQLQQEFVNFFLLHYKKDVSVSDQMEFVNGWYIMIIISDILTIIGSILKMEIQAKSLTSYDVCSILLGTSTMLVWLGVIRYLGFFAKYNLLILTLQAALPNVIRFCCCAAMIYLGYCFCGWIVLGPYHNKFRSLNMVSECLFSLINGDDMFATFAKMQQKSYLVWLFSRIYLYSFISLFIYMILSLFIALITDTYETIKHYQQDGFPETELRTFISECKDLPNSGKFRLEDDPPVSLFCCCKK | null | null | monoatomic cation transmembrane transport [GO:0098655]; protein homotetramerization [GO:0051289] | autophagosome membrane [GO:0000421]; early endosome membrane [GO:0031901]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; stereocilium membrane [GO:0060171] | identical protein binding [GO:0042802]; intracellularly phosphatidylinositol-3,5-bisphosphate-gated monatomic cation channel activity [GO:0097682]; NAADP-sensitive calcium-release channel activity [GO:0072345]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025] | PF21381;PF08016; | 1.10.287.70; | Transient receptor (TC 1.A.4) family, Polycystin subfamily, MCOLN3 sub-subfamily | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8TDD5}. | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:29019979}; Multi-pass membrane protein {ECO:0000269|PubMed:29019979}. Early endosome membrane {ECO:0000250|UniProtKB:Q8TDD5}; Multi-pass membrane protein {ECO:0000269|PubMed:29019979}. Late endosome membrane {ECO:0000250|UniProtKB:Q8R4F0}; Multi-pass membrane protein {ECO:0000269|PubMed:29019979}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q8R4F0}; Multi-pass membrane protein {ECO:0000269|PubMed:29019979}. Cell projection, stereocilium membrane {ECO:0000250|UniProtKB:Q8R4F0}; Multi-pass membrane protein {ECO:0000269|PubMed:29019979}. Note=Recycles between the plasma membrane and intracellular compartments by a dynamin-dependent endocytic pathway (By similarity). In the cochlea located at the base of stereocilia near the position of the ankle links (By similarity). {ECO:0000250|UniProtKB:Q8R4F0, ECO:0000250|UniProtKB:Q8TDD5}. | null | null | null | null | null | FUNCTION: Nonselective ligand-gated cation channel probably playing a role in the regulation of membrane trafficking events (PubMed:29019979). Acts as a Ca(2+)-permeable cation channel with inwardly rectifying activity (By similarity). Mediates release of Ca(2+) from endosomes to the cytoplasm, contributes to endosomal acidification and is involved in the regulation of membrane trafficking and fusion in the endosomal pathway (By similarity). Does not seem to act as mechanosensory transduction channel in inner ear sensory hair cells. Proposed to play a critical role at the cochlear stereocilia ankle-link region during hair-bundle growth. Involved in the regulation of autophagy. Through association with GABARAPL2 may be involved in autophagosome formation possibly providing Ca(2+) for the fusion process (By similarity). Through a possible and probably tissue-specific heteromerization with MCOLN1 may be at least in part involved in many lysosome-dependent cellular events. Possible heteromeric ion channel assemblies with TRPV5 show pharmacological similarity with TRPML3 (By similarity). {ECO:0000250|UniProtKB:Q8R4F0, ECO:0000250|UniProtKB:Q8TDD5}. | Callithrix jacchus (White-tufted-ear marmoset) |
F6SEU4 | SYGP1_MOUSE | MSRSRASIHRGSIPAMSYAPFRDVRGPPMHRTQYVHSPYDRPGWNPRFCIISGNQLLMLDEDEIHPLLIRDRRSESSRNKLLRRTVSVPVEGRPHGEHEYHLGRSRRKSVPGGKQYSMEAAPAAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLDEDSIIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDMLYARTTSKPRSASGDTVFWGEHFEFNNLPAVRALRLHLYRDSDKKRKKDKAGYVGLVTVPVATLAGRHFTEQWYPVTLPTGSGGSGGMGSGGGGGSGGGSGGKGKGGCPAVRLKARYQTMSILPMELYKEFAEYVTNHYRMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMEREHLIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASSLAEHQANLRMCCELALCKVVNSHCVFPRELKEVFASWRLRCAERGREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEALLKLGPLPRLLNDISTALRNPNIQRQPSRQSERTRSQPMVLRGPSAEMQGYMMRDLNSSIDLQSFMARGLNSSMDMARLPSPTKEKPPPPPPGGGKDLFYVSRPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGDGPGGRLNSSSVSNLAAVGDLLHSSQASLTAALGLRPAPAGRLSQGSGSSITAAGMRLSQMGVTTDGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSSGHGPPSSHHHHHHHHHHRGGEPPGDTFAPFHGYSKSEDLSSGVPKPPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQITIGPQRPAPSGPGGGSGGGSGGGQPPPLQRGKSQQLTVSAAQKPRPSSGNLLQSPEPSYGPARPRQQSLSKEGSIGGSGGSGGGGGGGLKPSITKQHSQTPSTLNPTMPASERTVAWVSNMPHLSADIESAHIEREEYKLKEYSKSMDESRLDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQERQLPPLGPTNPRVTLAPPWNGLAPPAPPPPPRLQITENGEFRNTADH | null | null | axonogenesis [GO:0007409]; dendrite development [GO:0016358]; maintenance of postsynaptic specialization structure [GO:0098880]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of axonogenesis [GO:0050771]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of Ras protein signal transduction [GO:0046580]; neuron apoptotic process [GO:0051402]; pattern specification process [GO:0007389]; Ras protein signal transduction [GO:0007265]; receptor clustering [GO:0043113]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of MAPK cascade [GO:0043408]; regulation of synapse structure or activity [GO:0050803]; regulation of synaptic plasticity [GO:0048167]; visual learning [GO:0008542] | dendritic shaft [GO:0043198]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic density, intracellular component [GO:0099092]; synapse [GO:0045202] | GTPase activator activity [GO:0005096]; protein kinase binding [GO:0019901]; SH3 domain binding [GO:0017124] | PF00168;PF12004;PF00616; | 2.60.40.150;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Synapse {ECO:0000250}. Note=Mostly in excitatory glutamatergic synapses (By similarity). receptor activation or SYNGAP1/MPDZ complex disruption. Phosphorylation by PLK2 promotes its activity (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Major constituent of the PSD essential for postsynaptic signaling. Inhibitory regulator of the Ras-cAMP pathway. Member of the NMDAR signaling complex in excitatory synapses, it may play a role in NMDAR-dependent control of AMPAR potentiation, AMPAR membrane trafficking and synaptic plasticity. Regulates AMPAR-mediated miniature excitatory postsynaptic currents. Exhibits dual GTPase-activating specificity for Ras and Rap. May be involved in certain forms of brain injury, leading to long-term learning and memory deficits (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
F6SZT2 | KHDC3_MACMU | MDTPRRFPTLVQLMQPKAMPVEVLGHLPKRFSWFHSEFLKNPKVVRLEVWLVEKIFGRDRERIPHVQGMSQILIHVNRLDPNGEAEILVFGRPSYQEDTIKMIMNLADYHRQLQAKGSGKALAQDVATKKAEIQLSSTEVREAGTQRSVEVREVGTQGSPVEVRETGTQQSLEAANQSGTQRSPEAASKAVTQRFSEDTRAPVTRL | null | null | positive regulation of dendrite development [GO:1900006]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of neurogenesis [GO:0050769]; regulation of protein localization [GO:0032880] | cell cortex [GO:0005938]; centrosome [GO:0005813]; chromosome [GO:0005694]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; subcortical maternal complex [GO:0106333] | RNA binding [GO:0003723] | PF16005; | 3.30.1370.10; | KHDC1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9CWU5}. Nucleus {ECO:0000250|UniProtKB:Q9CWU5}. Mitochondrion {ECO:0000250|UniProtKB:Q9CWU5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9CWU5}. Chromosome {ECO:0000250|UniProtKB:Q587J8}. Note=Localized to centrosomes during interphase and mitosis (By similarity). Localizes to sites of DNA double-strand break repair (By similarity). {ECO:0000250|UniProtKB:Q587J8, ECO:0000250|UniProtKB:Q9CWU5}. | null | null | null | null | null | FUNCTION: As part of the OOEP-KHDC3 scaffold, recruits BLM and TRIM25 to DNA replication forks, thereby promoting the ubiquitination of BLM by TRIM25, enhancing BLM retainment at replication forks and therefore promoting stalled replication fork restart (PubMed:33115731). Regulates homologous recombination-mediated DNA repair via recruitment of RAD51 to sites of DNA double-strand breaks, and sustainment of PARP1 activity, which in turn modulates downstream ATM activation (PubMed:33115731). Activation of ATM or ATR in response to DNA double-strand breaks may be cell-type specific (By similarity). Its role in DNA double-strand break repair is independent of its role in restarting stalled replication forks (By similarity). As a member of the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (By similarity). Required for maintenance of euploidy during cleavage-stage embryogenesis (By similarity). Required for the formation of F-actin cytoplasmic lattices in oocytes which in turn are responsible for symmetric division of zygotes via the regulation of mitotic spindle formation and positioning (By similarity). Ensures proper spindle assembly by regulating the localization of AURKA via RHOA signaling and of PLK1 via a RHOA-independent process (By similarity). Required for the localization of MAD2L1 to kinetochores to enable spindle assembly checkpoint function (By similarity). Promotes neural stem cell neurogenesis and neuronal differentiation in the hippocampus. May regulate normal development of learning, memory and anxiety (By similarity). Capable of binding RNA (By similarity). {ECO:0000250|UniProtKB:D3ZVV1, ECO:0000250|UniProtKB:Q9CWU5, ECO:0000269|PubMed:33115731}. | Macaca mulatta (Rhesus macaque) |
F6TQD1 | RN212_MOUSE | MASWVFCNRCFQSPHRKSSFSLTSCGHVYCHSCLLKGTKNECVICQAPCQTVLLSKHTNSNIQTFFLGIDGLCKKYSQETSQISEFQEKHRRRLVAFYQEKISQLEESLRKSVLQIKQLQSMRSSQQPAFNKIKNSVSTKPNGYLFLPPNSSLPDRIESMDIDLTPPARKPEMSAGPSRISVISPPQDGRMGSVTCRGPQHLSLTPSHASMTKASRVPPLQMPYKELSPPPASQLSSRATQGPSPSVSSSWTGPPRQPISISGLLQRQCAGSASPRGMDTEKMSPFLPSTPTNLRSVASPWHACVHR | 2.3.2.- | null | chiasma assembly [GO:0051026]; homologous chromosome pairing at meiosis [GO:0007129]; meiotic gene conversion [GO:0006311]; protein sumoylation [GO:0016925]; reciprocal meiotic recombination [GO:0007131] | synaptonemal complex [GO:0000795] | metal ion binding [GO:0046872]; SUMO transferase activity [GO:0019789] | PF14634; | 3.30.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associates to the synaptonemal complex. Localizes to a minority of double-strand breaks (DSBs) sites. Marks crossover sites during midpachynema. | null | null | PATHWAY: Protein modification; protein sumoylation. | null | null | FUNCTION: SUMO E3 ligase that acts as a regulator of crossing-over during meiosis: required to couple chromosome synapsis to the formation of crossover-specific recombination complexes. Localizes to recombination sites and stabilizes meiosis-specific recombination factors, such as MutS-gamma complex proteins (MSH4 and MSH5) and TEX11. May mediate sumoylation of target proteins MSH4 and/or MSH5, leading to enhance their binding to recombination sites. Acts as a limiting factor for crossover designation and/or reinforcement and plays an antagonist role with CCNB1IP1/HEI10 in the regulation of meiotic recombination. {ECO:0000269|PubMed:23396135, ECO:0000269|PubMed:24390283}. | Mus musculus (Mouse) |
F6UA42 | UHRF1_XENTR | MWIQVRTMDGRDTRRIDSLSKLTKVEDLRARIQQIFGVALESQRLFYRGKQMENGHTLFDYSVGLNDIVQLLVRQIPDSVPTKDKECGISDADSGCGSGQGESDKNSSCGEGATDVDGQPAGINSENVGPSLYKKNDLVDARDLNMGAWFEAQIVSVSKRVNPDGMSAEILDTSAASDDIIYHVKYEDYPENGVVQLTYKDVRLRARTTLPWHDLKVGQVVMVNYNPDEPKERGYWYDAEILRKRETRTIKEIYVKVLLGDAGDSLNDCRIRFVDEIYKIEEPGSAYITTESPQKRQNGPECKHCKDNPKRACRMCACYVCGGKQDPEKQLLCDECDMAFHIYCLKPPLSAIPQDEDWYCPDCRNDASEVVLAGEKLKESKKKAKMASASSSSQRDWGKGMACVGRSRECTIVPSNHYGPIPGVPVGTLWKFRVQVSESGVHRPHVAGIHGRSNDGSYSLVLAGGYEDDVDNGSEFTYTGSGGRDLSGNKRTAEQSCDQKLTNMNRALALNCSAPINDKEGAVAKDWRAGKPVRVVRNTKGKKHSKYAPEDGNRYDGIYKVVKYWPEKGKSGFLVWRYLLRRDDEEPAPWSKEGKERIKKLGLVMQYPDGYLESLASKEREKENKTEDELSESPSKGKRKRNSAGSGLSDAKSTPKKTKVESYKLSLDQKTLIKQDDLNAKLWREVMSFLKEGPKFLSKVEETFLCICCQEVVYEPITTECHHNICKGCLDRSFKALVHNCPACRHDLGKNYSLNVNKPLQAILSQLFPGYERGR | 2.3.2.27 | null | cell cycle [GO:0007049]; heterochromatin formation [GO:0031507]; negative regulation of gene expression via chromosomal CpG dinucleotide methylation [GO:0044027]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511] | chromatin [GO:0000785]; euchromatin [GO:0000791]; heterochromatin [GO:0000792]; nucleus [GO:0005634]; replication fork [GO:0005657] | hemi-methylated DNA-binding [GO:0044729]; histone binding [GO:0042393]; methylated histone binding [GO:0035064]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF00628;PF02182;PF12148;PF00240; | 2.30.30.1150;2.30.30.140;2.30.280.10;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358}. Note=Localizes to replication foci. Enriched in pericentric heterochromatin. Also localizes to euchromatic regions (By similarity). {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=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits dnmt1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins. However, it is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
F6UH96 | SPRTN_XENTR | MQLSVVDPTWELLDPNPDIRALFLEFNDTFFWGQLSGIEVKWSARMTLCAGVCSYEGRGGLCSIRLSEPLLKLRPRKDLVQTLLHEMIHALLFVTHNNKDHDSHGPEFCKHMERINKRTGANISVYHNFHDEVDEYRKHWWLCNGPCQKRKPYFGYVKRAMNRAPSSLDPWWADHQRTCGGEFVKIKEPENYSQKRKRNNDPTKSELGNSSHVKINKGKSNGVDIRTVIPFSGTGYKLFEPSKSDAQLKIQNDNPTKDKAVMHHTPPSTNQTDSTFLSRKIVSAKKISVANTKVFINLNGSPIKLPSSSNNKSHQDSSKQKSVLHFFKTQKDNSIDLTSSSQSFPSTSQGPNREETEHFYKKLQMDDKESKDTFIIHSLNKTNVSDSLNNKSCAGPAATINSGLNHTKVCCPVCGTEIFESKINDHLDTCLQNYNT | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9H040}; | DNA damage response [GO:0006974]; positive regulation of protein ubiquitination [GO:0031398]; protein autoprocessing [GO:0016540]; protein-DNA covalent cross-linking repair [GO:0106300]; proteolysis [GO:0006508]; response to UV [GO:0009411]; translesion synthesis [GO:0019985] | chromatin [GO:0000785]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; single-stranded DNA binding [GO:0003697]; ubiquitin binding [GO:0043130] | PF10263; | 3.30.160.60; | Spartan family | PTM: Autocatalytically cleaved in response to double-stranded DNA-binding: autocatalytic cleavage takes place in trans and leads to inactivation. {ECO:0000250|UniProtKB:Q9H040}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H040}. Chromosome {ECO:0000250|UniProtKB:A0A1L8G2K9}. Note=Localizes to sites of UV damage via the PIP-box. Recruited to stalled replication forks at sites of replication stress. {ECO:0000250|UniProtKB:Q9H040}. | null | null | null | null | null | FUNCTION: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde. Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis. Catalyzes proteolytic cleavage of the hmces DNA-protein cross-link following unfolding by the brip1/fancj helicase. Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as top1, top2a, histones H3 and H4. Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs. SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs. May also act as a 'reader' of ubiquitinated pcna: facilitates chromatin association of rad18 and is required for efficient pcna monoubiquitination, promoting a feed-forward loop to enhance pcna ubiquitination and translesion DNA synthesis. Acts as a regulator of translesion DNA synthesis by recruiting vcp/p97 to sites of DNA damage. {ECO:0000250|UniProtKB:A0A1L8G2K9, ECO:0000250|UniProtKB:Q9H040}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
F6VAN0 | ATF6A_MOUSE | MESPFSPVLPHGPDEDWESTLFAELGYFTDTDDVHFDAAHEAYENNFDHLNFDLDLMPWESDLWSPGSHFCSDMKAEPQPLSPASSSCSISSPRSTDSCSSTQHVPEELDLLSSSQSPLSLYGDSCNSPSSVEPLKEEKPVTGPGNKTEHGLTPKKKIQMSSKPSVQPKPLLLPAAPKTQTNASVPAKAIIIQTLPALMPLAKQQSIISIQPAPTKGQTVLLSQPTVVQLQSPAVLSSAQPVLAVTGGAAQLPNHVVNVLPAPVVSSPVNGKLSVTKPVLQSATRSMGSDIAVLRRQQRMIKNRESACQSRKKKKEYMLGLEARLKAALSENEQLKKENGSLKRQLDEVVSENQRLKVPSPKRRAVCVMIVLAFIMLNYGPMSMLEQESRRVKPSVSPANQRRHLLEFSAKEVKDTSDGDNQKDSYSYDHSVSNDKALMVLSEEPLLYMPPPPCQPLINTTESLRLNHELRGWVHRHEVERTKSRRMTNSQQKARILQGALEQGSNSQLMAVQYTETTSISRNSGSELQVYYASPGSYQGFFDAIRRRGDTFYVVSFRRDHLLLPATTHNKTTRPKMSIVLPAININDNVINGQDYEVMMQIDCQVMDTRILHIKSSSVPPYLRDHQRNQTSTFFGSPPTTTETTHVVSTIPESLQ | null | null | endoplasmic reticulum unfolded protein response [GO:0030968]; eye development [GO:0001654]; positive regulation of apoptotic process [GO:0043065]; positive regulation of ATF6-mediated unfolded protein response [GO:1903893]; positive regulation of autophagy [GO:0010508]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; visual perception [GO:0007601] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF00170; | 1.20.5.170; | BZIP family, ATF subfamily | PTM: During unfolded protein response, a fragment of approximately 50 kDa containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage seems to be performed sequentially by site-1 (MBTPS1, S1P) and site-2 (MBTPS2, S2P) proteases (By similarity). {ECO:0000250|UniProtKB:P18850}.; PTM: N-glycosylated. The glycosylation status may serve as a sensor for ER homeostasis, resulting in ATF6 activation to trigger the unfolded protein response (UPR) (By similarity). {ECO:0000250|UniProtKB:P18850}.; PTM: Ubiquitinated by RNF186 at Lys-139, which is required for pattern recognition receptor-induced unfolded protein response-associated outcomes. {ECO:0000250|UniProtKB:P18850}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22682248}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P18850}; Single-pass type II membrane protein {ECO:0000255}. Note=Translocates from the endoplasmic reticulum to the Golgi, where it is processed. {ECO:0000250|UniProtKB:P18850}.; SUBCELLULAR LOCATION: [Processed cyclic AMP-dependent transcription factor ATF-6 alpha]: Nucleus {ECO:0000269|PubMed:22682248}. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus (PubMed:22682248). THBS4 promotes its nuclear shuttling (PubMed:22682248). {ECO:0000269|PubMed:22682248}. | null | null | null | null | null | FUNCTION: [Cyclic AMP-dependent transcription factor ATF-6 alpha]: Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 alpha), which is embedded in the endoplasmic reticulum membrane. Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR). {ECO:0000250|UniProtKB:P18850}.; FUNCTION: [Processed cyclic AMP-dependent transcription factor ATF-6 alpha]: Transcription factor that initiates the unfolded protein response (UPR) during endoplasmic reticulum stress by activating transcription of genes involved in the UPR. Binds DNA on the 5'-CCAC[GA]-3'half of the ER stress response element (ERSE) (5'-CCAAT-N(9)-CCAC[GA]-3') and of ERSE II (5'-ATTGG-N-CCACG-3'). Binding to ERSE requires binding of NF-Y to ERSE. Could also be involved in activation of transcription by the serum response factor. May play a role in foveal development and cone function in the retina. {ECO:0000250|UniProtKB:P18850}. | Mus musculus (Mouse) |
F6Y5S8 | IMPA3_CALJA | MAPMGIRLSPLGVAVFCLLGLGVLYHLYSGFLAGRFSLFGLGGEPAGGAAGPPAAADGGTVDLREMLAVSVLAAVRGGDEVRRVRESNVLHEKSKGKTREGADDKMTSGDVLSNRKMFYLLKTAFPSVQINTEEHVDAADQEVILWDHKIPEDILKEVTAPKEVPAESVTVWIDPLDATQEYTEDLRKYVTTMVCVAVNGKPVLGVIHKPFSEYTAWAMVDGGSNVKARSSYNEKTPRIVVSRSHSGMVKQVALQTFGNQTTIIPAGGAGYKVLALLDVPDKSQEKADLYIHVTYIKKWDICAGNAILKALGGHMTTLSGEEISYTGSDGIEGGLLASIRMNHQALVRKLPDLEKMGH | 3.1.3.7 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | phosphatidylinositol phosphate biosynthetic process [GO:0046854]; skeletal system development [GO:0001501] | trans-Golgi network membrane [GO:0032588] | 3'(2'),5'-bisphosphate nucleotidase activity [GO:0008441]; 3',5'-nucleotide bisphosphate phosphatase activity [GO:0097657]; 3'-nucleotidase activity [GO:0008254]; metal ion binding [GO:0046872] | PF00459; | 3.40.190.80;3.30.540.10; | Inositol monophosphatase superfamily | PTM: Contains N-linked glycan resistant to endoglycosydase H. {ECO:0000250|UniProtKB:Q9NX62}. | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q80V26, ECO:0000250|UniProtKB:Q9NX62}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q80V26, ECO:0000250|UniProtKB:Q9NX62}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9NX62}. Note=The catalytic core is predicted to reside within the Golgi lumen. {ECO:0000250|UniProtKB:Q9NX62}. | CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate; Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7; Evidence={ECO:0000250|UniProtKB:Q80V26}; | null | PATHWAY: Sulfur metabolism. {ECO:0000250|UniProtKB:Q80V26}. | null | null | FUNCTION: Exhibits 3'-nucleotidase activity toward adenosine 3',5'-bisphosphate (PAP), namely hydrolyzes adenosine 3',5'-bisphosphate into adenosine 5'-monophosphate (AMP) and a phosphate. May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',5'-bisphosphate produced by Golgi sulfotransferases during glycosaminoglycan sulfation. Has no activity toward 3'-phosphoadenosine 5'-phosphosulfate (PAPS) or inositol phosphate (IP) substrates including I(1)P, I(1,4)P2, I(1,3,4)P3, I(1,4,5)P3 and I(1,3,4,5)P4. {ECO:0000250|UniProtKB:Q80V26}. | Callithrix jacchus (White-tufted-ear marmoset) |
F6ZDS4 | TPR_MOUSE | MTSGGSASRSGHRGVPMTSRGFDGSRRGSLRRAGARETASEAADGAAPAAGLRASPCSLASPSAAAAVAAIPADMAAVLQQVLERPELNKLPKSTQNKLEKFLAEQQSEIDCLKGRHEKFKVESEQQYFEIEKRLSQSQERLVTETRECQNLRLELEKLNNQVKVLTEKTKELETAQDRNLGIQSQFTRAKEELEAEKRDLIRTNERLSQEVEYLTEDVKRLNEKLKESNTTKGELQLKLDELQASDVAVKYREKRLEQEKELLHNQNSWLNTELKTKTDELLALGREKGNEILELKCNLENKKEEVLRLEEQMNGLKTSNEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVDELHKLLKEAGEANKTIQDHLLQVEESKDQMEKEMLEKIGKLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYNAYVETQDQLLLEKQENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSAKLEQAMKEIQRLQEDTDKANKHSSVLERDNQRMEIQIKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLFALRELGETREREEQETTSSKIAELQHKLENSLAELEQLRESRQHQMQLVDSIVRQRDMYRILLSQTTGMAIPLQASSLDDISLLSTPKRSSTSQTVSTPAPEPVIDSTEAIEAKAALKQLQEIFENYKKEKIDSEKLQNEQLEKLQEQVTDLRSQNTKISTQLDFASKRYEMLQDNVEGYRREITSLQERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQQRESLLAEQRGQNLLLTNLQTIQGILERSETETKQRLNSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQLDTEINLHLNTKELLKNAQKDIATLKQHLNNMEAQLASQSTQRTGKGQPGDRDDVDDLKSQLRQAEEQVNDLKERLKTSTSNVEQYRAMVTSLEDSLNKEKQVTEEVHKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRKAIESMEQQLSELKKTLSTVQNEVQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMTSIRQHLEETTQKAESQLLECKASWEERERVLKDEVSKSVSRCEDLEKQNRLLHDQIEKLSDKVVTSMKDAVQAPLNVSLNEEGKSQEQILEILRFIRREKEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNVEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLREEKERLEQNLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQQLINQQKDPDTEEYRKLLSEKEIHTKRIQQLNEEVGRLKAEIARSNASLTNNQNLIQSLREDLSKARTEKEGIQKDLDAKIIDIQEKVKTITQVKKIGRRYKTQFEELKAQQNKAMETSTQSSGDHQEQHISVQEMQELKDTLSQSETKTKSLEGQVENLQKTLSEKETEARSLQEQTVQLQSELSRLRQDLQDKTTEEQLRQQMNEKTWKTLALAKSKITHLSGVKDQLTKEIEELKQRNGALDQQKDELDVRMTALKSQYEGRISRLERELREHQERHLEQRDEPQEPTNKAPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSKVTAAAMAGNKSTPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGNASGSVRSTSPNVQPSISQPILTVQQQTQATAFVQPTQQSHPQIEPTNQELSPNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRTREEEEDSTMEAGDQVSEDTVEMPLPKKLKMVTPVGTEEEVMAEESTDGEAETQAYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDLGPLQSDQQTTSSQDGQGKGDDVIVIDSDDEDDDEENDGEHEDYEEDEDDDDDEEDDTGMGDEGEDSNEGTGSADGNDGYEADDAEGGDGTDPGTETEESMGGAESHQRAADSQNSGEGNTSAAESSFSQEVAREQQPTSASERQTPQAPQSPRRPPHPLPPRLTIHAPPQELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDMPQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQSVPMVTTSTGTLSTTNETAAGDDGDEVFVEAESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQPKPFRRVRLQTTLRQGVRGRQFNRQRGISHAMGGRGGINRGNIN | null | null | cell division [GO:0051301]; cellular response to heat [GO:0034605]; cellular response to interferon-alpha [GO:0035457]; mitotic spindle assembly checkpoint signaling [GO:0007094]; mRNA export from nucleus [GO:0006406]; mRNA export from nucleus in response to heat stress [GO:0031990]; negative regulation of RNA export from nucleus [GO:0046832]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of translational initiation [GO:0045947]; nucleocytoplasmic transport [GO:0006913]; positive regulation of heterochromatin formation [GO:0031453]; positive regulation of intracellular protein transport [GO:0090316]; positive regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090267]; positive regulation of protein export from nucleus [GO:0046827]; positive regulation of protein import into nucleus [GO:0042307]; protein export from nucleus [GO:0006611]; regulation of mitotic sister chromatid separation [GO:0010965]; regulation of mitotic spindle assembly [GO:1901673]; response to epidermal growth factor [GO:0070849]; RNA export from nucleus [GO:0006405]; RNA import into nucleus [GO:0006404] | chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; cytoplasmic dynein complex [GO:0005868]; mitotic spindle [GO:0072686]; nuclear envelope [GO:0005635]; nuclear inclusion body [GO:0042405]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nuclear pore nuclear basket [GO:0044615] | chromatin binding [GO:0003682]; dynein complex binding [GO:0070840]; heat shock protein binding [GO:0031072]; mitogen-activated protein kinase binding [GO:0051019]; mRNA binding [GO:0003729]; protein homodimerization activity [GO:0042803]; structural constituent of nuclear pore [GO:0017056]; tubulin binding [GO:0015631] | PF07926; | 1.10.287.1490; | TPR family | PTM: Phosphorylated. Phosphorylation occurs on serine and threonine residues (comprised in the C-terminal region) by MAPK1/ERK2 and stabilizes the interaction between these two proteins (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Nucleoplasmic side {ECO:0000250|UniProtKB:P12270}. Nucleus envelope {ECO:0000269|PubMed:12424524, ECO:0000269|PubMed:12513910}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P12270, ECO:0000269|PubMed:12513910}. Cytoplasm {ECO:0000250|UniProtKB:P12270}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P12270}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Cytoplasmic side {ECO:0000250|UniProtKB:P12270}. Note=Detected as discrete intranuclear foci with IFI204 (By similarity). In interphase, localizes to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Detected exclusively to the cytoplasmic margin of NPC (By similarity). Docking to the inner nucleoplasmic side of the NPC is mediated through binding to nucleoporins. Anchored by NUP153 to the NPC. The assembly of the NPC is a stepwise process in which Trp-containing peripheral structures assemble after other components, including p62. Detected as filaments that emanate from the nuclear basket of the NPC and extend to the nucleolus to delineate a chromatin-free network extending from the nuclear envelope to the perinucleolar region. Detected in diffuse and discrete spheroidal intranuclear foci. Nucleocytoplasmic shuttling protein imported into the nucleus in a XPO1/CRM1- and Importin alpha/Importin beta receptor-dependent manner. Remains localized to the nuclear membrane after poliovirus (PV) infection. During mitosis, remains associated with the nuclear envelope until prometaphase. Associated with the mitotic spindle from late prometaphase until anaphase. Reorganized during mitosis in a viscous and dynamic nuclear-derived spindle matrix that embeds the microtubule spindle apparatus from pole to pole in a microtubule-independent manner. Recruited to the reforming nuclear envelope during telophase and cytokinesis. Detected at kinetochores during prometaphase. Colocalizes with MAD2L1 in the spindle matrix but not at kinetochore. Colocalizes with dynein, dynactin, tubulin at kinetochore during the metaphase-anaphase transition. Colocalizes with DYNLL1 at the mitotic spindle (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12270}. | null | null | null | null | null | FUNCTION: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress-induced conditions. Plays a limited role in the regulation of nuclear protein export. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. Also plays a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC-associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
F7B113 | SL9A9_HORSE | MERQRRFMSEKDEYQFQHQGAVELLVFNFLLILTILTIWLFKNHRFRFLHETGGAMVYGLIMGLILRYATAPTDIESGTVYDCGKLAFSPSTLLINITDQVYEYKYKREISQHNINPHLGNAILEKMTFDPEIFFNVLLPPIIFHAGYSLKKRHFFQNLGSILTYAFLGTAISCIVIGLIMYGFVKAMVYAGQLKNGDFHFTDCLFFGSLMSATDPVTVLAIFHELHVDPDLYTLLFGESVLNDAVAIVLTYSISIYSPKENPNAFDAAAFFQSVGNFLGIFAGSFAMGSAYAVVTALLTKFTKLCEFPMLETGLFFLLSWSAFLSAEAAGLTGIVAVLFCGVTQAHYTYNNLSLDSKMRTKQLFEFMNFLAENVIFCYMGLALFTFQNHIFNALFILGAFLAIFVARACNIYPLSFLLNLGRKHKIPWNFQHMMMFSGLRGAIAFALAIRDTESQPKQMMFSTTLLLVFFTVWVFGGGTTPMLTWLQIRVGVDLDEDLKERPSSHQEANNLEKSTTKTESAWLFRMWYGFDHKYLKPILTHSGPPLTTTLPEWCGPISRLLTSPQAYGEQLKEDDAECIVNQDELAMNYQEQAASPCSPPTRLGLDQKAAPQTPGKENIYEGDLGLGGYELKLEQTPGQSQLN | null | null | potassium ion transmembrane transport [GO:0071805]; proton transmembrane transport [GO:1902600]; regulation of intracellular pH [GO:0051453]; sodium ion import across plasma membrane [GO:0098719]; sodium ion transmembrane transport [GO:0035725] | early endosome membrane [GO:0031901]; late endosome membrane [GO:0031902]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038] | potassium:proton antiporter activity [GO:0015386]; protein homodimerization activity [GO:0042803]; sodium:proton antiporter activity [GO:0015385] | PF00999; | 6.10.140.1330; | Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family | null | SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q8IVB4}; Multi-pass membrane protein {ECO:0000269|PubMed:33118634}. Early endosome membrane {ECO:0000250|UniProtKB:Q8IVB4}; Multi-pass membrane protein {ECO:0000269|PubMed:33118634}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q8IVB4}; Multi-pass membrane protein {ECO:0000269|PubMed:33118634}. Cell membrane {ECO:0000250|UniProtKB:Q8BZ00}; Multi-pass membrane protein {ECO:0000269|PubMed:33118634}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q8BZ00}; Multi-pass membrane protein {ECO:0000269|PubMed:33118634}. Note=Localized to the plasma membrane in inner ear hair cell bundle. {ECO:0000250|UniProtKB:Q8BZ00}. | CATALYTIC ACTIVITY: Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out); Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:33118634}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out); Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:Q8BZ00}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20.5 mM for Na(+) {ECO:0000269|PubMed:33118634}; | null | null | null | FUNCTION: Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+) (PubMed:33118634). By facilitating proton efflux, SLC9A9 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Regulates organellar pH and consequently, endosome maturation and endocytic trafficking of plasma membrane receptors and neurotransporters (By similarity). Promotes the recycling of transferrin receptors back to the cell surface to facilitate additional iron uptake in the brain (By similarity). Regulates synaptic transmission by regulating the luminal pH of axonal endosomes. Regulates phagosome lumenal pH, thus affecting phagosome maturation, and consequently, microbicidal activity in macrophages. Can also be active at the cell surface of specialized cells, e.g., in the inner ear hair bundles uses the high K(+) of the endolymph to regulate intracelular pH (By similarity). {ECO:0000250|UniProtKB:Q8BZ00, ECO:0000250|UniProtKB:Q8IVB4, ECO:0000269|PubMed:33118634}. | Equus caballus (Horse) |
F7BJB9 | MORC3_MOUSE | MAAQPPTGIRLSALCPKFLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVISDHICLTFTDNGNGMTADKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGSMRLGKDAMVFTKNGETMSVGFLSQTYLEVIKAEHVVVPIVTFNKHRQMINLTESKASLAAILEHSLFSTEQKLLAELNAIMGKKGTRIIIWNLRSYKNATEFDFEKDKYDIRIPEDLDETAGRKGYKKQERMDQIAPESDYSLRAYCSILYLKPRMQIIIRGQKVKTQLVSKSLAYIERDVYRPKFLTRTVRITFGFNCRNKDHYGIMMYHKNRLIKAYEKVGCQLKANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTILALGEKLNDYWNEMKVKKNAEYPVNLPVEDIQKRPDQTWVQCDACLKWRKLPDGIDQLPEKWYCSNNPDPQFRNCEVPEEPEDEDLVHPTYEKTYKKTSKERFRIRQPEILPRILPQINPELLYQTSVSSQSFSPVKESVPRPHLSEVTSPFAARIINLNLASPASEPENSSMKRKLGVHSSILNAKTRRLSNPPVENSSYKNDDDEDVIILEENSTPKPAVDLEVKSDIEVKSEQSHTEQSGIHVDLVSSPKPCVQASSTSTSTSRSDPGITVSTQTDAPGLTVKKEESMEEDMGVRNGTATLSCVGTEAKVQETSAESVDATSHQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLQQRLLEMNDKCVKKEKCHQSTETDAVFLLDSVNGQAESLDHLGSQYQQALQEIERLKRQCSALQQVKSECSQASCTESKSEVDEMAVQLDDVFRQLDKCTIERDQYKNEVQLLEIEKSHIHSQCEELQTEVEQLKSTGQQAAADGSTASNAEEPVSYVDGESLKLRSLRVNVGQLLAMIVPDLDLQQVNYDVDVVDEILGQVVEQMSEISST | null | null | antiviral innate immune response [GO:0140374]; maintenance of protein location in nucleus [GO:0051457]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of interferon-beta production [GO:0032688]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cellular senescence [GO:2000774]; post-embryonic development [GO:0009791]; protein stabilization [GO:0050821] | chromatin [GO:0000785]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605] | ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; methylated histone binding [GO:0035064]; protein-macromolecule adaptor activity [GO:0030674]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270] | PF13589;PF17942;PF07496; | 3.30.40.100;3.30.565.10; | null | PTM: Sumoylation is involved in interaction with PML and localization to PML nuclear bodies. {ECO:0000250|UniProtKB:Q14149}. | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:17332504}. Nucleus matrix {ECO:0000250|UniProtKB:Q14149}. Nucleus, PML body {ECO:0000269|PubMed:17332504}. Chromosome {ECO:0000269|PubMed:27528681}. Note=Also found in PML-independent nuclear bodies. Localization to nuclear bodies is ATP-dependent. {ECO:0000250|UniProtKB:Q14149}. | null | null | null | null | null | FUNCTION: Nuclear matrix protein which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism and plays a role in innate immunity by restricting different viruses through modulation of the IFN response. Mechanistically, possesses a primary antiviral function through a MORC3-regulated element that activates IFNB1, and this function is guarded by a secondary IFN-repressing function. Sumoylated MORC3-NBs associates with PML-NBs and recruits TP53 and SP100, thus regulating TP53 activity (PubMed:17332504). Binds RNA in vitro. Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3. The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0. {ECO:0000250|UniProtKB:Q14149, ECO:0000269|PubMed:17332504}. | Mus musculus (Mouse) |
F7BWT7 | TSN15_MOUSE | MPRGDSEQVRYCARFSYLWLKFSLIIYSTVFWLIGGLVLSVGIYAEAERQKYKTLESAFLAPAIILILLGVVMFIVSFIGVLASLRDNLCLLQSFMYILGICLVMELIGGIVALIFRNQTIDFLNDNIRRGIENYYDDLDFKNIMDFVQKKFKCCGGEDYRDWSKNQYHDCSAPGPLACGVPYTCCIRNTTDVVNTMCGYKTIDKERLNAQNIIHVRGCTNAVLIWFMDNYTIMAGLLLGILLPQFLGVLLTLLYITRVEDIILEHSVTDGLLGPGAKSRTDTAGTGCCLCYPD | null | null | negative regulation of Notch signaling pathway [GO:0045746]; protein localization to plasma membrane [GO:0072659]; protein maturation [GO:0051604]; regulation of membrane protein ectodomain proteolysis [GO:0051043] | cell junction [GO:0030054]; cell surface [GO:0009986]; cytosol [GO:0005829]; late endosome membrane [GO:0031902]; nuclear body [GO:0016604]; plasma membrane [GO:0005886]; tetraspanin-enriched microdomain [GO:0097197] | enzyme binding [GO:0019899] | PF00335; | 1.10.1450.10; | Tetraspanin (TM4SF) family | PTM: Palmitoylated. {ECO:0000250|UniProtKB:O95858}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30463011}; Multi-pass membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:O95858}. | null | null | null | null | null | FUNCTION: Part of TspanC8 subgroup, composed of 6 members that interact with the transmembrane metalloprotease ADAM10. This interaction is required for ADAM10 exit from the endoplasmic reticulum and for enzymatic maturation and trafficking to the cell surface as well as substrate specificity. Different TspanC8/ADAM10 complexes have distinct substrates (PubMed:23035126, PubMed:26668317). Promotes ADAM10-mediated cleavage of CDH2 (PubMed:26668317). Negatively regulates ligand-induced Notch activity probably by regulating ADAM10 activity (By similarity). {ECO:0000250|UniProtKB:O95858, ECO:0000269|PubMed:23035126, ECO:0000269|PubMed:26668317}. | Mus musculus (Mouse) |
F7D4X9 | SIR5_MONDO | MSLLHFATRRLILQVLRELGLKAPPVHKTLKICIAMSRPSSNMADFRRFFARAKHIAIITGAGVSAESGVPTFRGPGGFWRKWKAEDLATPEAFAQNPSLVWEFYHYRREVILKKHPNAAHVAIAACEERLSLQGRRVVVITQNIDEFHTKAGTKNILELHGSLFKTRCCSCGNVRVNYNNPICPALEGKGLPDPNAPDAQIPLENLPRWKTTGDFSVLFLLDASPLYPSNLSCSHPVGAPALSEVADLGRWVGTSSLVYPAGMFGPHVALRGIPVAEFNTVTTPVTQNFRFHFSGLCGTTIPEALSPHESEKTG | 2.3.1.- | null | negative regulation of reactive oxygen species metabolic process [GO:2000378]; protein demalonylation [GO:0036046]; protein desuccinylation [GO:0036048]; regulation of ketone biosynthetic process [GO:0010566] | cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity [GO:0017136]; protein-glutaryllysine deglutarylase activity [GO:0061697]; protein-malonyllysine demalonylase activity [GO:0036054]; protein-succinyllysine desuccinylase activity [GO:0036055]; transferase activity [GO:0016740]; zinc ion binding [GO:0008270] | PF02146; | 3.30.1600.10;3.40.50.1220; | Sirtuin family, Class III subfamily | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03160}. Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03160}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03160}. Note=Mainly mitochondrial. Also present extramitochondrially, with a fraction present in the cytosol and very small amounts also detected in the nucleus. {ECO:0000255|HAMAP-Rule:MF_03160}. | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-malonyl-L-lysyl-[protein] + NAD(+) = 2''-O-malonyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:47672, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11878, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:87831, ChEBI:CHEBI:87833; Evidence={ECO:0000255|HAMAP-Rule:MF_03160}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:47668, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:87830, ChEBI:CHEBI:87832; Evidence={ECO:0000255|HAMAP-Rule:MF_03160}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-glutaryl-L-lysyl-[protein] + NAD(+) = 2''-O-glutaryl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:47664, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11875, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:87828, ChEBI:CHEBI:87829; Evidence={ECO:0000255|HAMAP-Rule:MF_03160}; | null | null | null | null | FUNCTION: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species. Activates SHMT2 by mediating its desuccinylation. Modulates ketogenesis through the desuccinylation and activation of HMGCS2. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX. {ECO:0000255|HAMAP-Rule:MF_03160}. | Monodelphis domestica (Gray short-tailed opossum) |
F7E540 | TTLL7_XENTR | MPSLPNESDHQATCSLSLHSDLPYQPSSSIKRKVRKKKKNGAITANVVGTKYEIVRLVTEEMMFTKARDDDETANLIWNDCAVQHEKIAELRNYQRINHFPGMGEICRKDCLARNMTKMIKCQPHEYNFIPRTWIFPAEYTQFQTYIKELKKKRRQKTFIIKPANGAMGHGISLTRNGEKLQAQDHLIVQEYLEKPFLLESYKFDLRIYILVTSCDPLRIFLYNDGLVRMGTEKYHPPSESNLSQLYMHLTNYSVNKHNENFERDETENRGSKRSIKWFTEFLRANDYDISKFWNDISDLVVKTLIVAEPHVLHAYRMCRPGQHPTSESVCFEVLGFDIILDRKLKPWLLEINRAPSFGTDQKIDHDVKKGVLLNALKLLNIRASDKKKNLAKQKAEAQKRLYGQGSMKRLSPASSDWEKQRHTLERRKEELKERLAQVRKQISREEYENRHLGNYRRIYPPEDKLLLEKYEGLLATAFQTFLAGRAASLQREMNNPLKRMKEEDILDLLEQCELDDEKLSGKPTRPKEPRTLSSMPESTQTLKKLKNYSSHSSSNSTGSSSDTEEEEDEKEGKEKKVSYDLEEHKYKSLERSSRIHWKPPLKAARPFSNSSSPSSAASMRRSVSCPRSITALNTQSPTTDQRPFSSRISSTITRPLSGNRTNSLNRSSSSNRVPQSGTSGSVYPSISESRLDHLTKEQEEELTKQTLYALRDMRIRIPGKGVEEITHSHIDEIMDNWTYHKSKVASYWLIKLDSVKQRKVLDIVRTNIRSVLQRIWKVSDVECLHIYRSFNRVFNRLLWNHGQGLWSCFSNSGTSWETIFCKSTEVVTPQQFQCCQRLVQLCKDCLLAVYKYATDSRVAGMSPDWDDSRYLFPVVPQFTMKSSSSGVNCSSSRLPRSSILFNPRHNHY | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | cell differentiation [GO:0030154]; microtubule cytoskeleton organization [GO:0000226]; nervous system development [GO:0007399]; protein polyglutamylation [GO:0018095] | cilium [GO:0005929]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; microtubule [GO:0005874]; perikaryon [GO:0043204] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; tubulin binding [GO:0015631]; tubulin-glutamic acid ligase activity [GO:0070740] | PF03133; | 3.30.470.20; | Tubulin--tyrosine ligase family | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:A4Q9F0}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:A4Q9F0}. Cell projection, dendrite {ECO:0000250|UniProtKB:A4Q9F0}. Perikaryon {ECO:0000250|UniProtKB:A4Q9F0}. Note=In cells with primary cilia, found in both cilia and basal bodies. In neuronal cells, found in dendrites and perikaryon. {ECO:0000250|UniProtKB:A4Q9F0}. | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-glutamyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:26875866, ECO:0000269|PubMed:28576883}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145; Evidence={ECO:0000305|PubMed:26875866, ECO:0000305|PubMed:28576883}; CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP + L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143623, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:26875866}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149; Evidence={ECO:0000305|PubMed:26875866}; | null | null | null | null | FUNCTION: Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin (PubMed:26875866, PubMed:28576883). Mediates both ATP-dependent initiation and elongation steps of the polyglutamylation reaction (PubMed:26875866). Preferentially modifies the beta-tubulin tail over an alpha-tail (PubMed:26875866, PubMed:28576883). Competes with monoglycylase TTLL3 for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions (PubMed:28576883). {ECO:0000269|PubMed:26875866, ECO:0000269|PubMed:28576883}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
F7EQ49 | GPER1_MACMU | MEVTSQARGMGLEMYPGTMQPAAPNTTSPELNLSHPLLGASLANGTGELSEHQQYVIGLFLSCLYTIFLFPIGFVGNILILVVNISFREKMTIPDLYFINLAVADLILVADSLIEVFNLHEQYYDIAVLCTFMSLFLQVNMYSSVFFLTWMSFDRYIALARAMRCSLFRTKHHARLSCGLIWMASVSATLVPFTAVHLQHTDEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRVLVRAHRHRGLRPRRQKALRMILAVVLVFFVCWLPENVFISVHLLQRTQPGAAPCKQSFRHAHPLTGHIVNLAAFSNSCLNPLIYSFLGETFREKLRLYIEQKTNLPALNRFCHAALKAVIPDSTEQSDVRFSSAV | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; apoptotic chromosome condensation [GO:0030263]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to estradiol stimulus [GO:0071392]; cellular response to glucose stimulus [GO:0071333]; cellular response to mineralocorticoid stimulus [GO:0071389]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of gene expression [GO:0010629]; negative regulation of inflammatory response [GO:0050728]; negative regulation of leukocyte activation [GO:0002695]; negative regulation of lipid biosynthetic process [GO:0051055]; nervous system development [GO:0007399]; neuronal action potential [GO:0019228]; nuclear fragmentation involved in apoptotic nuclear change [GO:0030264]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of endothelial cell apoptotic process [GO:2000353]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of G protein-coupled receptor signaling pathway [GO:0045745]; positive regulation of gene expression [GO:0010628]; positive regulation of inositol trisphosphate biosynthetic process [GO:0032962]; positive regulation of insulin secretion [GO:0032024]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of neurogenesis [GO:0050769]; positive regulation of neurotransmitter secretion [GO:0001956]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell cycle [GO:0051726]; regulation of cytosolic calcium ion concentration [GO:0051480]; steroid hormone mediated signaling pathway [GO:0043401]; vasodilation [GO:0042311] | axon [GO:0030424]; axon terminus [GO:0043679]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; dendritic spine head [GO:0044327]; dendritic spine membrane [GO:0032591]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; keratin filament [GO:0045095]; mitochondrial membrane [GO:0031966]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; presynaptic active zone [GO:0048786]; presynaptic membrane [GO:0042734]; recycling endosome [GO:0055037]; trans-Golgi network [GO:0005802] | chromatin binding [GO:0003682]; G protein-coupled estrogen receptor activity [GO:0038054]; nuclear estrogen receptor activity [GO:0030284]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | PTM: Ubiquitinated; ubiquitination occurs at the plasma membrane and leads to proteasome-mediated degradation. {ECO:0000250}.; PTM: Glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Basolateral cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, axon {ECO:0000250}. Postsynaptic density {ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Endocytosed in a agonist- and arrestin-independent manner. Colocalized with RAMP3 and clathrin-coated pits at the plasma membrane. Colocalized with transferrin receptor at the plasma membrane and perinuclear region. Accumulated and colocalized with RAB11 proteins in recycling endosomes and trans-Golgi network (TGN), but does neither recycle back to the cell surface nor traffics to late endosome or lysosome. Colocalized with calnexin in the endoplasmic reticulum. Traffics to intracellular sites via cytokeratin intermediate filaments like KRT7 and KRT8 after constitutive endocytosis in epithelial cells. Colocalized with EGFR in the nucleus of agonist-induced cancer-associated fibroblasts (CAF) (By similarity). Colocalized with BSN to the active zone of presynaptic density. Colocalized with DLG4/PSD95 and neurabin-2 PPP1R9B in neuronal synaptosomes (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: G-protein coupled estrogen receptor that binds to 17-beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Stimulates cAMP production, calcium mobilization and tyrosine kinase Src inducing the release of heparin-bound epidermal growth factor (HB-EGF) and subsequent transactivation of the epidermal growth factor receptor (EGFR), activating downstream signaling pathways such as PI3K/Akt and ERK/MAPK. Mediates pleiotropic functions among others in the cardiovascular, endocrine, reproductive, immune and central nervous systems. Has a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a RAMP3-dependent manner. Regulates arterial blood pressure by stimulating vasodilation and reducing vascular smooth muscle and microvascular endothelial cell proliferation. Plays a role in blood glucose homeostasis contributing to the insulin secretion response by pancreatic beta cells. Triggers mitochondrial apoptosis during pachytene spermatocyte differentiation. Stimulates uterine epithelial cell proliferation. Enhances uterine contractility in response to oxytocin. Contributes to thymic atrophy by inducing apoptosis. Attenuates TNF-mediated endothelial expression of leukocyte adhesion molecules. Promotes neuritogenesis in developing hippocampal neurons. Plays a role in acute neuroprotection against NMDA-induced excitotoxic neuronal death. Inhibits early osteoblast proliferation at growth plate during skeletal development. Inhibits mature adipocyte differentiation and lipid accumulation. Involved in the recruitment of beta-arrestin 2 ARRB2 at the plasma membrane in epithelial cells. Functions also as a receptor for aldosterone mediating rapid regulation of vascular contractibility through the PI3K/ERK signaling pathway. Involved in cancer progression regulation. Stimulates cancer-associated fibroblast (CAF) proliferation by a rapid genomic response through the EGFR/ERK transduction pathway. Associated with EGFR, may act as a transcription factor activating growth regulatory genes (c-fos, cyclin D1). Promotes integrin alpha-5/beta-1 and fibronectin (FN) matrix assembly in breast cancer cells (By similarity). Increases firing activity and intracellular calcium oscillations in luteinizing hormone-releasing hormone (LHRH) neurons. {ECO:0000250, ECO:0000269|PubMed:19131510}. | Macaca mulatta (Rhesus macaque) |
F7EZ75 | SIR5_MACMU | MRPLQIVPSRLISQLYCGLKPPASTRNQICLKMARPSSSMADFRKCFAKAKHIVIISGAGVSAESGVPTFRGAGGYWRKWQAQDLATPLAFAHNPSRVWEFYHYRREVMGSKEPNAGHRAIAECETRLGKQGRRVVVITQNIDELHRKAGTKNLLEIHGSLFKTRCTSCGIVAENYKSPICPALSGKGAPEPGTQDASIPVEKLPRCEEAGCGGLLRPHVVWFGENLDPAILEEVDKELGRCDLCLVVGTSSVVYPAAMFAPQVAARGVPVAEFNTETTPATNRFRFHFQGPCGTTLPEALARHENETVS | 2.3.1.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03160}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03160}; | protein demalonylation [GO:0036046]; protein desuccinylation [GO:0036048]; regulation of ketone biosynthetic process [GO:0010566] | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | NAD+ binding [GO:0070403]; NAD-dependent histone deacetylase activity [GO:0017136]; protein-glutaryllysine deglutarylase activity [GO:0061697]; protein-malonyllysine demalonylase activity [GO:0036054]; protein-succinyllysine desuccinylase activity [GO:0036055]; transferase activity [GO:0016740]; zinc ion binding [GO:0008270] | PF02146; | 3.30.1600.10;3.40.50.1220; | Sirtuin family, Class III subfamily | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03160}. Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03160}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03160}. Note=Mainly mitochondrial. Also present extramitochondrially, with a fraction present in the cytosol and very small amounts also detected in the nucleus. {ECO:0000255|HAMAP-Rule:MF_03160}. | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-malonyl-L-lysyl-[protein] + NAD(+) = 2''-O-malonyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:47672, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11878, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:87831, ChEBI:CHEBI:87833; Evidence={ECO:0000255|HAMAP-Rule:MF_03160}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:47668, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:87830, ChEBI:CHEBI:87832; Evidence={ECO:0000255|HAMAP-Rule:MF_03160}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-glutaryl-L-lysyl-[protein] + NAD(+) = 2''-O-glutaryl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:47664, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11875, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:87828, ChEBI:CHEBI:87829; Evidence={ECO:0000255|HAMAP-Rule:MF_03160}; | null | null | null | null | FUNCTION: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species. Activates SHMT2 by mediating its desuccinylation. Modulates ketogenesis through the desuccinylation and activation of HMGCS2. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX. {ECO:0000255|HAMAP-Rule:MF_03160}. | Macaca mulatta (Rhesus macaque) |
F7FIH8 | NNRE_MONDO | MSGLRTLLGLGLLVSSSRFPRVVARGGPRCPGPAWWAARPMHLGDSTMAGGTVKYLSQEEAQAVDEELFNEYKFSVDQLMELAGLSCATAIAKAYPLSSFGSNPPAVLVICGPGNNGGDGLVCARHLKLFGYEPKIHYPKKPNKPLFDALVTQCQKMDIPFLPEVPPEPMLIDELYELVVDAIFGFSFKGAVREPFGTILSIMNGLTVPIASIDIPSGWDVEKGNPEGIRPDLLISLTAPKKAATLFKGRHHYLGGRFVPSDLEKKYQLNLPPYPGTDCVLQLQ | 5.1.99.6 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-Rule:MF_03159}; Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03159}; | lipid transport [GO:0006869]; membrane raft distribution [GO:0031580]; negative regulation of angiogenesis [GO:0016525]; nicotinamide nucleotide metabolic process [GO:0046496]; regulation of cholesterol efflux [GO:0010874]; sprouting angiogenesis [GO:0002040] | cell body [GO:0044297]; cilium [GO:0005929]; extracellular space [GO:0005615]; mitochondrion [GO:0005739] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; NADHX epimerase activity [GO:0052856]; NADPHX epimerase activity [GO:0052857]; nucleotide binding [GO:0000166] | PF03853; | 3.40.50.10260; | NnrE/AIBP family | PTM: Undergoes physiological phosphorylation during sperm capacitation, downstream to PKA activation. {ECO:0000255|HAMAP-Rule:MF_03159}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03159}. Secreted {ECO:0000255|HAMAP-Rule:MF_03159}. Note=In sperm, secretion gradually increases during capacitation. {ECO:0000255|HAMAP-Rule:MF_03159}. | CATALYTIC ACTIVITY: Reaction=(6R)-NADHX = (6S)-NADHX; Xref=Rhea:RHEA:32215, ChEBI:CHEBI:64074, ChEBI:CHEBI:64075; EC=5.1.99.6; Evidence={ECO:0000250|UniProtKB:Q8NCW5}; CATALYTIC ACTIVITY: Reaction=(6R)-NADPHX = (6S)-NADPHX; Xref=Rhea:RHEA:32227, ChEBI:CHEBI:64076, ChEBI:CHEBI:64077; EC=5.1.99.6; Evidence={ECO:0000250|UniProtKB:Q8NCW5}; | null | null | null | null | FUNCTION: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. Accelerates cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis (By similarity). {ECO:0000250|UniProtKB:Q8NCW5, ECO:0000255|HAMAP-Rule:MF_03159}. | Monodelphis domestica (Gray short-tailed opossum) |
F7FQM7 | APOA1_MACMU | MKATVLTLAVLFLTGSQARHFWQQDEPPQTPWDRVKDLVTVYVEALKDSGKDYVSQFEGSALGKQLNLKLLDNWDSVTSTVSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELHEGTRQKLHELHEKLSPLGEEVRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKASEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLSTQ | null | null | acylglycerol homeostasis [GO:0055090]; cholesterol efflux [GO:0033344]; cholesterol metabolic process [GO:0008203]; lipoprotein metabolic process [GO:0042157]; phosphatidylcholine metabolic process [GO:0046470]; phospholipid efflux [GO:0033700]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of phagocytosis [GO:0050766]; positive regulation of phospholipid efflux [GO:1902995]; protein stabilization [GO:0050821]; regulation of intestinal cholesterol absorption [GO:0030300] | 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]; high-density lipoprotein particle receptor binding [GO:0070653]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803] | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:P02648}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02647}. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. {ECO:0000250|UniProtKB:P02647}. | Macaca mulatta (Rhesus macaque) |
F7IX06 | PETH2_THEAE | MSVTTPRRETSLLSRALRATAAAATAVVATVALAAPAQAANPYERGPNPTESMLEARSGPFSVSEERASRFGADGFGGGTIYYPRENNTYGAIAISPGYTGTQSSIAWLGERIASHGFVVIAIDTNTTLDQPDSRARQLNAALDYMLTDASSAVRNRIDASRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKSWRDITVPTLIIGAEYDTIASVTLHSKPFYNSIPSPTDKAYLELDGASHFAPNITNKTIGMYSVAWLKRFVDEDTRYTQFLCPGPRTGLLSDVEEYRSTCPF | 3.1.1.101; 3.1.1.74 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:30761732, ECO:0000269|Ref.5, ECO:0000305|PubMed:22183084}; Note=Can also bind other divalent metal ions with lower efficiency (PubMed:22183084). Calcium ion binding contributes to the thermostability of the protein (PubMed:22183084). {ECO:0000269|PubMed:22183084}; | null | extracellular region [GO:0005576]; periplasmic space [GO:0042597] | cutinase activity [GO:0050525]; metal ion binding [GO:0046872] | PF12146; | 3.40.50.1820; | AB hydrolase superfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:G8GER6}. Periplasm {ECO:0000250|UniProtKB:G8GER6}. | CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; Evidence={ECO:0000269|PubMed:20393707, ECO:0000269|PubMed:22183084}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12958; Evidence={ECO:0000269|PubMed:20393707, ECO:0000269|PubMed:22183084}; CATALYTIC ACTIVITY: Reaction=(ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+); Xref=Rhea:RHEA:49528, Rhea:RHEA-COMP:12420, Rhea:RHEA-COMP:12421, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:131701, ChEBI:CHEBI:131704; EC=3.1.1.101; Evidence={ECO:0000305|PubMed:20393707, ECO:0000305|PubMed:22183084}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49529; Evidence={ECO:0000305|PubMed:20393707, ECO:0000305|PubMed:22183084}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:20393707, ECO:0000269|PubMed:22183084, ECO:0000269|PubMed:25910960, ECO:0000269|PubMed:33387709}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000269|PubMed:20393707, ECO:0000269|PubMed:22183084, ECO:0000269|PubMed:25910960, ECO:0000269|PubMed:33387709}; CATALYTIC ACTIVITY: Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000305|PubMed:20393707, ECO:0000305|PubMed:22183084, ECO:0000305|PubMed:25910960, ECO:0000305|PubMed:33387709}; CATALYTIC ACTIVITY: Reaction=a hexanoate ester + H2O = an aliphatic alcohol + H(+) + hexanoate; Xref=Rhea:RHEA:47352, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:87656; Evidence={ECO:0000269|PubMed:20393707, ECO:0000269|PubMed:22183084}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47353; Evidence={ECO:0000269|PubMed:20393707, ECO:0000269|PubMed:22183084}; CATALYTIC ACTIVITY: Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657; Evidence={ECO:0000269|PubMed:20393707, ECO:0000269|PubMed:22183084}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47357; Evidence={ECO:0000269|PubMed:20393707, ECO:0000269|PubMed:22183084}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.22 mM for pNP-acetate (at 37 degrees Celsius and pH 7) {ECO:0000269|PubMed:22183084}; KM=3.41 mM for pNP-butyrate (at 37 degrees Celsius and pH 7) {ECO:0000269|PubMed:22183084}; KM=2.37 mM for pNP-hexanoate (at 37 degrees Celsius and pH 7) {ECO:0000269|PubMed:22183084}; KM=1.87 mM for pNP-octanoate (at 37 degrees Celsius and pH 7) {ECO:0000269|PubMed:22183084}; Note=kcat is 2.06 sec(-1) with pNP-acetate as substrate (at 37 degrees Celsius and pH 7) (PubMed:22183084). kcat is 4.48 sec(-1) with pNP-butyrate as substrate (at 37 degrees Celsius and pH 7) (PubMed:22183084). kcat is 3.28 sec(-1) with pNP-hexanoate as substrate (at 37 degrees Celsius and pH 7) (PubMed:22183084). kcat is 2.45 sec(-1) with pNP-octanoate as substrate (at 37 degrees Celsius and pH 7) (PubMed:22183084). {ECO:0000269|PubMed:22183084}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:20393707}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:20393707}; | FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:20393707, PubMed:22183084, PubMed:25910960, PubMed:33387709). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:20393707, PubMed:22183084, PubMed:25910960, PubMed:33387709). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (By similarity). Can also depolymerize the synthetic polyesters poly(epsilon-caprolactone) (PCL), poly(butylene succinate-co-adipate) (PBSA), poly(butylene succinate) (PBS), and poly(lactic acid) (PLA) (PubMed:20393707, PubMed:22183084). {ECO:0000250|UniProtKB:D4Q9N1, ECO:0000269|PubMed:20393707, ECO:0000269|PubMed:22183084, ECO:0000269|PubMed:25910960, ECO:0000269|PubMed:33387709}. | Thermobifida alba (Thermomonospora alba) |
F7J0M4 | RGA4R_ORYSJ | MEAALLSGFIKAILPRLFSLVDDKHKLHKGVKGDIDFLIKELRMIVGAIDDDLSLDHPAAAAVQTLCMEDLRELAHGIEDCIDGVLYRAARDQQQSPVRRAVQAPKKLQRNLQLAQQLQRLKRMAAEANQRKQRYTAAAPGQHGQVYSSAAAQVDEPWPSCSSASDPRIHEADLVGVDADREELLEQLAERQPEQLKVIAIVGFCGLGKTALAAEAYNRETGGGRFERHAWVCAGHRSAREVLGELLRRLDADGRSFHGDSDAGQLCVDIRQQLEKNRYFIVIDDIQTEDQWKSIKSAFPTDKDIGSRIVVTTTIQSVANACCSANGYLHKMSRLDKNCSKQLLSKKACPERYSHYKQPDSAAILKKCDGQPLALVTIGEFLQANGWPTGPNCEDLCNRLHYHLENDKTLERMWRVLVRNYTSLPGHALKACLLYFGMFPSDHPIRRKSLLRRWLAEGFVEPLSSSSNIDSTAAFNVLMDRNIIEPINVSNNDKVKTCQTYGMMREFISHMSISQNFVTFFCDDKFVPKYVRRLSLHGDTVVNGDNFNGIDLSLVRSLAVFGEAGTTVLDFSKYQLLRVLDLEKCDDLKDDHLKEICNLVLLKYLSLGGNISKLPKDIAKLKDLEALDVRRSKVKIMPVEVFGLPCLIHLLGKFKLSDKVKQKTEVQEFLLKGKSNLQTLAGFASNGSEGFLHLMRYMNKLRKLKIWCTSSAGSTDWTDLREAIQQFILDEKEANIGTRSLSLHFSGCSEDAINSLKEPCYLSSLKLHGNFPQLPQFVTSLRGLKELCLSSTKFTTGLLEALSNLSYLQYLKLVADELEKFIIKVQGFPRLLRLCIVLQYPTFPVIEEGALPFLVTLQLLCKDLHGLSDIQIECFKHLQEVTLHSGVTPATRQEWVKAAKEHPNRPKVLLLKSVDTAESEHTDVDSVMEAVKSETTEYSIAPEGPEQVNNKMQLDHGLESSSVLNKQNNFADQSSSKDQLHYSFNNMGLSDVSCCE | null | null | defense response to bacterium [GO:0042742]; innate immune response-activating signaling pathway [GO:0002758]; plant-type hypersensitive response [GO:0009626] | cytoplasm [GO:0005737] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; protein self-association [GO:0043621] | PF00931;PF18052; | 1.20.5.4130;1.10.8.430;3.40.50.300;3.80.10.10;1.10.10.10; | Disease resistance NB-LRR family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25024433}. | null | null | null | null | null | FUNCTION: Disease resistance (R) protein. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. Contribution of RGA5 is required to recognize the effector avirulence proteins AVR-Pia and AVR1-CO39 from M.oryzae (PubMed:21251109, PubMed:23548743). Acts as a constitutively active cell death inducer that is repressed by RGA5 (PubMed:25024433). Immune response triggered by the RGA4-RGA5 -mediated recognition of AVR1-CO39 confers resistance to X.oryzae pathovars (PubMed:27289079). {ECO:0000269|PubMed:21251109, ECO:0000269|PubMed:23548743, ECO:0000269|PubMed:25024433, ECO:0000269|PubMed:27289079}. | Oryza sativa subsp. japonica (Rice) |
F7J0N2 | RGA5R_ORYSJ | MDAPASFSLGAMGPLLRKLDSLLVAPEIRLPKPLKEGIELLKEDLEEIGVSLVEHSVVDSPTHKARFWMDEVRDLSYHIEDCIDTMFSMRSGGDDGKPRSERRHKVGRAKIDGFSKKPKPCTRMARIAELRALVREASERLERYQLGDVCGSSSPVVFTADGRARPLHHGVSANLVGVDEFKTKLNRWLSDEEGPHLKVAAIVGPAGIGKTALATELYRDHRWQFECRAFVRASRKPDMQRLLGGILSQVQRRQRSSDAYADSTVQSLIDNLREHLQDRRYLIIIDGLWETAVWNIANSAFPDVNSFSRILITADIEQVALECCGYKYDYIMRMEPLGSLDSKKVFFNKVFGSEDQCPPELKEVSNTILEKCGGLPLAIISIAGLLGSQPENPVLWDYVTKYLCSSLGTNPTLKDVVKETLNLSYNSLPHPFKTCLLYLGMYPDGHIMLKADLMKQWSAEGFVSANEAKDTEEIVDKYFDELVNRGILEPVEINKNGKVLSCTLHHAVHDLVMPKFNDDKFTMSVDYSQTITGPSTMVRRLSLHFSSTRYATKPAGIILSRVRSLAFFGLLNCMPCIGEFKLLRVLILEFWGSHGEQRSLNLIPVCRLFQLRYLKTSGDVVVQLPAQISGLQYLETLEIDARVSAVPFDLVHLPNLLHLQLQDETKLPDGIGCMRSLRTLQYFDLGNNSVDNLRGLGELTNLQDLHLSYSAPSSNEGLMINLNAITSSLSRLSNLKSLILSPGAISMVIFFDISSIISVVPVFLQRLELLPPICIFCRLPKSIGQLHKLCILKVSVRELLTTDIDNLTGLPSLTVLSLYAQTAPEGRFIFKDGTLPVLKYFKFGCGELCLAFMAGAMPNLQRLKLVFNIRKSEKYRHTLFGIEHLVSLQDIATRIGVDTSTGESDRRAAESAFKETVNKHPRCLRSSLQWVVSTEEESHPLEKQHHKREKGSSAGHGVLEKESVEDSEKNTDRVQTLLSPQLSNMESVVESALTGQRTKIVVKVHMPCGKSRAKAMALAASVNGVDSVEITGEDKDRLVVVGRGIDPVRLVALLREKCGLAELLMVELVEKEKTQLAGGKKGAYKKHPTYNLSPFDYVEYPPSAPIMQDINPCSTM | null | null | defense response to bacterium [GO:0042742]; innate immune response-activating signaling pathway [GO:0002758]; plant-type hypersensitive response [GO:0009626] | cytoplasm [GO:0005737] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein self-association [GO:0043621] | PF00931;PF18052; | 1.20.5.4130;3.30.70.100;1.10.8.430;3.40.50.300;3.80.10.10; | Disease resistance NB-LRR family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25024433}. | null | null | null | null | null | FUNCTION: Disease resistance (R) protein that recognizes the AVR-Pia and AVR1-CO39 effector avirulence proteins from M.oryzae. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. Contribution of RGA4 is required to recognize the effector avirulence proteins AVR-Pia and AVR1-CO39 from M.oryzae (PubMed:21251109, PubMed:23548743). Acts as a repressor of the RGA4-mediated cell death activation. Upon infection, recognition and binding of the AVR effectors relieve the RGA5-mediated repression and triggers the hypersensitive response (PubMed:25024433). Immune response triggered by the RGA4-RGA5 -mediated recognition of AVR1-CO39 confers resistance to X.oryzae pathovars (PubMed:27289079). {ECO:0000269|PubMed:21251109, ECO:0000269|PubMed:23548743, ECO:0000269|PubMed:25024433, ECO:0000269|PubMed:27289079}. | Oryza sativa subsp. japonica (Rice) |
F8G0M4 | HSPB_PSEP6 | MSMKQRVIIVGGGPVGLLTALGLAKAGTNVVVLEAESQPSDSPRALVYHFPVLPHLKRLGVLDDCVAAGLMRQNFAWRVHSTSEMIFWDLSCLEGDVELPYALHLGQDKLSRILIEHLKALPNVEVRYSSPVVDCEVGPRSVRVVLGGESPGVIVEGDWLIGADGANSFVRREVLNQNFFGITWPQRYVATNTRFDFDKLGFGKTTMQVDDVYGSVICNIDADSLWRVTFMEDPNLPMEGIRGRIDQVFKELLPTNDPYEVVAFSPYRMHQRVTDRMRNGRVILIGDAAHVTNPTGGLGLTGGMFDAFALTSVLNQVIHDGRSEDILDVFEADRRRKFIELVSPRASDNLRNLYHQKPGEGKNDWVNNTRSISKDIDRMRDALRFPETMETFL | 1.14.13.163 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305|PubMed:21949128}; Note=Binds 1 FAD per subunit. {ECO:0000305|PubMed:21949128}; | alkaloid metabolic process [GO:0009820]; nicotine catabolic process [GO:0019608] | null | FAD binding [GO:0071949]; monooxygenase activity [GO:0004497] | PF01494; | 3.30.70.2450;3.50.50.60; | PheA/TfdB FAD monooxygenase family | null | null | CATALYTIC ACTIVITY: Reaction=4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 H(+) + 2 NADH + O2 = 2,5-dihydroxypyridine + H2O + 2 NAD(+) + succinate semialdehyde; Xref=Rhea:RHEA:33927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57706, ChEBI:CHEBI:57945, ChEBI:CHEBI:66893; EC=1.14.13.163; Evidence={ECO:0000269|PubMed:21949128}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.175 mM for HSP {ECO:0000269|PubMed:21949128}; KM=0.2 mM for NADH {ECO:0000269|PubMed:21949128}; Note=kcat is 2 sec(-1). {ECO:0000269|PubMed:21949128}; | PATHWAY: Alkaloid degradation; nicotine degradation. {ECO:0000305|PubMed:21949128}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. At pH below 7.0 or above 9.0, there is substantial loss of activity. {ECO:0000269|PubMed:21949128}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25 degrees Celsius. The enzyme activity measured at 5 degrees Celsius is maintained up to 25 degrees Celsius but is lost quickly at higher temperatures. {ECO:0000269|PubMed:21949128}; | FUNCTION: Involved in the nicotine degradation (PubMed:21949128). Catalyzes the cleavage of 6-hydroxy-3-succinoylpyridine (HSP) by incorporation of oxygen at the 3-position to produce to 2,5-dihydroxypyridine (DHP) and succinic semialdehyde (PubMed:21949128). {ECO:0000269|PubMed:21949128}. | Pseudomonas putida (strain DSM 28022 / S16) |
F8G0P1 | PNAO_PSEP6 | MTKDGDEGSKSGVSRRKFLGSAAVGVATAGIASQLLTLSAPAEAAVKTNVGPSRAGVGYDVIVIGGGFAGVTAAREASRSGLKTLILEGRSRLGGRTFTSKLQNQKVELGGTWVHWTQPNVWTEIMHYGLEVEETVGLANPETVIWVTEDNVKRAPAAEAFEIFGSACNEYYKEARNIYPRPFEPFFERKKLQHVDGLSAADYLEKLPLTREQKDMMDSWLSGNGHNYPETIAYSEIMRWFALSNFNMPTMFDSIARYKIKTGTHSLLEAIMADGNSEVKLSTPVTKVNQDKDKVTVTTEDGVFTASAVIVAVPINTLHDIEYSPKLSAAKVDMGSQRHAGAGVKGYIRVKQNVGNVMTYAPARNKLTPFTSVFTDHVDESGTLLIAFSADPKLIDINDIKAVEKALQPLLPGVEVTASYGYDWNLDPFSKGTWCTYRPNQTTRYLTELQKREGRLFFAGSDMANGWRGFIDGAIENGREVGHQVATYLKRENDNA | 1.4.2.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:26634650, ECO:0000269|PubMed:35835223}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:35835223}; | alkaloid metabolic process [GO:0009820]; nicotine catabolic process [GO:0019608] | periplasmic space [GO:0042597] | oxidoreductase activity [GO:0016491] | PF01593; | 3.90.660.10;3.50.50.60; | Flavin monoamine oxidase family | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. {ECO:0000255|PROSITE-ProRule:PRU00648}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:35835223}. | CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + H2O + pseudooxynicotine = 4-oxo-4-(pyridin-3-yl)butanal + 2 Fe(II)-[cytochrome c] + 2 H(+) + methylamine; Xref=Rhea:RHEA:75351, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:59338, ChEBI:CHEBI:66878, ChEBI:CHEBI:66879; EC=1.4.2.3; Evidence={ECO:0000269|PubMed:35835223}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75352; Evidence={ECO:0000269|PubMed:35835223}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.073 mM for pseudooxynicotine (at 30 degrees Celsius) {ECO:0000269|PubMed:26634650}; Note=kcat is 0.790 sec(-1) (at 30 degrees Celsius). {ECO:0000269|PubMed:26634650}; | PATHWAY: Alkaloid degradation; nicotine degradation. {ECO:0000269|PubMed:24204321}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:26634650}; | null | FUNCTION: Involved in nicotine degradation (PubMed:26634650, PubMed:35835223). Catalyzes the deamination of pseudooxynicotine to 3-succinoylsemialdehyde-pyridine (PubMed:26634650, PubMed:35835223). Functions as a dehydrogenase that uses the c-type cytochrome protein CycN as the physiological electron acceptor (PubMed:35835223). O(2) is a poor electron acceptor (PubMed:35835223). Pnao is oxidized by CycN 230 times faster than O(2) at equivalent oxidant concentrations (PubMed:35835223). {ECO:0000269|PubMed:26634650, ECO:0000269|PubMed:35835223}. | Pseudomonas putida (strain DSM 28022 / S16) |
F8G0P2 | NICA2_PSEP6 | MSDKTKTNEGFSRRSFIGSAAVVTAGVAGLGAIDAASATQKTNRASTVKGGFDYDVVVVGGGFAGATAARECGLQGYRTLLLEARSRLGGRTFTSRFAGQEIEFGGAWVHWLQPHVWAEMQRYGLGVVEDPLTNLDKTLIMYNDGSVESISPDEFGKNIRIAFEKLCHDAWEVFPRPHEPMFTERARELDKSSVLDRIKTLGLSRLQQAQINSYMALYAGETTDKFGLPGVLKLFACGGWNYDAFMDTETHYRIQGGTIGLINAMLTDSGAEVRMSVPVTAVEQVNGGVKIKTDDDEIITAGVVVMTVPLNTYKHIGFTPALSKGKQRFIKEGQLSKGAKLYVHVKQNLGRVFAFADEQQPLNWVQTHDYSDELGTILSITIARKETIDVNDRDAVTREVQKMFPGVEVLGTAAYDWTADPFSLGAWAAYGVGQLSRLKDLQAAEGRILFAGAETSNGWHANIDGAVESGLRAGREVKQLLS | 1.4.2.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:24204321, ECO:0000269|PubMed:27933790, ECO:0000269|PubMed:29812904, ECO:0000269|PubMed:32873764, ECO:0000269|PubMed:33432238, ECO:0000269|PubMed:33464876}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:27933790, ECO:0000269|PubMed:29812904, ECO:0000269|PubMed:32873764, ECO:0000269|PubMed:33464876}; | alkaloid metabolic process [GO:0009820]; nicotine catabolic process [GO:0019608] | periplasmic space [GO:0042597] | nucleotide binding [GO:0000166]; oxidoreductase activity [GO:0016491] | PF01593; | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. {ECO:0000255|PROSITE-ProRule:PRU00648}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(S)-nicotine + 2 Fe(III)-[cytochrome c] = 2 Fe(II)-[cytochrome c] + 2 H(+) + N-methylmyosmine; Xref=Rhea:RHEA:73655, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:59806, ChEBI:CHEBI:193521; EC=1.4.2.2; Evidence={ECO:0000269|PubMed:33432238}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73656; Evidence={ECO:0000269|PubMed:33432238}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=43.5 nM for nicotine (at room temperature) {ECO:0000269|PubMed:26237398}; KM=91.9 nM for nicotine (at 37 degrees Celsius) {ECO:0000269|PubMed:26237398}; KM=114 nM for nicotine (at 22 degrees Celsius) {ECO:0000269|PubMed:29812904}; Note=kcat is 0.00664 sec(-1) with O(2) as electron acceptor (at room temperature) (PubMed:26237398). kcat is 0.0132 sec(-1) with O(2) as electron acceptor (at 37 degrees Celsius) (PubMed:26237398). kcat is 0.00611 sec(-1) with O(2) as electron acceptor (at 22 degrees Celsius) (PubMed:29812904). {ECO:0000269|PubMed:26237398, ECO:0000269|PubMed:29812904}; | PATHWAY: Alkaloid degradation; nicotine degradation. {ECO:0000269|PubMed:24204321}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:26237398}; | FUNCTION: Involved in nicotine degradation (PubMed:24204321, PubMed:26237398, PubMed:29812904, PubMed:33432238). Catalyzes the conversion of nicotine to N-methylmyosmine (PubMed:24204321, PubMed:29812904, PubMed:33432238, PubMed:33464876). N-methylmyosmine undergoes spontaneous hydrolysis to form pseudooxynicotine (PN) (PubMed:24204321). S-nicotine is the optimal substrate (PubMed:29812904). Has lower activity with some nicotine analogs, but shows no activity towards neurotransmitters, including serotonin, dopamine, and norepinephrine, nicotine metabolites and common neuroactive drugs (PubMed:29812904). The enzyme is stereospecific with poor activity with (R)-nicotine as the substrate (PubMed:29812904). The c-type cytochrome protein CycN is the physiological electron acceptor (PubMed:33432238). O(2) is a poor electron acceptor (PubMed:33432238, PubMed:33464876). {ECO:0000269|PubMed:24204321, ECO:0000269|PubMed:26237398, ECO:0000269|PubMed:29812904, ECO:0000269|PubMed:33432238, ECO:0000269|PubMed:33464876}. | Pseudomonas putida (strain DSM 28022 / S16) |
F8J4S0 | TOP4A_OXYTA | MKISQVFIFVFLLMISVAWANEAYEEESNYLSERFDADVEEITPEFRGIRCPKSWKCKAFKQRVLKRLLAMLRQHAF | null | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; hemolysis in another organism [GO:0044179] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | toxin activity [GO:0090729] | null | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21933345, ECO:0000303|PubMed:21933345}. Target cell membrane {ECO:0000305|PubMed:21933345}. Note=Probably forms a transmembrane alpha-helix in the target cell membrane. {ECO:0000269|PubMed:21933345, ECO:0000303|PubMed:21933345}. | null | null | null | null | null | FUNCTION: Disrupts cell membranes through the formation of pores (Probable). Has antibacterial activity against Gram-positive bacteria S.aureus (MIC=10 uM) and B.subtilis (MIC=0.5 uM) as well as Gram-negative bacteria P.fluorescens (MIC=1 uM) and E.coli (MIC=0.5 uM). Has hemolytic activity against human erythrocytes (EC(50)=7 uM). {ECO:0000269|PubMed:21933345, ECO:0000305}. | Oxyopes takobius (Lynx spider) (Oxyopes foliiformis) |
F8KAY7 | RSAKS_PSESP | MSRFIRASQRRTLLATLIAATLAQPLLAAESLDSKPASAITAAKNAEVLKNLPFADREEFEAAKRGLIAPFSGQIKNAEGQVVWDMGAYQFLNDKDAADTVNPSLWHQAQLNNIAGLFEVMPKLYQVRGLDPANMTIIEGDSGLVLIDTLTTAETARAALDLYFQHRPKKPIVAVVYSHSHIDHFGGARGIIDEADVKAGKVKVFAPSGFMEHAVSENILAGTAMARRGQYQSGVMVPRGAQAQVDSGLFKTTATNATNTLVAPNVLIEKPYERHTVDGVELEFQLTLGSEAPSDMNIYLPQFKVLNTADNAPPAMHNLLTPRGAEVRDAKAWAGYIDASLEKYGDRTDVLIQQHNWPVWGGDKVRTYLADQRDMYAFLNNRALNLMNKGLTLHEIAAEVSKLPGELDRKWYLRSYYGALSTNLRAVYQRYLGFYDGNPANLDPFPPVEAGKRYVEAMGGADAVLKQMRAAIDKGDYRWAVQLGNHLVFADPANKDARALQADAMEQLGYQTENALWRNMYMTGAMELRHGVPTYDSRGKSEMGRALTPDMFFDLLAIRLDTDKAVGHDMTLNWVFEDLKQDIALTLRNGVLTQRVGSLNPKADVTVKLTKPTLDQIAARKLDLPTAIKQGTVKLDGDGKKLGEFFGLLDSFSPKFNIVEPLE | 3.1.6.19 | null | dodecyl sulfate metabolic process [GO:0018909] | outer membrane-bounded periplasmic space [GO:0030288] | linear primary-alkylsulfatase activity [GO:0018741]; metal ion binding [GO:0046872]; protein dimerization activity [GO:0046983] | PF14864;PF14863;PF00753; | 1.25.40.880;3.60.15.30;3.30.1050.10; | Metallo-beta-lactamase superfamily, Type III sulfatase family | null | null | CATALYTIC ACTIVITY: Reaction=an (R)-secondary-alkyl sulfate + H2O = an (S)-secondary-alcohol + sulfate.; EC=3.1.6.19; Evidence={ECO:0000269|PubMed:21770430, ECO:0000269|PubMed:23061549, ECO:0000269|Ref.2}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=151 uM for (R)-2-octyl sulfate {ECO:0000269|PubMed:23061549}; KM=651 uM for 1-octyl sulfate {ECO:0000269|PubMed:23061549}; Note=kcat is 262 min(-1) with (R)-2-octyl sulfate as substrate. kcat is 52 min(-1) with 1-octyl sulfate as substrate. {ECO:0000269|PubMed:23061549}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Is very stable at 20-30 degrees Celsius. {ECO:0000269|Ref.2}; | FUNCTION: Alkylsulfatase that catalyzes the enantioselective hydrolysis of secondary-alkylsulfates with strict inversion of configuration, leading to the formation of homochiral (S)-configurated alcohols and nonreacted sulfate esters (PubMed:21770430, PubMed:23061549, Ref.2). The substrate spectrum includes a range of linear, branched or cyclic sec-alkylsulfates (PubMed:21770430). Can use sec-alkylsulfate esters bearing aromatic, olefinic and acetylenic moieties (Ref.2). Acts by cleaving the C-O bond, resulting in inversion at the carbon (PubMed:23061549). {ECO:0000269|PubMed:21770430, ECO:0000269|PubMed:23061549, ECO:0000269|Ref.2}. | Pseudomonas sp |
F8QN53 | PA2A2_VIPRE | MRILWIVAVCLIGVEGNLYQFGKMIRYKTGKSALLSYSDYGCYCGWGGQGKPKDATDRCCFVHDCCYGRVNGCDPKLTIYSYSFENGDIVCGGDDSCKRAVCECDRVAAICFGENLNTYDKKYKNYPSSQCTETEQC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21185324}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036, ECO:0000269|PubMed:21185324}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=3592 umol/min/mg enzyme (Vur-PL2B) {ECO:0000269|PubMed:21185324}; Note=Vmax=1736 umol/min/mg enzyme (Vur-PL2A). {ECO:0000269|PubMed:21185324}; | null | null | null | FUNCTION: Snake venom phospholipase A2 that causes internal bleeding, shows very strong anticoagulant activities and inhibits ADP-induced platelet aggregation (PubMed:21185324). Shows very low cytotoxicity (PubMed:21185324). Is not able (or very weakly) to suppress the acetylcholine (ACh)-evoked current mediated by alpha-7-similar nAChRs in L.stagnalis neurons (IC(50)>30 uM) and to compete with alpha-bungarotoxin for binding to muscle- and alpha-7 neuronal nAChR types, as well as to AChBPs (PubMed:25522251). In inhibition of alpha-bungarotoxin binding, this toxin is similarly active against T.californica nAChR (IC(50)>100 uM), human alpha-7 nAChR (IC(50)=29 uM), and L.stagnalis AChBP (IC(50)>30 uM) (PubMed:25522251). {ECO:0000269|PubMed:21185324, ECO:0000269|PubMed:25522251}. | Vipera renardi (Steppe viper) (Vipera ursinii renardi) |
F8QN54 | PA2B_VIPRE | MRTLWIVAVCLIGVEGSLLEFGMMILEETGKNPLTSYSFYGCYCGVGGKGTPKDATDRCCFVHDCCYGNLPDCNPKIDRYKYHRKNGAIVCGKGTSCENRICECDRAAAICFRKNLKTYNHIYKYYPDFLCKKESEKC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | acetylcholine receptor inhibitor activity [GO:0030550]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21185324}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036, ECO:0000269|PubMed:25522251}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=0.7 mmol/min/umol enzyme {ECO:0000269|PubMed:25522251}; | null | null | null | FUNCTION: Snake venom phospholipase A2 that may have a strong anticoagulant activity (PubMed:21185324). Is able to suppress the acetylcholine (ACh)-evoked current mediated by alpha-7 (CHRNA7)-similar nAChRs in L.stagnalis neurons (IC(50)=10.5 uM) and to compete with alpha-bungarotoxin for binding to muscle- and alpha-7 neuronal nAChR types, as well as to AChBPs (PubMed:25522251). In inhibition of alpha-bungarotoxin binding, this toxin is mostly active against T.californica nAChR (IC(50)=0.26 uM), it is moderately active against human alpha-7 nAChR (IC(50)=14 uM), and is not active against L.stagnalis and A.californica AChBP (IC(50)>30 uM) (PubMed:25522251). {ECO:0000269|PubMed:21185324, ECO:0000269|PubMed:25522251}. | Vipera renardi (Steppe viper) (Vipera ursinii renardi) |
F8S296 | ATG2_ARATH | MVFPWNIAKSAEEAFSRWAVKRVVKFLLKKKLGKLILGDIDLDQLDIQLRDGTIQLSDLAINVDYLNDKFDAPLVIKEGSIGSLLVKMPWKTNGCQVEVDELELVLAPRLESNKSSSNEASTSASTREDLHNIRLEIGKHENEMLMNAAKSASIDVHEGVKTVAKIVKWFLTSFHVKIKNLIIAFDPDFGKKQSEAGPRPTLVLRMTEIECGISEEQVSANEVSPDNFLGINRLANCVKFQGAVVELLNMDDDDDGDKTCDKKTSNDVTLIMTGVGGGFSGSLNFSIPWKNGSLDIRKVDADISIDPVEVRFQPSTIRWFLQLWKTFTSFGSDCFPSVSHSDFLTDSPTIPTNVMVTPPATLSLSGGQELEHDTTPNLQFIPDWFPSSFSKKEEDGEVDIGASVDQFFECFDAMRSYQSASGSQGMWNWTSSVFTAINAASSLASGSLLLPSEQQHVETSCKVSFAGVSVVLFFQDEVNWKGVSTRIHYLGAELRDISVSFQVCLHDLRLEGEVNSMEIADYCQGGNVVDTANAESQTCLIKDLQAKVQTSLPPFASSDMHSDSERLSEIVSDGFLFRNKGFAVKTLLVIAAGGSGFQFTVNFQSSKASHRGSNSFSLSLPPTTFWLNLHSVEMLVNLFNDVSESIPITSHERNQVASSSKSESLRGSVSICNARVILWFPFESISERFCNSLGQQFIVVDLSSSPPSDKERAKERSPGEMHFPSATRSICFSVGDASIYLVTSDLKDSETNSYHRQVEFSAYNILHTNNKTRHQLSTIGMFWQDRPTVSPWLVERAKMLATQEESIQTDKSGGRGLEFAAVATPKDQDDIYSRSRKEIILASSFCLYVHLLPLAIHLDSWQYSKLCNLIEEAKNWLSRMAANTAEQTEESVVCQTSLVVDCDSIDILVRPEPRMGIKKQLQTELPGSWIQFNLRVQKLNLMSVPNLGSVSGADFFWLAHGEGTLLGSVTGLPDQELLLLSCNNSAIKRGNGGGSNALSSRFAGLDFLHLQEPGICNDYLAVSARGCTISAVGGRLDWIEVATSFFSFEDEKKTQEINSSSSSGSSFILNFVDVGLSYEPHHENTDHLRQASDPWVACLVAASSFSLSKKSLVDSIRNDYRIRIQDLGLLLSVDFDLSKLGGTYSSEHLHESGYVKVANDSLIEAILRTNSENGLLWELECSKSHLVIETCSDTTSGLIRLATQLQQLLAPDLEESAVHLQTRWDSIQQANARNDLDISDRLSSSDSSGEMKYLRLESENETGVIGLMDEINEDAFQFDVNPTYQSDSVECQNNYMSPHGISHGQAYNWVPATEKLPSNQSICGSSSRINSESSQVFLERESLPEIFENYCLSEFRPSSEVPQEGDSSGRELFPETDLRRGNSGWYDDASLRIVEDHVSEATEEDHEEHILDGECSSFGQTSYSAVAANGRILLKNIDLKWRIYSGSDWHDSRKKGENFKHTKGRDTTSCLELELSGVQFLYETFPIGEICTSKLSLMVQDFYLYDRSDNAPWTLVLGYYNSKDHPRDSSSYAFKLELKAVRPDPETPLEENRLRVALLPILLHLHQSQLDFLISFFGANSLEKPVVSMGDSGGSTMSVSVQGHNIIEEALLPYFQKFDIWPVNVRVDYSPHHVDIAALTGGKYAELVNLVPWKGIELQLKHVHAAGIYGWGNVCETILGEWLEDVSQNQIHQLLKGIPTVRSLSALYAAALKLVSSPVESYRKDRRLVKGVQRGTVAFLRSISLEAVGLGVHLAAGAHDILLRAEYIFASSPSLPQPQGRTKTNVRHNQPRNAKQGMLKACESIGDGIGKTASALVRTPLKKYQRGDGAGSAFATVVQGVPTAAIAPASACARAVHSALVGIRNSLDPEHKKESMEKYLGPDKQRKQDQHR | null | null | autophagosome assembly [GO:0000045]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; leaf senescence [GO:0010150]; lipid transport [GO:0006869]; piecemeal microautophagy of the nucleus [GO:0034727]; protein transport [GO:0015031]; reticulophagy [GO:0061709] | endoplasmic reticulum membrane [GO:0005789]; phagophore assembly site membrane [GO:0034045] | phosphatidylinositol-3-phosphate binding [GO:0032266] | PF09333;PF13329;PF12624; | null | ATG2 family | null | SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q96BY7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96BY7}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P53855}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53855}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663, ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:Q2TAZ0}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895, ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:Q2TAZ0}; | null | null | null | null | FUNCTION: Lipid transfer protein involved in autophagosome assembly (PubMed:21645148). Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion (By similarity). Binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, and extracts phospholipids from the membrane source to the IM for membrane expansion (By similarity). Plays an essential role in plant nutrient recycling (PubMed:19773385, PubMed:21645148). Involved in the negative regulation of plant defense responses to biotrophic pathogens (PubMed:21645148). Involved in a negative feedback loop that modulates NPR1-dependent salicylic acid (SA) signaling and limits senescence and immunity-related programmed cell death (PCD) in plants (PubMed:19773385). Involved in the degradation of damaged peroxisomes (PubMed:24368788). {ECO:0000250|UniProtKB:Q2TAZ0, ECO:0000269|PubMed:19773385, ECO:0000269|PubMed:21645148, ECO:0000269|PubMed:24368788}. | Arabidopsis thaliana (Mouse-ear cress) |
F8VPJ6 | RFX7_MOUSE | MAEEQQQPPPQQLDAPQQLPLSAPNPGVALPALVPGLPGTEANALQHKIKNSICKTVQSKVDCILQEVEKFTDLEKLYLYLQLPSGLSSAEKSDQNAMSSSRAQQMHAFSWIRNTLEEHPETSLPKQEVYDEYKSYCDNLGYHPLSAADFGKIMKNVFPNMKARRLGTRGKSKYCYSGLRKKAFVHMPTLPNLDFHKTGDGLEGVEPSGQLQNIDEEVISSACRLVCEWAQKVLSQPFDTVLELAHFLVKSHYIGTKSMAALTVMAAAPAGLKGIPQPSAFIPTAESNSFQPQVKTLPSPIDAKQQLQRKIQKKQQEQKLQSPLPGESSAKKPEGTTANGVANLPNGNPAILSPQPIGIVVAAVPSPIPVQRTRQLVTSPSPMNSPDGKVLPLNVQVVTQHMQSVKQTPKTPQNVPASPGGDRSARHRYPQILPKPANTSALTIRSPTTVLFTSSPIKTAVVPASHMSSLNVVKMTTISLTPSNSNAPLKHSASVSSATGTTEESRIVPQIKNGSVVSLQSPGSRASSTGGTSAVEVKMEPEGSSDEHPLQCQENSEETKAPLTTSSALWGQKSNTDGTVPKPSNEGVTEVKTTKVCDQRTKCKNRCNEILSGISAGNNQSTVTLSVATQNLPFTSTSSPSNGDSVNKDPKICTKSPRKRLSATLQESQVPPVKKPIVEQLSAVTIEGQKPGTVKKDQKVPHSGKTESSTAGAQIPNKVSISVSSQIIEDQPVNPALVTSEPVLEQQTTPSSSPDVKVKLEGSVFLLDRESKSDGSFNRNEWQQVTKDSDFIAASCEHQQDISVMTIAEHPDIHDLEKSVWELEGMPQDTYSQQLHSQIPESSLNEIQAQSSDQLPLQSELKEFESSVSQTNESYFPFDDELTQDSIVEELVLMEQQMSMNNSHSYGNCLGMSLQNQSVTPGAPMSSHASSTHFYHPIHSNGTPIHTPTPTPTPTPTPTPTPTPTSEMIAGSQSLSRESPCSRLAQTTPVDSALGSSRHTPIGTPHSNCSSSVPPSPVECRNPFAFTPISSSMAYHDASIVSSSPVKPMQRPMATHPDKTKLEWMNNGYGGVGNSSVSGHGILPSYQELVEDRFRKPHAFAVPGQSYQSQSRHHDTHFGRLTPVSPVQHQGATVNTNKQEGFAVPAPLDNKGTNSSAGSNFRCRSVSPAVHRQRNLSGSTLYPVSNIPRSNVTPFGSPVTPEVHVFTNVHTDACANNIAQRSQSVPLTVMMQTAFPNALQKQTNSKKITNVLLSKLDSDNDDSVRGLGINNVPSNYTARMNLTQILETSPVFPSANSQNMIDSSTSVYEFQTPSYLTKSNSTDQISFSPGDNQAQSEIGEQQLDFNSTVKDLLSGDNLQTSQQLVGQVASDLTNTASDFSSDIRLSSDLSGSINDLNTLDPNLLFDPGRQQGQDDEATLEELKNDPLFQQICSESMNSMTSSGFEWIESKDHPTVEMLG | null | null | positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979] | PF18326;PF02257; | 6.10.140.1290;1.10.10.10; | RFX family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29967452}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:29967452). Acts as a transcriptional activator by binding to promoter regions of target genes, such as Rec8, Mxd4 and Ddit4 (PubMed:29967452). Plays a role in natural killer (NK) cell maintenance and immunity (PubMed:29967452). May play a role in the process of ciliogenesis in the neural tube and neural tube closure (By similarity). {ECO:0000250|UniProtKB:A0A1L8H0H2, ECO:0000269|PubMed:29967452}. | Mus musculus (Mouse) |
F8VPN2 | TEX15_MOUSE | MTYFFIYVSTERACSLNNCTIAKRIGKGKDATVIFEHFRKPVDPFVQENCPCKALNSEMGPFSSDTSSSYGNVQNGNNSVLEAYNRQTENSSNLRDASQVYTHNSGFSFIPTGNTASGNGDLFSVTYLRSILSSISAAFPSHNNTGSSTVITSKLIKDPRLMKREQSMRNKSDTAGLSDVLPLDKSLGCGDSQIKLTCMPTSSISSSEVPADNTITSCLNASCFKFSSESSHYQAHNSSSKGHDCIASSSIAVTEQFKEQHSSSFPSSLSNAFSDVRKQKHSEEQVQRAQMRSNVPVLTALSSESRNSDESENTCSNDSQGHFSQESPSSDINSIYKVGHQMSTVFPAQKKGNLCEYIQDTGMMRASISTEDSTKDGVNHTWCKETVLSNETVSSPIDNSNTLYQEHKEGGNLNSLSGNCEKIGVTHKLQVPKFPISSTGDKNELYRAALELECSLTPTIECLSQKYPQHSLEHEDNTNFAMTQGLIELKTVQNNQNFGNILSDAFQEAKDVPLASEKLIDRVISSAAIDISLDSSVCNIIGEYTCVRRENENGEASPYNCHKEEASRVKDGVQDHSLSYDAELSCDLNLKINLQEQRDDKNPNEAKEHNTDNINGSEKQDCLANDHFTNIVEMREIKSNTEVEILNSEECFTFNSFRGKNGKPAETASSESEAVEQRHAPNDQRGLEHLVSSFPEIEGSSVCVASNATKQIVGTTVLTVSTSLGDHQKDELKEICSSESSDLGLVKHSISECEIDTDKDKLQDFHQLVNENSALKTGLGSEIEVDLEHDNASVFQQNMHSQGNDLCEEFELYESLKSRIDWEGLFGSSYEEIESSSFARREGTDQHSSTECNCVSFCSQDKRELHNPIFLPDLQVTITNLLSLRISPTDESLELKDNFYKQVTESTEPETNKEGNASGFGMCSQPSGENSSFSCANKFGNSVQESGDVSKSESSHSSNSSHNTHVDQGSGKPNNDSLSTEPSNVTVMNDKSKCPTKSKPVFNDTRNKKDMQSRSSKRTLHASSSRGQNIANKDLREHETHEKKRRPTSHGSSDRFSSLSQGRIKTFSQSEKHIRNVLNILNNEASLCKSKHLSRKLNKAVLHLKKAHRRVHTSLQLISKVGQKRKGPLPKAYAVIHNNFWESCDHQGDSLMSERRYSKHFLSKRKYDKQGDKRFLRFDIEESLTPVSKHRLYRTNRERIAECLSNEVMSGHVSSSLTTFHVREFCDEEQFPEPQLPLAYTSQSISQLEYTNSIVGNESSSELEHFSETSGNMLDPKETLTEKEYQTHTQLCNSDSAKLKNHTTHSIRDIAKECNSEDKTVLCESNPVYLSFIKENTSHSPDKSYDSNCKANTDIHISVLGSKKKHILSVDIYEQDNCVSDGVKSGEAIFPIEKCTVPMETTSSIPTENIASKSYTIPPVSSILVTAGEEESSVGENGLFDVNENEMNITMHSKLDLTSVTEESKICKKNMKNLSCNDSSMLLKENITGPSKRYMAKYIEEEKIRKIEQAVYKKIITEGSPISFKYKSQNKILKEKSFHVNKKIITNNLTDSHLSIKNSTVDTIALKDIPNQLKERKEAGQIKVNNNSHSDCLSKPAIVETNHRPVLHGNPKVATLQKELKEHRSPNYTSHVTELSQILQRADEAASLQILEEETKLCQNILPLFVQAFERQQECSIDQILISRKLLVEQNLWNNCRLKLKPCAVDTWVELQMAMETIQFIENKKRFLEGKPTFRSLLWYDESLYSELLRRPRGYQLQSNFYPGFQGRLKYNAFCELQNYHNQLVEFLTETKKENNSYYALLKYKRQINECEAIMKHYSDCFDFCLSVPFACGVNFGDSLGDLETLRKSTLKLISVPGGSPKVHSYPGKKDHLWIIIEIVSSKVSFIKSNEEISIKICLYGLEHIYFDAAKSLVWKEKSCSLPKKHSEKNREMEEINERAFSKLKKIYDVLSKGLNNEPTSIGLQEDAIIASKQSTLGSISNCRLNKAWLSYPDISCVGEILDQAKSADLEELQGLTLRCTDHLEILKKYFQMLQEDNIDNIFIMEENVLDMLSNHNLGAVILKPEAIEIYIEIVMISETIHYLKNLIAKKLHNQRFRGMLWFDWSLLPELIGCQEEVVSLSVGDTQTHCLWKLVETAISVLKKELAVIYEYGEASNCSYALHLFYRELKELTGVKRLLNNSKYSVSTYIDLVPHTASVNFGNTVAELEHNYKQFFLLLKNVMSVPQKDFGKMVHIIKVMKTIEHMKLLSAKDTKLSTHLLFLQMLRNKRNALQQNRQEKMETPVTEPGEDSSQPGVSEQTPPGTECTVKNISDSSKKRPVTADTCEVSQGKGNTDTVPSWKKQKVTMKDVGNIQTVSKHPSTTGSPPNDENKIGSNSSDSLKSISASPEVVKRQSSVLGSVSPAESVQDTCTPKSESKVEPTDSLPDSLASLTEQQENSNVIEKRNGNSSVAETNDKKDCPLVTCDQKDIDASYSPDHTPAQESHKTPVDHTQISPSNLTAGNDDPLVPDASLLSVSASQSEKDVYLSGTDFHHENNKILNLSTEDCTGTSSPEPVCIKDKISVLQVDKTQPIKSESPKKSMTDAPNPNTAPFGSYGNSALNVNGTVQHTHSEQNSKVLTQKVGTSRNIPPQSACSPVHNSSAHSFGTSYPYYSWCFYQYSSSNGTAVTHTYQGMTAYEIQQPPPPVLTTVASTVQSTHFNRSYSEHFSYFPGQPQANSFNPGNGYFPSHTPVSYNYQQPVYSQFASHQPVPQATYPYPPNPGAPPQVPWTYAPWQQNPFLRRP | null | null | cell differentiation [GO:0030154]; DNA methylation-dependent heterochromatin formation [GO:0006346]; DNA repair [GO:0006281]; fertilization [GO:0009566]; homeostasis of number of cells within a tissue [GO:0048873]; homologous chromosome pairing at meiosis [GO:0007129]; male genitalia development [GO:0030539]; male meiotic nuclear division [GO:0007140]; piRNA-mediated retrotransposon silencing by heterochromatin formation [GO:0141006]; protein localization to chromosome [GO:0034502]; regulation of double-strand break repair via homologous recombination [GO:0010569]; regulation of protein localization [GO:0032880]; retrotransposon silencing [GO:0010526]; spermatogenesis [GO:0007283]; synaptonemal complex assembly [GO:0007130] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | null | PF15326; | null | TEX15 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18283110, ECO:0000269|PubMed:32381626}. Nucleus {ECO:0000269|PubMed:18283110, ECO:0000269|PubMed:32381626, ECO:0000269|PubMed:32719317}. | null | null | null | null | null | FUNCTION: Required during spermatogenesis for normal chromosome synapsis and meiotic recombination in germ cells. Necessary for formation of DMC1 and RAD51 foci on meiotic chromosomes, suggesting a specific role in DNA double-stranded break repair (PubMed:18283110). Essential executor of PIWIL4-piRNA pathway directed transposon DNA methylation and silencing in the male embryonic germ cells (PubMed:32381626, PubMed:32719317). PIWIL4-piRNA binds to nascent transposon transcripts and interacts with TEX15, which may in turn recruit the epigenetic silencing machinery to the transposon loci (PubMed:32381626). Not required for piRNA biosynthesis (PubMed:32381626, PubMed:32719317). {ECO:0000269|PubMed:18283110, ECO:0000269|PubMed:32381626, ECO:0000269|PubMed:32719317}. | Mus musculus (Mouse) |
F8VPQ2 | ARI4A_MOUSE | MKAADEPAYLTVGTDVSAKYRGAFCEAKIKTVKRLVKVKVLLKQDNTTQLVQDDQVKGPLRVGAIVETRTSDGSIQEAIISKLTDASWYTVVFDDGDERTLRRTSLCLKGERHFAESETLDQLPLTNPEHFGTPVIAKKTNRGRRSSLPITEDEKEEESSEEEDEDKRRLNDELLGKVVSVASTAESTGWYPALVVSPSCNDDVTVKKDQCLVRSFIDSKFYSIARKDIKELDILTLPESELCARPGLRRASVFLKGRIVPDNWKMDISEILESSSSDDEECPAEEHEEEKEKEAKKEEEELPEEELDPEERDNFLQQLYKFMEDRGTPINKPPVLGYKDLNLFKLFRLVYHQGGCGNIDSGAVWKQIYMDLGIPILNSAASYNVKTAYRKYLYGFEEYCRSANIQFRTIHHHEPKVKEEKKDFEDSMDEALKEAPEMPLLDVKSEPEENTDSNSESDREDTELKSPRGRRKIVRDANCIKKEIEEEKIEDKFLRDDLENKDAGDDDDDGDPAAKREHELLFGRKSTPKNKEKKIKKPEDSERDSDEEEEKSQEREETESRCDSEGEDEEDDTEPCLTGTKVKVKYGRGKTQKIYEASIKSTEMDDGEILYLVHYYGWNVRYDEWVKADRIIWPLDKGGPKKKQKKKVKNKEDSEKDEKRDEERQKSKRGRPPLKSTFSPNMPYSLSKTSNSEGKSDSCSSDSEADDQLEKSSGGEDLSPDVKEELEKNENAHDDKLDEENPKIVHISKENDRTQAQPSDTLTVEAGDSDQIVHIFGDKVDQVEEFKKQVEKSPKGKGRRSKTKDLSLELIKISPFGQEEAGSEAHGDVHSLEFSSLECKNFSSTEDDIDPYEKEKKLKRKILGQQSPEKKLRLDNGMEMTTGVSQERSDDGAGAEGMKGAHVEQHFETEGEGMPSLTAEPDQGLQELTSEKSDSPAEEEPVHTPLKEEEDAMPLIGPETLVCHEVDLDDLDEKDKTSIEDVVVEGSESNSLASVPPALPPVAQHNFSVASPLTLSQDESRSIKSESDITIEVDSIAEESQEGLCERESANGFEASVASGACSIIAHERESREKGQKRPSDGNSGLIAKKQKRTPKRTSAAAKTEKNGAGQSSDSEDLPAMDSSSNCTPVKRLTLPKSQKLPRSPARTSPHIKDAEKEKHREKHPNSSPRTYKWSFQLNELDNMNSTERISFLQEKLQEIRKYYMSLKSEVATIDRRRKRLKKKDREVSHAGASMSSASSDTGMSPSSSSPPQNVLAVECR | null | null | chromatin organization [GO:0006325]; erythrocyte development [GO:0048821]; establishment of Sertoli cell barrier [GO:0097368]; genomic imprinting [GO:0071514]; negative regulation of cell migration [GO:0030336]; negative regulation of stem cell population maintenance [GO:1902455]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of stem cell population maintenance [GO:1902459]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; spermatogenesis [GO:0007283]; transcription by RNA polymerase II [GO:0006366] | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; transcription repressor complex [GO:0017053] | transcription cis-regulatory region binding [GO:0000976] | PF01388;PF08169;PF11717; | 2.30.30.140;1.10.150.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305|PubMed:17043311, ECO:0000305|PubMed:23487765}. | null | null | null | null | null | FUNCTION: DNA-binding protein which modulates activity of several transcription factors including RB1 (retinoblastoma-associated protein) and AR (androgen receptor) (PubMed:17043311, PubMed:23487765). May function as part of an mSin3A repressor complex (By similarity). Has no intrinsic transcriptional activity (PubMed:23487765). Plays a role in the regulation of epigenetic modifications at the PWS/AS imprinting center near the SNRPN promoter, where it might function as part of a complex with RB1 and ARID4B (PubMed:17043311). Involved in spermatogenesis, together with ARID4B, where it acts as a transcriptional coactivator for AR and enhances expression of genes required for sperm maturation (PubMed:23487765). Regulates expression of the tight junction protein CLDN3 in the testis, which is important for integrity of the blood-testis barrier (PubMed:23487765). Plays a role in myeloid homeostasis where it regulates the histone methylation state of bone marrow cells and expression of various genes involved in hematopoiesis (PubMed:18728284). May function as a leukemia suppressor (PubMed:18728284). {ECO:0000250|UniProtKB:P29374, ECO:0000269|PubMed:17043311, ECO:0000269|PubMed:18728284, ECO:0000269|PubMed:23487765}. | Mus musculus (Mouse) |
F8VPU2 | FARP1_MOUSE | MGEIEQKPTPASRLGAPENSGISTLERGQKPPPTPSGKLMTVKIQMLDDTQEAFEVPQRAPGKVLFDAVCNHLNLVEGDYFGLEFPDHRKIVVWLDLLKPIVKQIRRPKHVVVKFVVKFFPPDHTQLQEELTRYLFALQVKQDLAQGRLTCNDTSAALLISHIVQSEIGDFDEALDREHLAKNKYVPQQDALEDRIMEFHHSHVGQTPAESDFQLLEVARRLEMYGIRLHPAKDREGTKINLAVANTGILVFQGFTKINAFNWAKVRKLSFKRKRFLIKLRPDVNSSYQDTLEFLMAGRDFCKSFWKICVEHHAFFRLFEEPKPKPKPVLFSRGSSFRFSGRTQKQVLDYVKEGGHKKVQFERKHSKIHSTRSLVSQPTAPNSEVPKQSPQSASLTFGEGTESPGGQSCQQAKETKACTLELGPHQSPALPKSPPGSKAADGTTVVPPEEEEEEEGGKDGIRPSNPQPPQPSTGSLTGSPHLSELSINSQGGAAPANVTLSPNLSPDNKQASPLISPLLNDQACPRTDDEEEGRRKRFPTDKAYYIAKEVSTTERTYLKDLEVIASWFQSTVSKEDSMPEALKSLIFPNFEPLHKFHTNFLKEIEQRLALWEGRSNAHVRGDYQRIGDVMLKNIQGMKHLAAHLWKHSEALEALETSIKGSRRLEHFCRDFELQKVCYLPLNTFLLRPLHRLMHYKHVLERLCKHHPPNHADFRDCRAALAEITEMVAQLHGTMIKMENFQKLHELKKDLIGIDNLVTPGREFIRLGSLSKLSGKGLQQRMFFLFNDVLLYTSRGLTASNQFKVHGQLPLYGMTIEESEEEWGVPHCLTLRGQRQSIIVAASSRSEMEKWMEDIQMAIDLAEKSNGPTPELLASSPPDNKSPDEATAADQESEDDLSASRTSLERQAPHRGNTMVHVCWHRSTSVSMVDFSIAVENQLSGNLLRKFKNSNGWQKLWVVFTNFCLFFYKSHQDSHPLASLPLLGYSLTIPSESENIHKDYVFKLHFKSHVYYFRAESEYTFERWMEVIRSATSSASRAHILSHKESHLY | null | null | dendrite morphogenesis [GO:0048813]; enzyme-linked receptor protein signaling pathway [GO:0007167]; positive regulation of skeletal muscle acetylcholine-gated channel clustering [GO:1904395]; postsynaptic actin cytoskeleton organization [GO:0098974]; Rac protein signal transduction [GO:0016601]; regulation of presynapse assembly [GO:1905606]; retrograde trans-synaptic signaling by trans-synaptic protein complex [GO:0098942]; synapse assembly [GO:0007416] | cytoplasmic side of plasma membrane [GO:0009898]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; extrinsic component of postsynaptic membrane [GO:0098890]; filopodium [GO:0030175]; glutamatergic synapse [GO:0098978] | cytoskeletal protein binding [GO:0008092]; guanyl-nucleotide exchange factor activity [GO:0005085]; small GTPase binding [GO:0031267] | PF08736;PF09380;PF00373;PF09379;PF00169;PF00621; | 1.20.80.10;1.20.900.10;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23209303}; Peripheral membrane protein {ECO:0000269|PubMed:23209303}; Cytoplasmic side {ECO:0000269|PubMed:23209303}. Synapse {ECO:0000269|PubMed:23209303}. Synapse, synaptosome {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Note=Recruited to the cell membrane via interaction with CADM1. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Functions as a guanine nucleotide exchange factor for RAC1. May play a role in semaphorin signaling. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
F8VPZ5 | ERCC6_MOUSE | MFHEEVPNSTHPQEQDCLPSQHANAYKDMPVGQENGGVSEAGECLSSTSCEYGPSTSAEACVLAATRRGPTLLHIDRHQIPAVEPSAQALELQGLGVDVYDQAVLEQGVLQQVDSAMHEASCVAQLADAEKEYQSVLDDLMSCTTSLRQINKIIEQLSPQAASNRDINRKLDSVKRQKYNKEQQLKKITAKQKRLQAILGGAGVQVELDHASLEEDDAEPGPSCLGSMLMPAQETAWEELIRTGQMTPFGTPAPQKQEKKPRKIMLNEASGFEKYLAEQAQLSFERKKQAATKRTAKKAIVISESSRAAIETKADQRSQVLSQTDKRLKKHSRKLQRRALQFQGKVGLPSGKKPLEPEVRPEAEGDTEGEESGSSPTDGEEEEEQEEEEGVASLSSDDVSYELKPLRKRQKYQKKVPVQEIDDDFFPSSEEEDEAMEGRGGGRKVARRQDDGDEDYYKQRLRRWNRLRLQDKEKRLKLEDDSEESDAEFDEGFKVPGFLFKKLFKYQQTGVRWLWELHCQQAGGILGDEMGLGKTIQIIAFLAGLSYSKIRTRGSNYRFEGLGPTIIVCPTTVMHQWVKEFHTWWPPFRVAVLHETGSYTHKKERLIRDIVYCHGVLITSYSYIRLMQDDISRHDWHYVILDEGHKIRNPNAAVTLACKQFRTPHRIILSGSPMQNNLRELWSLFDFIFPGKLGTLPVFMEQFSVPITMGGYSNASPVQVKTAYKCACVLRDTINPYLLRRMKSDVKMSLSLPDKNEQVLFCRLTDEQHKVYQNFIDSKAVYRILNGENQIFSGLVALRKICNHPDLFSGGPKNASGPPEDELEEEQFGHWRRSGKMIVVESLLKIWHRQGQRVLLFSQSRQMLHILEVFLRAHKYSYLKMDGTTTIASRQPLITKYNEDTSIFVFLLTTRVGGLGVNLTGANRVIIYDPDWNPSTDTQARERAWRIGQKKQVTVYRLLTAGTIEEKIYHRQIFKQFLTNRVLKDPKQRRFFKSNDLYELFTLTSPDASQGTETSAIFAGTGSSIQTPKCQLKKRTSTVLGTDPKCKKPPVSDTPANAATLIGEKPKAAGATGRSVTSGESGPFKGDHDTNGNRASSVAFGEETDAGSTLEHLSVMSGDGKHSDSPTVDHTSRPPVEASTSEKQGSSYAGARCQAQTEPVPMSEQMEGQFSKYKSKRKHDASEEETTEKRPQPKQKAKNSKHCRDAKFEGTRVPHLVKKRRYRQQTSEQEGGAKDRSSDDYVLEKLFKKSVGVHSVVRHDAIIDGSSPDYVLVEAEANRVAQDALKALRLSRQQCLGAASGVPTWTGHRGISGAPTGVKNRFGQKRDSSLPVQHPSSLTEKTQNNMKKEGKAHTPEHFSGKEDGASVSGAPSSSSLLARMRARNHMILPERLESDSEHLAEAAAVPPCGTEHDDLLVDMRNFIAFQAQVDGQASTQEILQEFESKLSVAQSCVFRELLRNLCNFHRTPGGEGIWKLKPEYC | 3.6.4.- | null | base-excision repair [GO:0006284]; chromatin remodeling [GO:0006338]; DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; DNA protection [GO:0042262]; DNA repair [GO:0006281]; double-strand break repair via classical nonhomologous end joining [GO:0097680]; double-strand break repair via synthesis-dependent strand annealing [GO:0045003]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; JNK cascade [GO:0007254]; multicellular organism growth [GO:0035264]; negative regulation of double-strand break repair via nonhomologous end joining [GO:2001033]; neurogenesis [GO:0022008]; neuron differentiation [GO:0030182]; neuron projection development [GO:0031175]; photoreceptor cell maintenance [GO:0045494]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of transcription by RNA polymerase I [GO:0045943]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription by RNA polymerase III [GO:0045945]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; pyrimidine dimer repair [GO:0006290]; reciprocal meiotic recombination [GO:0007131]; regulation of transcription elongation by RNA polymerase II [GO:0034243]; response to gamma radiation [GO:0010332]; response to oxidative stress [GO:0006979]; response to superoxide [GO:0000303]; response to toxic substance [GO:0009636]; response to UV [GO:0009411]; response to UV-B [GO:0010224]; response to X-ray [GO:0010165]; single strand break repair [GO:0000012]; transcription elongation by RNA polymerase I [GO:0006362]; transcription-coupled nucleotide-excision repair [GO:0006283] | B-WICH complex [GO:0110016]; nucleolus [GO:0005730]; nucleus [GO:0005634]; site of DNA damage [GO:0090734]; transcription elongation factor complex [GO:0008023] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA translocase activity [GO:0015616]; helicase activity [GO:0004386]; protein tyrosine kinase activator activity [GO:0030296] | PF00271;PF00176; | 3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | PTM: Phosphorylated in a cell cycle-dependent manner at Ser-158 by cyclin A-CDK2 in response to DNA damage (By similarity). Phosphorylation at this site promotes the intramolecular interaction of the N-terminal domain with the helicase ATP-binding domain, thereby probably releasing the inhibitory effect of the N-terminal domain on its ATPase activity (By similarity). Phosphorylation is essential for its chromatin remodeling activity (By similarity). {ECO:0000250|UniProtKB:Q03468}.; PTM: Ubiquitinated at the C-terminus (By similarity). Ubiquitination by the CSA complex leads to ERCC6 proteasomal degradation in a UV-dependent manner (By similarity). Stabilized following interaction with KIAA1530/UVSSA, which promotes recruitment of deubiquitinating enzyme USP7, leading to deubiquitination of ERCC6 thereby preventing UV-induced degradation of ERCC6 by the proteasome (By similarity). {ECO:0000250|UniProtKB:Q03468}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03468}. | 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; Evidence={ECO:0000250|UniProtKB:Q03468}; | null | null | null | null | FUNCTION: Essential factor involved in transcription-coupled nucleotide excision repair which allows RNA polymerase II-blocking lesions to be rapidly removed from the transcribed strand of active genes (By similarity). Upon DNA-binding, it locally modifies DNA conformation by wrapping the DNA around itself, thereby modifying the interface between stalled RNA polymerase II and DNA (By similarity). It is required for transcription-coupled repair complex formation. It recruits the CSA complex (DCX(ERCC8) complex), nucleotide excision repair proteins and EP300 to the sites of RNA polymerase II-blocking lesions (By similarity). Plays an important role in regulating the choice of the DNA double-strand breaks (DSBs) repair pathway and G2/M checkpoint activation; DNA-dependent ATPase activity is essential for this function (By similarity). Regulates the DNA repair pathway choice by inhibiting non-homologous end joining (NHEJ), thereby promoting the homologous recombination (HR)-mediated repair of DSBs during the S/G2 phases of the cell cycle (By similarity). Mediates the activation of the ATM- and CHEK2-dependent DNA damage responses thus preventing the premature exit from the G2/M checkpoint (By similarity). Acts as a chromatin remodeler at DSBs; DNA-dependent ATPase-dependent activity is essential for this function (By similarity). Remodels chromatin by evicting histones from chromatin flanking DSBs, limiting RIF1 accumulation at DSBs thereby promoting BRCA1-mediated HR (By similarity). Required for stable recruitment of ELOA and CUL5 to DNA damage sites (By similarity). Involved in UV-induced translocation of ERCC8 to the nuclear matrix (By similarity). Essential for neuronal differentiation and neuritogenesis; regulates transcription and chromatin remodeling activities required during neurogenesis (By similarity). {ECO:0000250|UniProtKB:Q03468}. | Mus musculus (Mouse) |
F8VQ03 | ADAM3_MOUSE | MLPLFLVLSYLGQVIAAGKDVETPLLQITVPEKIDTNIQDAKEAETQVTYVVRIEGKAYTLQLEKQSFLHPLFGTYLRDKLGTLQPYFSLVKTHCFYQGHAAEIPVSTVTLSTCSGLRGLLQLENITYGIEPLESSATFEHILYEIKNNKIDYSPLKENFANSEQESQSYRILVKPEKGSNSTLTKRILRIKIIMDKAMFDHMGSEVGVATQKVVHIFGLINTMFSQLKMTVMLNSLEIWSEQDKIETNGDADEVLQRFLLWKSKEISQKAQDITYLLLYKDHPDYVGATYHGMACNPNFTAGIALHPKTLAVEGFAIVLSQLLGINLGLAYDDVYNCFCPGSTCIMNPSAIRSQGIKVFSSCSVDEFKQLASQPELDCLRNTSETEFVVQPQGGSYCGNHLLEVPEQCDCGPPETCTHKKCCNPKDCTLIDAAQCGTGPCCDKRTCTIAERGRLCRKSKDQCDFPEFCNGETEGCAPDTKAADLEPCNNETAYCFGGVCRDPDRQCTDLFGKYAKGPNYVCAQEVNLQNDKFGNCHGRCNYSAIFCGKAVCYWNFAEVIQTEKYDVQYTYLGGQVCVSAHLRSQTGTRDDTYVHDGTVCGSGQVCFRGDCLRVHVLRGTRECEADDKCQGHGICNNLNNCQCESGFAPPECDMTPSSPGGSMDDGFWLPFDKSTPLIFKRHGLKYKKVLLISFYILLPFLVVLAFMAVKRMIGKRLAKQNISKALEHKEEAFNRGSMNPGVVSGGNTDQNLMTVPGSFNSYAYHGNTDQNFMTVPGSFNSYSYHGNTDQNFMTVPGSFNSYSYQDVPYYRSIPEDGNDSQQ | null | null | binding of sperm to zona pellucida [GO:0007339]; cell adhesion [GO:0007155]; fertilization [GO:0009566]; flagellated sperm motility [GO:0030317]; male gonad development [GO:0008584]; positive regulation of gene expression [GO:0010628]; proteolysis [GO:0006508]; regulation of mRNA processing [GO:0050684]; single fertilization [GO:0007338] | cell surface [GO:0009986]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; sperm head [GO:0061827] | metalloendopeptidase activity [GO:0004222] | PF08516;PF00200;PF07974;PF01562;PF01421; | 3.40.390.10;4.10.70.10; | null | PTM: Initially synthesized as a 110-kDa precursor in round spermatids, and the precursor is then processed into a 42-kDa mature protein during the sperm transport into and/or once in the epididymis. {ECO:0000269|PubMed:15514464, ECO:0000269|PubMed:24501175}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15514464}; Single-pass membrane protein {ECO:0000255}. Note=Localized in round and elongating spermatids. Localized on the anterior part of the sperm head, and is removed during the acrosome reaction. {ECO:0000269|PubMed:15514464}. | null | null | null | null | null | FUNCTION: Involved in fertilization by controlling sperm migration into the oviduct (PubMed:19339711). Promotes the binding of sperm to the oocyte zona pellucida (PubMed:32529245). {ECO:0000269|PubMed:19339711, ECO:0000269|PubMed:32529245}. | Mus musculus (Mouse) |
F8VQB6 | MYO10_MOUSE | MDSFFPEGARVWLRENGQHFPSTVNSCAEGVVVFQTDYGQVFTYKQSTITNQKVTAMHPLHEEGVDDMASLAELHGGSIMYNLFQRYKRNQIYTYIGSIIASVNPYQPIAGLYERATMEEYSRCHLGELPPHIFAIANECYRCLWKRHDNQCVLISGESGAGKTESTKLILKFLSVISQQTLDLGLQEKTSSVEQAILQSSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQQGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLDQGEREEFYLSLPENYHYLNQSGCTEDKTISDQESFRQVITAMEVMQFSKEEVREVLRLLAGILHLGNIEFITAGGAQIPFKTALGRSADLLGLDPTQLTDALTQRSMILRGEEILTPLSVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKDDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNTQKMPDQFDQVVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPDDIRGKCTVLLQVYDASNSEWQLGKTKVFLRESLEQKLEKRREEEIDRAAMVIRAHILGYLARKQYRKVLCGVVTIQKNYRAFLARKKFLHLKKAAIVFQKQLRGQLARRVYRQLLAEKRELEEKKRREEEKKREEEERERERAQREADLLRAHQEAETRRQQELEALQKSQREADLTRELEKQRENKQVEEILRLEKEIEDLQRMKERQELSLTEASLQKLQQLRDEELRRLEDEACRAAQEFLESLNFDEIDECVRNIERSLSVGSEISGEELSELAESASGEKPNFNFSQPYPAEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIRTSDDSSEEDPYMNYTVVPTSPSADSTVLLAASMQDSASLHNSSSGESTYCMPQNNGDLPSPDGDYDYDQDDYEDGAITSGSSVTFSNSYGSQWSPDYRYSVGTYNSSGAYRFSSEGAQSSFEDSEEDFDSRFDTDDELSYRRDSVYSCVTLPYFHSFLYMKGGLMNSWKRRWCVLKDETFLWFRSKQEALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQSKLMYFENDSEEKLKGTVEVRTAKEIIDNTSKENGIDIILADRTFHLIAESPEDASQWFSVLSQVHSSTDQEIREMHDEQANPQNAVGTLDVGLIDSVCASDSPDRPNSFVIITANRVLHCNADTPEEMHHWITLLQRSKGDTRVEGQEFIVRGWLHKEVKNSPKMSSLKLKKRWFVLTHNSLDYYKSSEKNALKLGTLVLNSLCSVVPPDEKIFKETGYWNVTVYGRKHCYRLYTKLLNEATRWSSAIQNVTDTKAPIDTPTQQLIQDIKENCLNSDVVEQIYKRNPILRYTHHPLHSPLLPLPYGDINLNLLKDKGYTTLQDEAIKIFNSLQQLESMSDPIPIIQGILQTGHDLRPLRDELYCQLIKQTNKVPHPGSVGNLYSWQILTCLSCTFLPSRGILKYLKFHLKRIREQFPGTEMEKYALFIYESLKKTKCREFVPSRDEIEALIHRQEMTSTVYCHGGGSCKITINSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGQVDKAIESRTIVADVLAKFEKLAATSEAGDAPWKFYFKLYCFLDTDSMPKDSVEFAFMFEQAHEAVIHGHHPAPEESLQVLAALRLQYLQGDYTPHTSIPPLEEVYSVQRLRARISQSTKTFTPYERLEKRRTSFLEGTLRRSFRTGSVVRQKAEEEQMLDMWIKEEVCSARTSIIDKWKKLQGMNQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQELWLGVSADAVSVYKRGEGKPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKRYSTTRSVSSQGSSR | null | null | cell motility [GO:0048870]; cytoskeleton-dependent intracellular transport [GO:0030705]; positive regulation of cell-cell adhesion [GO:0022409]; regulation of cell shape [GO:0008360]; regulation of filopodium assembly [GO:0051489] | cell cortex [GO:0005938]; cytosol [GO:0005829]; filopodium [GO:0030175]; filopodium membrane [GO:0031527]; filopodium tip [GO:0032433]; lamellipodium [GO:0030027]; myosin complex [GO:0016459]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nucleolus [GO:0005730]; ruffle [GO:0001726] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; plus-end directed microfilament motor activity [GO:0060002]; spectrin binding [GO:0030507] | PF00373;PF00612;PF16735;PF00063;PF00784;PF00169;PF18597; | 1.10.10.820;1.20.5.170;1.20.5.190;1.20.58.530;1.20.80.10;6.20.240.20;3.40.850.10;1.20.120.720;1.25.40.530;2.30.29.30; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | PTM: The initiator methionine for isoform Headless is removed. | SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell projection, lamellipodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm, cytoskeleton. Cell projection, filopodium tip. Cytoplasm, cell cortex. Cell projection, filopodium membrane; Peripheral membrane protein. Note=May be in an inactive, monomeric conformation in the cytosol. Detected in cytoplasmic punctae and in cell projections. Colocalizes with actin fibers. Interacts with microtubules. Undergoes forward and rearward movements within filopodia. Interaction with membranes containing phosphatidylinositol 3,4,5-trisphosphate mediates localization at filopodium membranes (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as a plus end-directed motor. Moves with higher velocity and takes larger steps on actin bundles than on single actin filaments (By similarity). The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments (By similarity). Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation. Plays a role in formation of the podosome belt in osteoclasts. {ECO:0000250|UniProtKB:Q9HD67, ECO:0000269|PubMed:17237772, ECO:0000269|PubMed:20081229}.; FUNCTION: [Isoform Headless]: Functions as a dominant-negative regulator of isoform 1, suppressing its filopodia-inducing and axon outgrowth-promoting activities. In hippocampal neurons, it increases VASP retention in spine heads to induce spine formation and spine head expansion. {ECO:0000269|PubMed:23943878}. | Mus musculus (Mouse) |
F8VQN3 | GPR31_MOUSE | MERTNCSAASTVVETAVGTMLTLECVLGLMGNAVALWTFFYRLKVWKPYAVYLFNLVVADLLLATSLPFFAAFYLKGKTWKLGHMPCQVLLFLLAFSRGVGVAFLTTVALDRYLRVVHPRLRVNLLSLRAAWGISSLIWLLMVVLTPQNLLTCRTTQNSTECPSFYPTGGAKAIATCQEVLFFLQVLLPFGLISFCNSGLIRTLQKRLRESDKQPRIRRARVLVAIVLLLFGLCFLPSVLTRVLVHIFQEFKSCSVQQAIVRASDIAGSLTCLHSTLSPAIYCFSNPAFTHSYRKVLKSLRGRRKAAESPSDNLRDSYS | null | null | G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of inflammatory response [GO:0050728]; positive regulation of immune response [GO:0050778]; response to acidic pH [GO:0010447]; response to ischemia [GO:0002931]; response to molecule of bacterial origin [GO:0002237] | plasma membrane [GO:0005886] | arachidonic acid binding [GO:0050544]; bioactive lipid receptor activity [GO:0045125]; G protein-coupled receptor activity [GO:0004930] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O00270}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: High-affinity receptor for 12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid (12-S-HETE), with much lower affinities for other HETE isomers (By similarity) (PubMed:29227475). 12-S-HETE is a eicosanoid, a 12-lipoxygenase (ALOX12) metabolite of arachidonic acid, involved in many physiologic and pathologic processes, such as cell growth, adhesion, inflammation and cancer promotion. 12-S-HETE-binding leads to activation of ERK1/2 (MAPK3/MAPK1), MEK, and NF-kappa-B pathways and leads to cell growth. Plays a crucial role for proliferation, survival and macropinocytosis of KRAS-dependent cancer cells by mediating the translocation of KRAS from the endoplasmic reticulum to the plasma membrane (PM) and its association with the PM (By similarity). Contributes to enhanced immune responses by inducing dendrite protrusion of small intestinal CX3CR1(+) phagocytes for the uptake of luminal antigens (PubMed:30675063). Acts also as a key receptor for 12-(S)-HETE-mediated liver ischemia reperfusion injury (PubMed:29227475). {ECO:0000250|UniProtKB:O00270, ECO:0000269|PubMed:29227475, ECO:0000269|PubMed:30675063}.; FUNCTION: Proton-sensing G protein-coupled receptor. {ECO:0000250|UniProtKB:O00270}. | Mus musculus (Mouse) |
F8W2M1 | HACE1_DANRE | MERAMEHLNVQLNRLTRSLRRARTVELPEDSETAVYTLMPMVMADQHRSVSELLLNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKRGANPNYQDISGCTPLHLAARNGQKKCMGRLLEYNADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVTNVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAKYLPDRNGVTPLDLCVQGGYGETCEILIQHHGRLFQTLIQMTQNDDIKENMLRQVLEHVSQQNDSNYQRILTSLAEVATTNGHKLLSLSSNFEVQTKSLLRIIRIFCHVFCLGPSSPNNGNDMGYNGNKTPRSQVFKPLELLWHSLDEWLVLISTELEKEITDTTRSSSGNDIASLFLKKQEVDHSVSSENPQLLLDASSVMKTPEVYADGQDVISMIANRLSAVIQAFYMCCSCQMPHGMTSPRFIEFVCKHDEVLKCFVTRNPKIIFNHFHFLLECPELMSRFMHIIKGQPFKDRCEWFYEHLLAGQPDSDMVHRPVNENDILLVHRDSLFRSSCEVVSKSSNEKLKQGIAVRFHGEEGMGQGVVREWFDILSNEIINPDYALFTQSADGTTFQPNSNSSVNPDHLNYFRFAGQILGLALYHRQLVNIYFTRSFYKHILGIPVSYQDVSSIDPEYAKNLQWILDNDISDLGLELTFSVETDVFGTMEEVPLKPGGTTIQVTQDNKEEYVQLVTELRMTRAIQPQINAFLQGFHTFIPPSLIQLFDEYELELLLSGMPEIDVMDWKRNTEYTSGYDLQEPVIQWFWEVVENLTQEERVLLLQFVTGSSRVPHGGFAFLMGGSGLQKFTVAAVPYTSNLLPTSSTCINMLKLPEYPSKDVLRDRLLVALHCGSYGYTMA | 2.3.2.26 | null | atrioventricular valve formation [GO:0003190]; cardiac ventricle morphogenesis [GO:0003208]; cell cycle [GO:0007049]; Golgi organization [GO:0007030]; heart looping [GO:0001947]; membrane fusion [GO:0061025]; negative regulation of reactive oxygen species biosynthetic process [GO:1903427]; 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;PF13637;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}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F8W2M8 | TPP1_DANRE | MRVAVFVLSFIWLVNGELLEADQDAVVPGDWTFLGRVGPLEEVELTFALKQQNVSKMEELLKLVSDPDSHQYGKYLSLDEVAALSRPSPLTEKVVENWLRSHGVMDCHTIITRDFLQCVMTVEVAEALLPGSKFHRFSKNTKTLLRSTSQYSVHEDVHQHLDFVGGVHRFPQKRKIVSKGWEGARQAILGYHLGVTPAVIRNRYNLTAKDVGTAANNSQAVAQFLEQYYHPADLAEFMSLFGGGFTHMSTVERVVGTQGGGKAGIEASLDVEYIMSSGANISTWVFTNPGRHESQEPFLQWMLLLSNMSAVPWVHTISYGDDEDSLSEAYMNRINIEFMKAGLRGISMLFASGDSGAGCRHLTKERNTFRPSFPASSPYVTTVGGTSFQNPFKLSYEVTDYISGGGFSNVFPMPDYQVDAVRAYLKSVQSLPPQTYFNTTGRAYPDLAALSDNYWVVSNRVPIPWVSGTSASTPVVGGILSLINDQRFLKGLPALGFINPRLYKMQGKGLYDVTVGCHLSCLDDKVEGKGFCASPSWDPVTGWGTPNYPVFLASLMD | 3.4.14.9 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:O14773}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:O14773}; | central nervous system development [GO:0007417]; locomotory behavior [GO:0007626]; neurogenesis [GO:0022008]; proteolysis [GO:0006508] | lysosome [GO:0005764] | endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]; tripeptidyl-peptidase activity [GO:0008240] | PF00082;PF09286; | 3.40.50.200; | null | PTM: Activated by autocatalytic proteolytical processing. {ECO:0000250|UniProtKB:O14773}. | SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:O14773}. | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.; EC=3.4.14.9; Evidence={ECO:0000269|PubMed:23587805}; | null | null | null | null | FUNCTION: Lysosomal serine protease with tripeptidyl-peptidase I activity (PubMed:23587805). May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases (By similarity). Requires substrates with an unsubstituted N-terminus (By similarity). {ECO:0000250|UniProtKB:O14773, ECO:0000269|PubMed:23587805}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F8W3R9 | ALK_DANRE | MIARILYFFLWSAAFLPELQCASQRTADALTTFPTSAFINGTDRKDSNQTSTSRIKRKTLSVDFAVPSLLRYYLALFIKRPLNGDCLSFNGCYTVRANLLMRCVPLQKTIAGLLDAKLAAMNVNRSSTGQLPYRQKRPVPKVLNLGLTSASRKSNQVVVEVGEEMVKTGCGGLHVYEDAPVVFLEMDLTRILEWWLGAEGGRLRVRLMPERKVQVPGKEDKYSAAIRASDARLFIQIASSERPSSTISRNPTVAPKYWNFSWIAEDELTFPEDPVSTSDCTSKAKSCDRRPDGYYPEFAWSLTSAEDSWAIDQTMVKTKASSQGWEEGRFLTVNSSALTGPWVLSPWFRAAHRPCGLDITVFLHPRQSGRYTVWLIERDKPPLALLTTEHPHVIGWAVVHLSLAARSKPFRISSSYSQPGEIETATYDPRYSTNCTTRSSQNVTLRGRYHCRGGREINVSQLCDFSIDCPQGDDEGEHCRQFLNGSYCSFGREDCGWQPVQGRGPQWRAHPSIPQSLRSSCPSPGALLAIDSQPKGQRGSAQVRSPLFFYPLRNAPCMVKFWVCGSSNGALSLWITENSTGPEGQRSLWNSTSEANMGKGWKLITLPLFGLVDLFYLQFSADISSSSGIAFAVDNFTLSMECFLETNGEFPPVAPISPTQALFTQSNENIKTTTTLYGGPGASTESVKWIFHTCGATGQDGPTPTQCSNSYRNTNVNVTVGTKGPFKGIQMWQVPETRKYRITAYGAAGGRSVLAVHKSHGVYMTGDFLLQKDELLYILVGQEGEDACPNMVPTMDRICREQQGPSINKTQLKGGGGGGGGGTYVFKVVNGVHIPLLIAAGGGGRGYSSQSETPEEVMDRDPSIPGRNGKSGTAGGGGGWNDSAPVPQGGRPLILGGQGGEPCQAMGWKTRGGFGGGGGACTAGGGGGGYRGGSAWHDNDPRKDGDDGTSYISPDGEMYLEPLKGMEGNGEVIINPVQNCSHCESGDCHETSEGMVCYCDEELTLAPDGVSCINSTELPLLPAQPSLSHLALGLSVGTSALIAALLLAVSGVMIMYRRKHTELQSIQLELQSPDCKLSKLRASTIMTDYNPNYCFGGKTASVNDLKEVPRRNISLTRGLGHGAFGEVYEGLAVGIPGEPSPMQVAVKTLPEVCSEQDELDFLMEALIISKFSHQNIVRCIGVSLQALPHFILLELMAGGDLKSFLRETRPRLEHPSSLTMVDLLNIARDIARGCQYLEENQFIHRDIAARNCLLTCKGPGRVAKIGDFGMARDIYRASYYRKGGRAMLPVKWMPPEAFMEGIFTSKTDTWSFGVLLWEIFSLGYMPYPSRSNQEVLEFVTNGGRMDPPKNCPGPVYRIMTQSWQHQPEDRPNFSTILERIDYCLQDPDVVNVPLPVEYGPIPEEEERVPMRPEDPSAPSLLVSPQGTEDVPSATHSAQSKKDGEAIHMANLSTDSKLPPVPPSQPHPHHHLQTPVVTAPVPASKPSSTTSNAQDGGHVNLGFMQAHSSEKESRNRKPTNLWNPTYGSWFLQQQQKRQQVQAQRQTSGPRIPGEGQEQVGRTVTVAEALGLQQQHKQQQYQQQLQRQQQQQQQQQQQQGLCRPLLPPPPPPAPTPLLLDSATLAPVPLYRLRRFPCGNIGYGYQEQGLPMEPMQGPQLPPPHPGQQRPISLTRASGPEDSRPLLVTMGTVQDSRLPKMEGHNATVL | 2.7.10.1 | null | phosphorylation [GO:0016310]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of neurogenesis [GO:0050769]; regulation of cell population proliferation [GO:0042127]; regulation of neuron differentiation [GO:0045664]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF12810;PF00629;PF07714; | 2.60.120.200;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UM73}; Single-pass type I membrane protein {ECO:0000255}. | 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=2.7.10.1; Evidence={ECO:0000250|UniProtKB:Q9UM73}; | null | null | null | null | FUNCTION: Receptor tyrosine kinase required for neurogenesis in the developing central nervous system (PubMed:23667670). Following activation by alkal ligands (alkal1, alkal2a or alkal2b) at the cell surface, transduces an extracellular signal into an intracellular response (PubMed:29078341). Ligand-binding to the extracellular domain induces tyrosine kinase activation, resulting in the activation of the mitogen-activated protein kinase (MAPK) pathway (PubMed:23667670). Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif (By similarity). {ECO:0000250|UniProtKB:Q9UM73, ECO:0000269|PubMed:23667670, ECO:0000269|PubMed:29078341}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F8W3X3 | PCD19_DANRE | MHSKDMDFVQMFVCFLLCWTGVDAVFNLKYTVEEELRAGTKIANVTADAKVAGFALGNRQPYLRVISNSEPRWVNLSPAGLLITKQKIDRDAVCRQTPKCFISLEVMSNSMEICVIKIEIIDVNDNAPRFPTNHIDIEISENAAPGTRFPLEGASDPDSGSNGIQTYTITPNDIFGLEIKTRGDGSKIAELVVEKTLDRETQSRYTFELTAEDGGDPPKSGTVQLNIKVIDSNDNNPVFDEPVYTVNVLENSPINTLVIDLNATDPDEGTNGEVVYSFINFVSNLTKQMFKIDPKTGVITVNGVLDHEELHIHEIDVQAKDLGPNSIPAHCKVIVNVIDINDNAPEIKLLSENSEMVEVSENAPLGYVIALVRVSDNDSGANGKVQCRLQGNVPFRLNEFESFSTLLVDGRLDREQRDMYNLTILAEDSGYPPLRSSKSFAVKVTDENDNPPYFTKPHYQAMVLENNVPGAFLLAVSARDPDLGMNGTVSYEIIKSEVRGMSVESYVTVNSNGEIYGVRAFNHEDTRTFEFKVSAKDGGDPPLTSNATVRIVVLDVNDNTPVMTTPPLVNGTAEVSIPKNAGVGYLVTQIKADDYDEGENGRLTYSISEGDMAYFEIDQINGEVRTTKTFGENAKPSYQITVVAHDHGQTSLSASAYIVIYLSPDLNAQEQIGPVNLSLIFIIALGSIAVILFVTMIFVAVKCKRDNKEIRTYNCRVAEYSYGNQKKSSKKKKLSKNDIRLVPRDVEETDKMNVVSCSSLTSSLNYFDYHQQTLPLGCRRSESTFLNVENQNSRNAAPNHGYHHTFTGQGPQQPDLIINGMPLPETENYSIDSSYVNSRAHLIKSTSTFKDMEGNSLKDSGHEESDQTDSEHDVQRGHYADTAVNDVLNMTVPSNNSQIPDQDQSEGFHCQDECRILGHSDRCWMPRVPIPARAKSPEHGRNVIALSIEATTVDVPHYEDCGTTKRTFATFGKDGPDEDRAEQRGRRQTAEPAVCSPKTNGAVREAGNGREAVSPITSPVHLKSPQSKASSTYNTLKCRDAERIANHSLLRQPEGKDSEPAMREINTLLQDGRDKESPGSKRLKDIVL | null | null | brain morphogenesis [GO:0048854]; cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609]; excitatory postsynaptic potential [GO:0060079]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; neural tube formation [GO:0001841]; regulation of neuronal action potential [GO:0098908]; visual perception [GO:0007601] | membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynapse [GO:0098794] | cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802] | PF00028;PF08266; | 2.60.40.60; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21115806}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Calcium-dependent cell-adhesion protein (PubMed:21115806). Essential for the early stages of neurulation in the anterior neural plate (PubMed:19615992). Shows little cell adhesion activity on its own but exhibits robust homophilic cell adhesion when in a complex with cadherin cdh2 and appears to mediate the adhesion while cdh2 acts as a cell adhesion cofactor in the complex (PubMed:21115806, PubMed:22184198, PubMed:33004519). Functions with cdh2 to coordinate cell adhesion and cell movements during neurulation (PubMed:21115806). Contributes to neural progenitor cell patterning with cdh2 by promoting homophilic cell interactions (PubMed:33004519). Regulates the columnar organization of neurons in the optic tectum (PubMed:26598617). {ECO:0000269|PubMed:19615992, ECO:0000269|PubMed:21115806, ECO:0000269|PubMed:22184198, ECO:0000269|PubMed:26598617, ECO:0000269|PubMed:33004519}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F8W463 | P2X4A_DANRE | MSESVGCCDSVSQCFFDYYTSKILIIRSKKVGTLNRFTQALVIAYVIGYVCVYNKGYQDTDTVLSSVTTKVKGIALTNTSELGERIWDVADYIIPPQEDGSFFVLTNMIITTNQTQSKCAENPTPASTCTSHRDCKRGFNDARGDGVRTGRCVSYSASVKTCEVLSWCPLEKIVDPPNPPLLADAENFTVLIKNNIRYPKFNFNKRNILPNINSSYLTHCVFSRKTDPDCPIFRLGDIVGEAEEDFQIMAVHGGVMGVQIRWDCDLDMPQSWCVPRYTFRRLDNKDPDNNVAPGYNFRFAKYYKNSDGTETRTLIKGYGIRFDVMVFGQAGKFNIIPTLLNMGAGLALLGLVNVICDWIVLTFMKRKQHYKEQKYTYVDDFGLLHNEDK | null | null | calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; monoatomic cation transport [GO:0006812]; response to ATP [GO:0033198] | membrane [GO:0016020]; monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; transmembrane transporter complex [GO:1902495] | ATP binding [GO:0005524]; ATP-gated ion channel activity [GO:0035381]; CTP binding [GO:0002135]; extracellularly ATP-gated monoatomic cation channel activity [GO:0004931]; ligand-gated monoatomic ion channel activity [GO:0015276]; purine nucleotide binding [GO:0017076]; purinergic nucleotide receptor activity [GO:0001614] | PF00864; | 1.10.287.940;2.60.490.10; | P2X receptor family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99571}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q99571}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:Q99571}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q99571}; CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q99571}; | null | null | null | null | FUNCTION: ATP-gated nonselective transmembrane cation channel permeable to potassium, sodium and calcium (By similarity). CTP, but not GTP or UTP, functions as a weak affinity agonist for P2RX4 (PubMed:28332633). Activated by extracellularly released ATP, it plays multiple role in immunity and central nervous system physiology (By similarity). Could also function as an ATP-gated cation channel of lysosomal membranes (By similarity). {ECO:0000250|UniProtKB:P51577, ECO:0000250|UniProtKB:Q99571, ECO:0000250|UniProtKB:Q9JJX6, ECO:0000269|PubMed:28332633}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F8W4H9 | MRP2A_DANRE | MPRFQLSNSTSVPNHNYEWSYEYYDDEEPVSFEGLKAHRYSIVIGFWVGLAVFVIFMFFVLTLLTKTGAPHPEAAEPYEKRMRLTSCADGLGRQRETDGRTGLSRPLLEESRSLFHCYINEEEREGGRAATDAGALTHGRSGIGNSRGQVEEVGLVVQNMVLESRAEREAALLAHFNIPNFVNSELNSALGDEDLLLGDPPIIMEEARPRCTHHIID | null | null | developmental growth [GO:0048589]; energy homeostasis [GO:0097009]; energy reserve metabolic process [GO:0006112]; negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106072]; protein localization to cell surface [GO:0034394]; protein localization to plasma membrane [GO:0072659]; regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106070]; regulation of growth [GO:0040008] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886] | corticotropin hormone receptor binding [GO:0031780]; signaling receptor regulator activity [GO:0030545]; type 1 melanocortin receptor binding [GO:0070996]; type 3 melanocortin receptor binding [GO:0031781]; type 4 melanocortin receptor binding [GO:0031782]; type 5 melanocortin receptor binding [GO:0031783] | PF15183; | null | MRAP family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Inhibitor of melanocortin receptor 4 (mc4r), a receptor involved in energy homeostasis. Plays a role during larval development in the control of energy homeostasis and body weight regulation by decreasing ligand-sensitivity of mc4r and mc4r-mediated generation of cAMP, leading to stimulate growth during larval development. Acts by stabilizing an inactive conformation of mc4r during embryonic development, when all the energy consumed is obtained from the yolk sac, possibly to speed the rapid maturation to the mobile free-feeding juvenile stage reached at 5 dpf. {ECO:0000269|PubMed:23869017}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
F8WQK8 | DPP11_POREA | MNKRFFPTLLLAFVCSTLAYADGGMWLMQQINGQVARMKSLGMQLEAADIYNPNGSSLKDAVVMFDGGCTGVLVSNQGLLLTNHHCGYDQIQKHSSVQHNYLKDGFWSYSLAEELVNPGLEVEIVDEITDVTAAVKKELERIKKPSGLEFLSPRYLSSLAPEIVGKKAASRPGYRYEIKAFYGGNRYYMFTKKVFRDVRLVAAPPSSIGKFGSDTDNWAWPRHTGDFSIFRLYADKNGNPAEYSKDNVPYRPKRWVKVNAQGVKEGDFALIMGYPGTTYKFFTADEVTEWSEIDNNIRIEMRGILQDVMLREMLADPKINIMYAAKYASSQNGYKRAQGANWAIRRRSLREIKLAQQQEVLAWAKQKGIATTEEAVRAISKAIEGRQDLRMRQRYLLEGILMGIEMSNAPAADSDIADHWDDPARREAGLQSIRKQFEAFFNKDYSPEVEKDQLAIALLTRYAERIPAEKQPISIREGIAEYGSAKAYVEMIFDKSIYASRERFEEFMKNPDRDRLLRDPMSRFAASVAYEHQKLAKEVAAFDAPLAAAQRSYVASVLDMKGQPNLAPDANLTLRFTYGEIKGYQPRDVVTYGAKSTLEGVMEKEDPNNWEYVVDPKLKALYEAKNYGRYANSDGSMPVNFCATTHTTGGNSGSPVMNARGELIGLNFDRNWEGVGGDIEYLPNYQRSIILDIRYLLFIIDKFAGCQRLIDEIQPQF | 3.4.14.- | null | peptide catabolic process [GO:0043171]; proteolysis [GO:0006508] | cell surface [GO:0009986]; extracellular region [GO:0005576] | dipeptidyl-peptidase activity [GO:0008239]; serine-type aminopeptidase activity [GO:0070009] | PF10459; | 2.40.10.10; | Peptidase S46 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21896480}. Cell surface {ECO:0000269|PubMed:21896480}. Note=Is observed in both cell-associated and soluble extracellular forms. {ECO:0000269|PubMed:21896480}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:21896480}; | null | FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Shows a strict specificity for acidic residues (Asp or Glu) in the P1 position, and has a hydrophobic residue preference at the P2 position. Is likely involved in amino acid metabolism and bacterial growth/survival of asaccharolytic P.endodontalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources. {ECO:0000269|PubMed:21896480}. | Porphyromonas endodontalis (strain ATCC 35406 / DSM 24491 / JCM 8526 / CCUG 16442 / BCRC 14492 / NCTC 13058 / HG 370) (Bacteroides endodontalis) |
F9FRH4 | MNLOX_FUSOF | MVALLIFLGIFTCVETLPLSDSPSSYIPEEVPSSQTADIGLPPPTEFTLPNEDDEILIRKLNIQKTRKEILYGPSLIGKTSFFISGPLGDQISQRDQTLWSRDAAPVVQAVSHDAAAALHDIQIHGGLQNLDDYKILYQGHWSSSVPGGIAKGQFSNFTSDLLFSMERLSTNPYILRRLHPHADELPFAVDSKIVQKLTGSTLPSLHKAGRLFLADHSYQKDYVAQEGRYAAACQALFYLDDRCHQFLPLAIKTNVGSNLTYTPLDEPNDWLLAKVMFNVNDLFHGQMYHLASTHAVAEIVHLAALRTMSSRHPVLALLQRLMYQAYAIRPIGNNILFNPGGLIDQNSVFSNVAVRKFATDFYPTVAGPVRSNYFEANLRSRGLLNATHGPDLPHFPFYEDGARIIKVIRTFIQSFVKSIYKSDKVLAKDWELQAWIAEANGAAEVIDFPPTPLKKRKHLVDILTHMAWLTGVSHHVLNQGEPVTTSGVLPLHPGSLYAPVPGEKGVVDSLLPWLPNEQKSVDQISFLALFNRPQIVENNRTLRYMFNSESLLAGTVRAVAAANERFMEEMGHISQEISNRKFDDDGLSQGMPFIWTGMDPGVIPFYLSV | 1.13.11.-; 1.13.11.45 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:26113537}; Note=Three His residues, the carboxyl oxygen of the C-terminal Ile or Val residue, and a fifth residue, usually Asn, ligate the metal, which binds water to form a catalytic base Mn(2+)OH(2) for hydrogen abstraction. {ECO:0000250|UniProtKB:Q8X151}; | arachidonic acid metabolic process [GO:0019369]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; lipid oxidation [GO:0034440]; lipoxygenase pathway [GO:0019372] | extracellular region [GO:0005576] | linoleate 11-lipoxygenase activity [GO:0050584]; linoleate 13S-lipoxygenase activity [GO:0016165]; metal ion binding [GO:0046872] | PF00305; | 3.10.450.60; | Lipoxygenase family, Manganese lipoxygenase subfamily | PTM: N- and O-glycosylated. {ECO:0000269|PubMed:26113537}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8X151}. | CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (11S)-hydroperoxy-(9Z,12Z)-octadecadienoate; Xref=Rhea:RHEA:18993, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57467; EC=1.13.11.45; Evidence={ECO:0000250|UniProtKB:Q8X151}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (11R)-hydroperoxy-(9Z,12Z)-octadecadienoate; Xref=Rhea:RHEA:51640, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:134248; Evidence={ECO:0000269|PubMed:26113537}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; Evidence={ECO:0000269|PubMed:26113537}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (11S)-hydroperoxy-(9Z,12Z,15Z)-octadecatrienoate; Xref=Rhea:RHEA:51440, ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:134110; Evidence={ECO:0000269|PubMed:26113537}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=29 uM for linoleate {ECO:0000269|PubMed:26113537}; | null | null | null | FUNCTION: Lipoxygenase that metabolizes linoleic and alpha-linolenic acids to 9-, 11- and 13-hydroperoxy fatty acids. Oxidizes linoleic acid to mainly 11R-, 13S- and racemic 9-HPODE, and alpha-linolenic acid to 11-HPOTrE. {ECO:0000269|PubMed:26113537}. | Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt) |
F9UMS6 | MLES_LACPL | MTKTASEILNNPFLNKGTAFTKEERQALGLTGTLPSKVQTIDEQATQAYAQFKSKPSRLEQRIFLMNLFNENRTLFFHLMDEHVVEFMPIVYDPVVADSIEQYNELFLDPQNAAFVSVDAPEDIEATLKNAADGRDIRLVVVTDAEGILGMGDWGVNGVDIAIGKLMVYTAAAGIDPSQVLPVSIDAGTNNQKLLDDPLYLGNRHKCVSGEQYYDVIDKFVAAEQQLFPDSLLHFEDFGRDNAQVILDKYKDQIATFNDDIQGTGMVVLAGILGALNISKESIKDQKILSFGAGTAGMGIANQILDELMQAGLTEEEAKQHFYAVDKQGLLFDDTEGLTPAQKAFTRKRSEFSNADELTNLEAVVKAVHPTVMIGTSTQPGTFTESIIKEMAAHTERPIIFPLSNPTKLAEAKAEDLIKWTDGRALVATGIPADDVEYKGVTYQIGQGNNALMYPGLGFGLIASTAKVLNAETLSAACHALGGIVDTSKPGAAVLPPVAKITEFSQKLAEVVAQSVIDQKLNKEPIADAKQAVADMKWVPEYRAISK | 4.1.1.101 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:6833282}; COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000269|PubMed:6833282}; | malate metabolic process [GO:0006108]; malolactic fermentation [GO:0043464]; pyruvate metabolic process [GO:0006090] | cytosol [GO:0005829] | carboxy-lyase activity [GO:0016831]; malate dehydrogenase (decarboxylating) (NAD+) activity [GO:0004471]; malolactic enzyme activity [GO:0043883]; manganese ion binding [GO:0030145]; NAD binding [GO:0051287] | PF00390;PF03949; | 3.40.50.10380;3.40.50.720; | Malic enzymes family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-malate + H(+) = (S)-lactate + CO2; Xref=Rhea:RHEA:46276, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16526, ChEBI:CHEBI:16651; EC=4.1.1.101; Evidence={ECO:0000269|PubMed:6833282}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.012 mM for manganese {ECO:0000269|PubMed:6833282}; KM=0.059 mM for NAD {ECO:0000269|PubMed:6833282}; KM=9.5 mM for (S)-malate {ECO:0000269|PubMed:6833282}; | null | null | null | FUNCTION: Involved in the malolactic fermentation (MLF) of wine, which results in a natural decrease in acidity and favorable changes in wine flavors. Catalyzes the decarboxylation of L-malate to L-lactate. {ECO:0000269|PubMed:6833282}. | Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (Lactobacillus plantarum) |
F9UPU7 | KT3K_LACPL | MHLTKTWLAQLPLTDIQQVQPVSGGDINAAFQIITRHHQYFLKVQPHNDVTFFDHEVAGLRLLGAVTKTPRVIASGTIATDGYLLLDWLATGTGSQSALGAAVAKVHHQHHAQFGLDHDFTAGKLPKINHWQTDWATFYTQQRLDVLVNLAKEHHLWSETREMHYHRLRQQLLQDSHMHTVKPSLLHGDLWSGNYLFDTTGTPVLIDPDVFYGDREMDLAMTTIFGGFDTDFYQAYQAAYPVAPGMQDRLPSYQLYYLLAHLNLFGETYGPAVDRILMQY | 2.7.1.- | null | phosphorylation [GO:0016310] | null | ATP binding [GO:0005524]; kinase activity [GO:0016301]; phosphotransferase activity, alcohol group as acceptor [GO:0016773]; protein-ribulosamine 3-kinase activity [GO:0102193] | PF03881; | 3.90.1200.10; | Fructosamine kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + N(6)-(D-ribulosyl)-L-lysine = ADP + H(+) + N(6)-(3-O-phospho-D-ribulosyl)-L-lysine; Xref=Rhea:RHEA:61400, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:144590, ChEBI:CHEBI:144611, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17681011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61401; Evidence={ECO:0000269|PubMed:17681011}; CATALYTIC ACTIVITY: Reaction=ATP + N-(D-ribulosyl)-cadaverine = ADP + H(+) + N-(3-O-phospho-D-ribulosyl)-cadaverine; Xref=Rhea:RHEA:61404, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:144612, ChEBI:CHEBI:144614, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17681011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61405; Evidence={ECO:0000269|PubMed:17681011}; CATALYTIC ACTIVITY: Reaction=ATP + N(6)-(D-erythrulosyl)-L-lysine = ADP + H(+) + N(6)-(3-O-phospho-D-erythrulosyl)-L-lysine; Xref=Rhea:RHEA:61408, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:144617, ChEBI:CHEBI:144618, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17681011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61409; Evidence={ECO:0000269|PubMed:17681011}; CATALYTIC ACTIVITY: Reaction=ATP + N-(D-erythrulosyl)-cadaverine = ADP + H(+) + N-(3-O-phospho-D-erythrulosyl)-cadaverine; Xref=Rhea:RHEA:61412, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:144619, ChEBI:CHEBI:144620, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17681011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61413; Evidence={ECO:0000269|PubMed:17681011}; CATALYTIC ACTIVITY: Reaction=ATP + N(6)-D-ribulosyl-L-lysyl-[protein] = ADP + H(+) + N(6)-(3-O-phospho-D-ribulosyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:48432, Rhea:RHEA-COMP:12103, Rhea:RHEA-COMP:12104, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:90418, ChEBI:CHEBI:90420, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17681011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48433; Evidence={ECO:0000269|PubMed:17681011}; CATALYTIC ACTIVITY: Reaction=ATP + N(6)-(D-erythrulosyl)-L-lysyl-[protein] = ADP + H(+) + N(6)-(3-O-phospho-D-erythrulosyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:61396, Rhea:RHEA-COMP:15794, Rhea:RHEA-COMP:15799, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:144587, ChEBI:CHEBI:144624, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17681011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61397; Evidence={ECO:0000269|PubMed:17681011}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=300 uM for free ribuloselysine {ECO:0000269|PubMed:17681011}; KM=340 uM for free ribulosecadaverine {ECO:0000269|PubMed:17681011}; KM=60 uM for free erythruloselysine {ECO:0000269|PubMed:17681011}; KM=63 uM for free erythrulosecadaverine {ECO:0000269|PubMed:17681011}; Vmax=510 nmol/min/mg enzyme with free ribuloselysine as substrate {ECO:0000269|PubMed:17681011}; Vmax=2860 nmol/min/mg enzyme with free ribulosecadaverine as substrate {ECO:0000269|PubMed:17681011}; Vmax=610 nmol/min/mg enzyme with free erythruloselysine as substrate {ECO:0000269|PubMed:17681011}; Vmax=800 nmol/min/mg enzyme with free erythrulosecadaverine as substrate {ECO:0000269|PubMed:17681011}; Vmax=16 nmol/min/mg enzyme with ribuloselysyl-protein (lysozyme) as substrate {ECO:0000269|PubMed:17681011}; Vmax=3.8 nmol/min/mg enzyme with erythruloselysyl-protein (lysozyme) as substrate {ECO:0000269|PubMed:17681011}; | null | null | null | FUNCTION: Ketoamine kinase that phosphorylates ketoamines, such as erythruloselysine, erythrulosecadaverine, ribuloselysine and ribulosecadaverine, on the third carbon of the sugar moiety to generate ketoamine 3-phosphate (PubMed:17681011). Has higher activity on free lysine (erythruloselysine and ribuloselysine), than on ribuloselysine and erythruloselysine residues on glycated proteins (PubMed:17681011). {ECO:0000269|PubMed:17681011}. | Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (Lactobacillus plantarum) |
F9USS9 | LARA_LACPL | MVAIDLPYDKRTITAQIDDENYAGKLVSQAATYHNKLSEQETVEKSLDNPIGSDKLEELARGKHNIVIISSDHTRPVPSHIITPILLRRLRSVAPDARIRILVATGFHRPSTHEELVNKYGEDIVNNEEIVMHVSTDDSSMVKIGQLPSGGDCIINKVAAEADLLISEGFIESHFFAGFSGGRKSVLPGIASYKTIMANHSGEFINSPKARTGNLMHNSIHKDMVYAARTAKLAFIINVVLDEDKKIIGSFAGDMEAAHKVGCDFVKELSSVPAIDCDIAISTNGGYPLDQNIYQAVKGMTAAEATNKEGGTIIMVAGARDGHGGEGFYHNLADVDDPKEFLDQAINTPRLKTIPDQWTAQIFARILVHHHVIFVSDLVDPDLITNMHMELAKTLDEAMEKAYAREGQAAKVTVIPDGLGVIVK | 5.1.2.1 | COFACTOR: Name=Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide; Xref=ChEBI:CHEBI:137373; Evidence={ECO:0000269|PubMed:26138974}; Note=Was originally shown to use Ni(2+) as a cofactor (PubMed:24710389), but in fact, the cofactor is a (SCS)Ni pincer complex, a nicotinic acid mononucleotide derivative that is covalently attached to Lys-184 and forms a tridentate pincer complex that coordinates nickel through one metal-carbon and two metal-sulfur bonds (PubMed:26138974, PubMed:27114550). {ECO:0000269|PubMed:24710389, ECO:0000269|PubMed:26138974, ECO:0000269|PubMed:27114550}; | null | null | lactate racemase activity [GO:0050043]; metal ion binding [GO:0046872] | PF09861;PF21113; | 3.40.50.11440;3.90.226.30; | Lactate racemase family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-lactate = (R)-lactate; Xref=Rhea:RHEA:10960, ChEBI:CHEBI:16004, ChEBI:CHEBI:16651; EC=5.1.2.1; Evidence={ECO:0000269|PubMed:24710389, ECO:0000269|PubMed:26138974}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=46 mM for L-lactate {ECO:0000269|PubMed:24710389}; KM=11 mM for D-lactate {ECO:0000269|PubMed:24710389}; Note=kcat is 4745 sec(-1) for conversion of L-lactate to D-lactate. kcat is 1333 sec(-1) for conversion of D-lactate to L-lactate. {ECO:0000269|PubMed:24710389}; | null | null | null | FUNCTION: Catalyzes the interconversion between the D- and L-isomers of lactate (PubMed:24710389, PubMed:26138974). May act as a rescue enzyme to ensure D-lactate production in physiological conditions where its production by the D-lactate dehydrogenase LdhD is not sufficient (PubMed:16166538). D-Lactate is absolutely required for growth of L.plantarum and is an essential component of the cell wall peptidoglycan in this species, where it is incorporated as the last residue of the muramoyl-pentadepsipeptide peptidoglycan precursor; its incorporation confers high level of vancomycin resistance (PubMed:16166538). {ECO:0000269|PubMed:16166538, ECO:0000269|PubMed:24710389, ECO:0000269|PubMed:26138974}. | Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (Lactobacillus plantarum) |
F9UST4 | LARE_LACPL | MATLATKKATLVAALKDLQRVTVAFSGGIDSTLVLKMALDVLGRDNVTAVVANSELFTDEEFDKAMSLAEELGANVQGTTLDYLSDDHIKNNTPDSWYYAKKMFYSRLNDIAANNGSAAVLDGMIKNDENDYRPGLKARSEAGARSLLQEADFFKTDVRALAQELGLTNWNKVASCSVSSRFPYGTTLTHDNIAQVMAAEKYLRSLGFPTVRVRFHNDIARIELPEARIGDFLVFNDRVNRQLQSLGFRYVTLDLGGFRSGRMNDTLTKAQLATFA | 4.4.1.37 | null | null | null | ATP binding [GO:0005524]; lyase activity [GO:0016829]; sulfurtransferase activity [GO:0016783] | PF02540; | 3.40.50.620; | LarE family | null | null | CATALYTIC ACTIVITY: Reaction=[LarE protein]-L-cysteine + ATP + pyridinium-3,5-dicarboxylate mononucleotide = [LarE protein]-dehydroalanine + AMP + diphosphate + H(+) + pyridinium-3-carboxylate-5-thiocarboxylate mononucleotide; Xref=Rhea:RHEA:54788, Rhea:RHEA-COMP:13982, Rhea:RHEA-COMP:13985, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90873, ChEBI:CHEBI:137353, ChEBI:CHEBI:138330, ChEBI:CHEBI:456215; EC=4.4.1.37; Evidence={ECO:0000269|PubMed:27114550}; CATALYTIC ACTIVITY: Reaction=[LarE protein]-L-cysteine + ATP + pyridinium-3-carboxylate-5-thiocarboxylate mononucleotide = [LarE protein]-dehydroalanine + AMP + diphosphate + H(+) + pyridinium-3,5-bisthiocarboxylate mononucleotide; Xref=Rhea:RHEA:54892, Rhea:RHEA-COMP:13982, Rhea:RHEA-COMP:13985, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90873, ChEBI:CHEBI:137372, ChEBI:CHEBI:138330, ChEBI:CHEBI:456215; EC=4.4.1.37; Evidence={ECO:0000269|PubMed:27114550}; | null | null | null | null | FUNCTION: Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Catalyzes the ATP-dependent incorporation of two sulfur atoms in pyridinium-3,5-biscarboxylic acid mononucleotide (P2CMN) to yield pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN). The source of sulfur is the enzyme itself: Cys-176 of LarE is the sulfur donor, thereby being converted into dehydroalanine, and is not regenerated in vivo. Thus, two molecules of LarE undergo sacrificial sulfur transfer to create one P2TMN (PubMed:27114550). Binds nickel (PubMed:24710389). Is required for the activation of the lactate racemase LarA (PubMed:24710389). May also be involved in the activation of other nickel-pincer cofactor-dependent enzymes (PubMed:27114550). {ECO:0000269|PubMed:24710389, ECO:0000269|PubMed:27114550}. | Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (Lactobacillus plantarum) |
F9VMT6 | FBPAP_SULTO | MKTTISVIKADIGSLAGHHIVHPDTMAAANKVLASAKEQGIILDYYITHVGDDLQLIMTHTRGELDTKVHETAWNAFKEAAKVAKDLGLYAAGQDLLSDSFSGNVRGLGPGVAEMEIEERASEPIAIFMADKTEPGAYNLPLYKMFADPFNTPGLVIDPTMHGGFKFEVLDVYQGEAVMLSAPQEIYDLLALIGTPARYVIRRVYRNEDNLLAAVVSIERLNLIAGKYVGKDDPVMIVRLQHGLPALGEALEAFAFPHLVPGWMRGSHYGPLMPVSQRDAKATRFDGPPRLLGLGFNVKNGRLVGPTDLFDDPAFDETRRLANIVADYMRRHGPFMPHRLEPTEMEYTTLPLILEKLKDRFKKESDVYKAKESIYAKEESQGHD | 3.1.3.11; 4.1.2.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15274916}; Note=Can also use Zn(2+) or Mn(2+) in vitro, although with much less efficiency than Mg(2+). {ECO:0000269|PubMed:15274916}; | dephosphorylation [GO:0016311]; gluconeogenesis [GO:0006094]; NADPH regeneration [GO:0006740] | null | fructose 1,6-bisphosphate 1-phosphatase activity [GO:0042132]; fructose-bisphosphate aldolase activity [GO:0004332]; magnesium ion binding [GO:0000287] | PF01950; | null | FBP aldolase/phosphatase family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000269|PubMed:15274916, ECO:0000269|PubMed:20348906, ECO:0000269|PubMed:21983966}; CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000269|PubMed:20348906, ECO:0000269|PubMed:21983966}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.027 mM for D-fructose 1,6-bisphosphate (when assaying the FBPase activity, at 80 degrees Celsius) {ECO:0000269|PubMed:15274916}; KM=0.027 mM for D-fructose 1,6-bisphosphate (when assaying the FBPase activity, at 48 degrees Celsius) {ECO:0000269|PubMed:21983966}; KM=0.19 mM for triosephosphates (when assaying the FBP aldolase activity in the anabolic direction, at 48 degrees Celsius) {ECO:0000269|PubMed:21983966}; Note=kcat is 2.5 sec(-1) for the FBPase activity (at 80 degrees Celsius) (PubMed:15274916). kcat is 0.62 sec(-1) for the FBPase activity (at 48 degrees Celsius). kcat is 0.91 sec(-1) for the FBP aldolase activity in the anabolic direction (at 48 degrees Celsius). kcat is 0.027 sec(-1) for the FBP aldolase activity in the catabolic direction (at 48 degrees Celsius) (PubMed:21983966). {ECO:0000269|PubMed:15274916, ECO:0000269|PubMed:21983966}; | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000305|PubMed:20348906, ECO:0000305|PubMed:21983966}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:15274916}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is over 100 degrees Celsius. {ECO:0000269|PubMed:15274916}; | FUNCTION: Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P). {ECO:0000269|PubMed:15274916, ECO:0000269|PubMed:20348906, ECO:0000269|PubMed:21983966}. | Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) |
F9VN79 | RNH_SULTO | MIIGYFDGLCEPKNPGGIATFGFVIYLDNRKIEGYGLAEKPFSINSTNNVAEYSGLICLMETMLRLGISSPIIKGDSQLVIKQMNGEYKVKAKRIIPLYEKAIELKKKLNATLIWVPREENKEADRLSRVAYELVRRGKLRDIGCIILT | 3.1.26.4 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:15520465}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15520465}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:15520465}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:15520465}; Note=Divalent metal cations; Mn(2+) and Mg(2+) are preferred over Co(2+) or Ni(2+). {ECO:0000269|PubMed:15520465}; | null | cytoplasm [GO:0005737] | DNA binding [GO:0003677]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA-DNA hybrid ribonuclease activity [GO:0004523] | PF13456; | 3.30.420.10; | null | PTM: The disulfide bond confers considerable stability to the protein. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408, ECO:0000269|PubMed:15520465}; | null | null | null | null | FUNCTION: Nuclease that specifically degrades the RNA of RNA-DNA hybrids. Endonucleolytically removes RNA primers from the Okazaki fragments of lagging strand synthesis on its own. In the presence of Mn(2+) or Co(2+) can also cleave an RNA-RNA hybrid; the dsRNase activity is 10- 100-fold lower than RNase H activity. Complements the temperature-sensitive phenotype of an E.coli double rnhA/rnhB (RNase H) disruption mutant. {ECO:0000269|PubMed:15520465}. | Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) |
F9W301 | KN1_ORYSJ | MSNVTVCVRFRPLSHKERKTNGDKVCFKRLDSESFVFKDEREEDVIFSFDRVFYEDAEQSDVYNFLAVPIVADAISGINGTIITYGQTGAGKTYSMEGPSILHCNKQKTGLVQRVVDELFQSLQSSESMAMWSVKLSMVEIYLEKVRDLLDLSKDNLQIKESKTQGIYISGATEVSIQNSSDALECLSEGIANRAVGETQMNLASSRSHCLYIFSVQQGSTSDERVRGGKIILVDLAGSEKVEKTGAEGRVLDEAKTINKSLSVLGNVVNALTTGKPNHVPYRDSKLTRILQDALGGNSRAALLCCCSPSASNAPESLSTVRFGTRTKLIKTTPKSISPEVDSIKKPIPDSHGQNDLRDRILNKLRLSLKEEDVDLLEELFVQEGIIFDPNYSVADIDSACQDAASQEVSLLTQAVEELKETVEELTDENERLRGELELAQEAAAAAAAARADGALLGFVPAVAISSLLRPFGFVPD | null | null | anterograde dendritic transport of neurotransmitter receptor complex [GO:0098971]; axon guidance [GO:0007411]; cytoskeleton-dependent intracellular transport [GO:0030705]; microtubule-based movement [GO:0007018]; synaptic vesicle transport [GO:0048489] | cytoplasm [GO:0005737]; kinesin complex [GO:0005871]; microtubule [GO:0005874] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; plus-end-directed microtubule motor activity [GO:0008574] | PF00225; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, KIN-1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21282525}. | null | null | null | null | null | FUNCTION: Kinesin-like motor protein that exhibits microtubule-stimulated ATPase activity. Plays an essential role in male meiotic chromosomal dynamics, male gametogenesis and anther dehiscence. May play a minor and nonessential role in regulating meiotic spindle formation. {ECO:0000269|PubMed:21282525}. | Oryza sativa subsp. japonica (Rice) |
F9WWF1 | GGS2_ZYMTI | MLDVRGSLPGQVNTGTISPYRRIDRSNDTIGTSDLAADEQVLLGPFNHLDARPGKEIRSQLIDAFDSWLQVPTASLAVIKNVVRMLHNASLLIDDIQDNSELRRGAPAAHHAFGTAQTINSANYVYFRALRELSTLHNPVMVQIYTAELLNLHHGQGMDLFWRETGTCPTESRYLEMVGNKTGGLFRLAIRCMCVEGSPKQSSADYIRLATMIGILFQILDDFRNLTDGSYTSSKGFCEDLTEGKFSFPIVHAIRSNPGDSFLHDILRQHTDDPAVKKEAVSYLERCGSLIYTQGVIHQLAGDVLTLADEVDAGQGRAQALKDIVQRLMVKL | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; mycotoxin biosynthetic process [GO:0043386]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744] | mitochondrion [GO:0005739]; transferase complex [GO:1990234] | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000250|UniProtKB:Q12051}; | null | null | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster 3 that mediates the biosynthesis of an isoprenoid secondary metabolite. {ECO:0000269|PubMed:28818040}. | Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch fungus) (Septoria tritici) |
F9WZD2 | GSS1_ZYMTI | MDKFSQSPPLRDDLVRGSSLNWTKEKENILKGPFNYLESHPGKDIRSQLIAAFNAWLDVPEESLNVIRRVVAMLHTASLLIDDVEDNSQLRRGIPVAHNVFGTAQTINSANYVYFCALKELAILNNPAVIQIYTEELVNLHRGQGMDLFWRDTLTCPSEDDYLEMVGNKTGGLFRLAIKLMCAESPSHNAHPDPFQRNDYVPLVNTIGLLFQILDDYKNLSDTIYTQNKGLCEDLTEGKFSFPIIHAIRADPGNLVLINILKQKTTDDEVKKYAVAYMDRAGSFSYTRKVLRGLTKKALTQVDEVDAGRGRGEQMKTILEKLRVDRNHQRGVLTPAAGGASIA | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; mycotoxin biosynthetic process [GO:0043386]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744] | mitochondrion [GO:0005739]; transferase complex [GO:1990234] | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000250|UniProtKB:Q12051}; | null | null | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster 4 that mediates the biosynthesis of an isoprenoid secondary metabolite. {ECO:0000269|PubMed:28818040}. | Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch fungus) (Septoria tritici) |
F9XLC1 | GGS3_ZYMTI | MHISTIKTAGSSGMSHMNEAYSSTTATEMVARGAGSEIIHTEIDSNGSKELAPNGAQSRVQKPSEDAVRAPYDYIRTLPSKRIRETFIDALDSWLAVPAGSSTSIKSIIGMLHQSSLMLDDIEDDSTLRRGKPTAHTLFGTAQTINSANWVFVCAFEELRQLRGVDAATVFVEELKNLHCGQALDLHWKHHTYIPSVDEYLNMVDHKTGGLFRLCVRLMQGESSTSCHHIDAERFITLLGRYFQIRDDYQNLVSDEYTNQKGFCEDLDEGKISLPLIYCLAGSDPTQIMIKGILQHKRTGEMPLSMKKLILEKMRSGGALNATISLLKDLQDDILEELKSLELAFGSGNPMLELVLRRLWI | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386] | null | dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000250|UniProtKB:Q12051}; | null | null | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster 25 that mediates the biosynthesis of an isoprenoid secondary metabolite. {ECO:0000269|PubMed:28818040}. | Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch fungus) (Septoria tritici) |
G0HV10 | PYRG_HALHT | MPTEPETDYDPELGRKFIFVTGGVMSGLGKGITAASTGRLLKNAGFDVTAVKIDPYLNVDAGTMNPFQHGEVYVLKDGGEVDLDLGNYERFLDIDMTFDHNVTTGKTYQHVIEKERSGDYLGRTVQIIPHITDDIKRRIREAAEGNDVCIIEVGGTVGDIEGMPYLEALRQFAHEEDEDDILFTHVTLVPYSKNGEQKTKPTQHSVKELRSIGLQPDILVGRCSDKLDIDTKEKIALFCDVPTEAVFSNPDVDDIYHVPLMVEEEGLDQYVMEELDIATEALPEDERENRWRDLVTQNTEGEVDIALVGKYDLEDAYMSVHEALKHAGLEKNVDVNVQWVNSEKMNDHHADRMREADAIVVPGGFGARGTEGKIEAIRYARENDIPFLGLCLGFQMAVVEYARNVLDLDDAHSAELDEDTPHPVIDILPEQYEIEDMGGTMRLGAHETEIDANTLAATLYGGESCTERHRHRYEVNPEYIDDLEAAGLKFSGYAENRMEILELAPEDHPYFIGTQFHPEFRSRPTRASPPFVGLLEAVLGDDPHTVTTEEVSH | 6.3.4.2 | null | 'de novo' CTP biosynthetic process [GO:0044210]; glutamine metabolic process [GO:0006541]; pyrimidine nucleobase biosynthetic process [GO:0019856] | cytoophidium [GO:0097268]; cytosol [GO:0005829] | ATP binding [GO:0005524]; CTP synthase activity [GO:0003883]; glutaminase activity [GO:0004359]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF06418;PF00117; | 3.40.50.880;3.40.50.300; | CTP synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32507415}. Note=Localizes to the cytoophidium, a short subcellular filamentary structure where CTP synthase is compartmentalized. Only a few cells form cytoophidia under standard growth conditions, they are observed in late log phase. Stress conditions such as treatment with 50 uM 6-diazo-5-oxo-l-norleucine (DON, an inhibitor) or growth at low salt (1.5 M instead of the usual 3.4 M) also induces their appearance. In all these conditions cells are barely growing. {ECO:0000269|PubMed:32507415}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01227}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; Evidence={ECO:0000255|HAMAP-Rule:MF_01227}; CATALYTIC ACTIVITY: Reaction=ATP + NH4(+) + UTP = ADP + CTP + 2 H(+) + phosphate; Xref=Rhea:RHEA:16597, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-Rule:MF_01227}; | null | PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01227}. | null | null | FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. {ECO:0000255|HAMAP-Rule:MF_01227}. | Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM B-1755) |
G0L322 | AGAA_ZOBGA | MKKNYLLLYFIFLLCGSIAAQDWNGIPVPANPGNGMTWQLQDNVSDSFNYTSSEGNRPTAFTSKWKPSYINGWTGPGSTIFNAPQAWTNGSQLAIQAQPAGNGKSYNGIITSKNKIQYPVYMEIKAKIMDQVLANAFWTLTDDETQEIDIMEGYGSDRGGTWFAQRMHLSHHTFIRNPFTDYQPMGDATWYYNGGTPWRSAYHRYGCYWKDPFTLEYYIDGVKVRTVTRAEIDPNNHLGGTGLNQATNIIIDCENQTDWRPAATQEELADDSKNIFWVDWIRVYKPVAVSGGGNNGNDGATEFQYDLGTDTSAVWPGYTRVSNTTRAGNFGWANTNDIGSRDRGASNGRNNINRDINFSSQTRFFTQDLSNGTYNVLITFGDTYARKNMNVAAEGQNKLTNINTNAGQYVSRSFDVNVNDGKLDLRFSVGNGGDVWSITRIWIRKVTSNSANLLAAKGLTLEDPVETTEFLYPNPAKTDDFVTVPNSEIGSSIIIYNSAGQVVKKVSVVSENQKISLEGFAKGMYFINLNGQSTKLIVQ | 3.2.1.81 | null | carbohydrate metabolic process [GO:0005975] | extracellular region [GO:0005576] | beta-agarase activity [GO:0033916] | PF21254;PF18962; | 2.60.120.200;2.60.120.430; | Glycosyl hydrolase 16 family | PTM: Proteolytically cleaved into mature beta-agarase A catalytic chain (AgaAc). {ECO:0000269|PubMed:15456406}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15456406}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product.; EC=3.2.1.81; Evidence={ECO:0000269|PubMed:15456406}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 mM for agarose {ECO:0000269|PubMed:15456406}; Note=kcat is 150 sec(-1).; | null | null | null | FUNCTION: Cleaves the beta-1,4-linkages between beta-D-galactose and alpha-L-3,6-anhydro-galactose residues in agarose. Cleaves agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place. {ECO:0000269|PubMed:15456406}. | Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij) |
G0LXV8 | LATA_LATHA | SLVRMRREGEEDLTLEEKAELCSELELQQKYVDIGSNIIGDLSSLPIVGKIVGTIAAAAMAVTHVASGRLDIEQTLGGCSDVPFDQIKEILEERFNEIDRKLESHSAALEEITKLVEKSISAVEKTRKQMNKRFDEVMRSIQDAKVSPLVSKINNFARYFDTEKERIRGLKLSDYILKLEEPNGILLHFKESRTPRDDSLQAPLFSIIQERYAVPKSIDDELAFKVLYALLYGTQTYVSVMFFLLEQYSFLANHYYEKGDLEKYDEYFNSLNNVFLDFKSSLVGTGTSNNEGLLDRVLQVLVTVKNSEFLGLEKNGVNEMLNEKINLFNKIKVEIEGKQRMTLSETPENFAQISFDKDITTPIGDWRDGREVRYAVQYASETLFSKISHWSDPVGVREKACPTLRMPVDQTRRNILVFRKFDSSKPQLVGEITPYQSNFIDIDRDLYNTANNPDSAVGFKEFTKLNYDGANIRATFEQGRTVFHAAAKSGNSRIMIGLTFLVKSNELNQPDKKGYTPIHVAADSGNAGIVNLLIQRGVSINSKTYNFLQTPLHLAAQRGFVTTFQRLMESPEININERDKDGFTPLHYAVRGGERILEAFINQIRIDLNAKSNKGLTPFHLAIIKDDWPVASTLLGSKKVDVNAVDENNMTALHYAAILGYLETTKQLINLKEINADVVSSPGLLSALHYAILYKHDDVASFLLRSSNVNVNLKALGGITPLHLAVIQGRTQILSLMFDIGVNIEQQTDEKYTPLHLAAMSKYPELIQILLDQGSNFEAKTNSGATPLHLATFKGKSKAALILLNNEVNWRDTDENGQMPIHGAAMNGLLDVAQAIISIDATVLDIKDKNSDTPLNLAAQKSHIDVIKYFIDQGADINTRNKTGHAPLLAFSKKGNLDMVKYLFDKNANVYIADNDGINFFYYAVRNGHLNIVKYAMSEKDKFEWSNIDNNRRDECPKEECAISHFAVCDAVQFDKIEIVKYFVTTLGNFAICGPLHQAARYGHLDIEKYLVEEEDLNVDGSKPDTPLCYASENGHLAVVQYLVSNGAKVNHDCGNGMTAIDKAITKNHLQVVQFLAANGVDFRRKNKLGATPFLTAVSENAFDIAEYLIRENRQDIDINEQNVDKETALHLAVYYKNLQMIKLLVKYGIDMTIRNAYDKTALDIATDLKNSNIVEYLKTKSGKFRREYKSSYGEHSLLQTNKISSFIDGKNIEHDHPQFINADNESSQLFSDTASNIDVIGPLLLIDVLIRYFSKQGYISKESDSASDGITQAAALSITEKFEDVLNSLHNESAKEQVDLAEVHGKVYAALKSGRNSQIHPILCSSLKSISTLKPEDMEKLGSVIMNSHS | null | null | exocytosis [GO:0006887] | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | toxin activity [GO:0090729] | PF00023;PF12796; | 1.25.40.20; | Cationic peptide 01 (latrotoxin) family, 03 (alpha-latrotoxin) subfamily | PTM: Processed by furin-like proteases at both the N- and C-termini. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22001442}. Target cell membrane {ECO:0000250|UniProtKB:P23631}. Note=Forms a membrane channel in the prey. {ECO:0000250|UniProtKB:P23631}. | null | null | null | null | null | FUNCTION: Presynaptic neurotoxin that causes massive release of neurotransmitters from vertebrate (but not invertebrate) nerve terminals and endocrine cells via a complex mechanism involving activation of receptor(s) and toxin insertion into the plasma membrane with subsequent pore formation. Binds to neurexin-1-alpha (NRXN1) in a calcium dependent manner, adhesion G protein-coupled receptor L1 (ADGRL1, also termed latrophilin-1 and calcium-independent receptor of latrotoxin (CIRL)), and receptor-type tyrosine-protein phosphatase S (PTPRS), also termed PTP sigma. NRXN1 and PTPRS are suggested to provide a platform for binding and subsequent pore formation events. In contrast, binding to ADGRL1 does not involve oligomerization and channel formation, but direct downstream stimulation of the synaptic fusion machinery (By similarity). Induces rapid muscle contracture and loss of twitch tension when added to the isolated and indirectly stimulated chick biventer cervicis nerve-muscle preparation (PubMed:22001442). {ECO:0000250|UniProtKB:P23631, ECO:0000269|PubMed:22001442}. | Latrodectus hasselti (Redback spider) |
G0R6T8 | LP9A_HYPJQ | MIQKLSNLLVTALAVATGVVGHGHINDIVINGVWYQAYDPTTFPYESNPPIVVGWTAADLDNGFVSPDAYQNPDIICHKNATNAKGHASVKAGDTILFQWVPVPWPHPGPIVDYLANCNGDCETVDKTTLEFFKIDGVGLLSGGDPGTWASDVLISNNNTWVVKIPDNLAPGNYVLRHEIIALHSAGQANGAQNYPQCFNIAVSGSGSLQPSGVLGTDLYHATDPGVLINIYTSPLNYIIPGPTVVSGLPTSVAQGSSAATATASATVPGGGSGPTSRTTTTARTTQASSRPSSTPPATTSAPAGGPTQTLYGQCGGSGYSGPTRCAPPATCSTLNPYYAQCLN | 3.2.1.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:28900033}; Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:28900033}; | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulose binding [GO:0030248]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872] | PF03443;PF00734; | 2.70.50.70; | Polysaccharide monooxygenase AA9 family | PTM: N-glycosylation at position Asn-158 is important to determine C1/C4-oxidation ratios. {ECO:0000269|PubMed:30238672}. | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:26285758}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:26285758, ECO:0000269|PubMed:28110665, ECO:0000269|PubMed:28900033, ECO:0000269|PubMed:30238672}; | null | null | null | null | FUNCTION: Lytic polysaccharide monooxygenase (LMPO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (PubMed:26285758, PubMed:28110665, PubMed:28900033, PubMed:30238672). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (PubMed:28900033, PubMed:32414932, PubMed:34597668). Produces both neutral and oxidized cello-oligosaccharides from cellulose (PubMed:26285758, PubMed:28900033). Acts also on soluble cello-oligosaccharides as short as a tetramer (PubMed:26285758). The oxidative activity displays a synergistic effect capable of boosting endoglucanase activity, and thereby substrate depolymerization of soy cellulose by 27% (PubMed:28110665). {ECO:0000269|PubMed:26285758, ECO:0000269|PubMed:28110665, ECO:0000269|PubMed:28900033, ECO:0000269|PubMed:30238672, ECO:0000269|PubMed:32414932, ECO:0000269|PubMed:34597668}. | Hypocrea jecorina (strain QM6a) (Trichoderma reesei) |
G0RUP7 | XYN2_HYPJQ | MVSFTSLLAGVAAISGVLAAPAAEVESVAVEKRQTIQPGTGYNNGYFYSYWNDGHGGVTYTNGPGGQFSVNWSNSGNFVGGKGWQPGTKNKVINFSGSYNPNGNSYLSVYGWSRNPLIEYYIVENFGTYNPSTGATKLGEVTSDGSVYDIYRTQRVNQPSIIGTATFYQYWSVRRNHRSSGSVNTANHFNAWAQQGLTLGTMDYQIVAVEGYFSSGSASITVS | 3.2.1.8 | null | xylan catabolic process [GO:0045493] | extracellular region [GO:0005576] | endo-1,4-beta-xylanase activity [GO:0031176] | PF00457; | 2.60.120.180; | Glycosyl hydrolase 11 (cellulase G) family | PTM: Glycosylated. {ECO:0000269|PubMed:8975597}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8975597}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; EC=3.2.1.8; Evidence={ECO:0000250|UniProtKB:P36217}; | null | PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-ProRule:PRU01097}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-6. {ECO:0000269|PubMed:8975597}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:8975597}; | FUNCTION: Glycoside hydrolase involved in the hydrolysis of xylan, a major plant cell wall hemicellulose made up of 1,4-beta-linked D-xylopyranose residues. Catalyzes the endohydrolysis of the main-chain 1,4-beta-glycosidic bonds connecting the xylose subunits yielding various xylooligosaccharides and xylose. {ECO:0000250|UniProtKB:P36217}. | Hypocrea jecorina (strain QM6a) (Trichoderma reesei) |
G0RV93 | GCE_HYPJQ | MASRFFALLLLAIPIQAQSPVWGQCGGIGWSGPTTCVGGATCVSYNPYYSQCIPSTQASSSIASTTLVTSFTTTTATRTSASTPPASSTGAGGATCSALPGSITLRSNAKLNDLFTMFNGDKVTTKDKFSCRQAEMSELIQRYELGTLPGRPSTLTASFSGNTLTINCGEAGKSISFTVTITYPSSGTAPYPAIIGYGGGSLPAPAGVAMINFNNDNIAAQVNTGSRGQGKFYDLYGSSHSAGAMTAWAWGVSRVIDALELVPGARIDTTKIGVTGCSRNGKGAMVAGAFEKRIVLTLPQESGAGGSACWRISDYLKSQGANIQTASEIIGEDPWFSTTFNSYVNQVPVLPFDHHSLAALIAPRGLFVIDNNIDWLGPQSCFGCMTAAHMAWQALGVSDHMGYSQIGAHAHCAFPSNQQSQLTAFVQKFLLGQSTNTAIFQSDFSANQSQWIDWTTPTLS | 3.1.1.117 | null | carbohydrate metabolic process [GO:0005975]; lignin catabolic process [GO:0046274] | extracellular region [GO:0005576] | carboxylic ester hydrolase activity [GO:0052689]; cellulose binding [GO:0030248] | PF00734; | 3.40.50.1820; | Carbohydrate esterase 15 (CE15) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 4-O-methyl-alpha-D-glucuronosyl ester derivative + H2O = 4-O-methyl-alpha-D-glucuronate derivative + an alcohol + H(+); Xref=Rhea:RHEA:67452, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:171667, ChEBI:CHEBI:171668; EC=3.1.1.117; Evidence={ECO:0000269|PubMed:17678650}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453; Evidence={ECO:0000305|PubMed:17678650}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.5 mM for 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside {ECO:0000269|PubMed:17678650}; Vmax=5.5 umol/min/mg enzyme toward 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside {ECO:0000269|PubMed:17678650}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:17678650}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-60 degrees Celsius. {ECO:0000269|PubMed:17678650}; | FUNCTION: Glucuronoyl esterase which may play a significant role in biomass degradation, as it is considered to disconnect hemicellulose from lignin through the hydrolysis of the ester bond between 4-O-methyl-D-glucuronic acid residues of glucuronoxylans and aromatic alcohols of lignin. Does not hydrolyze substrates of other carbohydrate esterases such as acetylxylan esterase, acetyl esterase and feruloyl esterase. {ECO:0000269|PubMed:12788920, ECO:0000269|PubMed:17678650}. | Hypocrea jecorina (strain QM6a) (Trichoderma reesei) |
G0S0Y3 | PAN3_CHATD | MAPLDLTRGQTDACSTENKDILCRNVLIYGHCRYEDQGCTYNHDQNKNSSQPEAPSKKMFNVDSPSFTPSGQSTVLPKKTTLSSQAASAAPFTPRGGGTPTLQTTAESTMFNPAAIREFTPQNYDLGNNNANGISQENGLYPDPFTMSTMGTALPTAGQYNLPLYGDHSGLAAPGAPFYPPHAAYPTGPIQPPHYHLYQPFGPYRQELQPWQRATYDFFMPQNLREDLQKKQFATLQVIPNSGLPQLEHWHSLVPLDTSNRKNTSCFGYPSWVYKAQNSRNGRHYALRRLEGYRLTNEKAILNVMKDWKKIKNASIVTIHEVFTTREFGDSSLIFAYDFHPLSKTLQEHHFQPIHGNRYRPPPAVPENTIWGYICQIANALKTIHSNRLAARCLEPSKIILTDINRIRLSACAILDVVQFGMNSRSVVELQQEDFVKFGKLILSLATGTLPAHLNNIPAALETLGNKYSANLKSAVNWLLDTSSGETKTIEHFMTGIASQMTTFFDLALQDNDEKLFHLAREVENGRIARSLMKLLTILERGDYDGVPSWSETGDRYQLKLFRDYVFHRVDADGKPNLSIGHMLTCMSKLEAGVDENILLTSRDNETVFVLSYRELRQMYDRAFNELVKASKTGAPGANT | null | null | mRNA processing [GO:0006397]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289] | P-body [GO:0000932]; PAN complex [GO:0031251] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; poly(A) binding [GO:0008143]; protein kinase activity [GO:0004672] | PF18101; | 1.10.287.3700;1.20.5.5160;6.10.250.3160;1.10.510.10; | Protein kinase superfamily, PAN3 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03181}. | null | null | null | null | null | FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and with PAB1. {ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:24872509}. | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) |
G0S196 | ATC5_CHATD | MAPPQEEGGGNGTELSMQRSRWATRRLTVKSGARKRLSLMTRAQAKNSATEKRQSGVTDDGSPAADGDQKEGSISSSNNGGSAPRKLYFNLPLPPELKDEEGHPIQQFPRNKIRTAKYTPLSFIPKNLWFQFHNIANIFFLFLVILVIFPIFGGVNPGLNSVPLIVIITVTAIKDAIEDYRRTILDIELNNAPVHRLQGWENVNVEKDNVSLWRRFKKANSRFFGSIWHLIERLWKEDAQSMRQRFASADPRMSIETRTAPWDPSHRRSVASHTEEIQMTPVPSPVPHDPDVPTVSSAIENEATLLQNLKGDLINHEIPVSGKARFHKDAWKNLVVGDFVRIYNDDELPADIIILATSDPDGACYVETKNLDGETNLKVRQALRCGRTLKHARDCERAQFVIESEPPQPNLYKYNGAIRWKQRVPWDPHGEPREMSEPIGIDNLLLRGCHLRNTEWALGVVVFTGHDTKIMMNAGITPSKRARIARELNFNVICNFGILLIMCLIAAIANGIAWGKTDASLAWFEYGSIGGTPALTGFITFWAAVIVFQNLVPISLYISLEIVRTLQAFFIYSDVGMYYEKIDQPCIPKSWNISDDVGQIEYIFSDKTGTLTQNVMEFKKATINGQPYGEAYTEAQAGMDRRRGINVEEEAKVIREEIAAAKVRAIRGLRELHDNPYLHDEDMTFIAPDFVEDLAGKNGPEQQQATEHFMLALALCHTVVAEKQPGDPPKMIFKAQSPDEAALVATARDMGFTVLGMSDGGINVNVMGKDMHFPVLSIIEFNSSRKRMSTIVRMPDGRILLFCKGADSVIYSRLKKGEQADMRRETAQHLEMFAVEGLRTLCIAERELSEEEYREWRREHDLAATALENREEKLEEVADKIERDLTLLGGTAIEDRLQDGVPDTIALLADAGIKLWVLTGDKVETAINIGFSCNLLNNDMDLLRLQVNESDASTEDDYLQLAEEQLKTNLERFNMTGDDEELKRARKDHNAPSPTYALVIDGFTLRWVLSDSLKQKFLLLCKQCKSVLCCRVSPAQKAAVVSMVKNGLDVMTLSIGDGANDVAMIQEADVGVGIAGEEGRQAVMSSDFAIGQFRFLQRLVLVHGRWSYRRLAETISNFFYKNMIWTWSIFWYQCYCNFDIAYIFEYTYILMFNLFFTSVPVILMGVLDQDVSDTVSLAVPQLYRRGIERKEWTQTKFWLYMIDGVYQSVMSFFIPFIFVVLTPTAAGNGLDVSERTRLGAYIAHPAVITINGYILINTYRWDWLMLLSIVLSDVFIFFWTGVYTATTYSAGFYQAAPQVYQELTFWMCLIVTPALCLLPRLVVKCIQKQRFPYDVDIIREQANRGDFAAADAAAVAALGGPERVEGESLGSLSSSGKGSGRSKKSKHQQYASVDEDRRPIYPPSIATHNTRAQNGSDGTTYIMQSRTSTELQQEMPFDRDREEETPAVRPSIERTRPSYDRIRRSIDRVRPSFEASNDFTSAARLSRIESTHSSLGHTYSHQRESYAGESSGAQQGQEPGQRRFNLATVRKRGLSAFSKKSIDTTEGEPPREPPM | 7.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32303992}; | Golgi organization [GO:0007030]; phospholipid translocation [GO:0045332] | endosome membrane [GO:0010008]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; magnesium ion binding [GO:0000287]; phosphatidylcholine floppase activity [GO:0090554]; phosphatidylethanolamine flippase activity [GO:0090555]; phosphatidylserine floppase activity [GO:0090556] | PF13246;PF16212;PF16209; | 3.40.1110.10;2.70.150.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P32660}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P32660}. Endosome membrane {ECO:0000250|UniProtKB:P32660}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P32660}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P32660}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P32660}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000305|PubMed:32303992}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64612, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P32660}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133; Evidence={ECO:0000250|UniProtKB:P32660}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:32303992}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584; Evidence={ECO:0000305|PubMed:32303992}; CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(out) + ATP + H2O = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66036, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:22801, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P32660}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66037; Evidence={ECO:0000250|UniProtKB:P32660}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57262, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:32303992}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568; Evidence={ECO:0000305|PubMed:32303992}; | null | null | null | null | FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine and phosphatidylserine from the lumenal to the cytosolic leaflet of membranes and ensures the maintenance of asymmetric distribution of phospholipids (PubMed:32303992). May also transport glucosylceramide and phosphatidylethanolamine (By similarity). {ECO:0000250|UniProtKB:P32660, ECO:0000269|PubMed:32303992}. | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) |
G0S3J5 | RIO1_CHATD | MTPAPEPQDPPTIHEPVATEQTDDISDWDVESDYEDGYGAPSKSQAQGGASAADRPKINAHARIDDQMTDLARHASKIRLDNLTMQQIFRDKDRTDNATSDQVLDNHTRMIILNMLNRNIISEIYGTISTGKEANVYNAVAYDNNGERIERAVKVYKTIILGFKDRERYLAGEQRFKTIVDKALSAPRKMIKLWAEKEFRNLKRLHTAGIPCPEPIYLKYNVMVMGFLGDHTNGYAFPRLHDTKITGETLEETEAEWRRLYINLLSMMRRMYQVCGLVHGDLSEYNILYNEGVLYIIDVSQSVEHDHIEATNFLRMDIRNVNDFFARRGVDTLSDRTVYHFITDSTGAVDENGMRKAIDNLYATRPPLAESEEARAEQEIDNQVFRNQFIPTTLEEVYNLEVELGKKVDTRLYQHMLADSKVPESTGGEHKSGEGGESGSEDEEGDEGESGEVESGDEEREEGEGDRFEKKRPRGKKHLDKAEKHAHKMAVKEAKREKRKEKMPKHVKKKLVAANKKRK | 2.7.11.1; 3.6.3.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:G0S5R3, ECO:0000250|UniProtKB:Q9BRS2}; | maturation of SSU-rRNA [GO:0030490]; phosphorylation [GO:0016310] | cytosol [GO:0005829]; preribosome, small subunit precursor [GO:0030688] | ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF01163; | 1.10.510.10; | Protein kinase superfamily, RIO-type Ser/Thr kinase family | PTM: Autophosphorylated. {ECO:0000269|PubMed:24948609}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | 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|PIRNR:PIRNR038147}; 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|PIRNR:PIRNR038147}; | null | null | null | null | FUNCTION: Involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit (By similarity). In vitro, has strong ATPase activity and only low protein kinase activity (PubMed:24948609). {ECO:0000250|UniProtKB:Q12196, ECO:0000269|PubMed:24948609}. | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) |
G0S4X6 | ODP2_CHATD | MLAQVLRRQALQHVRLARAAAPSLTRWYASYPPHTIVKMPALSPTMTSGNIGAWQKKPGDAITPGEVLVEIETDKAQMDFEFQEEGVLAKILKETGEKDVAVGSPIAVLVEEGTDINAFQNFTLEDAGGDAAAPAAPAKEELAKAETAPTPASTSAPEPEETTSTGKLEPALDREPNVSFAAKKLAHELDVPLKALKGTGPGGKITEEDVKKAASAPAAAAAAPGAAYQDIPISNMRKTIATRLKESVSENPHFFVTSELSVSKLLKLRQALNSSAEGRYKLSVNDFLIKAIAVACKRVPAVNSSWRDGVIRQFDTVDVSVAVATPTGLITPIVKGVEAKGLETISATVKELAKKARDGKLKPEDYQGGTISISNMGMNPAVERFTAIINPPQAAILAVGTTKKVAVPVENEDGTTGVEWDDQIVVTASFDHKVVDGAVGAEWMRELKKVVENPLELLL | 2.3.1.12 | COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000255|PROSITE-ProRule:PRU01066}; Note=Binds 1 lipoyl cofactor covalently. {ECO:0000255|PROSITE-ProRule:PRU01066}; | acetyl-CoA biosynthetic process from pyruvate [GO:0006086] | mitochondrial pyruvate dehydrogenase complex [GO:0005967] | dihydrolipoyllysine-residue acetyltransferase activity [GO:0004742] | PF00198;PF00364;PF02817; | 2.40.50.100;3.30.559.10;4.10.320.10; | 2-oxoacid dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein]; Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12; Evidence={ECO:0000269|PubMed:33567276}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17019; Evidence={ECO:0000269|PubMed:33567276}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=68 uM for coenzyme A {ECO:0000269|PubMed:33567276}; | null | null | null | FUNCTION: The 10-megadalton pyruvate dehydrogenase complex contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) and catalyzes the overall oxidative decarboxylation of pyruvate to form acetyl-CoA and CO(2) (PubMed:33567276, PubMed:34836937, PubMed:35093201). Within the complex, pyruvate and thiamine pyrophosphate (TPP or vitamin B1) are bound by pyruvate dehydrogenase E1 subunits alpha and beta and pyruvate is decarboxylated leading to the 2-carbon hydrohyethyl bound to TPP. The E2 component contains covalently-bound lipoyl cofactors and transfers the hydroxyethyl group from TPP to an oxidized form of covalently bound lipoamide, and the resulting acetyl group is then transferred to free coenzyme A to form acetyl-CoA and reduced dihydrolipoamide-E2. Finally, the flavoprotein dihydrolipoamide dehydrogenase (E3) re-oxidizes the lipoyl group of dihydrolipoamide-E2 to form lipoamide-E2 and NADH. A fourth subunit, E3BP, is responsible for tethering E3 in proximity to the core, forming the entire metabolon (Probable). {ECO:0000269|PubMed:33567276, ECO:0000269|PubMed:34836937, ECO:0000269|PubMed:35093201, ECO:0000305|PubMed:33567276}. | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) |
G0SAK3 | NU145_CHATD | MSFGFGSGGFGQNNNSSTFGGFGSTPTTNTGFGSTGTTAFGSTSNTTGGGLFGGGGGGFGSGNTFGSGFGSKPAFGTPATTSSTSLFGSTTTTAGGTGFGSGGFGSTNTSSPFGGGGTSLFGNKTTTGFGSGTSTFGSNTGGGLFGGGSTTTGFGATNNPGIGTNVGDPPGTAVVPFSPTVEKEVNNPSQSNSYQNILFMDAYKKWSAEELRLADYNQGRKTAAPGGTGAFGSSGFGGFGTTSNTGGFGSNTGGGLFGNTQQNTGGFGTTNTTGSAFGSGGGLFGNKPATGGLFGTSSSQPAQSGGLFGSGTASTFGSSNTGTTSTFGSNNNTGGGLFGSNNTSSKPAFSFGTSNTSTPGFGTATTGSGFGTGTTTNTGGGLFGNTAQNTNTGGGLFGNQQQSGSAFGSGTGFGQQNQSTGTSLFGNTQQKPGGLFGSTTTNTSGGLFGSTNTGTSTFGQTPATQNTGGGLFGSKPAGTGGLFGSTATNQPASTGGLFGNLNTNAQTQQPATGGLFGNLGQNNQAKPSLFGTSTTTGGGLFGNTNAQQQTGSLFGTSTAQQQPQTGLGASLFGSSQQQQQQPQTFSTSITDISAYGATTLFSGLPDDKIQNPGPLATPLSGKAKVKSRSILPMYKLSPANASRLVTTPQKRAYGFSFSAYGSPTSPSSSASSTPGAFGQSILSSSINRGLNKSISASNLRRSLNVEDSILQPGAFSANSSMRLLGGPGSHKKLVINKDMRTDLFSPPNKDKQPQEDGTAARKTVTKRVSFDTSNVETPEKTIESSIPATDDSGYLKPDARSTANGTNGANGAKSSPVAAASPPEMEQVKGKELAVVHEEESPAPAQTDKPRGSQIEPGAYWMSPTADDIRAMNRMQRQRVVGFTVGRENVGSVQFKVPVDLSNINLDDLFGTIVILEPRSATVYPNAAKKPPMGKGLNVPALISLEHSWPRGGPTIKGRRLERHIERLKSIPDTTFESYDPETGVWAFSVEHFTTYGLGDDDDYDDDDYETEPESAVKSTPRPVTSPSISKSSTSPIDPDDTFEFRRSRRALPGAFDDAALSDTDEVANHAQRQGTLSPEPQDADTPLPSREWPEDESMADGLDEYQLEAYEEASQQGSVDEQEDFLPSRFAADNDAPQVPAGIMRARMRAVKKLNAPTKIEVAGGDDWTQILQASVKAPRTMDRATLRALNESGAVWEMKDRGSPPPQATATVSDGMGFATSIDLMKSLFEQAKAPTQPALTTSGKGFVKWPYEQRSKTDTEENLAVPRTNWGPNELLISTQHNEPNLLPVDAADDSATSPSTLARLQQYINLVSSKKQLQRVAGPEFRELAQGDSVWELAALLFDDNGEGVSQFWQQLVSEATDRALSFTAGLEEKAIICLAGNRVDEACRHLLAAGNFRLATLVSTIGKVDNKDIRAQLKDWRESNVLAEFSEPIRAIYELLAGNASVCAGVKNVPIENRVNSFTISQRFGLDWMRSFGLRLWYTSGVIPDVAAAVRSFQEDIEQDREPEPDSALWTLLKAFASREYDWSDTRLGWLLTKAIYTTGKVSFGEDALQKLDKASVTFASALTAASHWVPATFVLLQLSDPASREAAVRDHLGRHAHRIGSPRNLMSPFFTLQKFGVPEAWIWEAKALDYRSRQDSQQEFLALIWAQNYAEANRTFVTRVGPDLVIERNLPRLFAFAQLLFKVKKHLPNWERSAAVYLLYPMAVMQNQGSGKLDRFDNQLIDGLVALHSQTHGDIRQEAAIADMAEELIKCKGAAAASDPRLLQLLPQDVRGKYLRAQVLEAF | 3.4.21.- | null | mRNA transport [GO:0051028]; post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery [GO:0000973]; protein import into nucleus [GO:0006606]; RNA export from nucleus [GO:0006405]; telomere tethering at nuclear periphery [GO:0034398] | nuclear membrane [GO:0031965]; nuclear pore cytoplasmic filaments [GO:0044614] | hydrolase activity [GO:0016787]; nuclear localization sequence binding [GO:0008139]; RNA binding [GO:0003723]; structural constituent of nuclear pore [GO:0017056] | PF04096;PF13634;PF12110; | 1.10.10.2360;1.25.40.690;3.30.1610.10; | Nucleoporin GLFG family | PTM: NUP145 is autocatalytically cleaved in NUP145N and NUP145C. {ECO:0000250|UniProtKB:P49687}. | SUBCELLULAR LOCATION: [Nucleoporin NUP145C]: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49687}. Nucleus membrane {ECO:0000250|UniProtKB:P49687}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49687}; Cytoplasmic side {ECO:0000250|UniProtKB:P49687}. Nucleus membrane {ECO:0000250|UniProtKB:P49687}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49687}; Nucleoplasmic side {ECO:0000250|UniProtKB:P49687}. Note=Symmetrically distributed on the cytoplasmic and nucleoplasmic side of nuclear envelope. {ECO:0000250|UniProtKB:P49687}.; SUBCELLULAR LOCATION: [Nucleoporin NUP145N]: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P49687}. Nucleus membrane {ECO:0000250|UniProtKB:P49687}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49687}; Nucleoplasmic side {ECO:0000250|UniProtKB:P49687}. Note=Biased towards the nucleoplasmic side, nuclear pore complex. {ECO:0000250|UniProtKB:P49687}. | null | null | null | null | null | FUNCTION: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. NUP145 is autocatalytically cleaved in vivo in 2 polypeptides which assume different functions in the NPC. NUP145N as one of the FG repeat nucleoporins participates in karyopherin interactions and contains part of the autocatalytic cleavage activity. NUP145C as part of the NUP84 complex is involved in nuclear poly(A)+ RNA and tRNA export. {ECO:0000250|UniProtKB:P49687}. | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) |
G0SAK8 | PAN2_CHATD | MDADWDEVTRIAYPAPGTNDFPRPATAVAFDPIAELLWAGFDRGRVCSFYGRDLTRYTAFKIQPASEGPVRQFLFHDKGVIVLGTRSVHMAMRRGPALWNIRHENMKDLRCMSFTSKGTQEIIVAGWQDTMLVIDVLKGDIIKQIPAQHHYSIMKKSRYICAATKTGSVDLIDPLSFKIVRSWQAHASYINDMDAQNDFIVTCGGSLKQQAAQTYMLDPYVNVFDLKNMASMKPMPFPPLAAHVRLHPRMLTTAIVTSQHGQMHVVDIMNPNSSTVRYANISSYVKLFEIAPSGEALVIGDADCNIHLWGSPTKIHFTDMAIPIELPEPEEPAPVLDWSIETPLSSIGLPYYREPLFSAWPADIISDVGAPPLQLEPSFVATLKQAEWGLYGKNTRNVRRNQVEDTRNTNKQSNALQAPKFLSERARESALSSGGDSSSDPQVDQEPEDPNEIESLKPEAPPLYRNLEIKYSKFGVDDFDFGYYNKTRYAGLENHIPNSYANSLLQLMHYTPLLRNMALQHAATACVSDLCLLCELGFVFDMLQKAEGATCQATNMFKALSGTPQAAPLGLLEEETHVPSLATMAQNLSRFLLEKIHNEYRTIPPISTALEQSLFNFPHPPTPDELVAKVLATSAVATIKCMNCRSETTRPGTTHVIDLLYPPPKTAGRGGRASKVTFSQVLKMGVERETTSKGWCSRCQRYQNLQMRKTIHSVPAVLVVNAGVSNQEHRKLWSTPGWLPEEIGIIVDQGQFFCFEGEDLKLHLQRGIHNITVYSLIGMVINIESHSPQKSHLVGIINVAHAEATPPGENKWHLFNDFSVRPVSAAEALTFNAAWKMPAVLLFQIKSANNKSNLDWKTNLDTSILYKDTNPNTEKKTYRTLDQERERPGPDTIVALDTEFVSLKQPEIQMNSDGERETIRPMSHALARVSVVRGQGENEGSAFIDDYIAIREPVVDYLTLYSGITASDLDPRTSKHNLVSLKTAYKKLWVLLNLGCKFLGHGLKQDFRVINIQVPRAQVIDTIEVFYLKSRLRKLSLAFLAWYLLKEDIQLETHDSIEDARTALKLYRKYLEFDDAGILEAMLEDIYKAGRATNFKPPRREDREKELQRQSTPPNSTAPNDCGAKPDGNGNENGGEPATPARKTGGITAPTFGAVNVFGTPSKASSPLPK | 3.1.13.4 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_03182}; Note=Binds 2 metal cations per subunit in the catalytic exonuclease domain. {ECO:0000255|HAMAP-Rule:MF_03182}; | mRNA processing [GO:0006397]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289] | P-body [GO:0000932]; PAN complex [GO:0031251] | metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; poly(A)-specific ribonuclease activity [GO:0004535] | PF20770;PF00929;PF13423; | 3.90.70.10;3.30.420.10;2.130.10.10; | Peptidase C19 family, PAN2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03182}. | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:24872509}; | null | null | null | null | FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:24872509}. | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) |
G0SGC7 | MGM1_CHATD | MSAQLRAAAAITPAARRVISGPAAVRRFHHYHHLPTGGIQRVEIAARGLRRSVQFPALANAYHNNAVIVRNASFTRLLPKLALKFIRVPALFGGMMLGAVGWVQYQAIKVSNSAQEFYGNIKATVADTAFSVWSSAVDIAEQTKRGWENTKNQFEIPEWLDRIMKGEGLAGEGSGSGEGGPNGGPEPPRQSRAGAATVAGASATVYGYGASDNDDRTPEEIMRDDNMMFITKKMIEIRNLLQKVGQGSTVTLPSIVVIGSQSSGKSSVLEAIVGHEFLPKGSNMITRRPIELTLVNDPEAKVDYGEFPDLGLARVTDFSLIQKTLTELNQSVPESECVTDDPIRLTIHSPNIPDLSLIDLPGYIQVAGENQPRELKRKITELCDKYIRGPNIILAISAADTDLANSTALQASRRVDPRGERTIGVITKMDLVEPEKGAAILSDRQYPLKLGYVGVISKLPPQSGLFRRDTGNLLASINRNEKNYFGSHPTEFGPDSGVSTGVMTLRKKLLQVLEQQMSSKLNETTEAIQRELEETTYQFKVQYNEQPMSAESYLAASLDDFKHQFHEFASSFGRPQLQTLLKDALDQKVLDQLAARYWNRPIEDLSPAPREPDNIIDLPKADPDSPYWHRQLDTACSGLTRLGVGRLAATVAASAIQQHVEKLLDKSSFAKHPSARKVISDAAATVLADRSYATSDGIEISLKPYKFDPDIQPNEWAQGREHVVGVLQAELEQCQAAMKALENSVGGRKKLKEVMSFVDKARKGEIIVEGDHPSGAGGFSAALLARGREAVFLRDRADILSLRIQAAKSRQCKTLTNKYYCPEVFLDAVATKLAQTAVLFLNVEMLNDFYVRFPREVEAKLHEHMHAGGGLEKFAREDPKVRRHLDLIRRKELLETVLGKIEELHRISSGTAGTLGLRGAGDLKKRIGAPSSSGRRSFF | 3.6.5.5 | null | defense response to virus [GO:0051607]; mitochondrial fusion [GO:0008053] | cytoplasm [GO:0005737]; membrane [GO:0016020]; microtubule [GO:0005874]; nucleus [GO:0005634] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; microtubule binding [GO:0008017] | PF01031;PF00350; | 3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family | PTM: Cleavage of the transit peptide by mitochondrial processing protease (MPP) produces a long integral membrane form of MGM1 (L-MGM1) (By similarity). Further processing by the rhomboid protease PCP1 produces a short peripheral membrane form of MGM1 (S-MGM1) (By similarity). Both forms are required for full activity (By similarity). {ECO:0000250|UniProtKB:P32266}. | SUBCELLULAR LOCATION: [Dynamin-like GTPase MGM1, long form]: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P32266}; Single-pass type II membrane protein {ECO:0000255}; Intermembrane side {ECO:0000250|UniProtKB:P32266}.; SUBCELLULAR LOCATION: [Dynamin-like GTPase MGM1, small form]: Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P32266}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5; Evidence={ECO:0000269|PubMed:31292547}; | null | null | null | null | FUNCTION: Dynamin-related GTPase that is essential for normal mitochondrial morphology by mediating fusion of the mitochondrial inner membranes, regulating cristae morphology and maintaining respiratory chain function (PubMed:31292547). Exists in two forms: the transmembrane, long form (Dynamin-like GTPase MGM1, long form; L-MGM1), which is tethered to the inner mitochondrial membrane, and the short soluble form (Dynamin-like GTPase MGM1, short form; S-MGM1), which results from proteolytic cleavage and localizes in the intermembrane space (By similarity). Both forms (L-MGM1 and S-MGM1) cooperate to catalyze the fusion of the mitochondrial inner membrane (By similarity). The equilibrium between L-MGM1 and S-MGM1 is essential: excess levels of S-MGM1, following loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-MGM1 and S-MGM1, inhibiting mitochondrial fusion (By similarity). Plays a role in the maintenance and remodeling of mitochondrial cristae, some invaginations of the mitochondrial inner membrane that provide an increase in the surface area (PubMed:31292547). Probably acts by forming helical filaments at the inside of inner membrane tubes with the shape and dimensions of crista junctions (PubMed:31292547). {ECO:0000250|UniProtKB:O60313, ECO:0000250|UniProtKB:P32266, ECO:0000269|PubMed:31292547}.; FUNCTION: [Dynamin-like GTPase MGM1, long form]: Constitutes the transmembrane long form (L-MGM1) that plays a central role in mitochondrial inner membrane fusion and cristae morphology (By similarity). L-MGM1 and the soluble short form (S-MGM1) form higher-order helical assemblies that coordinate the fusion of mitochondrial inner membranes (By similarity). Inner membrane-anchored L-MGM1 molecules initiate membrane remodeling by recruiting soluble S-MGM1 to rapidly polymerize into a flexible cylindrical scaffold encaging the mitochondrial inner membrane (By similarity). Once at the membrane surface, the formation of S-MGM1 helices induce bilayer curvature (By similarity). MGM1 dimerization through the paddle region, which inserts into cardiolipin-containing membrane, promotes GTP hydrolysis and the helical assembly of a flexible MGM1 lattice on the membrane, which drives membrane curvature and mitochondrial fusion (PubMed:31292547). {ECO:0000250|UniProtKB:O60313, ECO:0000250|UniProtKB:P32266, ECO:0000269|PubMed:31292547}.; FUNCTION: [Dynamin-like GTPase MGM1, small form]: Constitutes the soluble short form (S-MGM1) generated by cleavage by PCP1, which plays a central role in mitochondrial inner membrane fusion and cristae morphology (By similarity). The transmembrane long form (L-MGM1) and the S-MGM1 form higher-order helical assemblies that coordinate the fusion of mitochondrial inner membranes (By similarity). Inner membrane-anchored L-MGM1 molecules initiate membrane remodeling by recruiting soluble S-MGM1 to rapidly polymerize into a flexible cylindrical scaffold encaging the mitochondrial inner membrane (By similarity). Once at the membrane surface, the formation of S-MGM1 helices induce bilayer curvature (By similarity). MGM1 dimerization through the paddle region, which inserts into cardiolipin-containing membrane, promotes GTP hydrolysis and the helical assembly of a flexible MGM1 lattice on the membrane, which drives membrane curvature and mitochondrial fusion (PubMed:31292547). Excess levels of S-MGM1 produced by cleavage by PCP1 following stress conditions that induce loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-MGM1 and S-MGM1, thereby inhibiting mitochondrial fusion (By similarity). {ECO:0000250|UniProtKB:O60313, ECO:0000250|UniProtKB:P32266, ECO:0000269|PubMed:31292547}. | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) |
G0SHW7 | RAD50_CHATD | MSKIEKLSILGVRSFGPHHPETIAFNTPLTLIVGYNGSGKTTVIECLKYATTGELPPNSTRNGAFIHDPDLVGEKEVRAQVKLSFRSTIGESYVVTRNIQLLVQRNNKRTQKTLEGSLLLRNNGERTVISTRVAELDKLVSEKLGVPPAILDAVIFCHQDDSLWPMSEPAALKKRFDEIFEAQKYTKVIENIRLLKKKKGDELKILKEREVQDKANKERAEKVDRLMAQLTREILEAREKCNELSKQMEEESAKIKDKYEQANSFLKIMNDLQTKTEKLEYKKDAIVELRSRIEELPDPDEVLRNTLDEYEQTINRIVADRDHKAAQFHDLQAELKSARDQHTAKAAEQGKHQSDKEKYERQLVARERMIREAAERHEIRGYNGDLDDRRIAIFNERIQKILNDKRRELERLQRENQEELDRKTAVIAERESRKQSVIRDRKAAKDRIISLGKDMASIQGELSSIDIDEGTEEMLRAEMKELQARIEAAKADEQNANLDAQIKEVNEEIWKLESLSAKLARELVECTRLASERAQLDLRRKQLAERKRELEIMTNTWNEQFSTLLGEGWRPETLERDFSDVLKQQQLLVGEHRKKKDATQQELKQAEYQLSNARNLHNKLTNEMEACMRAVQTAMKEARDLDSAPPVDEYITMLETDEKELAEVETALKLYDELKKHYSTIKDRALRFNKCYICDRDFTNQEAAKTRLLEKVAKRLGDEEKKELLEDQAAFMKSLDILRAVRVKYDTYQRLSSELPQLSREIDSETNRREDLVRRLEDQDLAFREADNKLQEMETLNKHVMKITQLLKDISDAEKQVERSQQLSNIETRSADEINEEQTTCAEQTRAAQAKLTKLTAEKQRLKDLVRQLEVERLQLENKISSAVQQLERKKRLQESIARHKEDQNQARNAVQEADEELERLEPEIAGARAALDEARQACRAKEQKVAAERDAIAQTVSELNMINSEIQEYLDRGGPSSLAANQRAIANLETQMANLEGEMRELTVQINKLNKEIDNSDAKKRNIADNLTYRKNLREKDALEREIAELEARNAQEDYDRLIKEAHYLEAHRSKLNADRERLMGMMSTKDEEFRRLNEEYELDLKDAKAKYKETHIKVETTKAAIEDLGRGMAAVDHAIMQYHSKMMEQINRTIAELWQSTYQGTDIDTIQIRSDVESTTSSDSGTRRNYNYRVSMVKGDTEMDMRGRCSAGQKVLASIIIRLALAESFCANCGLIALDEPTTNLDSDNIRSLAESLHGIIKARQAQGNLQLIVITHDEEFLKYMQCSDFCDDFYRVKRDEKQNSVIVRESITRITE | 3.6.-.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:36577401}; Note=Binds 1 zinc ion per homodimer. {ECO:0000269|PubMed:36577401}; | chromosome organization involved in meiotic cell cycle [GO:0070192]; DNA duplex unwinding [GO:0032508]; double-strand break repair [GO:0006302]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via telomerase [GO:0007004] | condensed nuclear chromosome [GO:0000794]; Mre11 complex [GO:0030870] | ATP hydrolysis activity [GO:0016887]; double-stranded DNA binding [GO:0003690]; double-stranded telomeric DNA binding [GO:0003691]; G-quadruplex DNA binding [GO:0051880]; guanyl-nucleotide exchange factor activity [GO:0005085]; metal ion binding [GO:0046872]; single-stranded telomeric DNA binding [GO:0043047] | PF13476;PF13558; | 3.40.50.300; | SMC family, RAD50 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92878}. Chromosome {ECO:0000250|UniProtKB:Q92878}. Note=Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q92878}. | 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; Evidence={ECO:0000269|PubMed:36577401}; | null | null | null | null | FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (By similarity). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (By similarity). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (By similarity). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11, to initiate end resection, which is required for single-strand invasion and recombination (By similarity). Within the complex, RAD50 is both required to bind DNA ends and hold them in close proximity and regulate the activity of MRE11 (PubMed:26896444, PubMed:36577401). RAD50 provides an ATP-dependent control of MRE11 by positioning DNA ends into the MRE11 active site: ATP-binding induces a large structural change from an open form with accessible MRE11 nuclease sites into a closed form (PubMed:36577401). {ECO:0000250|UniProtKB:Q92878, ECO:0000269|PubMed:26896444, ECO:0000269|PubMed:36577401}. | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila) |
G0WXL9 | CS2H_ACIS1 | MVSEYIDSELKRLEDYALRRVKGIPNNRRLWVLTCMDERVHIEQSLGIQPDDAHIYRNAGGIVTDDAIRSASLTTNFFGTKEIIVVTHTDCGMLRFTGEEVAKYFISKGIKPTEVQLDPLLPAFRISSEEDFIKWFKFYEDLGVKSPDEMALKGVEILRNHPLIPKDVRITGYVYEVETHRLRKPNQIIYNETSKFEHGTIVKE | 3.13.1.5 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:22012399}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22012399}; | hydrogen sulfide biosynthetic process [GO:0070814] | null | carbonate dehydratase activity [GO:0004089]; hydrolase activity [GO:0016787]; identical protein binding [GO:0042802]; zinc ion binding [GO:0008270] | PF00484; | 3.40.1050.10; | Beta-class carbonic anhydrase family | null | null | CATALYTIC ACTIVITY: Reaction=carbon disulfide + 2 H2O = CO2 + 2 H(+) + 2 hydrogen sulfide; Xref=Rhea:RHEA:38143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:23012, ChEBI:CHEBI:29919; EC=3.13.1.5; Evidence={ECO:0000269|PubMed:22012399}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=130 uM for carbon disulfide {ECO:0000269|PubMed:22012399}; KM=22 uM for carbonyl sulfide {ECO:0000269|PubMed:22012399}; Vmax=40 nmol/min/ug enzyme towards hydrogen sulfide formation from carbon disulfide {ECO:0000269|PubMed:22012399}; Vmax=74 nmol/min/ug enzyme towards hydrogen sulfide formation from carbonyl sulfide {ECO:0000269|PubMed:22012399}; Note=kcat is 952 sec(-1) with carbon disulfide as substrate. kcat is 1800 sec(-1) with the intermediate carbonyl sulfide as substrate. {ECO:0000269|PubMed:22012399}; | PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis. {ECO:0000269|PubMed:22012399}. | null | null | FUNCTION: Catalyzes the conversion of carbon disulfide into hydrogen sulfide and carbon dioxide, with carbonyl sulfide as an intermediate. Likely plays a key role in sulfur metabolism that allows Acidianus sp. A1-3 to grow on carbon disulfide as the main carbon and energy source. Does not show carbonic anhydrase activity (hydration of CO(2) to carbonate). {ECO:0000269|PubMed:22012399}. | Acidianus sp. (strain A1-3) |
G0Y7D3 | TPS3_LITCU | MALQLLTPSFSFQHSPSPHRLTTLRYTHHTIRCTASAPSYSDLVGRRSANYKPSKWDSNFVETLESDYKKENHEMYIEKLMGDVKHLMKKVVNPIEKMELVDTIQRLGLGYLFNKEIKEVLNTIATSKATFKTKKDLHAVALQFRLLRQHGYEVSPDAFHKFKDEKGGFKESLCMDIKGMLSLYEASHLSFQGEVVLDEAREFTSTHLKAIEGNIDPVLLKKVRHSLEMPLHWRMLRLEARWYIETYDEEDRKNPSLAELAKHDFNSVQTIYQRSLKRMSRWWRDLGLGERLEFSRDRLVECFFWTTGVIFDPQFERCRGVLTKVNQLVSTIDDVYDVYGSLEELELFTDAVDRWDIRAMEQLPEYMKICYLALYNTTNDIAYEALKEEGLDVIPYLKKVWTDLCKSYIVEARWYSNGYKPTLEEYLENAWTSIAGPVALGHAYFSFGQKMPFEALNYSNTSSLIKWSSMIFRLCDDLATSSDEVARGDVPKSIQCYMYEAGVSESVARDHIKYLIDEAWKKMNECLVPSTPFLQPLINAGFNLARMAHCMYEHGDGHGFSNELDKKRVLLLLAEPFKFM | 4.2.3.-; 4.2.3.110 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102]; green leaf volatile biosynthetic process [GO:0010597]; monoterpene biosynthetic process [GO:0043693] | chloroplast [GO:0009507] | alpha-thujene synthase activity [GO:0102700]; magnesium ion binding [GO:0000287]; sabinene synthase activity [GO:0080015] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsb subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = alpha-thujene + diphosphate; Xref=Rhea:RHEA:68644, ChEBI:CHEBI:33019, ChEBI:CHEBI:50031, ChEBI:CHEBI:58057; Evidence={ECO:0000269|Ref.1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68645; Evidence={ECO:0000269|Ref.1}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (1R,5R)-sabinene + diphosphate; Xref=Rhea:RHEA:32547, ChEBI:CHEBI:33019, ChEBI:CHEBI:50029, ChEBI:CHEBI:58057; EC=4.2.3.110; Evidence={ECO:0000269|Ref.1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32548; Evidence={ECO:0000269|Ref.1}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|Ref.1}. | null | null | FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products used by traditional Chinese medicine to treat headache, inflammation and intoxication (Ref.1). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into alpha-thujene and (1R,5R)-sabinene (Ref.1). {ECO:0000269|Ref.1}. | Litsea cubeba (Aromatic litsea) (Laurus cubeba) |
G1FC92 | MIG21_CAEEL | MERDSNTAKSEIFYSNPAIWRHLKDGKGEGMSKSEKRNKHGCRNFTYSIWNCIRPGGWSTWSKWSKCREGIRKRRRTCNNPLPIGTTCSGQKVEKQSCAISSNVPEYLFGSWTSWNPWSRCDCDRSLRIRTRHCKGNSCEGCDKDYEDCRPDECPISKKWSEWTDWVNYGIEQVRFSAWCSSSNVANTEVGIRKETQDSMKHANWSEWHMHPGVAYRYRLLHNSSISIEHHLLSRFTSSCLPLHFAIPIFCFCILTGFLLQNIIYCVVNRFKRRFIRLNYSYDSNPRDYPSHLIRSPGSPKDESFW | null | null | determination of left/right asymmetry in nervous system [GO:0035545]; neuroblast migration [GO:0097402]; neuron migration [GO:0001764]; regulation of canonical Wnt signaling pathway [GO:0060828]; regulation of cell migration [GO:0030334] | plasma membrane [GO:0005886] | signaling receptor activity [GO:0038023] | PF00090; | 2.20.100.10; | null | PTM: Glycosylated via C-mannosylation by dpy-19 at Trp-58 and Trp-61. {ECO:0000269|PubMed:23562325}. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Required for determination of left/right asymmetry in nervous system. Acts together with unc-40 to control an initial left-right asymmetric polarization of the Q neuroblasts. Mig-21 and unc-40 may control the asymmetry in Wnt signaling response by restricting posterior polarization to one of the 2 Q neuroblasts. Involved in left-side QL posterior migration. In right-side QR, unc-40 and mig-21 pathways mutually inhibit each other in posterior migration, allowing anterior QR migration. {ECO:0000269|PubMed:22074987, ECO:0000269|PubMed:23051647}. | Caenorhabditis elegans |
G1FNI6 | TFP_THLAR | MARTLQGEWMKVEQKGGQVPAPRSSHGIAVIGDKLYCFGGEDPPYESIDNDLYVFDFNTHTWSIAPANGDVPKTRVLGTRMVAVGTKLYVFGGRNKQLEFEDFYSYDTVKEEWKFLTKLDEKGGPEARTFHSMTSDENHVYVFGGVSKGGLNATPFRFRTIEAYNIAEGKWAQLPDPGEDFEKRGMAGFLVVQGKLWVFYGFATANDPKIPTLYGSQDYESNRVHCYDPATQKWTEVETTGFEKPSRRSCFAHAAVGKYIIIFGGEIERDPEAHQGPGTLSREGFALDTETLVWERYEGGPIKPSNRGWVASTTTTINGKKGLLVHGGKLMTNERTDEMYFFAVNSST | 4.8.1.8 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:21783213, ECO:0000269|PubMed:26260516, ECO:0000269|PubMed:30900313}; | glucosinolate metabolic process [GO:0019760]; nitrile biosynthetic process [GO:0080028] | cytosol [GO:0005829]; nucleus [GO:0005634] | enzyme regulator activity [GO:0030234]; identical protein binding [GO:0042802]; lyase activity [GO:0016829]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803] | PF01344;PF13964; | 2.120.10.80; | null | null | null | CATALYTIC ACTIVITY: Reaction=(Z)-N-(sulfonatooxy)prop-2-enimidothioate = allyl thiocyanate + sulfate; Xref=Rhea:RHEA:69316, ChEBI:CHEBI:16189, ChEBI:CHEBI:183062, ChEBI:CHEBI:183082; EC=4.8.1.8; Evidence={ECO:0000269|PubMed:21783213}; CATALYTIC ACTIVITY: Reaction=(Z)-N-(sulfonatooxy)prop-2-enimidothioate = 2-(thiiran-2-yl)acetonitrile + sulfate; Xref=Rhea:RHEA:69252, ChEBI:CHEBI:16189, ChEBI:CHEBI:183062, ChEBI:CHEBI:183064; EC=4.8.1.8; Evidence={ECO:0000269|PubMed:21783213}; CATALYTIC ACTIVITY: Reaction=(Z)-N-(sulfonatooxy)prop-2-enimidothioate = allyl isothiocyanate + sulfate; Xref=Rhea:RHEA:69272, ChEBI:CHEBI:16189, ChEBI:CHEBI:73224, ChEBI:CHEBI:183062; Evidence={ECO:0000269|PubMed:21783213}; CATALYTIC ACTIVITY: Reaction=(Z)-phenyl-N-(sulfonatooxy)methanimidothioate = phenylacetonitrile + sulfate + sulfur; Xref=Rhea:RHEA:69308, ChEBI:CHEBI:16189, ChEBI:CHEBI:25979, ChEBI:CHEBI:26833, ChEBI:CHEBI:183061; Evidence={ECO:0000269|PubMed:21783213}; CATALYTIC ACTIVITY: Reaction=glucoerucin + H2O = (Z)-4-methylsulfanylbutyl-N-(sulfonatooxy)methanimidothioate + D-glucose; Xref=Rhea:RHEA:69320, ChEBI:CHEBI:4167, ChEBI:CHEBI:5404, ChEBI:CHEBI:15377, ChEBI:CHEBI:183222; Evidence={ECO:0000269|PubMed:21783213}; CATALYTIC ACTIVITY: Reaction=(Z)-4-methylsulfanylbutyl-N-(sulfonatooxy)methanimidothioate = 5-(methylsulfanyl)pentanenitrile + H(+) + sulfate + sulfur; Xref=Rhea:RHEA:69328, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:26833, ChEBI:CHEBI:183222, ChEBI:CHEBI:183223; Evidence={ECO:0000269|PubMed:21783213}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-6. {ECO:0000269|PubMed:21783213}; | null | FUNCTION: Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation (By similarity). Catalyzes allylthiocyanate and corresponding epithionitrile formation from allylglucosinolate in the presence of myrosinase (PubMed:21783213, PubMed:23999604, PubMed:26260516, PubMed:30900313). Converts also aliphatic glucosinolates, such as indol-3-ylmethylglucosinolate, 4-methylsulfinylbutylglucosinolate, 4-methylthiobutyl- and benzylisothiocyanate, to simple nitriles (PubMed:21783213). {ECO:0000250|UniProtKB:Q93XW5, ECO:0000269|PubMed:21783213, ECO:0000269|PubMed:23999604, ECO:0000269|PubMed:26260516, ECO:0000269|PubMed:30900313}. | Thlaspi arvense (Field penny-cress) |
G1JSL4 | PXG1_AVESA | MAEDAVVSDAVVVSDAMSSVAKGAPVTAQRPVRDDLEKHIPKPYLARALVAVDVNNPEGTKGGRHEHGQKSVLQQHVSFFDQNGDGIIYPWETFRGLRRLGFNLIVSFIVAIGIHTGLSYPTLPTWRPSLLFPVYIDRIHKAKHGSDTATFDTEGRFMPVNFENIFSKNARSQPDKLTLREIWMMTNDHRLAYDPFGWVANKGEWILLYMLAKDDEGYLPKEAIRGVYDGSLFEFLAEQRTKKAHGKQH | 1.11.2.3 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group. {ECO:0000250}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | null | endoplasmic reticulum [GO:0005783]; lipid droplet [GO:0005811]; membrane [GO:0016020] | 18-hydroxyoleate peroxygenase activity [GO:0102070]; calcium ion binding [GO:0005509]; monooxygenase activity [GO:0004497]; plant seed peroxidase activity [GO:1990137] | PF05042; | null | Caleosin family | null | SUBCELLULAR LOCATION: Microsome membrane. Lipid droplet. | CATALYTIC ACTIVITY: Reaction=RH + ROOH = ROH + ROH.; EC=1.11.2.3; Evidence={ECO:0000269|PubMed:14535881, ECO:0000269|PubMed:16956885, ECO:0000269|PubMed:21784965}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16.07 uM for 9-HPOD {ECO:0000269|PubMed:21784965}; KM=10.42 uM for 9-HPOT {ECO:0000269|PubMed:21784965}; KM=25.18 uM for 13-HPOD {ECO:0000269|PubMed:21784965}; KM=7.25 uM for 13-HPOT {ECO:0000269|PubMed:21784965}; KM=215.76 uM for cumene hydroperoxide {ECO:0000269|PubMed:21784965}; Vmax=214.04 pmol/sec/mg enzyme toward 9-HPOD {ECO:0000269|PubMed:21784965}; Vmax=188.69 pmol/sec/mg enzyme toward 9-HPOT {ECO:0000269|PubMed:21784965}; Vmax=306.57 pmol/sec/mg enzyme toward 13-HPOD {ECO:0000269|PubMed:21784965}; Vmax=173.49 pmol/sec/mg enzyme toward 13-HPOT {ECO:0000269|PubMed:21784965}; Vmax=883.34 pmol/sec/mg enzyme toward cumene hydroperoxide {ECO:0000269|PubMed:21784965}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:21784965}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:21784965}; | FUNCTION: Calcium-binding peroxygenase involved in cutin monomers biosynthesis. Can catalyze epoxidation of fatty acid and sulfoxidation reactions that can proceede competitively, although in favor of the sulfoxidation. Can only use unsaturated fatty acids with double bonds in the cis configuration as substrates. The preferred substrate is oleic acid and is inactive toward ricinoleic acid. Free fatty acid and fatty acid methyl esters are effective substrate forms, but not phospholipids and acyl-CoA. Hydroperoxy-trienoic (HPOT) acids are preferred over Hydroperoxy-dienoic (HPODT) acids as oxygen donors. {ECO:0000269|PubMed:14535881, ECO:0000269|PubMed:16956885, ECO:0000269|PubMed:21784965}. | Avena sativa (Oat) |
G1JUH1 | TPS3_SOLLC | MSIFSTRYLVTPFSSFSPPKAFVSKACSLSTGQPLNYSPNISTNIISSSNGIINPIRRSGNYEPTMWNYEYIQSTHNHHVGEKYMKRFNELKAEMKKHLMMMLHEESQELEKLELIDNLQRLGVSYHFKDEIIQILRSIHDQSSSEATSANSLYYTALKFRILRQHGFYISQDILNDFKDEQGHFKQSLCKDTKGLLQLYEASFLSTKSETSTLLESANTFAMSHLKNYLNGGDEENNWMVKLVRHALEVPLHCMMLRVETRWYIDIYENIPNANPLLIELAKLDFNFVQAMHQQELRNLSRWWKKSMLAEKLPFARDRIVEAFQWITGMIFESQENEFCRIMLTKVTAMATVIDDIYDVYGTLDELEIFTHAIQRMEIKAMDELPHYMKLCYLALFNTSSEIAYQVLKEQGINIMPYLTKSWADLSKSYLQEARWYYSGYTPSLDEYMENAWISVGSLVMVVNAFFLVTNPITKEVLEYLFSNKYPDIIRWPATIIRLTDDLATSSNEMKRGDVPKSIQCYMKENGASEEEARKHINLMIKETWKMINTAQHDNSLFCEKFMGCAVNIARTGQTIYQHGDGHGIQNYKIQNRISKLFFEPITISMP | 4.2.3.105; 4.2.3.117; 4.2.3.15; 4.2.3.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | diterpenoid biosynthetic process [GO:0016102] | chloroplast [GO:0009507] | (4S)-limonene synthase activity [GO:0050552]; camphene synthase activity [GO:0102703]; magnesium ion binding [GO:0000287]; myrcene synthase activity [GO:0050551]; tricyclene synthase activity [GO:0102701] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsb subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + tricyclene; Xref=Rhea:RHEA:32687, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:64266; EC=4.2.3.105; Evidence={ECO:0000269|PubMed:21813655}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (1S,4R)-camphene + diphosphate; Xref=Rhea:RHEA:25484, ChEBI:CHEBI:89, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.117; Evidence={ECO:0000269|PubMed:21813655}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate; Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.15; Evidence={ECO:0000269|PubMed:21813655}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (4S)-limonene + diphosphate; Xref=Rhea:RHEA:12869, ChEBI:CHEBI:15383, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.16; Evidence={ECO:0000269|PubMed:21813655}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. | null | null | FUNCTION: Monoterpene synthase that catalyzes the formation of camphene and tricyclene from geranyl diphosphate. Produces also lower amounts of limonene and beta-myrcene, and traces of several other monoterpenoids. {ECO:0000269|PubMed:21813655}. | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
G1NJB6 | MYG_MELGA | MGLSDQEWQQVLTIWGKVEADIAGHGHEVLMRLFHDHPETLDRFDKFKGLKTPDQMKGSEDLKKHGATVLTQLGKILKQKGNHESELKPLAQTHATKHKIPVKYLEFISEVIIKVIAEKHAADFGADSQAAMKKALELFRNDMASKYKEFGFQG | 1.11.1.-; 1.7.-.- | null | removal of superoxide radicals [GO:0019430] | extracellular exosome [GO:0070062]; sarcoplasm [GO:0016528] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitrite reductase activity [GO:0098809]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 6.10.140.2100;6.10.140.2110; | Globin family | null | SUBCELLULAR LOCATION: Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:P02144}. | CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P02144}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; Evidence={ECO:0000250|UniProtKB:P02144}; CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; Evidence={ECO:0000250|UniProtKB:P02144}; | null | null | null | null | FUNCTION: Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand. Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide. Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity. {ECO:0000250|UniProtKB:P02144}. | Meleagris gallopavo (Wild turkey) |
G1SJB4 | RACK1_RABIT | MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALSGSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNSSNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALCFSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR | null | null | apoptotic process [GO:0006915]; cell cycle [GO:0007049]; gastrulation [GO:0007369]; positive regulation of protein phosphorylation [GO:0001934]; rescue of stalled ribosome [GO:0072344]; rhythmic process [GO:0048511] | cytosol [GO:0005829]; dendrite [GO:0030425]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; phagocytic cup [GO:0001891]; ribonucleoprotein complex [GO:1990904]; ribosome [GO:0005840] | protein kinase C binding [GO:0005080]; ribosome binding [GO:0043022]; translation regulator activity [GO:0045182] | PF00400; | 2.130.10.10; | WD repeat G protein beta family, Ribosomal protein RACK1 subfamily | PTM: Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required for binding to SRC. {ECO:0000250|UniProtKB:P63244}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63244}; Peripheral membrane protein {ECO:0000250|UniProtKB:P63244}. Cytoplasm {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:30355441, ECO:0000269|PubMed:30517857, ECO:0000269|PubMed:31246176, ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:31768042, ECO:0000269|PubMed:32286223, ECO:0000269|PubMed:33296660, ECO:0000269|PubMed:35679869, ECO:0000269|PubMed:35822879, ECO:0000269|PubMed:36653451}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P63244}. Nucleus {ECO:0000250|UniProtKB:P63244}. Perikaryon {ECO:0000250|UniProtKB:P68040}. Cell projection, dendrite {ECO:0000250|UniProtKB:P68040}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:P63244}. Note=Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. Also associated with the membrane in oncogene-transformed cells. PKC activation induces translocation from the perinuclear region to the cell periphery (By similarity). In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei (By similarity). Localized to phagocytic cups following infection by Y.pestis (By similarity). {ECO:0000250|UniProtKB:P63244, ECO:0000250|UniProtKB:P68040}. | null | null | null | null | null | FUNCTION: Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules (By similarity). Interacts with a wide variety of proteins and plays a role in many cellular processes (By similarity). Component of the 40S ribosomal subunit involved in translational repression (PubMed:23873042, PubMed:25601755, PubMed:27863242, PubMed:30517857). Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (By similarity). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation (By similarity). May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6 (By similarity). Inhibits the activity of SRC kinases including SRC, LCK and YES1 (By similarity). Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle (By similarity). Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer (By similarity). Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC (By similarity). Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix (By similarity). Involved in PKC-dependent translocation of ADAM12 to the cell membrane (By similarity). Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A (By similarity). Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation (By similarity). Required for PTK2/FAK1 phosphorylation and dephosphorylation (By similarity). Regulates internalization of the muscarinic receptor CHRM2 (By similarity). Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L (By similarity). Inhibits TRPM6 channel activity (By similarity). Regulates cell surface expression of some GPCRs such as TBXA2R (By similarity). Plays a role in regulation of FLT1-mediated cell migration (By similarity). Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (By similarity). Promotes migration of breast carcinoma cells by binding to and activating RHOA (By similarity). Acts as an adapter for the dephosphorylation and inactivation of AKT1 by promoting recruitment of PP2A phosphatase to AKT1 (By similarity). {ECO:0000250|UniProtKB:P63244, ECO:0000250|UniProtKB:P68040, ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:30517857}. | Oryctolagus cuniculus (Rabbit) |
G1SK22 | RS27A_RABIT | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGAKKRKKKSYTTPKKNKHKRKKVKLAVLKYYKVDENGKISRLRRECPSDECGAGVFMASHFDRHYCGKCCLTYCFNKPEDK | null | null | modification-dependent protein catabolic process [GO:0019941]; protein ubiquitination [GO:0016567]; translation [GO:0006412] | cytosolic ribosome [GO:0022626]; nucleolus [GO:0005730]; ribonucleoprotein complex [GO:1990904] | metal ion binding [GO:0046872]; protein tag activity [GO:0031386]; structural constituent of ribosome [GO:0003735]; ubiquitin protein ligase binding [GO:0031625] | PF01599;PF00240; | 6.20.50.150; | Ubiquitin family; Eukaryotic ribosomal protein eS31 family | PTM: [Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30. {ECO:0000250|UniProtKB:P62979}.; PTM: [Ubiquitin]: Mono-ADP-ribosylated at the C-terminus by PARP9, a component of the PPAR9-DTX3L complex. ADP-ribosylation requires processing by E1 and E2 enzymes and prevents ubiquitin conjugation to substrates such as histones. {ECO:0000250|UniProtKB:P62979}.; PTM: [Small ribosomal subunit protein eS31]: Monoubiquitinated at Lys-107 and Lys-113 by RNF25 in response to ribosome collisions (ribosome stalling): ubiquitination promotes subsequent activation of RNF14, leading to EEF1A1 ubiquitination and degradation and rescue of stalled ribosomes. Deubiquitination at Lys-113 by USP16 is required for maturation of the 40S ribosomal complex. {ECO:0000250|UniProtKB:P62979}. | SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS31]: Cytoplasm {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:30355441, ECO:0000269|PubMed:30517857, ECO:0000269|PubMed:31246176, ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:31768042, ECO:0000269|PubMed:32286223, ECO:0000269|PubMed:33296660}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62979}.; SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250|UniProtKB:P62979}. Nucleus {ECO:0000250|UniProtKB:P62979}. | null | null | null | null | null | FUNCTION: [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. {ECO:0000250|UniProtKB:P62979}.; FUNCTION: [Small ribosomal subunit protein eS31]: Component of the 40S subunit of the ribosome (PubMed:23873042, PubMed:25601755, PubMed:27863242, PubMed:30517857). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:27863242, PubMed:30517857). During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:23873042, PubMed:25601755, PubMed:27863242, PubMed:30517857). {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:30517857}. | Oryctolagus cuniculus (Rabbit) |
G1SPE9 | GNPAT_RABIT | MDSSSSSNYFSVGSTNPSAVVLLYSKELKKWDEFEDILEERRHVSDLKFAMKCYTPLVYKGITPCKPSDIKNSVLNSEEIHYVIKQLSMESLQSVDVLREEVCEILDEMSHKLRLGAIRFFAFALSKIFKQIFSKVCVNEEGIQKLQRAIQEHPVVLLPSHRSYIDFLMLSFLLYNYDLPVPVIAAGMDFLGMKMIGELLRMSGAFFMRRTFGGNKLYWAVFSEYVKTMLRNGYAPVEFFLEGTRSRSAKTLTPKFGLLSIVMEPFFKREVFDTYLVPISISYDKILEETLYAYELLGVPKPKESTTGLLKARRILSENFGSIYVYFGDPVSLRSLASGRMSRSPYNLVPRYIPQKQSEDMHAFVTEVAYKMQLLQIENLVLSPWPLIVAVLLQNRPSMDFDALLEKTLWLKGLTQAFGGFLIWPDNEPAEEVVQHHILLHSNIASLVKDQVILKLESGDSEVVDGLIFQHITLLTCSTYRNQLLNIFVRPSLVAVALQMTPGFRKEDVYSAFRFLRDVFSDEFIFFPGNTVKDFEEGCYLLCKSETIQMTTRDILVTEKGNAVLEFLIGLFRPFVECYKLLCIYLLKEEEEHFTEKQYLAAVRKFTSQLLNQGASQCYDVLSSDVQKNALAAFVRLGVVEKKKVNNDYIFSVNEPATTKLEEMLGCKIPIGKPATAKL | 2.3.1.42 | null | cerebellum morphogenesis [GO:0021587]; ether lipid biosynthetic process [GO:0008611]; fatty acid metabolic process [GO:0006631]; glycerol-3-phosphate metabolic process [GO:0006072]; glycerophospholipid metabolic process [GO:0006650]; membrane organization [GO:0061024]; paranodal junction assembly [GO:0030913]; phospholipid biosynthetic process [GO:0008654]; synapse assembly [GO:0007416]; triglyceride biosynthetic process [GO:0019432] | mitochondrial membrane [GO:0031966]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; plasma membrane [GO:0005886] | glycerol-3-phosphate O-acyltransferase activity [GO:0004366]; glycerone-phosphate O-acyltransferase activity [GO:0016287] | PF01553;PF19277; | null | GPAT/DAPAT family | null | SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000250|UniProtKB:Q9ES71}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9ES71}; Matrix side {ECO:0000250|UniProtKB:Q9ES71}. Note=Exclusively localized to the lumenal side of the peroxisomal membrane. {ECO:0000250|UniProtKB:Q9ES71}. | CATALYTIC ACTIVITY: Reaction=an acyl-CoA + dihydroxyacetone phosphate = a 1-acylglycerone 3-phosphate + CoA; Xref=Rhea:RHEA:17657, ChEBI:CHEBI:57287, ChEBI:CHEBI:57534, ChEBI:CHEBI:57642, ChEBI:CHEBI:58342; EC=2.3.1.42; Evidence={ECO:0000269|PubMed:9459311}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17658; Evidence={ECO:0000305|PubMed:9459311}; CATALYTIC ACTIVITY: Reaction=dihydroxyacetone phosphate + hexadecanoyl-CoA = 1-hexadecanoylglycerone 3-phosphate + CoA; Xref=Rhea:RHEA:40715, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57642, ChEBI:CHEBI:58303; Evidence={ECO:0000269|PubMed:9459311}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40716; Evidence={ECO:0000305|PubMed:9459311}; | null | PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. {ECO:0000269|PubMed:9459311}. | null | null | FUNCTION: Dihydroxyacetonephosphate acyltransferase catalyzing the first step in the biosynthesis of plasmalogens, a subset of phospholipids that differ from other glycerolipids by having an alkyl chain attached through a vinyl ether linkage at the sn-1 position of the glycerol backbone, and which unique physical properties have an impact on various aspects of cell signaling and membrane biology. {ECO:0000269|PubMed:9459311}. | Oryctolagus cuniculus (Rabbit) |
G1SRW8 | SLN14_RABIT | MEIPKTGVETLYPEFVVEVGRVTFGEENRKKMTNSCLKRTENLNIIKATCALLNSGGGVIKAEIHDKNYNYQCHGLGHDLETSFQKLLPFGSQKYLDYMQQGHELLIFVKSWNPDVSSLLPLRICSLRSNLYQRDVTSAINLSASSALELLREKQHAAQRGRRRLHPPRASNSNLQEEEDMKMLASEVFKKDRLMYKEKLNFTESTHVEFKRFTTKKVVPRIKEMLPHYVSAFANTQGGYLIIGVDDKSKEVFGCKKEKVNPDLLKKEIENCIEKLPTFHFCHEKPKINFITKILNVYQKDVLYGYVCVVQVEPFCCAVFAEAPDSWVMRDNAATRLTAEDWVLMMLDIPSAPCNLVTDSNAHLKSPASSAFRSPVCPTKVLEFKGALQRHLFPVTQKTIQFKPESFCKKLFSDHKGLEDLMKTQTYPYSQGIVVFSRSWAGDVGLRKEDRVLCDALLIALHSPLVLYTVLIDPSWAGGREYAWNVALHLKRKLQSVGGYPGKVGIIPRLIQLAGTWCGPGDGSVHYPQSYQLATEDDMEDLLQALVVVSLCSRSLLSDQLGCEFFNLLIAEQCEVLSQSLQETRELFIHCFPGTRKTALAIKTLEKIRDLFRCRPKEILYVCESDFLRDFVIHQTACLAVTRKTFMQGEFPKIKHIVMDETENFCSKYGDWYSKARSITHPRVRGAGNEDLHHGILWIFLDPFQVRHSDVNGLPPPPAQFPRKTITNGIHCAQEIAKVMKGAMKRITENPPSNMSPHTLALFREAACGEALGAHALPGVCETKADLTVEQIANYVAERCHGLFQCGYLPKDVAILCRREEDRARYKLALLRAMELTETHSATEVVFSQAAGVQGEHIILDSVHQFSGLHRNIVFGLSPEQRLSEEFHQLCFASKAIKHLYLLYERGQVSENYYK | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25996083}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:25996083}; Note=C-terminally truncated SLFN14 endoribonuclease: Requires manganese and magnesium for its endoribonuclease activity. {ECO:0000269|PubMed:25996083}; | cellular response to magnesium ion [GO:0071286]; cellular response to manganese ion [GO:0071287]; mRNA catabolic process [GO:0006402]; platelet maturation [GO:0036345]; rRNA catabolic process [GO:0016075] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ribosome binding [GO:0043022]; RNA endonuclease activity [GO:0004521] | PF17057;PF04326;PF21026; | 3.30.950.30; | null | null | SUBCELLULAR LOCATION: [Protein SLFN14]: Nucleus {ECO:0000250|UniProtKB:P0C7P3}. | null | null | null | null | null | FUNCTION: [Protein SLFN14]: Shows no ribosome-associated and endoribonuclease activities. {ECO:0000269|PubMed:25996083}.; FUNCTION: [C-terminally truncated SLFN14 endoribonuclease]: Displays polysome-associated endoribonuclease activity towards mRNAs and rRNAs (PubMed:25996083). May play a role in RNA surveillance pathways by recognizing stalled ribosomes and triggering endonucleolytic cleavage of aberrant mRNAs (Probable). Cleaves RNAs in a magnesium-, manganese-dependent and ATP-independent manner (PubMed:25996083). Involved in correct maturation of megakaryocytes and especially important for proplatelet extension (By similarity). {ECO:0000250|UniProtKB:P0C7P3, ECO:0000269|PubMed:25996083, ECO:0000305|PubMed:25996083}. | Oryctolagus cuniculus (Rabbit) |
G1SW77 | SERB1_RABIT | MPGHLQEGFGCVVTNRFDQLFDDESDPFEVLKAAENKKKEAGGGGVGGPGAKSAAQAAAQTNSNAAGKQLRKESQKDRKNPLPPNVGVVDKKEETQPPVALKKEGIRRVGRRPDQQLQGEGKIIDRRPERRPPRERRFEKPLEEKGEGGEFSVDRPIIDRPIRGRGGLGRGRGGRGRGMGRGDGFDSRGKREFDRHSGSDRSSFSHYSGLKHEDKRGGSGSHNWGTVKDELTESPKYIQKQISYNCSDLDQSNVTEETPEGEEHPVADTENKENEVEEVKEEGPKEMTLDEWKAIQNKDRAKVEFNIRKPNEGADGQWKKGFVLHKSKSEEAHAEDSVMDHHFRKPANDITSQLEINFGDLGRPGRGGRGGRGGRGRGGRPNRGSRTDKSSASAPDVDDPEAFPALA | null | null | negative regulation of translation [GO:0017148]; PML body organization [GO:0030578]; ribosome hibernation [GO:0141014] | cytosol [GO:0005829]; non-membrane-bounded organelle [GO:0043228]; nucleus [GO:0005634] | mRNA 3'-UTR binding [GO:0003730]; ribosome binding [GO:0043022]; SUMO binding [GO:0032183]; translation elongation factor binding [GO:0061770]; translation repressor activity [GO:0030371] | PF04774;PF16174; | null | SERBP1-HABP4 family | PTM: Phosphorylation by MTOR inhibits SERBP1 and relieves ribosome hibernation. {ECO:0000250|UniProtKB:Q8NC51}. | null | null | null | null | null | null | FUNCTION: Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (PubMed:30355441). Acts via its association with EEF2/eEF2 factor, sequestering EEF2/eEF2 at the A-site of the ribosome and promoting ribosome stabilization and storage in an inactive state (PubMed:30355441). May also play a role in the regulation of mRNA stability: binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay. Seems to play a role in PML-nuclear bodies formation (By similarity). {ECO:0000250|UniProtKB:Q8NC51, ECO:0000269|PubMed:30355441}. | Oryctolagus cuniculus (Rabbit) |
G1T469 | NOD2_RABIT | MCSQEAFQAQRSQLVGLLVSGSLEGFESILDLLLSWEVLSWEDYEGLRLVGQPLSHLARRLLDTVWNKGTWGCQKLIAAVQEAQDSSQCPELHGCWDPHSLHPAQDLQSHRPAIVRRLYSHVEGVLDLALEQGFISQYECDEIRLPIFTSSQRARRLLDLATVKANGLAAFLLQHVQKLPVSLSLPFEAAACKKYMSKLRTIVAAQSRFLSTYDGAENLCLEDIYTENTLEVRTEVGMAGPLHKSPAALGLEELFSPNGHLNEDADTVLVVGEAGSGKSTLLQQVHLLWATGQDFQEFLFVFPFSCRQLQCVARPLSVMTLLFEHCCWPDVGQQDVFQFLLDHPDRILLTFDGFDEFKFKFTDHERHCSPTDPTSVQTLLFNLLQGNLLKNARKVLTSRPDAVSAFLRKYVRTEFNLKGFSEEGIELYLRKCHREPGVADRLIHLLQTTSALHGLCHLPVFSWMVSKCHQELLLQDGGSPKTTTDMYLLILQHFLRHASLPDSASQGLGPSLLQGRLPTLLRLGQLALWGLGMCCYVFSAQQLQAAQVDPDDISLGFLVQAQGVVPGSTAPLEFLHITFQCFLAAFYLVLSTDVPTASLRYLFNCRRPGSSPLSRLLPRLCVQGSEHKESTVAALLQKTEPHNLQITAAFLAGLLSREHRDLLAACQASERSLLRRRACARWCLARSLHKHFRSIPPAVPGEAKSMHAMPGFLWLIRSLYEMQEERLAQEAVRGLNVEHLKLTFCGVGPAECAALAFVLRHLRRPVALQLDHNSVGDIGVEQLLPCLGACKALYLRDNNISDRGICKLIEHALHCEQLQKLALFNNKLTDGCAHSVAQLLACKQNFLALRLGNNHITAEGAQVLAEGLRDNSSLQFLGFWGNKVGDKGAQALAEALSDHQSLKWLSLVGNNIGSVGAQALASMLEKNVALEELCLEENHLQDAGVCSLAEGLKRNSSLKVLKLSNNCITFVGAEALLQALASNDTILEVWLRGNPFSPEEMEALSHRDSRLLL | null | null | adaptive immune response [GO:0002250]; antibacterial innate immune response [GO:0140367]; biosynthetic process of antibacterial peptides active against Gram-positive bacteria [GO:0002815]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to muramyl dipeptide [GO:0071225]; cellular response to peptidoglycan [GO:0071224]; defense response to bacterium [GO:0042742]; detection of bacterium [GO:0016045]; detection of muramyl dipeptide [GO:0032498]; ERK1 and ERK2 cascade [GO:0070371]; establishment of localization in cell [GO:0051649]; host-mediated regulation of intestinal microbiota composition [GO:0048874]; innate immune response in mucosa [GO:0002227]; intestinal stem cell homeostasis [GO:0036335]; JNK cascade [GO:0007254]; maintenance of gastrointestinal epithelium [GO:0030277]; negative regulation of inflammatory response to antigenic stimulus [GO:0002862]; negative regulation of interleukin-12 production [GO:0032695]; negative regulation of interleukin-18 production [GO:0032701]; negative regulation of interleukin-2 production [GO:0032703]; negative regulation of macrophage apoptotic process [GO:2000110]; negative regulation of macrophage cytokine production [GO:0010936]; negative regulation of T cell mediated immunity [GO:0002710]; negative regulation of toll-like receptor 2 signaling pathway [GO:0034136]; negative regulation of tumor necrosis factor production [GO:0032720]; negative regulation of type II interferon production [GO:0032689]; nucleotide-binding oligomerization domain containing 2 signaling pathway [GO:0070431]; phagocytosis [GO:0006909]; positive regulation of B cell activation [GO:0050871]; positive regulation of biosynthetic process of antibacterial peptides active against Gram-positive bacteria [GO:0006965]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cytokine production involved in inflammatory response [GO:1900017]; positive regulation of dendritic cell antigen processing and presentation [GO:0002606]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of humoral immune response mediated by circulating immunoglobulin [GO:0002925]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-17 production [GO:0032740]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of JNK cascade [GO:0046330]; positive regulation of macrophage cytokine production [GO:0060907]; positive regulation of mitophagy [GO:1901526]; positive regulation of monocyte chemotactic protein-1 production [GO:0071639]; positive regulation of nitric-oxide synthase biosynthetic process [GO:0051770]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of Notch signaling pathway [GO:0045747]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phagocytosis [GO:0050766]; positive regulation of protein K63-linked ubiquitination [GO:1902523]; positive regulation of stress-activated MAPK cascade [GO:0032874]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type 2 immune response [GO:0002830]; positive regulation of xenophagy [GO:1904417]; regulation of appetite [GO:0032098]; regulation of neutrophil chemotaxis [GO:0090022]; response to endoplasmic reticulum stress [GO:0034976]; response to exogenous dsRNA [GO:0043330]; response to muramyl dipeptide [GO:0032495]; stress-activated MAPK cascade [GO:0051403]; temperature homeostasis [GO:0001659]; toll-like receptor 2 signaling pathway [GO:0034134]; xenophagy [GO:0098792] | basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extrinsic component of plasma membrane [GO:0019897]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; phagocytic vesicle [GO:0045335]; protein-containing complex [GO:0032991] | actin binding [GO:0003779]; ADP binding [GO:0043531]; ATP binding [GO:0005524]; CARD domain binding [GO:0050700]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; muramyl dipeptide binding [GO:0032500]; pattern recognition receptor activity [GO:0038187]; peptidoglycan binding [GO:0042834]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877]; ubiquitin binding [GO:0043130] | PF00619;PF13516;PF05729;PF17776;PF17779; | 1.10.533.10;3.40.50.300;3.80.10.10; | NOD1-NOD2 family | PTM: Palmitoylated by ZDHHC5; palmitoylation is required for proper recruitment to the bacterial entry site and hence for proper signaling upon cognate peptidoglycan detection. Palmitoylation promotes localization to the cell membrane. Palmitoylation protects from SQSTM1/p62-dependent autophagic degradation. {ECO:0000250|UniProtKB:Q9HC29}.; PTM: Polyubiquitinated by TRIM27, leading to proteasome-mediated degradation. Polyubiquitinated and degraded following muramyl dipeptide (MDP) stimulation, conferring MDP tolerance and preventing septic shock. {ECO:0000250|UniProtKB:Q9HC29}.; PTM: Degraded via selective autophagy following interaction with IRGM. IRGM promotes NOD2-RIPK2 RIPosome recruitment to autophagosome membranes, promoting their SQSTM1/p62-dependent autophagic degradation. {ECO:0000250|UniProtKB:Q9HC29}.; PTM: O-glycosylated by OGT, O-GlcNAcylation increases protein stability. {ECO:0000250|UniProtKB:Q9HC29}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9HC29}; Lipid-anchor {ECO:0000250|UniProtKB:Q9HC29}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9HC29}. Cytoplasm {ECO:0000250|UniProtKB:Q9HC29}. Mitochondrion {ECO:0000250|UniProtKB:Q9HC29}. Note=Palmitoylation promotes localization to the cell membrane, where it detects bacterial invasion at the point of entry. {ECO:0000250|UniProtKB:Q9HC29}. | null | null | null | null | null | FUNCTION: Pattern recognition receptor (PRR) that detects bacterial peptidoglycan fragments and other danger signals and plays an important role in gastrointestinal immunity. Specifically activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan found in every bacterial peptidoglycan type. NOD2 specifically recognizes and binds 6-O-phospho-MDP, the phosphorylated form of MDP, which is generated by NAGK. 6-O-phospho-MDP-binding triggers oligomerization that facilitates the binding and subsequent activation of the proximal adapter receptor-interacting RIPK2. Following recruitment, RIPK2 undergoes 'Met-1'- (linear) and 'Lys-63'-linked polyubiquitination by E3 ubiquitin-protein ligases XIAP, BIRC2, BIRC3 and the LUBAC complex, becoming a scaffolding protein for downstream effectors, triggering activation of the NF-kappa-B and MAP kinases signaling. This in turn leads to the transcriptional activation of hundreds of genes involved in immune response (By similarity). Its ability to detect bacterial MDP plays a central role in maintaining the equilibrium between intestinal microbiota and host immune responses to control inflammation. An imbalance in this relationship results in dysbiosis, whereby pathogenic bacteria prevail on commensals, causing damage in the intestinal epithelial barrier as well as allowing bacterial invasion and inflammation. Acts as a regulator of appetite by sensing MDP in a subset of brain neurons: microbiota-derived MDP reach the brain, where they bind and activate NOD2 in inhibitory hypothalamic neurons, decreasing neuronal activity, thereby regulating satiety and body temperature. NOD2-dependent MDP-sensing of bacterial cell walls in the intestinal epithelial compartment contributes to sustained postnatal growth upon undernutrition (By similarity). Also plays a role in antiviral response by acting as a sensor of single-stranded RNA (ssRNA) from viruses: upon ssRNA-binding, interacts with MAVS, leading to activation of interferon regulatory factor-3/IRF3 and expression of type I interferon. Also acts as a regulator of autophagy in dendritic cells via its interaction with ATG16L1, possibly by recruiting ATG16L1 at the site of bacterial entry (By similarity). NOD2 activation in the small intestine crypt also contributes to intestinal stem cells survival and function: acts by promoting mitophagy via its association with ATG16L1. In addition to its main role in innate immunity, also regulates the adaptive immune system by acting as regulator of helper T-cell and regulatory T-cells (Tregs) (By similarity). Besides recognizing pathogens, also involved in the endoplasmic reticulum stress response: acts by sensing and binding to the cytosolic metabolite sphingosine-1-phosphate generated in response to endoplasmic reticulum stress, initiating an inflammation process that leads to activation of the NF-kappa-B and MAP kinases signaling. May also be involved in NLRP1 activation following activation by MDP, leading to CASP1 activation and IL1B release in macrophages (By similarity). {ECO:0000250|UniProtKB:Q8K3Z0, ECO:0000250|UniProtKB:Q9HC29}. | Oryctolagus cuniculus (Rabbit) |
G1T6D1 | RL23_RABIT | MSKRGRGGSSGAKFRISLGLPVGAVINCADNTGAKNLYIISVKGIKGRLNRLPAAGVGDMVMATVKKGKPELRKKVHPAVVIRQRKSYRRKDGVFLYFEDNAGVIVNNKGEMKGSAITGPVAKECADLWPRIASNAGSIA | null | null | cellular response to actinomycin D [GO:0072717]; G1 to G0 transition [GO:0070314]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of ubiquitin-dependent protein catabolic process [GO:2000059]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of signal transduction by p53 class mediator [GO:1901798]; protein stabilization [GO:0050821]; protein-DNA complex disassembly [GO:0032986]; regulation of G1 to G0 transition [GO:1903450]; translation [GO:0006412] | cytosolic large ribosomal subunit [GO:0022625]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; synapse [GO:0045202] | large ribosomal subunit rRNA binding [GO:0070180]; structural constituent of ribosome [GO:0003735]; transcription coactivator binding [GO:0001223]; ubiquitin ligase inhibitor activity [GO:1990948]; ubiquitin protein ligase binding [GO:0031625] | PF00238; | 2.40.150.20; | Universal ribosomal protein uL14 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:30355441, ECO:0000269|PubMed:30517857, ECO:0000269|PubMed:31246176, ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:31768042, ECO:0000269|PubMed:33296660, ECO:0000269|PubMed:35679869, ECO:0000269|PubMed:36653451}. | null | null | null | null | null | FUNCTION: Component of the large ribosomal subunit (PubMed:26245381, PubMed:27863242, PubMed:30517857). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:26245381, PubMed:27863242, PubMed:30517857). {ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:30517857}. | Oryctolagus cuniculus (Rabbit) |
G1T7U7 | NAAA_RABIT | MQGTGHPVRPVLELLLLLLLLAGVGGSTTASTPGPPLFNVSLDVAPERWLPVLRHYDVELVRAAVAQVIGDRVPKWVLALIEKGALKLERLLPPPFTAEIRGMCDFLNLSLADGLLVNLAYEYSAFCTSIVAQDSRGHVYHGRNLDYPYGSILRKLTVDVQFLKNGQIAFTGTTFIGYVGLWTGQSPHKFTVSGDERDRGWWWENLVAALFLRHSPISWLLRTTLSEAESFEAAVYRLAKTPLIADVYYIVGGTNPREGVVITRNRDGPADIWPLDPLKGVWFLVETNYDHWKPAPEEDDRRTPAIKALNATGQAKLSLETLFQVLSVVPVYNNYTIYTTVMSAASPDKYMTRIRNPS | 3.5.1.23; 3.5.1.60 | null | fatty acid metabolic process [GO:0006631]; lipid catabolic process [GO:0016042]; N-acylethanolamine metabolic process [GO:0070291]; N-acylphosphatidylethanolamine metabolic process [GO:0070292]; sphingosine metabolic process [GO:0006670] | lysosome [GO:0005764]; membrane [GO:0016020] | ceramidase activity [GO:0102121]; fatty acid amide hydrolase activity [GO:0017064]; N-(long-chain-acyl)ethanolamine deacylase activity [GO:0047412]; N-acylsphingosine amidohydrolase activity [GO:0017040] | PF02275;PF15508; | null | Acid ceramidase family | PTM: N-glycosylated (PubMed:30301806). Tunicamycin treatment causes a reduction in specific activity against N-palmitoylethanolamine (By similarity). {ECO:0000250|UniProtKB:Q02083, ECO:0000269|PubMed:30301806}.; PTM: Autoproteolytic cleavage at pH 4.5 gives rise to the alpha and beta subunit (PubMed:30301806). Cleavage gives rise to a conformation change that activates the enzyme. The same catalytic Cys residue mediates the autoproteolytic cleavage and subsequent hydrolysis of lipid substrates (By similarity). {ECO:0000250|UniProtKB:Q02083, ECO:0000269|PubMed:30301806}. | SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q02083}. Membrane {ECO:0000250|UniProtKB:Q02083}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q02083}. | CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoylethanolamine = ethanolamine + hexadecanoate; Xref=Rhea:RHEA:45064, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:57603, ChEBI:CHEBI:71464; Evidence={ECO:0000250|UniProtKB:Q02083}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45065; Evidence={ECO:0000250|UniProtKB:Q02083}; CATALYTIC ACTIVITY: Reaction=H2O + N-(long-chain fatty acyl)ethanolamine = a long-chain fatty acid + ethanolamine; Xref=Rhea:RHEA:17505, ChEBI:CHEBI:15377, ChEBI:CHEBI:15897, ChEBI:CHEBI:57560, ChEBI:CHEBI:57603; EC=3.5.1.60; Evidence={ECO:0000250|UniProtKB:Q02083}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17506; Evidence={ECO:0000250|UniProtKB:Q02083}; CATALYTIC ACTIVITY: Reaction=H2O + N-dodecanoylethanolamine = dodecanoate + ethanolamine; Xref=Rhea:RHEA:45456, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:57603, ChEBI:CHEBI:85263; Evidence={ECO:0000250|UniProtKB:Q02083}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45457; Evidence={ECO:0000250|UniProtKB:Q02083}; CATALYTIC ACTIVITY: Reaction=H2O + N-tetradecanoylethanolamine = ethanolamine + tetradecanoate; Xref=Rhea:RHEA:45452, ChEBI:CHEBI:15377, ChEBI:CHEBI:30807, ChEBI:CHEBI:57603, ChEBI:CHEBI:85262; Evidence={ECO:0000250|UniProtKB:Q02083}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45453; Evidence={ECO:0000250|UniProtKB:Q02083}; CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine; Xref=Rhea:RHEA:20856, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868, ChEBI:CHEBI:52639, ChEBI:CHEBI:57756; EC=3.5.1.23; Evidence={ECO:0000250|UniProtKB:Q02083}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20857; Evidence={ECO:0000250|UniProtKB:Q02083}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoylsphing-4-enine = hexadecanoate + sphing-4-enine; Xref=Rhea:RHEA:38891, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:57756, ChEBI:CHEBI:72959; Evidence={ECO:0000250|UniProtKB:Q02083}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38892; Evidence={ECO:0000250|UniProtKB:Q02083}; CATALYTIC ACTIVITY: Reaction=H2O + N-dodecanoylsphing-4-enine = dodecanoate + sphing-4-enine; Xref=Rhea:RHEA:41291, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:57756, ChEBI:CHEBI:72956; Evidence={ECO:0000250|UniProtKB:Q02083}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41292; Evidence={ECO:0000250|UniProtKB:Q02083}; | null | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000250|UniProtKB:Q02083}. | null | null | FUNCTION: Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine > N-myristoylethanolamine > N-stearoylethanolamine > N-oleoylethanolamine > N-linoleoylethanolamine > N-arachidonoylethanolamine. {ECO:0000250|UniProtKB:Q5KTC7}. | Oryctolagus cuniculus (Rabbit) |
G1TGF1 | TEBP_RABIT | MQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMNNMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE | 5.3.99.3 | null | chaperone-mediated protein complex assembly [GO:0051131]; positive regulation of telomerase activity [GO:0051973]; prostaglandin biosynthetic process [GO:0001516]; protein folding [GO:0006457]; telomerase holoenzyme complex assembly [GO:1905323]; telomere maintenance via telomerase [GO:0007004] | cytosol [GO:0005829]; nucleus [GO:0005634] | DNA polymerase binding [GO:0070182]; Hsp90 protein binding [GO:0051879]; prostaglandin-E synthase activity [GO:0050220]; protein-folding chaperone binding [GO:0051087] | PF04969; | 2.60.40.790; | P23/wos2 family | PTM: Proteolytically cleaved by caspase-7 (CASP7) in response to apoptosis, leading to its inactivation. {ECO:0000250|UniProtKB:Q15185}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3ZBF7}. | CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin E2; Xref=Rhea:RHEA:12893, ChEBI:CHEBI:57405, ChEBI:CHEBI:606564; EC=5.3.99.3; Evidence={ECO:0000250|UniProtKB:Q15185}; | null | PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000250|UniProtKB:Q15185}. | null | null | FUNCTION: Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway. {ECO:0000250|UniProtKB:Q15185}. | Oryctolagus cuniculus (Rabbit) |
G1TLT8 | RSSA_RABIT | MSGALDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVISSRNTGQRAVLKFAAATGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPLTEASYVNLPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKAVTKEEFQGEWTAPAPEFTATQPEVADWSEGVQVPSVPIQQFPTEDWSAQPATEDWSAAPTAQATEWVGTTTEWS | null | null | cytoplasmic translation [GO:0002181]; ribosomal small subunit assembly [GO:0000028] | 90S preribosome [GO:0030686]; cytosolic small ribosomal subunit [GO:0022627]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | laminin binding [GO:0043236]; laminin receptor activity [GO:0005055]; structural constituent of ribosome [GO:0003735]; virus receptor activity [GO:0001618] | PF16122;PF00318; | null | Universal ribosomal protein uS2 family | PTM: Acylated. Acylation may be a prerequisite for conversion of the monomeric 37 kDa laminin receptor precursor (37LRP) to the mature dimeric 67 kDa laminin receptor (67LR), and may provide a mechanism for membrane association. {ECO:0000255|HAMAP-Rule:MF_03016}.; PTM: Cleaved by stromelysin-3 (ST3) at the cell surface. Cleavage by stromelysin-3 may be a mechanism to alter cell-extracellular matrix interactions. {ECO:0000255|HAMAP-Rule:MF_03016}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_03016}. Cytoplasm {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:32286223, ECO:0000269|PubMed:33296660, ECO:0000269|PubMed:35679869, ECO:0000269|PubMed:35709277, ECO:0000269|PubMed:35822879, ECO:0000269|PubMed:36653451}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03016}. Note=67LR is found at the surface of the plasma membrane, with its C-terminal laminin-binding domain accessible to extracellular ligands. 37LRP is found at the cell surface, in the cytoplasm and in the nucleus. Co-localizes with PPP1R16B in the cell membrane. {ECO:0000255|HAMAP-Rule:MF_03016}. | null | null | null | null | null | FUNCTION: Required for the assembly and/or stability of the 40S ribosomal subunit (PubMed:23873042, PubMed:25601755). Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits (PubMed:23873042, PubMed:25601755). Also functions as a cell surface receptor for laminin (By similarity). Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways (By similarity). May play a role in cell fate determination and tissue morphogenesis (By similarity). Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate of PPP1CA (By similarity). {ECO:0000255|HAMAP-Rule:MF_03016, ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755}. | Oryctolagus cuniculus (Rabbit) |
G1TM55 | RS6_RABIT | MKLNISFPATGCQKLIEVDDERKLRTFYEKRMATEVAADALGEEWKGYVVRISGGNDKQGFPMKQGVLTHGRVRLLLSKGHSCYRPRRTGERKRKSVRGCIVDANLSVLNLVIVKKGEKDIPGLTDTTVPRRLGPKRASRIRKLFNLSKEDDVRQYVVRKPLNKEGKKPRTKAPKIQRLVTPRVLQHKRRRIALKKQRTKKNKEEAAEYAKLLAKRMKEAKEKRQEQIAKRRRLSSLRASTSKSESSQK | null | null | activation-induced cell death of T cells [GO:0006924]; cytoplasmic translation [GO:0002181]; erythrocyte development [GO:0048821]; G1/S transition of mitotic cell cycle [GO:0000082]; gastrulation [GO:0007369]; glucose homeostasis [GO:0042593]; mammalian oogenesis stage [GO:0022605]; negative regulation of apoptotic process [GO:0043066]; placenta development [GO:0001890]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell population proliferation [GO:0008284]; ribosomal small subunit biogenesis [GO:0042274]; rRNA processing [GO:0006364]; T cell differentiation in thymus [GO:0033077]; T cell proliferation involved in immune response [GO:0002309]; TOR signaling [GO:0031929] | cell body [GO:0044297]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosolic ribosome [GO:0022626]; cytosolic small ribosomal subunit [GO:0022627]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]; small-subunit processome [GO:0032040] | protein kinase binding [GO:0019901]; structural constituent of ribosome [GO:0003735] | PF01092; | 1.20.5.2650; | Eukaryotic ribosomal protein eS6 family | PTM: Ribosomal protein S6 is the major substrate of protein kinases in eukaryote ribosomes. The phosphorylation is stimulated by growth factors, tumor promoting agents, and mitogens. It is dephosphorylated at growth arrest. Phosphorylated at Ser-235 and Ser-236 by RPS6KA1 and RPS6KA3; phosphorylation at these sites facilitates the assembly of the pre-initiation complex. {ECO:0000250|UniProtKB:P62753}.; PTM: Specifically hydroxylated (with R stereochemistry) at C-3 of Arg-137 by KDM8. {ECO:0000250|UniProtKB:P62753}.; PTM: Mono-ADP-ribosylation at Glu-35 by PARP16 inhibits polysome assembly and mRNA loading, thereby inhibiting protein translation. {ECO:0000250|UniProtKB:P62753}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:30355441, ECO:0000269|PubMed:30517857, ECO:0000269|PubMed:31246176, ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:31768042, ECO:0000269|PubMed:32286223, ECO:0000269|PubMed:33296660, ECO:0000269|PubMed:35679869, ECO:0000269|PubMed:36653451}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62753}. | null | null | null | null | null | FUNCTION: Component of the 40S small ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857). Plays an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857). During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857). {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:30517857}. | Oryctolagus cuniculus (Rabbit) |
G1TNM3 | RS3_RABIT | 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]; positive regulation of protein-containing complex assembly [GO:0031334]; regulation of translation [GO:0006417]; translation [GO:0006412] | cytosolic ribosome [GO:0022626]; cytosolic small ribosomal subunit [GO:0022627]; mitochondrial inner membrane [GO:0005743]; nucleolus [GO:0005730]; spindle [GO:0005819]; synapse [GO:0045202] | 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:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:31246176, ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:31768042, ECO:0000269|PubMed:32286223, ECO:0000269|PubMed:33296660, ECO:0000269|PubMed:35679869, ECO:0000269|PubMed:35709277, ECO:0000269|PubMed:35822879, ECO:0000269|PubMed:36653451}. 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 (By similarity). 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 (By similarity). {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 (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242). Has endonuclease activity and plays a role in repair of damaged DNA (By similarity). Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (By similarity). Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (By similarity). Has also been shown to bind with similar affinity to intact and damaged DNA (By similarity). Stimulates the N-glycosylase activity of the base excision protein OGG1 (By similarity). Enhances the uracil excision activity of UNG1 (By similarity). Also stimulates the cleavage of the phosphodiester backbone by APEX1 (By similarity). When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (By similarity). Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (By similarity). 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 (By similarity). Represses its own translation by binding to its cognate mRNA (By similarity). Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (By similarity). Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (By similarity). Involved in induction of apoptosis through its role in activation of CASP8 (By similarity). 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 (By similarity). Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (By similarity). {ECO:0000250|UniProtKB:P23396, ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242}. | Oryctolagus cuniculus (Rabbit) |
G1TZ76 | RS27_RABIT | MPLAKDLLHPSPEEEKRKHKKKRLVQSPNSYFMDVKCPGCYKITTVFSHAQTVVLCVGCSTVLCQPTGGKARLTEGCSFRRKQH | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P42677}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P42677}; | ribosomal small subunit assembly [GO:0000028]; translation [GO:0006412] | cytosolic ribosome [GO:0022626]; cytosolic small ribosomal subunit [GO:0022627]; nucleolus [GO:0005730] | metal ion binding [GO:0046872]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF01667; | 2.20.25.100; | Eukaryotic ribosomal protein eS27 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:31246176, ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:31768042, ECO:0000269|PubMed:33296660, ECO:0000269|PubMed:35679869, ECO:0000269|PubMed:35822879, ECO:0000269|PubMed:36653451}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P42677}. | null | null | null | null | null | FUNCTION: Component of the small ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242). Required for proper rRNA processing and maturation of 18S rRNAs (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242). During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (By similarity). {ECO:0000250|UniProtKB:P42677, ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242}. | Oryctolagus cuniculus (Rabbit) |
G1TZA0 | PLM_RABIT | MAYLHHTLLVCMGLLAMANAEAPQEQDPFTYDYQSLRIGGLIIAGILFILGILIILKRGAWERFDTARRTGEPDEEEGTFRSSIRRLSTRRR | null | null | negative regulation of protein glutathionylation [GO:0010734]; potassium ion transport [GO:0006813]; regulation of monoatomic ion transport [GO:0043269]; sodium ion transport [GO:0006814] | apical plasma membrane [GO:0016324]; caveola [GO:0005901]; intercalated disc [GO:0014704]; T-tubule [GO:0030315] | sodium channel regulator activity [GO:0017080] | PF02038; | 1.20.5.780; | FXYD family | PTM: Major plasma membrane substrate for cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) in several different tissues. Phosphorylated in response to insulin and adrenergic stimulation. Phosphorylation at Ser-88 stimulates sodium/potassium-transporting ATPase activity while the unphosphorylated form inhibits sodium/potassium-transporting ATPase activity. Phosphorylation increases tetramerization, decreases binding to ATP1A1 and reduces inhibition of ATP1A1 activity. Phosphorylation at Ser-83 leads to greatly reduced interaction with ATP1A1, ATP1A2 and ATP1A3. May be phosphorylated by DMPK. {ECO:0000250|UniProtKB:O00168, ECO:0000250|UniProtKB:O08589, ECO:0000250|UniProtKB:P56513}.; PTM: Palmitoylation increases half-life and stability and is enhanced upon phosphorylation at Ser-88 by PKA. {ECO:0000250|UniProtKB:O00168}.; PTM: Glutathionylated. {ECO:0000269|PubMed:21454534}. | SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P56513}; Single-pass type I membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O08589}; Single-pass type I membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:O08589}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O08589}. Note=Detected in the apical cell membrane in brain. In myocytes, localizes to sarcolemma, t-tubules and intercalated disks. {ECO:0000250|UniProtKB:O08589}. | null | null | null | null | null | FUNCTION: Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell. Inhibits NKA activity in its unphosphorylated state and stimulates activity when phosphorylated. Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1. Contributes to female sexual development by maintaining the excitability of neurons which secrete gonadotropin-releasing hormone. {ECO:0000250|UniProtKB:O08589, ECO:0000250|UniProtKB:P56513, ECO:0000250|UniProtKB:Q9Z239}. | Oryctolagus cuniculus (Rabbit) |
G1UB11 | ERG5_CANAL | MNSTEVDNLPFQQQLTSFVELAVAKATGSPITTLFTIIFLILSYDQLSYQINKGSIAGPRFKFYPIIGPFLESLDPKFEEYKAKWDSGELSCVSIFHKFVVIASSRDLARKILSSPKYVKPCVVDVAIKILRPTNWVFLDGKQHTDYRRSLNGLFSSKALEIYIPVQEKYMDIYLERFCKYDGPREFFPEFRELLCALSLRTFCGDYITEDQIALVADNYYRVTAALELVNFPIIIPYTKTWYGKKIADDTMKIFENCAAMAKKHINENNGTPKCVMDEWIHLMKEAREKHSEDPDSKLLVREFSNREISEAIFTFLFASQDASSSLACWLFQIVADRPDIVAKIREEQLRVRNNNPDVRLSLDLINEMTYTNNVVKESLRYRPPVLMVPYVVKKSFPVTESYTAPKGAMIIPTLYPALHDPEVYDEPDSFIPERWENASGDMYKRNWLVFGTGPHVCLGKNYVLMLFTGMLGKFVMNSDMIHHKTDLSEEIKVFATIFPKDDLILEWKKRDPLKSL | 1.14.19.41 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | cellular response to starvation [GO:0009267]; ergosterol biosynthetic process [GO:0006696]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; filamentous growth of a population of unicellular organisms in response to starvation [GO:0036170]; sterol metabolic process [GO:0016125] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886] | C-22 sterol desaturase activity [GO:0000249]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity [GO:0016491] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=5-dehydroepisterol + H(+) + NADPH + O2 = ergosta-5,7,22,24(28)-tetraen-3beta-ol + 2 H2O + NADP(+); Xref=Rhea:RHEA:33467, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18249, ChEBI:CHEBI:52972, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.19.41; Evidence={ECO:0000250|UniProtKB:P54781}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33468; Evidence={ECO:0000250|UniProtKB:P54781}; | null | PATHWAY: Steroid metabolism; ergosterol biosynthesis; ergosterol from zymosterol: step 4/5. {ECO:0000305|PubMed:20547793}. | null | null | FUNCTION: C-22 sterol desaturase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (Probable). ERG5 converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable). {ECO:0000250|UniProtKB:P54781, ECO:0000305, ECO:0000305|PubMed:20547793}. | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
G1UB61 | CDC11_CANAL | MNYSTENVSSAALRKRKTLKKSINFSIMIIGESGSGRSTLINTLCGGNSIVPTSSTATQDPFTKKLTLRHENVELEDNEGHKISLNIIDTPNFANSINCDDDFKIIVDFIRHQFDEVLLEESRVKRNPRFKDGRIHVLIYMINPTGHGLSDIDVKFLQHVNNLVNIIPIISKADSLTPKELKLNKELILEDLNNYGINFYKFNEYDYEQDYIDEEIIEYNKYLNSLIPFAIIGANEYRSNPNGSEDEDDILKLRILNKDFKPIDIDNAEINDFTILKNVLLVTHLNEFKDITHDSIYENYRTEALSGKQFQYVNKDSAKQEISESDYLMKEEQIKLEEERLRKFEERVHQDLINKRKELLERENELKEIEKRLLAEGLKFDENGDVVKVHEEESSENEVKVI | null | null | actomyosin contractile ring assembly [GO:0000915]; cellular bud neck septin ring organization [GO:0032186]; chitin localization [GO:0006033]; chlamydospore formation [GO:0001410]; cytoskeleton-dependent cytokinesis [GO:0061640]; division septum assembly [GO:0000917]; growth of unicellular organism as a thread of attached cells [GO:0070783]; hyphal growth [GO:0030448]; maintenance of cell polarity [GO:0030011]; nuclear migration [GO:0007097]; positive regulation of protein phosphorylation [GO:0001934]; protein localization [GO:0008104]; protein localization to bud neck [GO:0097271]; septin ring assembly [GO:0000921] | ascospore wall [GO:0005619]; cell division site [GO:0032153]; cellular bud neck [GO:0005935]; cellular bud neck septin ring [GO:0000144]; cellular bud neck septin structure [GO:0000399]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; Gin4 complex [GO:1990317]; hyphal septin ring [GO:0032168]; hyphal tip [GO:0001411]; mating projection base [GO:0001400]; medial cortex septin ring [GO:0036391]; meiotic spindle [GO:0072687]; microtubule cytoskeleton [GO:0015630]; mitotic actomyosin contractile ring, proximal layer [GO:0120104]; mitotic septin complex [GO:0032151]; prospore membrane [GO:0005628]; septin complex [GO:0031105]; septin filament array [GO:0032160]; septin ring [GO:0005940]; spindle microtubule [GO:0005876] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]; structural constituent of cytoskeleton [GO:0005200] | PF00735; | 3.40.50.300; | TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family | PTM: Hyphal induction causes immediate phosphorylation at Ser-395 by GIN4 and at Ser-394 by CDC28-CCN1. GIN4 phosphorylation at Ser-395 primes CDC11 for further phosphorylation by CDC28-CCN1. CDC28-HGC1 then maintains CDC11 phosphorylation throughout hyphal growth. Ser-4 is also phosphorylated in yeast cells but not hyphal cells. {ECO:0000269|PubMed:17765684}.; PTM: Met-1 is acetylated. {ECO:0000269|PubMed:17765684}. | SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:11454197, ECO:0000269|PubMed:12181342, ECO:0000269|PubMed:19915075, ECO:0000269|PubMed:22687514}. Note=Localizes to a tight ring at the bud and pseudohyphae necks and as a more diffuse array in emerging germ tubes of hyphae. | null | null | null | null | null | FUNCTION: Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinase GIN4. Septins are also involved in cell morphogenesis, chlamydospores morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization, and spore wall formation. CDC11 is required for the correct localization of SEC3 at bud tips and bud necks. Plays a key role in invasive growth and virulence. {ECO:0000269|PubMed:11454197, ECO:0000269|PubMed:12181342, ECO:0000269|PubMed:12819094, ECO:0000269|PubMed:16002645, ECO:0000269|PubMed:17504812, ECO:0000269|PubMed:17765684}. | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
G1UB63 | CSA1_CANAL | MLPSIVISIVLASFVSAESSITEAPTTTAEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSICSVAGVWDPYWMVPANVQSSLSAAATAVASSSEQPVETSSEPAGSSQSVESSQPAETSSSEPAETSSSEPAETSSETSSEQPASSEPAETSSEESSTITSAPSTPEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGTSICSVAGVWDPYWMVPANVQSSLSAAATAVPSSSEQSVETSSESAESSQSVESSQPAETSSEQPSETSSETSSQQLSSITSAPDSSATSSSSTTSTFIRTASINGFADKLYDQLPECAKPCMFQNTGITPCPYWDAGCLCVMPQFAGAIGSCVADSCKGQDIVSVTSLGTSVCSVAGVNAPYWMLPASVKSSLSVAATAVPTSDSASETASQEPSETSSEQPSETASQQPAETSSEESSTITSAPSTPEDNPYTIYPSVAKTASINGFADRIYDQLPECAKPCMFQNTGVTPCPYWDTGCLCIMPTFAGAIGSCIAEKCKGQDVVSATSLGSSICSVAGVWDPYWMLPANVQSSLNAAATAVATSDSASEVASASESASQVPQETSAASSQSANNSVASAAPSNSSVSAAPSSNSSGVPAAPSNNSSGASVVPSQSANNSSASAAPSNNSSSAISESVAPSSYGNSTIAQPSTSTKSDAASITGPITTDKVITNESGIVFTSTVIITHVSEYCDQTSAAAVQSSACEEQSSAKSEQASASSEQVKVITSVVWCESSIQSIESVKTSAEAAHKTEVIASCASELSSLSSAKSEAMKTVSSLVEVQKSAVAKQTSLAAVQSSAASVQLSAAHAQKSSEAVEVAQTAVAEASKAGDEISTEIVNITKTVSSGKETGVSQATVAANTHSVAIANMANTKFASTMSLLVASFVFVGLFI | null | null | intracellular iron ion homeostasis [GO:0006879]; single-species biofilm formation on inanimate substrate [GO:0044011] | cell surface [GO:0009986]; cellular bud [GO:0005933]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; hyphal cell wall [GO:0030446]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF05730; | null | RBT5 family | PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. {ECO:0000305}. | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10652105, ECO:0000269|PubMed:19555771, ECO:0000269|PubMed:23243062, ECO:0000269|PubMed:23728625}. Membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. | null | null | null | null | null | FUNCTION: Heme-binding protein involved in heme-iron utilization. The ability to acquire iron from host tissues is a major virulence factor of pathogenic microorganisms. Required for biofilm formation. {ECO:0000269|PubMed:15306022, ECO:0000269|PubMed:17042757, ECO:0000269|PubMed:21205162}. | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
G1UB67 | EED1_CANAL | MERRQFNTSNIRNGTGRPRKTPRSKLYMVYPPLSGEDSTNPEPEEGSSQENNPTEPSSSQSNSVQNQDQSEDQSQLPQQESNTQQESNTQQESNTPSPRASNTSTETPAPLSPIQPGIRNIPSGLLLPQEKVGRLMGYPFYRDFNFTLNPERYQKLIYVFQILKNAARNHRNGASLLRKYFSLARRSKRTTDMFVTTIEEMRKRSLENSRKRELEEAQEREESNKRQHTESSAEPNAESSTESTTESNAESGAEPNAEPSAESTTESNVESGAEPNAESGAESGAEPTAESNAELKQRIWEILSYRLEQSNNETNNTGESNSTSQQPRQLPNNELIMNIRVLQKNTHAKPVLGRIKFTPDKSNKTSLTGSQNKVHSTNTQQSQKHPQQILTNSETHKPQQYSAQSQQQMVHQTNSHEPSQKRSPPPQQQQQKQPSVPTSSVPLQVSQKQNQQQQELPLPPQPQPQQRTAPSAVKQQQSMQMQPPPQQQQQQQRHQPLQQSPPTMPLQQQPVPPVQQVQTVPPPSSQPQTQLSQQQQQQQQAQLQMQVPRCYQYQNRPPSQQRQYSQTPQYNQPPPQQKVYALPPQQVYAPPPRQVYAQPTIACKQQYPQQLYEQAPQEGSSYQHHYQQVQQRQNQQPYMQSAPTYQQPHVQTPKSTRSNKQEKQRLPKGQEQVPKATRTMFEAFTGSNIAVEKLRQRTLDNGREPERLRTEYVNVLSSPERAAEKSTSRSKQSSNQKPVVKQQSSFPPPIKHQQTQEQQGNILPPVSQLLAIQSSTVTSRGSNASGAVMGSGNTQRVASRSFTNTFVAEAVVNNANNRGGPVPPTGPETNTRGGRASTRSSGRPRGNRSTQRAEGNVTGRVARSTDGSQSQNSGKASKISNIRNLLN | null | null | cell adhesion involved in single-species biofilm formation [GO:0043709]; development of symbiont in host [GO:0044114]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms [GO:0044182]; positive regulation of cell adhesion involved in single-species biofilm formation [GO:1900189]; positive regulation of filamentous growth of a population of unicellular organisms [GO:1900430]; quorum sensing [GO:0009372]; single-species biofilm formation on inanimate substrate [GO:0044011] | nucleus [GO:0005634] | null | null | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Transcriptional regulator involved in extension of germ tubes into elongated hyphae and maintenance of filamentous growth. Regulates expression of UME6. Acts in a pathway that regulates maintenance of hyphal growth by repressing hyphal-to-yeast transition and allows dissemination within host epithelial tissues. Dispensable for invasion into both host oral epithelial cells and enterocytes, but required for epithelial damage. {ECO:0000269|PubMed:17645752, ECO:0000269|PubMed:21407800, ECO:0000269|PubMed:21512583}. | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
G1UBC2 | PGA47_CANAL | MKVSQILPLAGAISVASGFWIPDFSNKQNSNSYPGQYKGKGGYQDDCGDDYKKGYKSKTYSKVKPITSTDCTTPIQPTGTTTGYTKDVVESTSYTTDTAYTTTVITVTKCDGGSCSHTAVTTGVTIITVTTNDVITEYTTYCPLTSTPATESTPATESTPATESTPATESTPATESTPATESTPCTTSTETTPATESTPATESTPATESTPATESTPATESTPATESTPATESTPATESTPCTTSTETTPATESTASTETASSTPVESTVIVPSTTVITVSSCYEDKCSVSSVTTGVVTISSEETIYTTYCPITSSITIPVPNTSTPAAPGTPVESQPVIPGTETTPAAPGTPVESQPVIPGTETTPAAPGTPVESQPATTPVAPGTETTPAAPGTPVESQPATTPVAPGTETTPAAPGTPVESQPVIPGTETTPAAPGTPVESQPATTPVAPGTETTPAAPGTPVESQPVIPGTETTPAAPGTPVESQPATTPVAPGTETTPAAPGTPVESQPVIPGTETTPAAPGTPGTEATPVTTQPVSVLSTSQVVTASGEFSTVTAHSTSIVASCPEGGCVPEGQQTETSPSVPTNGPEVEASSSVLSIPVSSVTTSTIASSSETSVPPAQVSTFEGSGSALKKPYYGLAVAALVYFM | null | null | adhesion of symbiont to host [GO:0044406]; cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609]; single-species biofilm formation in or on host organism [GO:0044407]; single-species biofilm formation on inanimate substrate [GO:0044011] | extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; side of membrane [GO:0098552] | cell adhesion molecule binding [GO:0050839] | PF13928; | null | PGA18 family | PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:17416898, ECO:0000269|PubMed:18375812}. Membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. | null | null | null | null | null | FUNCTION: Cell wall protein which mediates cell-cell and cell-substrate adhesion. Required for biofilm formation and plays a role in virulence. {ECO:0000269|PubMed:14665461, ECO:0000269|PubMed:16321041, ECO:0000269|PubMed:17416898, ECO:0000269|PubMed:18375812, ECO:0000269|PubMed:20709785}. | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
G1UBD1 | PMOB_METCA | MKTIKDRIAKWSAIGLLSAVAATAFYAPSASAHGEKSQAAFMRMRTIHWYDLSWSKEKVKINETVEIKGKFHVFEGWPETVDEPDVAFLNVGMPGPVFIRKESYIGGQLVPRSVRLEIGKTYDFRVVLKARRPGDWHVHTMMNVQGGGPIIGPGKWITVEGSMSEFRNPVTTLTGQTVDLENYNEGNTYFWHAFWFAIGVAWIGYWSRRPIFIPRLLMVDAGRADELVSATDRKVAMGFLAATILIVVMAMSSANSKYPITIPLQAGTMRGMKPLELPAPTVSVKVEDATYRVPGRAMRMKLTITNHGNSPIRLGEFYTASVRFLDSDVYKDTTGYPEDLLAEDGLSVSDNSPLAPGETRTVDVTASDAAWEVYRLSDIIYDPDSRFAGLLFFFDATGNRQVVQIDAPLIPSFM | 1.14.18.3 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:12379148, ECO:0000269|PubMed:15674245, ECO:0000269|PubMed:22013879}; Note=Binds 3 copper ions per subunit. Two of these (copper ion 1 and 3) form a binuclear cluster. {ECO:0000269|PubMed:12379148, ECO:0000269|PubMed:15674245, ECO:0000269|PubMed:22013879}; | null | membrane [GO:0016020] | metal ion binding [GO:0046872]; monooxygenase activity [GO:0004497] | PF04744; | 1.10.287.710;2.60.120.570;2.60.40.1580; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12379148, ECO:0000269|PubMed:15674245}; Multi-pass membrane protein {ECO:0000269|PubMed:12379148, ECO:0000269|PubMed:15674245}. Note=Located in intracellular membranes. | CATALYTIC ACTIVITY: Reaction=a quinol + methane + O2 = a quinone + H2O + methanol; Xref=Rhea:RHEA:30355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16183, ChEBI:CHEBI:17790, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.14.18.3; Evidence={ECO:0000269|PubMed:7646068}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=24.2 nmol/min/mg enzyme (with NADH as reductant) {ECO:0000269|PubMed:7646068}; Vmax=4.4 nmol/min/mg enzyme (with decyl-plastoquinol as reductant) {ECO:0000269|PubMed:7646068}; Vmax=2.9 nmol/min/mg enzyme (with duroquinol as reductant) {ECO:0000269|PubMed:7646068}; Note=Kinetic parameters have been established with the pMMO heteromeric complex.; | null | null | null | FUNCTION: Methane monooxygenase is responsible for the initial oxygenation of methane to methanol in methanotrophs. At least in vitro, specific quinols can replace NADH as reductants. {ECO:0000269|PubMed:10376840, ECO:0000269|PubMed:17002291, ECO:0000269|PubMed:20410881}. | Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) |
G1UH28 | CHIT_PUNGR | MAKTLPFSRALLLSLSILLVARAISAGDIAIYWGQNGGEGTLASTCDTGRYAYVIVSFVTTFGNFRAPVVNLAGHCDPAAGTCTGLSDEIRSCQGKDIKVLMSIGGGAGDYSLVSEADADNFADYLWNNFLGGQSSSRPLGDAVLDGIDFDIELGTTTFYDTLARALSSRSTQAAKVYLTAAPQCPHPDSHLDAALNTGLFDNVWIQFYNNPLAQCQYSSGNTNDILSSWNTWTSSTTAGKIFLGLPAAPEAAGSGYIPPDVLTGQILPQIKTSAKYGGVMLYSKFYDTTYSTTIKDQV | 3.2.1.14 | null | chitin catabolic process [GO:0006032]; polysaccharide catabolic process [GO:0000272]; seed germination [GO:0009845]; seedling development [GO:0090351] | amyloplast [GO:0009501]; extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; chitinase activity [GO:0004568] | PF00704; | 3.20.20.80; | Glycosyl hydrolase 18 family, Chitinase class III subfamily | null | SUBCELLULAR LOCATION: Plastid, amyloplast {ECO:0000269|PubMed:21790816, ECO:0000269|PubMed:22112454}. Note=Localizes to stroma in amyloplasts of the embryonic cells of the seed. {ECO:0000269|PubMed:21790816, ECO:0000269|PubMed:22112454}. | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000255|PROSITE-ProRule:PRU10053, ECO:0000269|PubMed:21790816}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat/KM is 0.119 M(-1)sec(-1) for native protein, 0.130 M(-1)sec(-1) for native protein with 10 mM Ca(2+) and 0.116 M(-1)sec(-1) for EDTA-treated protein, using 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside (4-MU(GlcNAc)(3)) as substrate at pH 4.5 and 37 degrees Celsius. {ECO:0000269|PubMed:21790816}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 2.5 and 5.0. Removal of Ca(2+) from the protein by EDTA treatment narrows the pH range to 2.5-3.5. {ECO:0000269|PubMed:21790816}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is approximately 45 degrees Celsius. Removal of Ca(2+) from the protein by EDTA treatment decreases the optimum temperature to 35 degrees Celsius. {ECO:0000269|PubMed:21790816}; | FUNCTION: Hydrolyzes chitin. Probable calcium storage protein of the seeds. Binds calcium ions with high capacity and low affinity. Involved in seed germination. {ECO:0000269|PubMed:21790816}. | Punica granatum (Pomegranate) |
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