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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O09000 | NCOA3_MOUSE | MSGLGESSLDPLAAESRKRKLPCDAPGQGLVYSGEKWRREQESKYIEELAELISANLSDIDNFNVKPDKCAILKETVRQIRQIKEQGKTISSDDDVQKADVSSTGQGVIDKDSLGPLLLQALDGFLFVVNRDGNIVFVSENVTQYLQYKQEDLVNTSVYSILHEPRRKDFLNTYQNPQLMEFLGLMRTRDKKAPYILIVRMLMKTHDILEDVNASPETRQRYETMQCFALSQPRAMLEEGEDLQCCMICVARRVTAPFPSSPESFITRHDLSGKVVNIDTNSLRSSMRPGFEDIIRRCIQRFFSLNDGQSWSQKRHYQEAYVHGHAETPVYRFSLADGTIVSAQTKSKLFRNPVTNDRHGFISTHFLQREQNGYRPNPIPQDKGIRPPAAGCGVSMSPNQNVQMMGSRTYGVPDPSNTGQMGGARYGASSSVASLTPGQSLQSPSSYQNSSYGLSMSSPPHGSPGLGPNQQNIMISPRNRGSPKMASHQFSPAAGAHSPMGPSGNTGSHSFSSSSLSALQAISEGVGTSLLSTLSSPGPKLDNSPNMNISQPSKVSGQDSKSPLGLYCEQNPVESSVCQSNSRDPQVKKESKESSGEVSETPRGPLESKGHKKLLQLLTCSSDDRGHSSLTNSPLDPNCKDSSVSVTSPSGVSSSTSGTVSSTSNVHGSLLQEKHRILHKLLQNGNSPAEVAKITAEATGKDTSSTASCGEGTTRQEQLSPKKKENNALLRYLLDRDDPSDVLAKELQPQADSGDSKLSQCSCSTNPSSGQEKDPKIKTETNDEVSGDLDNLDAILGDLTSSDFYNNPTNGGHPGAKQQMFAGPSSLGLRSPQPVQSVRPPYNRAVSLDSPVSVGSGPPVKNVSAFPGLPKQPILAGNPRMMDSQENYGANMGPNRNVPVNPTSSPGDWGLANSRASRMEPLASSPLGRTGADYSATLPRPAMGGSVPTLPLRSNRLPGARPSLQQQQQQQQQQQQQQQQQQQQQQQMLQMRTGEIPMGMGVNPYSPAVQSNQPGSWPEGMLSMEQGPHGSQNRPLLRNSLDDLLGPPSNAEGQSDERALLDQLHTFLSNTDATGLEEIDRALGIPELVNQGQALESKQDVFQGQEAAVMMDQKAALYGQTYPAQGPPLQGGFNLQGQSPSFNSMMGQISQQGSFPLQGMHPRAGLVRPRTNTPKQLRMQLQQRLQGQQFLNQSRQALEMKMENPAGTAVMRPMMPQAFFNAQMAAQQKRELMSHHLQQQRMAMMMSQPQPQAFSPPPNVTASPSMDGVLAGSAMPQAPPQQFPYPANYGMGQPPEPAFGRGSSPPSAMMSSRMGPSQNAMVQHPQPTPMYQPSDMKGWPSGNLARNGSFPQQQFAPQGNPAAYNMVHMNSSGGHLGQMAMTPMPMSGMPMGPDQKYC | 2.3.1.48 | null | cell dedifferentiation [GO:0043697]; cellular response to hormone stimulus [GO:0032870]; labyrinthine layer morphogenesis [GO:0060713]; mammary gland branching involved in thelarche [GO:0060744]; multicellular organism growth [GO:0035264]; negative regulation of apoptotic process [GO:0043066]; negative regulation of stem cell differentiation [GO:2000737]; positive regulation of cell growth [GO:0030307]; positive regulation of gene expression [GO:0010628]; positive regulation of intracellular estrogen receptor signaling pathway [GO:0033148]; positive regulation of intracellular steroid hormone receptor signaling pathway [GO:0033145]; positive regulation of stem cell population maintenance [GO:1902459]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of stem cell division [GO:2000035]; regulation of stem cell population maintenance [GO:2000036]; regulation of stem cell proliferation [GO:0072091] | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; RNA polymerase II transcription regulator complex [GO:0090575] | chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; histone acetyltransferase activity [GO:0004402]; nuclear androgen receptor binding [GO:0050681]; nuclear estrogen receptor binding [GO:0030331]; nuclear receptor binding [GO:0016922]; nuclear receptor coactivator activity [GO:0030374]; peroxisome proliferator activated receptor binding [GO:0042975]; protein dimerization activity [GO:0046983]; protein-containing complex binding [GO:0044877]; RNA polymerase II complex binding [GO:0000993]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; transcription coactivator activity [GO:0003713] | PF07469;PF16279;PF16665;PF08815;PF00989;PF14598;PF08832; | 6.10.140.410;4.10.280.10;3.30.450.20; | SRC/p160 nuclear receptor coactivator family | PTM: Acetylated by CREBBP. Acetylation occurs in the RID domain, and disrupts the interaction with nuclear receptors and regulates its function (By similarity). {ECO:0000250}.; PTM: Methylated by CARM1. {ECO:0000269|PubMed:11701890}.; PTM: Phosphorylated by IKK complex. Regulated its function (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. Note=Mainly cytoplasmic and weakly nuclear. Upon TNF activation and subsequent phosphorylation, it translocates from the cytoplasm to the nucleus (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; | null | null | null | null | FUNCTION: Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, probably via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit (By similarity). {ECO:0000250, ECO:0000269|PubMed:10823921}. | Mus musculus (Mouse) |
O09005 | DEGS1_MOUSE | MGSRVSREEFEWVYTDQPHAARRKEILAKYPEIKSLMKPDHNLIWIVAMMLLVQLASFYLVKDLDWKWVIFWSYVFGSCLNHSMTLAIHEISHNFPFGHHKALWNRWFGMFANLSLGVPYSISFKRYHMDHHRYLGADKIDVDIPTDFEGWFFCTTFRKFVWVILQPLFYAFRPLFINPKPITYLEIINTVIQITFDIIIYYVFGVKSLVYMLAATLLGLGLHPISGHFIAEHYMFLKGHETYSYYGPLNLLTFNVGYHNEHHDFPNVPGKNLPMVRKIASEYYDDLPHYNSWIKVLYDFVTDDTISPYSRMKRPPKGNEILE | 1.14.19.17; 5.2.1.- | null | ceramide biosynthetic process [GO:0046513]; fatty acid biosynthetic process [GO:0006633]; myelin maintenance [GO:0043217]; positive regulation of apoptotic process [GO:0043065] | endoplasmic reticulum membrane [GO:0005789]; mitochondrial membrane [GO:0031966] | retinol isomerase activity [GO:0050251]; sphingolipid delta-4 desaturase activity [GO:0042284] | PF00487;PF08557; | null | Fatty acid desaturase type 1 family, DEGS subfamily | PTM: Myristoylation can target the enzyme to the mitochondria leading to an increase in ceramide levels. {ECO:0000250|UniProtKB:O15121}. | SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250|UniProtKB:O15121}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O15121}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O15121}. | CATALYTIC ACTIVITY: Reaction=an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an N-acylsphing-4-enine + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46544, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:31488, ChEBI:CHEBI:52639; EC=1.14.19.17; Evidence={ECO:0000269|PubMed:11937514}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46545; Evidence={ECO:0000305|PubMed:11937514}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol = 11-cis-retinol; Xref=Rhea:RHEA:19141, ChEBI:CHEBI:16302, ChEBI:CHEBI:17336; Evidence={ECO:0000269|PubMed:23143414}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19142; Evidence={ECO:0000305|PubMed:23143414}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19143; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol = 9-cis-retinol; Xref=Rhea:RHEA:55348, ChEBI:CHEBI:17336, ChEBI:CHEBI:78272; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55349; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol = 13-cis-retinol; Xref=Rhea:RHEA:55352, ChEBI:CHEBI:17336, ChEBI:CHEBI:45479; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55353; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; CATALYTIC ACTIVITY: Reaction=11-cis-retinol = 13-cis-retinol; Xref=Rhea:RHEA:55356, ChEBI:CHEBI:16302, ChEBI:CHEBI:45479; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55357; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; CATALYTIC ACTIVITY: Reaction=11-cis-retinol = 9-cis-retinol; Xref=Rhea:RHEA:55360, ChEBI:CHEBI:16302, ChEBI:CHEBI:78272; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55361; Evidence={ECO:0000250|UniProtKB:Q5F3C1}; | null | null | null | null | FUNCTION: Has sphingolipid-delta-4-desaturase activity. Converts D-erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine). Catalyzes the equilibrium isomerization of retinols (By similarity). {ECO:0000250|UniProtKB:Q5F3C1, ECO:0000269|PubMed:11937514}. | Mus musculus (Mouse) |
O09008 | MFNG_MOUSE | MHCRLFRGMAGALFTLLCVGLLSLRYHSSLSQRMIQGALRLNQRNPGPLELQLGDIFIAVKTTWAFHRSRLDLLLDTWVSRIRQQTFIFTDSPDERLQERLGPHLVVTNCSAEHSHPALSCKMAAEFDAFLVSGLRWFCHVDDDNYVNPKALLQLLKTFPQDRDVYVGKPSLNRPIHASELQSKNRTKLVRFWFATGGAGFCINRQLALKMVPWASGSHFVDTSALIRLPDDCTVGYIIECKLGGRLQPSPLFHSHLETLQLLGAAQLPEQVTLSYGVFEGKLNVIKLPGPFSHEEDPSRFRSLHCLLYPDTPWCPLLAAP | 2.4.1.222 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16221665, ECO:0000269|PubMed:16964258}; Note=Has some activity with cobalt, magnesium and calcium, but not zinc. {ECO:0000269|PubMed:16221665}; | blastocyst formation [GO:0001825]; marginal zone B cell differentiation [GO:0002315]; pattern specification process [GO:0007389]; positive regulation of Notch signaling pathway [GO:0045747]; regulation of Notch signaling pathway [GO:0008593] | Golgi membrane [GO:0000139] | metal ion binding [GO:0046872]; O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity [GO:0033829] | PF02434; | 3.90.550.50; | Glycosyltransferase 31 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70531, Rhea:RHEA-COMP:17922, Rhea:RHEA-COMP:17923, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:189631, ChEBI:CHEBI:189634; EC=2.4.1.222; Evidence={ECO:0000269|PubMed:10935626, ECO:0000269|PubMed:16221665}; CATALYTIC ACTIVITY: Reaction=3-O-(alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70511, Rhea:RHEA-COMP:17919, Rhea:RHEA-COMP:17920, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:189632, ChEBI:CHEBI:189633; EC=2.4.1.222; Evidence={ECO:0000269|PubMed:10935626, ECO:0000269|PubMed:16221665}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=196 uM for UDP-N-acetyl-alpha-D-glucosamine {ECO:0000269|PubMed:16221665}; Vmax=3.3 nmol/min/mg enzyme {ECO:0000269|PubMed:16221665}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. {ECO:0000269|PubMed:16221665}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:16221665}; | FUNCTION: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules (PubMed:10935626). Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1 (PubMed:10935626, PubMed:28089369). {ECO:0000269|PubMed:10935626, ECO:0000269|PubMed:28089369}. | Mus musculus (Mouse) |
O09009 | RFNG_MOUSE | MSRARRVLCRACLALAAVLAVLLLLPLPLPLPLPRAPAPDPDRVPTRSLTLEGDRLQPDDVFIAVKTTRKNHGPRLRLLLRTWISRAPRQTFIFTDGDDPELQMLAGGRMINTNCSAVRTRQALCCKMSVEYDKFLESGRKWFCHVDDDNYVNPKSLLHLLSTFSSNQDIYLGRPSLDHPIEATERVQGGGTSNTVKFWFATGGAGFCLSRGLALKMSPWASLGSFMSTAERVRLPDDCTVGYIVEGLLGARLLHSPLFHSHLENLQRLPSGAILQQVTLSYGGPENPHNVVNVAGSFNIQQDPTRFQSVHCLLYPDTHWCPMKNRVEGAFQ | 2.4.1.222 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16221665}; Note=Has some activity with cobalt but not with magnesium, calcium and zinc. {ECO:0000269|PubMed:16221665}; | cell differentiation [GO:0030154]; negative regulation of Notch signaling pathway [GO:0045746]; nervous system development [GO:0007399]; pattern specification process [GO:0007389]; positive regulation of Notch signaling pathway [GO:0045747]; regulation of Notch signaling pathway [GO:0008593] | Golgi membrane [GO:0000139] | metal ion binding [GO:0046872]; O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity [GO:0033829] | PF02434; | 3.90.550.50; | Glycosyltransferase 31 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70531, Rhea:RHEA-COMP:17922, Rhea:RHEA-COMP:17923, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:189631, ChEBI:CHEBI:189634; EC=2.4.1.222; Evidence={ECO:0000269|PubMed:16221665}; CATALYTIC ACTIVITY: Reaction=3-O-(alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70511, Rhea:RHEA-COMP:17919, Rhea:RHEA-COMP:17920, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:189632, ChEBI:CHEBI:189633; EC=2.4.1.222; Evidence={ECO:0000269|PubMed:16221665}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=53.6 uM for UDP-N-acetyl-alpha-D-glucosamine {ECO:0000269|PubMed:16221665}; Vmax=1.6 nmol/min/mg enzyme {ECO:0000269|PubMed:16221665}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:16221665}; | FUNCTION: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in enhancement of NOTCH1 activation by DLL1 and JAG1 (PubMed:28089369). May be involved in limb formation and in neurogenesis (By similarity). {ECO:0000250|UniProtKB:O12972, ECO:0000250|UniProtKB:Q9R1U9, ECO:0000269|PubMed:28089369}. | Mus musculus (Mouse) |
O09010 | LFNG_MOUSE | MLQRCGRRLLLALVGALLACLLVLTADPPPTPMPAERGRRALRSLAGSSGGAPASGSRAAVDPGVLTREVHSLSEYFSLLTRARRDADPPPGVASRQGDGHPRPPAEVLSPRDVFIAVKTTRKFHRARLDLLFETWISRHKEMTFIFTDGEDEALAKLTGNVVLTNCSSAHSRQALSCKMAVEYDRFIESGKKWFCHVDDDNYVNLRALLRLLASYPHTQDVYIGKPSLDRPIQATERISEHKVRPVHFWFATGGAGFCISRGLALKMGPWASGGHFMSTAERIRLPDDCTIGYIVEALLGVPLIRSGLFHSHLENLQQVPTTELHEQVTLSYGMFENKRNAVHIKGPFSVEADPSRFRSVHCHLYPDTPWCPRSAIF | 2.4.1.222 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16221665}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:16221665}; Note=Manganese is the most effective. Can also use cobalt with lower efficiency. Has some activity with magnesium and calcium, but not zinc. {ECO:0000269|PubMed:16221665}; | compartment pattern specification [GO:0007386]; marginal zone B cell differentiation [GO:0002315]; negative regulation of Notch signaling pathway involved in somitogenesis [GO:1902367]; ovarian follicle development [GO:0001541]; positive regulation of meiotic cell cycle [GO:0051446]; positive regulation of Notch signaling pathway [GO:0045747]; regulation of Notch signaling pathway [GO:0008593]; regulation of somitogenesis [GO:0014807]; somitogenesis [GO:0001756]; T cell differentiation [GO:0030217] | Golgi membrane [GO:0000139] | metal ion binding [GO:0046872]; O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity [GO:0033829] | PF02434; | 3.90.550.50; | Glycosyltransferase 31 family | PTM: A soluble form may be derived from the membrane form by proteolytic processing. | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:16385447}. Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70531, Rhea:RHEA-COMP:17922, Rhea:RHEA-COMP:17923, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:189631, ChEBI:CHEBI:189634; EC=2.4.1.222; Evidence={ECO:0000269|PubMed:10935626, ECO:0000269|PubMed:16221665}; CATALYTIC ACTIVITY: Reaction=3-O-(alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70511, Rhea:RHEA-COMP:17919, Rhea:RHEA-COMP:17920, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:189632, ChEBI:CHEBI:189633; EC=2.4.1.222; Evidence={ECO:0000269|PubMed:10935626, ECO:0000269|PubMed:16221665}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=78 uM for UDP-N-acetyl-alpha-D-glucosamine {ECO:0000269|PubMed:16221665}; Vmax=20 nmol/min/mg enzyme {ECO:0000269|PubMed:16221665}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. {ECO:0000269|PubMed:16221665}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:16221665}; | FUNCTION: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules (PubMed:10935626). Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1 (PubMed:16385447, PubMed:28089369). Decreases the binding of JAG1 to NOTCH2 but not that of DLL1 (By similarity). Essential mediator of somite segmentation and patterning. During somite boundary formation, it restricts Notch activity in the presomitic mesoderm to a boundary-forming territory in the posterior half of the prospective somite. In this region, Notch function activates a set of genes that are involved in boundary formation and in anterior-posterior somite identity (PubMed:10330372). Ectopically expressed in the thymus, Lfgn inhibits Notch signaling which results in inhibition of T-cell commitment and promotes B-cell development in lymphoid progenitors (PubMed:11520458). May play a role in boundary formation of the enamel knot (PubMed:12167404). {ECO:0000250|UniProtKB:Q8NES3, ECO:0000269|PubMed:10330372, ECO:0000269|PubMed:10935626, ECO:0000269|PubMed:11520458, ECO:0000269|PubMed:12167404, ECO:0000269|PubMed:16385447, ECO:0000269|PubMed:28089369}. | Mus musculus (Mouse) |
O09012 | PEX5_MOUSE | MAMRELVEGECGGANPLMKLATHFTQDKALRQEGLRPGPWPPGASAAETVSKPLGVGTEDELVSEFLQDQNATLVSRAPQTFKMDDLLAEMQEIEQSNFRQAPQRAPGVADLALSENWAQEFLAAGDAVDVAQDYNETDWSQEFIAEVTDPLSVSPARWAEEYLEQSEEKLWLGDQEGSSTADRWYDEYHPEEDLQHTASDFVSKVDDPKLANSEFLKFVRQIGEGQVSLESAAGSGGAQAEQWAAEFIQQQGTSEAWVDQFTRPGNKIAALQVEFERAKSAIESDVDFWDKLQAELEEMAKRDAEAHPWLSDYDDLTSASYDKGYQFEEENPLRDHPQPFEEGLHRLEEGDLPNAVLLFEAAVQQDPKHMEAWQYLGTTQAENEQELLAISALRRCLELKPDNRTALMALAVSFTNESLQRQACETLRDWLRYSPAYAHLVAPGEEGATGAGPSKRILGSLLSDSLFLEVKDLFLAAVRLDPTSIDPDVQCGLGVLFNLSGEYDKAVDCFTAALSVRPNDYLMWNKLGATLANGNQSEEAVAAYRRALELQPGYIRSRYNLGISCINLGAHREAVEHFLEALNMQRKSRGPRGEGGAMSENIWSTLRLALSMLGQSDAYGAADARDLSALLAMFGLPQ | null | null | cell development [GO:0048468]; cellular lipid metabolic process [GO:0044255]; cellular response to reactive oxygen species [GO:0034614]; cerebral cortex cell migration [GO:0021795]; cerebral cortex neuron differentiation [GO:0021895]; endoplasmic reticulum organization [GO:0007029]; fatty acid beta-oxidation [GO:0006635]; mitochondrial membrane organization [GO:0007006]; mitochondrion organization [GO:0007005]; negative regulation of protein-containing complex assembly [GO:0031333]; neuromuscular process [GO:0050905]; neuron migration [GO:0001764]; peroxisome organization [GO:0007031]; pexophagy [GO:0000425]; positive regulation of multicellular organism growth [GO:0040018]; protein import into peroxisome matrix [GO:0016558]; protein import into peroxisome matrix, docking [GO:0016560]; protein import into peroxisome matrix, receptor recycling [GO:0016562]; protein import into peroxisome matrix, substrate release [GO:0044721]; protein import into peroxisome membrane [GO:0045046]; protein targeting to peroxisome [GO:0006625]; very long-chain fatty acid metabolic process [GO:0000038] | cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; protein-containing complex [GO:0032991] | peroxisome matrix targeting signal-1 binding [GO:0005052]; peroxisome membrane targeting sequence binding [GO:0033328]; peroxisome targeting sequence binding [GO:0000268]; protein carrier chaperone [GO:0140597]; small GTPase binding [GO:0031267] | PF13432;PF13181; | 1.25.40.10; | Peroxisomal targeting signal receptor family | PTM: Monoubiquitinated at Cys-11 by PEX2 during PEX5 passage through the retrotranslocation channel (By similarity). Cys-11 monoubiquitination acts as a recognition signal for the PEX1-PEX6 complex and is required for PEX5 extraction and export from peroxisomes. Monoubiquitination at Cys-11 is removed by USP9X in the cytosol, resetting PEX5 for a subsequent import cycle (By similarity). When PEX5 recycling is compromised, polyubiquitinated by PEX10 during its passage through the retrotranslocation channel, leading to its degradation (By similarity). Monoubiquitination at Lys-472 by TRIM37 promotes its stability by preventing its polyubiquitination and degradation by the proteasome. Ubiquitination at Lys-527 is not mediated by the PEX2-PEX10-PEX12 ligase complex and is not related to PEX5 recycling. Monoubiquitinated at Lys-210 by PEX2 following phosphorylation by ATM in response to starvation or reactive oxygen species (ROS), leading to PEX5 recognition by p62/SQSTM1 and induction of pexophagy (By similarity). {ECO:0000250|UniProtKB:P35056, ECO:0000250|UniProtKB:P50542}.; PTM: Phosphorylated at Ser-141 by ATM in response to reactive oxygen species (ROS), promoting monoubiquitination at Lys-210 and induction of pexophagy. {ECO:0000250|UniProtKB:P50542}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P50542}. Peroxisome matrix {ECO:0000250|UniProtKB:P50542}. Note=Cycles between the cytosol and the peroxisome matrix (By similarity). Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the docking complex, composed of PEX13 and PEX14, leading to translocation into the peroxisome matrix along with cargo proteins. Export and recycling to the cytosol is initiated by binding to the PEX2-PEX10-PEX12 ligase complex via its unstructured N-terminus that inserts into the ligase pore and emerges in the cytosol (By similarity). Cys-11 of PEX5 is then monoubiquitinated, promoting its extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex (By similarity). Extraction is accompanied by unfolding of the TPR repeats and release of bound cargo in the peroxisome matrix. The TPR repeats refold in the cytosol and ubiquitination is removed by deubiquitinating enzymes, resetting PEX5 for a subsequent import cycle (By similarity). {ECO:0000250|UniProtKB:A0A1L8FDW4, ECO:0000250|UniProtKB:P50542}. | null | null | null | null | null | FUNCTION: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14 docking complex along with cargo proteins. PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle. {ECO:0000250|UniProtKB:P50542}.; FUNCTION: [Isoform 1]: In addition to promoting peroxisomal translocation of proteins containing a PTS1 peroxisomal targeting signal, mediates peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal via its interaction with PEX7. Interaction with PEX7 only takes place when PEX7 is associated with cargo proteins containing a PTS2 peroxisomal targeting signal. PEX7 along with PTS2-containing cargo proteins are then translocated through the PEX13-PEX14 docking complex together with PEX5. {ECO:0000250|UniProtKB:P50542}.; FUNCTION: [Isoform 2]: Does not mediate translocation of peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal. {ECO:0000250|UniProtKB:P50542}. | Mus musculus (Mouse) |
O09014 | S15A4_RAT | MEGERAPLLGSRRAAAAAGVFAGRRAACGAVLLAELLERAAFYGVTANLVLFLNGAPFNWEGAQASQALLLFMGLTYLGSPFGGWLADARLGRARAILLSLALYLLGMLAFPLLAAPRSRSFLCGDPHPELVRNCSAPFPNGTAVCPDAAARRCAPATFAGLVLVGLGVATVKANITPFGADQVKDRGPEATRRFFNWFYWSINLGAILSLGGIAYIQQNVSFLTGYLIPTVCVAIAFLVFLCGQSVFITKPPDGSAFTDMFRILTYSCCSQRGGQRRSGEGLGVFQQSSKHSLFDSCKMSRGGPFTEDKVEDVKALVKIVPVFLALIPYWTVYFQMQTTYVLQSLHLKIPEISSITTTHHTLPAAWLTMFDAVLILLLIPLKDKLVDPVLRRHGLLPSSLKRIAVGMFFVTCSAFAAGILESKRLDLVKEKTINQTIGGVVYHAADLPIWWQIPQYVLIGISEIFASIAGLEFAYSAAPKSMQSAIMGLFFFFSGIGSFVGSGLLALVSLKAIGWMSSHTDFGNINSCHLHYYFFLLAAIQGATLLLFLIVSVKYDRQRARTDGGTASTRT | null | null | dipeptide import across plasma membrane [GO:0140206]; histidine transport [GO:0015817]; innate immune response [GO:0045087]; L-histidine transmembrane export from vacuole [GO:0089708]; mast cell homeostasis [GO:0033023]; peptidoglycan transport [GO:0015835]; positive regulation of innate immune response [GO:0045089]; positive regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway [GO:0070430]; positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway [GO:0070434]; positive regulation of toll-like receptor 7 signaling pathway [GO:0034157]; positive regulation of toll-like receptor 8 signaling pathway [GO:0034161]; positive regulation of toll-like receptor 9 signaling pathway [GO:0034165]; protein transport [GO:0015031]; regulation of isotype switching to IgG isotypes [GO:0048302]; regulation of nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0070424] | early endosome membrane [GO:0031901]; endolysosome membrane [GO:0036020]; endosome membrane [GO:0010008]; lysosomal membrane [GO:0005765]; membrane [GO:0016020] | dipeptide transmembrane transporter activity [GO:0071916]; L-histidine transmembrane transporter activity [GO:0005290]; peptide:proton symporter activity [GO:0015333]; peptidoglycan transmembrane transporter activity [GO:0015647] | PF00854; | 1.20.1250.20; | Major facilitator superfamily, Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family | null | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8N697}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q8N697}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q91W98}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=n H(+)(out) + L-histidine(out) = n H(+)(in) + L-histidine(in); Xref=Rhea:RHEA:76379, ChEBI:CHEBI:15378, ChEBI:CHEBI:57595; Evidence={ECO:0000269|PubMed:9092568}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76380; Evidence={ECO:0000305|PubMed:9092568}; CATALYTIC ACTIVITY: Reaction=n H(+)(out) + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate(out) = n H(+)(in) + L-alanyl-gamma-D-glutamyl-meso-diaminoheptanedioate(in); Xref=Rhea:RHEA:64412, ChEBI:CHEBI:15378, ChEBI:CHEBI:61401; Evidence={ECO:0000250|UniProtKB:Q8N697}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64413; Evidence={ECO:0000250|UniProtKB:Q8N697}; CATALYTIC ACTIVITY: Reaction=glycylglycylglycine(out) + n H(+)(out) = glycylglycylglycine(in) + n H(+)(in); Xref=Rhea:RHEA:76391, ChEBI:CHEBI:15378, ChEBI:CHEBI:195214; Evidence={ECO:0000250|UniProtKB:Q8N697}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76392; Evidence={ECO:0000250|UniProtKB:Q8N697}; CATALYTIC ACTIVITY: Reaction=n H(+)(out) + N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine(out) = n H(+)(in) + N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine(in); Xref=Rhea:RHEA:76371, ChEBI:CHEBI:15378, ChEBI:CHEBI:155830; Evidence={ECO:0000250|UniProtKB:Q8N697}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76372; Evidence={ECO:0000250|UniProtKB:Q8N697}; CATALYTIC ACTIVITY: Reaction=carnosine(out) + n H(+)(out) = carnosine(in) + n H(+)(in); Xref=Rhea:RHEA:76383, ChEBI:CHEBI:15378, ChEBI:CHEBI:57485; Evidence={ECO:0000250|UniProtKB:Q8N697}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76384; Evidence={ECO:0000250|UniProtKB:Q8N697}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17 uM for histidine (at pH 5.5) {ECO:0000269|PubMed:9092568}; | null | null | null | FUNCTION: Proton-coupled amino-acid transporter that mediates the transmembrane transport of L-histidine and some di- and tripeptides from inside the lysosome to the cytosol, and plays a key role in innate immune response (PubMed:9092568). Able to transport a variety of di- and tripeptides, including carnosine and some peptidoglycans (By similarity). Transporter activity is pH-dependent and maximized in the acidic lysosomal environment (PubMed:9092568). Involved in the detection of microbial pathogens by toll-like receptors (TLRs) and NOD-like receptors (NLRs), probably by mediating transport of bacterial peptidoglycans across the endolysosomal membrane: catalyzes the transport of certain bacterial peptidoglycans, such as muramyl dipeptide (MDP), the NOD2 ligand, and L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate (tri-DAP), the NOD1 ligand. Required for TLR7, TLR8 and TLR9-mediated type I interferon (IFN-I) productions in plasmacytoid dendritic cells (pDCs). Independently of its transporter activity, also promotes the recruitment of innate immune adapter TASL to endolysosome downstream of TLR7, TLR8 and TLR9: TASL recruitment leads to the specific recruitment and activation of IRF5 (By similarity). Required for isotype class switch recombination to IgG2c isotype in response to TLR9 stimulation. Required for mast cell secretory-granule homeostasis by limiting mast cell functions and inflammatory responses (By similarity). {ECO:0000250|UniProtKB:Q8N697, ECO:0000250|UniProtKB:Q91W98, ECO:0000269|PubMed:9092568}. | Rattus norvegicus (Rat) |
O09017 | NR2F6_RAT | MAMVTGGWGGPGGDTNGVDKAGGSYPRATEDDSASPPGATSDAEPGDEERPGLQVDCVVCGDKSSGKHYGVFTCEGCKSFFKRTIRRNLSYTCRSNRDCQIDQHHRNQCQYCRLKKCFRVGMRKEAVQPGPIPHALPGPAACSPPGAAGVEPFAGPPVSELIAQLLRAEPYPAAGRFGGGGAVLGIDNVCELAARLLFSTVEWARHAPFFPELPAADQVGLLRLSWSELFVLNAAQAPVPLHTAPLLAAAGLHAGPMAAERAVAFMDQVRAFQEQVDKLGRLQVDAAEYGCLKAIALFTPDACGLSDPAHVESLQEKAQVALTEYVRAQYPSQPQRFGRLLLRLPALRAVPASLISQLFFMRLVGKTPIETLIRDMLLSGSTFNWPYGSG | null | null | cell differentiation [GO:0030154]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; entrainment of circadian clock by photoperiod [GO:0043153]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron development [GO:0048666] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]; zinc ion binding [GO:0008270] | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Transcription factor predominantly involved in transcriptional repression. Binds to promoter/enhancer response elements that contain the imperfect 5'-AGGTCA-3' direct or inverted repeats with various spacings which are also recognized by other nuclear hormone receptors. Involved in modulation of hormonal responses. Represses transcriptional activity of the lutropin-choriogonadotropic hormone receptor/LHCGR gene, the renin/REN gene and the oxytocin-neurophysin/OXT gene. Represses the triiodothyronine-dependent and -independent transcriptional activity of the thyroid hormone receptor gene in a cell type-specific manner. The corepressing function towards thyroid hormone receptor beta/THRB involves at least in part the inhibition of THRB binding to triiodothyronine response elements (TREs) by NR2F6. Inhibits NFATC transcription factor DNA binding and subsequently its transcriptional activity. Acts as transcriptional repressor of IL-17 expression in Th-17 differentiated CD4(+) T cells and may be involved in induction and/or maintenance of peripheral immunological tolerance and autoimmunity. Involved in development of forebrain circadian clock; is required early in the development of the locus coeruleus (LC) (By similarity). {ECO:0000250, ECO:0000269|PubMed:9343308}. | Rattus norvegicus (Rat) |
O09018 | COT2_RAT | MAMVVSTWRDPQDEVPGSQGSQASQAPPVPGPPPGAPHTPQTPGQGGPASTPAQTAAGSQGGPGGPGSDKQQQQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLSYTCRANRNCPIDQHHRNQCQYCRLKKCLKVGMRREAVQRGRMPPTQPTHGQFALTNGDPLNCHSYLSGYISLLLRAEPYPTSRFGSQCMQPNNIMGIENICELAARMLFSAVEWARNIPFFPDLQITDQVALLRLTWSELFVLNAAQCSMPLHVAPLLAAAGLHASPMSADRVVAFMDHIRIFQEQVEKLKALHVDSAEYSCLKAIVLFTSDACGLSDVAHVESLQEKSQCALEEYVRSQYPNQPTRFGKLLLRLPSLRTVSSSVIEQLFFVRLVGKTPIETLIRDMLLSGSSFNWPYMAIQ | null | null | anterior/posterior pattern specification [GO:0009952]; blood vessel morphogenesis [GO:0048514]; cell differentiation [GO:0030154]; female gonad development [GO:0008585]; fertilization [GO:0009566]; forebrain development [GO:0030900]; in utero embryonic development [GO:0001701]; interneuron migration [GO:1904936]; lymph vessel development [GO:0001945]; lymphatic endothelial cell fate commitment [GO:0060838]; maternal placenta development [GO:0001893]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron migration [GO:0001764]; placenta blood vessel development [GO:0060674]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of systemic arterial blood pressure [GO:0003084]; positive regulation of transcription by RNA polymerase II [GO:0045944]; radial pattern formation [GO:0009956]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response to estradiol [GO:0032355]; skeletal muscle tissue development [GO:0007519]; trophoblast giant cell differentiation [GO:0060707] | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; nuclear receptor activity [GO:0004879]; protein homodimerization activity [GO:0042803]; retinoic acid binding [GO:0001972]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270] | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR2 subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Ligand-activated transcription factor. Activated by high concentrations of 9-cis-retinoic acid and all-trans-retinoic acid, but not by dexamethasone, cortisol or progesterone (in vitro). Regulation of the apolipoprotein A-I gene transcription. Binds to DNA site A. May be required to establish ovary identity during early gonad development. {ECO:0000250|UniProtKB:P24468}. | Rattus norvegicus (Rat) |
O09027 | ACKR2_RAT | MPTIASPLPLATTGPENGSSIYDYDYLDDVTVLVCSKDEVLSFGRVFLPVVYSLIFVLGLAGNLLLLVVLLHSVPQRRRMIELYLLNLAVSNLLFVVTMPFWAISVAWHWVFGSFLCKVVSTLYSINFYCGIFFITCMSLDKYLEIVHAQPLHRPKTRFRNLLLIVMVWITALAVSVPEMVFVKVHQTLDGVWHCYADFGGHATIWKLYLRFQMNLLGFLFPLLAMIFFYSRIGCVLVRLRPPGQGRALRMAAALVVVFFLLWFPYNLTLFLHSLLDLHVFGNCKISHRLDYMLQVTESLAFSHCCFTPVLYAFSSHSFRQYLKAVLSVVLRRHQAPGTAHAPPCSHSESSRVTAQEDVVSMNDLGERQADISLNKGEIGNN | null | null | calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; immune response [GO:0006955]; inflammatory response [GO:0006954]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; signal transduction [GO:0007165] | actin filament [GO:0005884]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037] | C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; chemokine receptor activity [GO:0004950]; scavenger receptor activity [GO:0005044] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Atypical chemokine receptor subfamily | PTM: Phosphorylated on serine residues in the C-terminal cytoplasmic tail. {ECO:0000250}. | SUBCELLULAR LOCATION: Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Cell membrane; Multi-pass membrane protein. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via clathrin-coated pits. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines including CCL2, CCL3, CCL3L1, CCL4, CCL5, CCL7, CCL8, CCL11, CCL13, CCL17, CCL22, CCL23, CCL24, SCYA2/MCP-1, SCY3/MIP-1-alpha, SCYA5/RANTES and SCYA7/MCP-3. Upon active ligand stimulation, activates a beta-arrestin 1 (ARRB1)-dependent, G protein-independent signaling pathway that results in the phosphorylation of the actin-binding protein cofilin (CFL1) through a RAC1-PAK1-LIMK1 signaling pathway. Activation of this pathway results in up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. By scavenging chemokines in tissues, on the surfaces of lymphatic vessels, and in placenta, plays an essential role in the resolution (termination) of the inflammatory response and in the regulation of adaptive immune responses. Plays a major role in the immune silencing of macrophages during the resolution of inflammation. Acts as a regulator of inflammatory leukocyte interactions with lymphatic endothelial cells (LECs) and is required for immature/mature dendritic cells discrimination by LECs. | Rattus norvegicus (Rat) |
O09028 | GBRP_RAT | MSYSLYLAFVCLNLLAQRMCIQGNQFNVEVSRSDKLSLPGFENLTAGYNKFLRPNFGGDPVRIALTLDIASISSISESNMDYTATIYLRQRWTDPRLVFEGNKSFTLDARLVEFLWVPDTYIVESKKSFLHEVTVGNRLIRLFSNGTVLYALRITTTVTCNMDLSKYPMDTQTCKLQLESWGYDGNDVEFSWLRGNDSVRGLENLRLAQYTIQQYFTLVTVSQQETGNYTRLVLQFELRRNVLYFILETYVPSTFLVVLSWVSFWISLESVPARTCIGVTTVLSMTTLMIGSRTSLPNTNCFIKAIDVYLGICFSFVFGALLEYAVAHYSSLQQMAVKDRGPAKDSEEVNITNIINSSISSFKRKISFASIEISGDNVNYSDLTMKASDKFKFVFREKIGRIIDYFTIQNPSNVDRYSKLLFPLIFMLANVFYWAYYMYF | null | null | chemical synaptic transmission [GO:0007268]; chloride transmembrane transport [GO:1902476]; nervous system process [GO:0050877]; regulation of membrane potential [GO:0042391]; signal transduction [GO:0007165] | chloride channel complex [GO:0034707]; GABA-A receptor complex [GO:1902711]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | chloride channel activity [GO:0005254]; extracellular ligand-gated monoatomic ion channel activity [GO:0005230]; GABA-A receptor activity [GO:0004890]; neurotransmitter receptor activity [GO:0030594] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily, GABRP sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:17003036}; Multi-pass membrane protein {ECO:0000255}. Note=Located on the apical plasma membrane of alveolar epithelial type II cells. {ECO:0000269|PubMed:17003036}. | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:17003036}; | null | null | null | null | FUNCTION: Pi subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA) (PubMed:17003036). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain GABA active binding site(s) located at the alpha and beta subunit interfaces (By similarity). When activated by GABA, GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (PubMed:17003036). Pi-containing GABAARs are mostly located in peripheral tissues (PubMed:17003036). In the uterus, pi subunits modulate uterus contraction by altering the sensitivity of GABAARs to pregnanolone (By similarity). In the lungs, pi-containing GABAARs contribute to pulmonary fluid transport via luminal secretion of chloride (PubMed:17003036). {ECO:0000250|UniProtKB:O00591, ECO:0000250|UniProtKB:P47870, ECO:0000269|PubMed:17003036}. | Rattus norvegicus (Rat) |
O09032 | ELAV4_RAT | MEWNGLKMIISTMEPQVSNGPTSNTSNGPSSNNRNCPSPMQTGAATDDSKTNLIVNYLPQNMTQEEFRSLFGSIGEIESCKLVRDKITGQSLGYGFVNYIDPKDAEKAINTLNGLRLQTKTIKVSYARPSSASIRDANLYVSGLPKTMTQKELEQLFSQYGRIITSRILVDQVTGVSRGVGFIRFDKRIEAEEAIKGLNGQKPSGATEPITVKFANNPSQKSSQALLSQLYQSPNRRYPGPLHHQAQRFRLDNLLNMAYGVKRLMSGPVPPSACPPRFSPITIDGMTSLVGMNIPGHTGTGWCIFVYNLSPDSDESVLWQLFGPFGAVNNVKVIRDFNTNKCKGFGFVTMTNYDEAAMAIASLNGYRLGDRVLQVSFKTNKAHKS | null | null | 3'-UTR-mediated mRNA stabilization [GO:0070935]; associative learning [GO:0008306]; cellular response to nerve growth factor stimulus [GO:1990090]; cerebral cortex neuron differentiation [GO:0021895]; dendrite morphogenesis [GO:0048813]; learning [GO:0007612]; locomotory behavior [GO:0007626]; mRNA processing [GO:0006397]; nervous system development [GO:0007399]; neuron differentiation [GO:0030182]; positive regulation of 3'-UTR-mediated mRNA stabilization [GO:1905870]; positive regulation of dendrite development [GO:1900006]; regeneration [GO:0031099]; regulation of mRNA stability [GO:0043488]; regulation of translation at postsynapse [GO:0140245]; response to cocaine [GO:0042220]; response to endoplasmic reticulum stress [GO:0034976]; RNA processing [GO:0006396]; RNA splicing [GO:0008380] | apical dendrite [GO:0097440]; axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; perikaryon [GO:0043204]; postsynapse [GO:0098794]; ribonucleoprotein complex [GO:1990904]; ribosome [GO:0005840] | mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; poly(A) binding [GO:0008143]; pre-mRNA intronic pyrimidine-rich binding [GO:0097158] | PF00076; | 3.30.70.330; | RRM elav family | PTM: Methylated by CARM1, which leads to reduced RNA-binding activity and enhanced interaction with SMN (By similarity). Methylation at Arg-248 by CARM1 weakens protective binding to the 3'-UTR of CDKN1A mRNA and down-regulates CDKN1A protein expression, thereby maintaining cells in a proliferative state (PubMed:16508003). Methylation is inhibited by NGF, which facilitates neurite outgrowth (PubMed:16508003). {ECO:0000250|UniProtKB:P26378, ECO:0000269|PubMed:16508003}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11948657, ECO:0000269|PubMed:12957493, ECO:0000269|PubMed:15519747, ECO:0000269|PubMed:16554442}. Perikaryon {ECO:0000269|PubMed:12957493, ECO:0000269|PubMed:25692578}. Cell projection, axon {ECO:0000250|UniProtKB:Q61701}. Cell projection, dendrite {ECO:0000269|PubMed:15519747}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q61701}. Note=Co-localizes with ribosomal RNA in polysomes. {ECO:0000269|PubMed:12957493, ECO:0000269|PubMed:15519747}. | null | null | null | null | null | FUNCTION: RNA-binding protein that is involved in the post-transcriptional regulation of mRNAs (PubMed:10982410, PubMed:16508003, PubMed:17577668). Plays a role in the regulation of mRNA stability, alternative splicing and translation (PubMed:10982410, PubMed:16508003, PubMed:17577668). Binds to AU-rich element (ARE) sequences in the 3' untranslated region (UTR) of target mRNAs, including GAP43, VEGF, FOS, CDKN1A and ACHE mRNA (PubMed:10982410). Many of the target mRNAs are coding for RNA-binding proteins, transcription factors and proteins involved in RNA processing and/or neuronal development and function (By similarity). By binding to the mRNA 3'UTR, decreases mRNA deadenylation and thereby contributes to the stabilization of mRNA molecules and their protection from decay (By similarity). Also binds to the polyadenylated (poly(A)) tail in the 3'UTR of mRNA, thereby increasing its affinity for mRNA binding (By similarity). Mainly plays a role in neuron-specific RNA processing by stabilization of mRNAs such as GAP43, ACHE and mRNAs of other neuronal proteins, thereby contributing to the differentiation of neural progenitor cells, nervous system development, learning and memory mechanisms (PubMed:10982410, PubMed:17577668). Involved in the negative regulation of the proliferative activity of neuronal stem cells and in the positive regulation of neuronal differentiation of neural progenitor cells (By similarity). Promotes neuronal differentiation of neural stem/progenitor cells in the adult subventricular zone of the hippocampus by binding to and stabilizing SATB1 mRNA (By similarity). Binds and stabilizes MSI1 mRNA in neural stem cells (By similarity). Exhibits increased binding to ACHE mRNA during neuronal differentiation, thereby stabilizing ACHE mRNA and enhancing its expression (By similarity). Protects CDKN1A mRNA from decay by binding to its 3'-UTR (PubMed:16508003). May bind to APP and BACE1 mRNAS and the BACE1AS lncRNA and enhance their stabilization (By similarity). Plays a role in neurite outgrowth and in the establishment and maturation of dendritic arbors, thereby contributing to neocortical and hippocampal circuitry function (By similarity). Stabilizes GAP43 mRNA and protects it from decay during postembryonic development in the brain (PubMed:10982410, PubMed:17234598). By promoting the stabilization of GAP43 mRNA, plays a role in NGF-mediated neurite outgrowth (PubMed:10982410). Binds to BDNF long 3'UTR mRNA, thereby leading to its stabilization and increased dendritic translation after activation of PKC (PubMed:25692578). By increasing translation of BDNF after nerve injury, may contribute to nerve regeneration (By similarity). Acts as a stabilizing factor by binding to the 3'UTR of NOVA1 mRNA, thereby increasing its translation and enhancing its functional activity in neuron-specific splicing (By similarity). Stimulates translation of mRNA in a poly(A)- and cap-dependent manner, possibly by associating with the EIF4F cap-binding complex (By similarity). May also negatively regulate translation by binding to the 5'UTR of Ins2 mRNA, thereby repressing its translation (By similarity). Upon glucose stimulation, Ins2 mRNA is released form ELAVL4 and translational inhibition is abolished (By similarity). Also plays a role in the regulation of alternative splicing (By similarity). May regulate alternative splicing of CALCA pre-mRNA into Calcitonin and calcitonin gene-related peptide 1 (CGRP) by competing with splicing regulator TIAR for binding to U-rich sequences of CALCA pre-mRNA (By similarity). {ECO:0000250|UniProtKB:P26378, ECO:0000250|UniProtKB:Q61701, ECO:0000269|PubMed:10982410, ECO:0000269|PubMed:16508003, ECO:0000269|PubMed:17234598, ECO:0000269|PubMed:17577668, ECO:0000269|PubMed:25692578}. | Rattus norvegicus (Rat) |
O09037 | REG3A_MOUSE | MLPHLVLNSISWMLLSCLLFVFQVQGEDFQKEVPSPRTSCPMGYKAYRSHCYALVMTPKSWFQADLVCQKRPSGHLVSILSGGEASFVSSLVNGRVDNYQDIWIGLHDPTMGQQPNGGGWEWSNSDVLNYLNWDGDPSSTVNRGHCGSLTASSGFLKWGDYYCDGTLPFVCKFKQ | null | null | acute-phase response [GO:0006953]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; disruption of cell wall in another organism [GO:0044278]; negative regulation of keratinocyte differentiation [GO:0045617]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of keratinocyte proliferation [GO:0010838]; positive regulation of wound healing [GO:0090303]; response to peptide hormone [GO:0043434] | collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615] | metal ion binding [GO:0046872]; oligosaccharide binding [GO:0070492]; peptidoglycan binding [GO:0042834]; signaling receptor activity [GO:0038023] | PF00059; | 3.10.100.10; | null | PTM: Proteolytic processing by trypsin removes an inhibitory N-terminal propeptide and is essential for peptidoglycan binding and antibacterial activity. {ECO:0000250|UniProtKB:Q06141}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q06141}. Note=Found in the apical region of pancreatic acinar cells. {ECO:0000250|UniProtKB:Q06141}. | null | null | null | null | null | FUNCTION: Bactericidal C-type lectin. The lack of the EPN motif may explain its inability to bind peptidoglycan. {ECO:0000269|PubMed:20382864}.; FUNCTION: Acts as a hormone in response to different stimuli like anti-inflammatory signals, such as IL17A, or gut microbiome. Secreted by different cell types to activate its receptor EXTL3 and induce cell specific signaling pathways. Induced by IL17A in keratinocytes, regulates keratinocyte proliferation and differentiation after skin injury via activation of EXTL3-PI3K-AKT signaling pathway (By similarity). In parallel, inhibits skin inflammation through the inhibition of inflammatory cytokines such as IL6 and TNF (PubMed:22727489). In pancreas, is able to permealize beta-cells membrane and stimulate their proliferation (PubMed:36240759). {ECO:0000250|UniProtKB:Q06141, ECO:0000269|PubMed:22727489, ECO:0000269|PubMed:36240759}. | Mus musculus (Mouse) |
O09039 | SH2B3_MOUSE | MNEPTVQPSRTSSAPASPASPRGWSDFCEQHAAAAARELARQYWLFARAHPQPPRADLVSLQFAELFQRHFCREVRESLAGPPGHDYRATAPPRPALPKARSSEDLGPRPACALQHLRRGLRQLFRRRSAGELPGATSDTNDIDTTAASRPGPARKLLPWGLREPPTEALKEVVLRYSLADEAAMDSGARWQRGRLVLRSPGPGHSHFLQLFDPPKSSKPKLQEACSSIREVRPCTRLEMPDNLYTFVLKVQDQTDIIFEVGDEQQLNSWLAELRASTGLGLEHPDTELPLSLAAEPGPARSPRGSTDSLDQGASPGVLLDPACQKTDHFLSCYPWFHGPISRVRAAQLVQLQGPDAHGVFLVRQSESRRGEYVLTFNLQGRAKHLRLVLTERGQCRVQHLHFPSVVDMLRHFQRSPIPLECGAACDVRLSGYVVVLSQAPGSSNTVLFPFSLPHWDSELGHPHLSSVGCPPSHGAEALPGQVTPPEQIFHLVPSPEELANSLRQLELESVSSARDSDYDMDSSSRGHLRAIDNQYTPLSQLCREADV | null | null | cellular response to chemokine [GO:1990869]; cellular response to interleukin-3 [GO:0036016]; embryonic hemopoiesis [GO:0035162]; erythrocyte development [GO:0048821]; hematopoietic stem cell differentiation [GO:0060218]; hemopoiesis [GO:0030097]; intracellular signal transduction [GO:0035556]; megakaryocyte development [GO:0035855]; monocyte homeostasis [GO:0035702]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of chemokine-mediated signaling pathway [GO:0070100]; negative regulation of Kit signaling pathway [GO:1900235]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of platelet aggregation [GO:0090331]; negative regulation of receptor signaling pathway via JAK-STAT [GO:0046426]; negative regulation of receptor signaling pathway via STAT [GO:1904893]; negative regulation of sprouting angiogenesis [GO:1903671]; neutrophil homeostasis [GO:0001780]; regulation of regulatory T cell differentiation [GO:0045589]; thrombopoietin-mediated signaling pathway [GO:0038163] | plasma membrane [GO:0005886] | phosphate ion binding [GO:0042301]; protein tyrosine kinase binding [GO:1990782]; protein-containing complex binding [GO:0044877]; signaling receptor complex adaptor activity [GO:0030159]; stem cell factor receptor binding [GO:0005173]; transmembrane receptor protein tyrosine kinase adaptor activity [GO:0005068] | PF08916;PF00017; | 6.10.140.110;2.30.29.30;3.30.505.10; | SH2B adapter family | PTM: Tyrosine phosphorylated. {ECO:0000250}. | null | null | null | null | null | null | FUNCTION: Links T-cell receptor activation signal to phospholipase C-gamma-1, GRB2 and phosphatidylinositol 3-kinase. {ECO:0000250}. | Mus musculus (Mouse) |
O09043 | NAPSA_MOUSE | MSPLLLLLLCLLLGNLEPEEAKLIRVPLQRIHLGHRILNPLNGWEQLAELSRTSTSGGNPSFVPLSKFMNTQYFGTIGLGTPPQNFTVVFDTGSSNLWVPSTRCHFFSLACWFHHRFNPKASSSFRPNGTKFAIQYGTGRLSGILSQDNLTIGGIHDAFVTFGEALWEPSLIFALAHFDGILGLGFPTLAVGGVQPPLDAMVEQGLLEKPVFSFYLNRDSEGSDGGELVLGGSDPAHYVPPLTFIPVTIPAYWQVHMESVKVGTGLSLCAQGCSAILDTGTSLITGPSEEIRALNKAIGGYPFLNGQYFIQCSKTPTLPPVSFHLGGVWFNLTGQDYVIKILQSDVGLCLLGFQALDIPKPAGPLWILGDVFLGPYVAVFDRGDKNVGPRVGLARAQSRSTDRAERRTTQAQFFKRRPG | 3.4.23.- | null | membrane protein proteolysis [GO:0033619]; proteolysis [GO:0006508]; surfactant homeostasis [GO:0043129] | alveolar lamellar body [GO:0097208]; extracellular space [GO:0005615]; lysosome [GO:0005764] | aspartic-type endopeptidase activity [GO:0004190]; endopeptidase activity [GO:0004175] | PF00026; | 2.40.70.10; | Peptidase A1 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in processing of pneumocyte surfactant precursors. {ECO:0000250}. | Mus musculus (Mouse) |
O09044 | SNP23_MOUSE | MDNLSPEEVQLRAHQVTDESLESTRRILGLAIESQDAGIKTITMLDEQGEQLNRIEEGMDQINKDMREAEKTLTELNKCCGLCICPCNRTKNFESGKNYKATWGDGGDNSPSNVVSKQPSRITNGQPQQTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKNMALDMGNEIDAQNQQIQKITEKADTNKNRIDIANTRAKKLIDS | null | null | exocytic insertion of neurotransmitter receptor to postsynaptic membrane [GO:0098967]; exocytosis [GO:0006887]; membrane fusion [GO:0061025]; protein-containing complex assembly [GO:0065003]; regulation of exocytosis [GO:0017157]; synaptic vesicle fusion to presynaptic active zone membrane [GO:0031629]; synaptic vesicle priming [GO:0016082]; vesicle-mediated transport [GO:0016192]; vesicle-mediated transport in synapse [GO:0099003] | cytoplasmic vesicle [GO:0031410]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; presynapse [GO:0098793]; SNARE complex [GO:0031201]; synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex [GO:0070032] | SNAP receptor activity [GO:0005484]; syntaxin binding [GO:0019905]; syntaxin-1 binding [GO:0017075] | PF00835; | 1.20.5.110; | SNAP-25 family | PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type A (BoNT/A, botA) which hydrolyzes the 202-Thr-|-Arg-203 bond; the in vitro reaction is not highly efficient (PubMed:9886085). {ECO:0000269|PubMed:9886085}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type E (BoNT/E) which hydrolyzes the 185-Arg-|-Ile-186 bond; the in vitro reaction is more efficient than that of BoNT/A (PubMed:9886085). {ECO:0000269|PubMed:9886085}. | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Synapse, synaptosome. Note=Mainly localized to the plasma membrane. | null | null | null | null | null | FUNCTION: Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion. {ECO:0000250}. | Mus musculus (Mouse) |
O09046 | OXLA_MOUSE | MAGLALRLVLAATLLGLAGSLDWKAASSLNPIEKCMEDHDYEQLLKVVTLGLNRTSKPQKVVVVGAGVAGLVAAKMLSDAGHKVTILEADNRIGGRIFTFRDEKTGWIGELGAMRMPSSHRILHKLCRTLGLNLTQFTQYDENTWTEVHNVKLRNYVVEKMPEKLGYNLNNRERGHSPEDIYQMALNKAFKDLKALGCKKAMNKFNKHTLLEYLLEEGNLSRPAVQLLGDVMSEEGFFYLSFAEALRAHACLSDRLRYSRIVGGWDLLPRALLSSLSGALLLNAPVVSITQGRNDVRVHIATSLHSEKTLTADVVLLTASGPALQRITFSPPLTRKRQEALRALHYVAASKVFLSFRRPFWHEEHIEGGHSNTDRPSRLIFYPARGEGSLLLASYTWSDAAAPFAGLSTDQTLRLVLQDVAALHGPVVFRLWDGRGVVKRWAEDPHSQGGFVVQPPLYGREAEDYDWSAPFGRIYFAGEHTALPHGWVETAVKSGLRAAVRINNNYGYGEVDPQMMEHAYAEANYLDQYPEGERPEEQQAREEVSPDEQEPSHKHLLVETSPEGQQHAFVEAIPELQGHVFVETVPQEKGHAHQNIYPSEHVQVHGEVIPEWHGHGGSGTPQMHRVGDHS | 1.4.3.2; 1.4.3.25 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:15383589}; | adaptive immune response [GO:0002250]; amino acid catabolic process [GO:0009063]; aromatic amino acid metabolic process [GO:0009072]; L-phenylalanine catabolic process [GO:0006559]; negative regulation of T cell activation [GO:0050868]; negative regulation of T cell mediated immune response to tumor cell [GO:0002841]; negative regulation of T cell proliferation [GO:0042130]; positive regulation of regulatory T cell differentiation [GO:0045591]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of adaptive immune response [GO:0002819]; regulation of B cell differentiation [GO:0045577]; tryptophan catabolic process [GO:0006569]; tryptophan catabolic process to indole-3-acetate [GO:0019440]; tyrosine catabolic process [GO:0006572] | acrosomal vesicle [GO:0001669]; extracellular region [GO:0005576]; immunological synapse [GO:0001772]; lysosome [GO:0005764]; sperm midpiece [GO:0097225] | L-amino-acid oxidase activity [GO:0001716]; L-phenylalaine oxidase activity [GO:0106329]; polyamine oxidase activity [GO:0046592] | PF01593; | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family, FIG1 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q96RQ9}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q96RQ9}. Note=Secreted at the immunological synapse. {ECO:0000250|UniProtKB:Q96RQ9}.; SUBCELLULAR LOCATION: [Isoform 1]: Lysosome {ECO:0000269|PubMed:15383589}.; SUBCELLULAR LOCATION: [Isoform 2]: Lysosome {ECO:0000269|PubMed:15383589}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:15383589}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13782; Evidence={ECO:0000269|PubMed:15383589}; CATALYTIC ACTIVITY: Reaction=H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+); Xref=Rhea:RHEA:61244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938, ChEBI:CHEBI:57912; Evidence={ECO:0000250|UniProtKB:Q96RQ9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61245; Evidence={ECO:0000250|UniProtKB:Q96RQ9}; CATALYTIC ACTIVITY: Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938, ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:15383589}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61241; Evidence={ECO:0000269|PubMed:15383589}; CATALYTIC ACTIVITY: Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; Evidence={ECO:0000250|UniProtKB:Q96RQ9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61249; Evidence={ECO:0000250|UniProtKB:Q96RQ9}; CATALYTIC ACTIVITY: Reaction=H2O + L-arginine + O2 = 5-guanidino-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:51404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32682, ChEBI:CHEBI:58489; EC=1.4.3.25; Evidence={ECO:0000250|UniProtKB:Q96RQ9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51405; Evidence={ECO:0000250|UniProtKB:Q96RQ9}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.5 mM for phenylalanine (at 37 degrees Celsius) {ECO:0000269|PubMed:15383589}; Vmax=0.0099 nmol/min/mg enzyme toward phenylalanine (at 37 degrees Celsius) {ECO:0000269|PubMed:15383589}; | PATHWAY: Amino-acid degradation; L-tryptophan degradation via pyruvate pathway. {ECO:0000250|UniProtKB:Q96RQ9}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0. {ECO:0000269|PubMed:15383589}; | null | FUNCTION: Secreted L-amino-acid oxidase that acts as a key immunoregulator (PubMed:32818467). Has preference for L-aromatic amino acids: converts phenylalanine (Phe), tyrosine (Tyr) and tryptophan (Trp) to phenylpyruvic acid (PP), hydroxyphenylpyruvic acid (HPP), and indole-3-pyruvic acid (I3P), respectively (PubMed:15383589). Also has weak L-arginine oxidase activity (By similarity). Acts as a negative regulator of anti-tumor immunity by mediating Trp degradation via an indole pyruvate pathway that activates the transcription factor AHR (PubMed:21469114, PubMed:28405502, PubMed:32818467). IL4I1-mediated Trp catabolism generates I3P, giving rise to indole metabolites (indole-3-acetic acid (IAA) and indole-3-aldehyde (I3A)) and kynurenic acid, which act as ligands for AHR, a ligand-activated transcription factor that plays important roles in immunity and cancer (By similarity). AHR activation by indoles following IL4I1-mediated Trp degradation enhances tumor progression by promoting cancer cell motility and suppressing adaptive immunity (PubMed:32818467). Also has an immunoregulatory function in some immune cell, probably by mediating Trp degradation and promoting downstream AHR activation: inhibits T-cell activation and proliferation, promotes the differentiation of naive CD4(+) T-cells into FOXP3(+) regulatory T-cells (Treg) and regulates the development and function of B-cells (PubMed:25778793, PubMed:29288206). Also regulates M2 macrophage polarization by inhibiting T-cell activation (PubMed:26599209). Also has antibacterial properties by inhibiting growth of Gram negative and Gram positive bacteria through the production of NH4(+) and H2O2 (By similarity). {ECO:0000250|UniProtKB:Q96RQ9, ECO:0000269|PubMed:15383589, ECO:0000269|PubMed:21469114, ECO:0000269|PubMed:25778793, ECO:0000269|PubMed:26599209, ECO:0000269|PubMed:28405502, ECO:0000269|PubMed:29288206, ECO:0000269|PubMed:32818467}. | Mus musculus (Mouse) |
O09047 | C3AR_MOUSE | MESFDADTNSTDLHSRPLFQPQDIASMVILGLTCLLGLLGNGLVLWVAGVKMKTTVNTVWFLHLTLADFLCCLSLPFSLAHLILQGHWPYGLFLCKLIPSIIILNMFASVFLLTAISLDRCLIVHKPIWCQNHRNVRTAFAICGCVWVVAFVMCVPVFVYRDLFIMDNRSICRYNFDSSRSYDYWDYVYKLSLPESNSTDNSTAQLTGHMNDRSAPSSVQARDYFWTVTTALQSQPFLTSPEDSFSLDSANQQPHYGGKPPNVLTAAVPSGFPVEDRKSNTLNADAFLSAHTELFPTASSGHLYPYDFQGDYVDQFTYDNHVPTPLMAITITRLVVGFLVPFFIMVICYSLIVFRMRKTNFTKSRNKTFRVAVAVVTVFFICWTPYHLVGVLLLITDPESSLGEAVMSWDHMSIALASANSCFNPFLYALLGKDFRKKARQSIKGILEAAFSEELTHSTNCTQDKASSKRNNMSTDV | null | null | calcium-mediated signaling [GO:0019722]; chemotaxis [GO:0006935]; complement receptor mediated signaling pathway [GO:0002430]; inflammatory response [GO:0006954]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell migration [GO:0030335]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of DNA biosynthetic process [GO:2000573]; positive regulation of glomerular mesangial cell proliferation [GO:0072126]; positive regulation of macrophage chemotaxis [GO:0010759]; positive regulation of neutrophil chemotaxis [GO:0090023]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of vascular endothelial growth factor production [GO:0010575]; regulation of blood pressure [GO:0008217]; tolerance induction to nonself antigen [GO:0002462] | plasma membrane [GO:0005886] | complement component C3a binding [GO:0001850]; complement component C3a receptor activity [GO:0004876]; complement component C5a receptor activity [GO:0004878]; G protein-coupled receptor activity [GO:0004930] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production. | Mus musculus (Mouse) |
O09049 | REG3G_MOUSE | MLPRITITIMSWMLLSCLMLLSQVQGEVAKKDAPSSRSSCPKGSRAYGSYCYALFSVSKNWYDADMACQKRPSGHLVSVLSGAEASFLSSMIKSSGNSGQYVWIGLHDPTLGYEPNRGGWEWSNADVMNYINWETNPSSSSGNHCGTLSRASGFLKWRENYCNLELPYVCKFKA | null | null | acute-phase response [GO:0006953]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; disruption of cell wall in another organism [GO:0044278]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; negative regulation of inflammatory response [GO:0050728]; negative regulation of inflammatory response to wounding [GO:0106015]; negative regulation of keratinocyte differentiation [GO:0045617]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of detection of glucose [GO:2000972]; positive regulation of keratinocyte proliferation [GO:0010838]; positive regulation of wound healing [GO:0090303]; response to bacterium [GO:0009617]; response to peptide hormone [GO:0043434]; response to symbiotic bacterium [GO:0009609] | collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; secretory granule [GO:0030141] | hormone activity [GO:0005179]; metal ion binding [GO:0046872]; oligosaccharide binding [GO:0070492]; peptidoglycan binding [GO:0042834]; signaling receptor activity [GO:0038023] | PF00059; | 3.10.100.10; | null | PTM: Proteolytic processing by trypsin removes an inhibitory N-terminal propeptide and is essential for peptidoglycan binding and antibacterial activity. {ECO:0000269|PubMed:19095652}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28811323, ECO:0000269|PubMed:36240758}. Cytoplasm {ECO:0000250|UniProtKB:P42854}. | null | null | null | null | null | FUNCTION: Bactericidal C-type lectin which acts exclusively against Gram-positive bacteria and mediates bacterial killing by binding to surface-exposed carbohydrate moieties of peptidoglycan. Restricts bacterial colonization of the intestinal epithelial surface and consequently limits activation of adaptive immune responses by the microbiota. {ECO:0000269|PubMed:16504538, ECO:0000269|PubMed:16931762, ECO:0000269|PubMed:17635956, ECO:0000269|PubMed:21998396, ECO:0000269|PubMed:22727489, ECO:0000269|PubMed:23401489}.; FUNCTION: Acts as a hormone in response to different stimuli like anti-inflammatory signals, such as IL17A, or gut microbiome. Is secreted by different cell types to activate its receptor EXTL3 and induce cell specific signaling pathways (PubMed:22727489, PubMed:27830702, PubMed:36240758). Induced by IL17A in keratinocytes, regulates keratinocyte proliferation and differentiation after skin injury (PubMed:22727489). In parallel, inhibits skin inflammation through the inhibition of inflammatory cytokines such as IL6 and TNF (PubMed:27830702). Induced by IL22 in lung epithelial cells, inhibits cytokine production and regulates allergic airway inflammation (PubMed:28811323). Induced in small intestine by inulin-enriched diet and Lactobacillus gasseri enriched microbiome, plays a role in the improvement of gut barrier function, the regulation of energy balance and glucose levels. Modulates microbiota composition in duodenal contents (PubMed:36240758). Produced by nociceptor in response to endotoxins, prevents endotoxic death by targeting kynurenine pathway in microglia (PubMed:35263589). {ECO:0000269|PubMed:22727489, ECO:0000269|PubMed:27830702, ECO:0000269|PubMed:28811323, ECO:0000269|PubMed:35263589, ECO:0000269|PubMed:36240758}.; FUNCTION: [Regenerating islet-derived protein 3-gamma 16.5 kDa form]: Has bacteriostatic activity. {ECO:0000269|PubMed:19095652}.; FUNCTION: [Regenerating islet-derived protein 3-gamma 15 kDa form]: Has bactericidal activity against L.monocytogenes and methicillin-resistant S.aureus. {ECO:0000269|PubMed:19095652}. | Mus musculus (Mouse) |
O09051 | GUC2B_MOUSE | MSRSQLWAAVVLLLLLQSAQGVYIKYHGFQVQLESVKKLNELEEKEMSNPQPRRSGLLPAVCHNPALPLDLQPVCASQEAASTFKALRTIATDECELCINVACTGC | null | null | adipose tissue development [GO:0060612]; body fluid secretion [GO:0007589]; cGMP-mediated signaling [GO:0019934]; energy homeostasis [GO:0097009]; glucose homeostasis [GO:0042593]; multicellular organism growth [GO:0035264]; negative regulation of blood pressure [GO:0045776]; reduction of food intake in response to dietary excess [GO:0002023]; renal sodium ion absorption [GO:0070294]; response to glucose [GO:0009749] | extracellular region [GO:0005576]; photoreceptor outer segment [GO:0001750] | guanylate cyclase activator activity [GO:0030250] | PF02058; | 3.90.1450.10; | Guanylin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Endogenous activator of intestinal guanylate cyclase. It stimulates this enzyme through the same receptor binding region as the heat-stable enterotoxins. May be a potent physiological regulator of intestinal fluid and electrolyte transport. May be an autocrine/paracrine regulator of intestinal salt and water transport (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
O09053 | WRN_MOUSE | METTSLQRKFPEWMSMQSQRCATEEKACVQKSVLEDNLPFLEFPGSIVYSYEASDCSFLSEDISMRLSDGDVVGFDMEWPPIYKPGKRSRVAVIQLCVSESKCYLFHISSMSVFPQGLKMLLENKSIKKAGVGIEGDQWKLLRDFDVKLESFVELTDVANEKLKCAETWSLNGLVKHVLGKQLLKDKSIRCSNWSNFPLTEDQKLYAATDAYAGLIIYQKLGNLGDTAQVFALNKAEENLPLEMKKQLNSISEEMRDLANRFPVTCRNLETLQRVPVILKSISENLCSLRKVICGPTNTETRLKPGSSFNLLSSEDSAAAGEKEKQIGKHSTFAKIKEEPWDPELDSLVKQEEVDVFRNQVKQEKGESENEIEDNLLREDMERTCVIPSISENELQDLEQQAKEEKYNDVSHQLSEHLSPNDDENDSSYIIESDEDLEMEMLKSLENLNSDVVEPTHSTWLEMGTNGRLPPEEEDGHGNEAIKEEQEEEDHLLPEPNAKQINCLKTYFGHSSFKPVQWKVIHSVLEERRDNVVVMATGYGKSLCFQYPPVYTGKIGIVISPLISLMEDQVLQLELSNVPACLLGSAQSKNILGDVKLGKYRVIYITPEFCSGNLDLLQQLDSSIGITLIAVDEAHCISEWGHDFRSSFRMLGSLKTALPLVPVIALSATASSSIREDIISCLNLKDPQITCTGFDRPNLYLEVGRKTGNILQDLKPFLVRKASSAWEFEGPTIIYCPSRKMTEQVTAELGKLNLACRTYHAGMKISERKDVHHRFLRDEIQCVVATVAFGMGINKADIRKVIHYGAPKEMESYYQEIGRAGRDGLQSSCHLLWAPADFNTSRNLLIEIHDEKFRLYKLKMMVKMEKYLHSSQCRRRIILSHFEDKCLQKASLDIMGTEKCCDNCRPRLNHCLTANNSEDASQDFGPQAFQLLSAVDILQEKFGIGIPILFLRGSNSQRLPDKYRGHRLFGAGKEQAESWWKTLSHHLIAEGFLVEVPKENKYIKTCSLTKKGRKWLGEASSQSPPSLLLQANEEMFPRKVLLPSSNPVSPETTQHSSNQNPAGLTTKQSNLERTHSYKVPEKVSSGTNIPKKSAVMPSPGTSSSPLEPAISAQELDARTGLYARLVEARQKHANKMDVPPAILATNKVLLDMAKMRPTTVENMKQIDGVSEGKAALLAPLLEVIKHFCQVTSVQTDLLSSAKPHKEQEKSQEMEKKDCSLPQSVAVTYTLFQEKKMPLHSIAENRLLPLTAAGMHLAQAVKAGYPLDMERAGLTPETWKIIMDVIRNPPINSDMYKVKLIRMLVPENLDTYLIHMAIEILQSGSDSRTQPPCDSSRKRRFPSSAESCESCKESKEAVTETKASSSESKRKLPEWFAKGNVPSADTGSSSSMAKTKKKGLFS | 3.1.-.-; 5.6.2.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:17229737}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17229737}; Note=Binds 2 zinc ions in the exonuclease domain. Has high activity with manganese and zinc ions, and no activity with Mg(2+) (in vitro) (PubMed:17229737). {ECO:0000269|PubMed:17229737}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q14191}; Note=Binds a Zn(2+) ion in the helicase domain. {ECO:0000250|UniProtKB:Q14191}; | base-excision repair [GO:0006284]; cellular response to gamma radiation [GO:0071480]; cellular response to starvation [GO:0009267]; cellular senescence [GO:0090398]; determination of adult lifespan [GO:0008340]; DNA metabolic process [GO:0006259]; DNA replication [GO:0006260]; DNA synthesis involved in DNA repair [GO:0000731]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; G-quadruplex DNA unwinding [GO:0044806]; positive regulation of strand invasion [GO:0098530]; protein localization to nucleolus [GO:1902570]; regulation of apoptotic process [GO:0042981]; regulation of growth rate [GO:0040009]; replication fork processing [GO:0031297]; replicative senescence [GO:0090399]; response to oxidative stress [GO:0006979]; response to UV-C [GO:0010225]; telomere maintenance [GO:0000723]; telomeric D-loop disassembly [GO:0061820] | centrosome [GO:0005813]; chromosome [GO:0005694]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; replication fork [GO:0005657] | 3'-5' DNA helicase activity [GO:0043138]; 3'-5' exonuclease activity [GO:0008408]; 3'-flap-structured DNA binding [GO:0070337]; 8-hydroxy-2'-deoxyguanosine DNA binding [GO:1905773]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; bubble DNA binding [GO:0000405]; chromatin binding [GO:0003682]; DNA helicase activity [GO:0003678]; exonuclease activity [GO:0004527]; forked DNA-dependent helicase activity [GO:0061749]; four-way junction DNA binding [GO:0000400]; four-way junction helicase activity [GO:0009378]; isomerase activity [GO:0016853]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; MutLalpha complex binding [GO:0032405]; protein homodimerization activity [GO:0042803]; telomeric D-loop binding [GO:0061821]; telomeric G-quadruplex DNA binding [GO:0061849]; Y-form DNA binding [GO:0000403] | PF00270;PF01612;PF00271;PF00570;PF14493;PF16124;PF09382; | 1.10.150.80;3.40.50.300;3.30.420.10;1.10.10.10; | Helicase family, RecQ subfamily | PTM: Phosphorylated by PRKDC. {ECO:0000250|UniProtKB:Q14191}. | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q14191}. Nucleus {ECO:0000269|PubMed:9618508}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q14191}. Chromosome {ECO:0000250|UniProtKB:Q14191}. Note=Gamma-irradiation leads to its translocation from nucleoli to nucleoplasm and PML regulates the irradiation-induced WRN relocation. Localizes to DNA damage sites. {ECO:0000250|UniProtKB:Q14191}. | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000250|UniProtKB:Q14191}; 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:17229737}; | null | null | null | null | FUNCTION: Multifunctional enzyme that has magnesium and ATP-dependent 3'-5' DNA-helicase activity (By similarity). Has 3'->5' exonuclease activity on forked dsDNA (PubMed:17229737). Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Important for genomic integrity. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity). Plays a role in double-strand break repair after gamma-irradiation (By similarity). {ECO:0000250|UniProtKB:Q14191, ECO:0000269|PubMed:10757812, ECO:0000269|PubMed:17229737}. | Mus musculus (Mouse) |
O09061 | PSB1_MOUSE | MLSTAAYRDVERELGMGPHGSAGPVQLRFSPYAFNGGTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLTLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVPLRKD | null | null | proteolysis involved in protein catabolic process [GO:0051603] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome core complex [GO:0005839]; proteasome core complex, beta-subunit complex [GO:0019774] | null | PF00227; | 3.60.20.10; | Peptidase T1B family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P20618}. Nucleus {ECO:0000250|UniProtKB:P20618}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000250|UniProtKB:P20618}. | null | null | null | null | null | FUNCTION: Non-catalytic component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:22341445}. | Mus musculus (Mouse) |
O09100 | GATA2_MOUSE | MEVAPEQPRWMAHPAVLNAQHPDSHHPGLAHNYMEPAQLLPPDEVDVFFNHLDSQGNPYYANPAHARARVSYSPAHARLTGGQMCRPHLLHSPGLPWLDGGKAALSAAAAHHHSPWTVSPFSKTPLHPSAAGAPGGPLSVYPGAAGGSGGGSGSSVASLTPTAAHSGSHLFGFPPTPPKEVSPDPSTTGAASPASSSAGGSVARGEDKDGVKYQVSLSESMKMEGGSPLRPGLATMGTQPATHHPIPTYPSYVPAAAHDYGSSLFHPGGFLGGPASSFTPKQRSKARSCSEGRECVNCGATATPLWRRDGTGHYLCNACGLYHKMNGQNRPLIKPKRRLSAARRAGTCCANCQTTTTTLWRRNANGDPVCNACGLYYKLHNVNRPLTMKKEGIQTRNRKMSSKSKKSKKGAECFEELSKCMQEKSPPFSAAALAGHMAPVGHLPPFSHSGHILPTPTPIHPSSSLSFGHPHPSSMVTAMG | null | null | angiogenesis [GO:0001525]; brown fat cell differentiation [GO:0050873]; cell differentiation in hindbrain [GO:0021533]; cell fate commitment [GO:0045165]; cell fate determination [GO:0001709]; central nervous system neuron development [GO:0021954]; cochlea development [GO:0090102]; commitment of neuronal cell to specific neuron type in forebrain [GO:0021902]; definitive hemopoiesis [GO:0060216]; embryonic placenta development [GO:0001892]; eosinophil fate commitment [GO:0035854]; GABAergic neuron differentiation [GO:0097154]; glandular epithelial cell differentiation [GO:0002067]; glandular epithelial cell maturation [GO:0002071]; hematopoietic progenitor cell differentiation [GO:0002244]; hematopoietic stem cell homeostasis [GO:0061484]; homeostasis of number of cells within a tissue [GO:0048873]; inner ear morphogenesis [GO:0042472]; myeloid cell differentiation [GO:0030099]; negative regulation of brown fat cell differentiation [GO:1903444]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of gene expression [GO:0010629]; negative regulation of hematopoietic progenitor cell differentiation [GO:1901533]; negative regulation of macrophage differentiation [GO:0045650]; negative regulation of myeloid cell differentiation [GO:0045638]; negative regulation of neural precursor cell proliferation [GO:2000178]; negative regulation of neuroblast proliferation [GO:0007406]; negative regulation of Notch signaling pathway [GO:0045746]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural precursor cell proliferation [GO:0061351]; neuroblast proliferation [GO:0007405]; neuroendocrine cell differentiation [GO:0061101]; neuron differentiation [GO:0030182]; neuron fate commitment [GO:0048663]; neuron maturation [GO:0042551]; neuron migration [GO:0001764]; phagocytosis [GO:0006909]; pituitary gland development [GO:0021983]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:1903589]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of erythrocyte differentiation [GO:0045648]; positive regulation of gene expression [GO:0010628]; positive regulation of mast cell degranulation [GO:0043306]; positive regulation of megakaryocyte differentiation [GO:0045654]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of phagocytosis [GO:0050766]; positive regulation of phagocytosis, engulfment [GO:0060100]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of forebrain neuron differentiation [GO:2000977]; regulation of primitive erythrocyte differentiation [GO:0010725]; response to lipid [GO:0033993]; semicircular canal development [GO:0060872]; somatic stem cell population maintenance [GO:0035019]; thyroid-stimulating hormone-secreting cell differentiation [GO:0060129]; transcription by RNA polymerase II [GO:0006366]; urogenital system development [GO:0001655]; vascular wound healing [GO:0061042]; ventral spinal cord interneuron differentiation [GO:0021514] | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | C2H2 zinc finger domain binding [GO:0070742]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; 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-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]; transcription coactivator binding [GO:0001223]; zinc ion binding [GO:0008270] | PF00320; | 3.30.50.10; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcriptional activator which regulates endothelin-1 gene expression in endothelial cells. Binds to the consensus sequence 5'-AGATAG-3'. | Mus musculus (Mouse) |
O09102 | GCM2_MOUSE | MPADSTQDEDAVLSYGMKLTWDINDPQMPQEPTHFDHFREWPDGYVRFIYSSQEKKAQRHLSGWAMRNTNNHNGHILKKSCLGVVVCARACALKDGSHLQLRPAICDKARLKQQKKACPNCHSPLELVPCRGHSGYPVTNFWRLDGNAIFFQAKGVHDHPRPESKSETEGRRSALKRQMASFYQPQKRRSEEPEARSTQDIRGHLNSTAALEPTELFDMTADTSFPIPGQPSPSFPNSDVHRVTCDLPTFQGDIILPFQKYPNPSIYFPGPPWGYELASSGVTGSSPYSTLYKDSSVVPDDPDWIPLNSLQYNVSSYGSYERTLDFTARYHSWKPTHGKPSLEEKVDCEQCQAVPTSPYYNLELPCRYLPVPAAGTQALQTVITTTVAYQAYQHPALKHSDSMQEVSSLASCTYASENLPMPIYPPALDPQEGVIQAASPSGRAPLKVPGDCQAPRPTLDFPQEADPSGTDGADVWDVCLSGVGSVMGYLDRTGQPFSFDNEDF | null | null | apoptotic process [GO:0006915]; cellular response to organic substance [GO:0071310]; epithelial cell apoptotic process [GO:1904019]; gene expression [GO:0010467]; glandular epithelial cell differentiation [GO:0002067]; gliogenesis [GO:0042063]; intracellular calcium ion homeostasis [GO:0006874]; intracellular phosphate ion homeostasis [GO:0030643]; negative regulation of epithelial cell apoptotic process [GO:1904036]; parathyroid gland development [GO:0060017]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription by RNA polymerase II [GO:0006366] | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF03615; | 2.20.25.670;3.30.70.3530; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75603}. | null | null | null | null | null | FUNCTION: Transcription factor that binds specific sequences on gene promoters and activate their transcription. Through the regulation of gene transcription, may play a role in parathyroid gland development. {ECO:0000250|UniProtKB:O75603}. | Mus musculus (Mouse) |
O09105 | NDF4_MOUSE | MAKMYMKSKDMVELVNTQSWMDKGLSSQNEMKEQERRPGSYGMLGTLTEEHDSIEEDEEEEEDGDKPKRRGPKKKKMTKARLERFRARRVKANARERTRMHGLNDALDNLRRVMPCYSKTQKLSKIETLRLARNYIWALSEVLETGQTLEGKGFVEMLCKGLSQPTSNLVAGCLQLGPQSTLLEKHEEKSSICDSTISVHSFNYQSPGLPSPPYGHMETHSLHLKPQPFKSLGDSFGSHPPDCSTPPYEGPLTPPLSISGNFSLKQDGSPDLEKSYNFMPHYTSASLSSGHVHSTPFQTGTPRYDVPVDLSYDSYSHHSIGTQLNTIFSD | null | null | amacrine cell differentiation [GO:0035881]; axon development [GO:0061564]; camera-type eye development [GO:0043010]; cell fate commitment [GO:0045165]; motor neuron migration [GO:0097475]; neuroblast proliferation [GO:0007405]; neuron development [GO:0048666]; Notch signaling pathway [GO:0007219]; oligodendrocyte differentiation [GO:0048709]; positive regulation of cell differentiation [GO:0045597]; positive regulation of transcription by RNA polymerase II [GO:0045944] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983] | PF00010;PF12533; | 4.10.280.10; | null | PTM: Serine or threonine phosphorylation within the basic region may regulate neurogenic activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. | null | null | null | null | null | FUNCTION: Probably acts as a transcriptional activator. Mediates neuronal differentiation. Required for the regulation of amacrine cell fate specification in the retina. {ECO:0000269|PubMed:11861467}. | Mus musculus (Mouse) |
O09106 | HDAC1_MOUSE | MAQTQGTKRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEEDPDKRISICSSDKRIACEEEFSDSDEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA | 3.5.1.-; 3.5.1.98 | null | chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; DNA methylation-dependent heterochromatin formation [GO:0006346]; embryonic digit morphogenesis [GO:0042733]; endoderm development [GO:0007492]; epidermal cell differentiation [GO:0009913]; eyelid development in camera-type eye [GO:0061029]; fungiform papilla formation [GO:0061198]; hair follicle placode formation [GO:0060789]; hippocampus development [GO:0021766]; negative regulation by host of viral transcription [GO:0043922]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell migration [GO:0030336]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; 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]; neuron differentiation [GO:0030182]; odontogenesis of dentin-containing tooth [GO:0042475]; oligodendrocyte differentiation [GO:0048709]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of oligodendrocyte differentiation [GO:0048714]; positive regulation of stem cell population maintenance [GO:1902459]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell fate specification [GO:0042659]; regulation of stem cell differentiation [GO:2000736] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; heterochromatin [GO:0000792]; histone deacetylase complex [GO:0000118]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; NuRD complex [GO:0016581]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]; Sin3-type complex [GO:0070822]; transcription regulator complex [GO:0005667]; transcription repressor complex [GO:0017053] | chromatin binding [GO:0003682]; deacetylase activity [GO:0019213]; DNA binding [GO:0003677]; DNA-binding transcription factor binding [GO:0140297]; E-box binding [GO:0070888]; histone deacetylase activity [GO:0004407]; histone deacetylase binding [GO:0042826]; histone decrotonylase activity [GO:0160009]; Krueppel-associated box domain binding [GO:0035851]; NF-kappaB binding [GO:0051059]; p53 binding [GO:0002039]; promoter-specific chromatin binding [GO:1990841]; protein-containing complex binding [GO:0044877]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription cis-regulatory region binding [GO:0000976]; transcription corepressor activity [GO:0003714]; transcription corepressor binding [GO:0001222] | PF00850; | 3.40.800.20; | Histone deacetylase family, HD type 1 subfamily | PTM: Sumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q13547}.; PTM: Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5. {ECO:0000250|UniProtKB:Q13547}.; PTM: Ubiquitinated by CHFR and KCTD11, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q13547}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11115394, ECO:0000269|PubMed:21454521}. | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Evidence={ECO:0000269|PubMed:10615135, ECO:0000269|PubMed:21960634, ECO:0000305|PubMed:30279482}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197; Evidence={ECO:0000269|PubMed:10615135, ECO:0000269|PubMed:21960634, ECO:0000305|PubMed:30279482}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl-[protein]; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; Evidence={ECO:0000250|UniProtKB:Q13547}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109; Evidence={ECO:0000250|UniProtKB:Q13547}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] = (2E)-2-butenoate + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:35899, ChEBI:CHEBI:137954; Evidence={ECO:0000269|PubMed:30279482}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173; Evidence={ECO:0000269|PubMed:30279482}; | null | null | null | null | FUNCTION: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:10615135, PubMed:15542849, PubMed:21960634, PubMed:30279482). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:10615135, PubMed:15542849, PubMed:21960634). Histone deacetylases act via the formation of large multiprotein complexes (PubMed:10615135, PubMed:21960634). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (By similarity). As part of the SIN3B complex is recruited downstream of the constitutively active genes transcriptional start sites through interaction with histones and mitigates histone acetylation and RNA polymerase II progression within transcribed regions contributing to the regulation of transcription (By similarity). Also functions as a deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3, STAT3 and TSHZ3 (By similarity). Deacetylates SP proteins, SP1 and SP3, and regulates their function (By similarity). Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons (By similarity). Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation (By similarity). Deacetylates TSHZ3 and regulates its transcriptional repressor activity (By similarity). Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B (By similarity). Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity (By similarity). Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (PubMed:17707228). Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-BMAL1 heterodimer (PubMed:15226430, PubMed:24736997). Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation (PubMed:15226430). In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones (PubMed:30279482). {ECO:0000250|UniProtKB:Q13547, ECO:0000269|PubMed:10615135, ECO:0000269|PubMed:15226430, ECO:0000269|PubMed:15542849, ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:21960634, ECO:0000269|PubMed:24736997, ECO:0000269|PubMed:30279482}. | Mus musculus (Mouse) |
O09107 | INSL3_MOUSE | MRAPLLLMLLALGSALRSPQPPEARAKLCGHHLVRTLVRVCGGPRWSPEATQPVETRDRELLQWLEQRHLLHALVADVDPALDPQLPRQASQRQRRSAATNAVHRCCLTGCTQQDLLGLCPH | null | null | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; in utero embryonic development [GO:0001701]; male gonad development [GO:0008584]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell population proliferation [GO:0008285]; oocyte maturation [GO:0001556]; positive regulation of cAMP-mediated signaling [GO:0043950]; positive regulation of cell population proliferation [GO:0008284]; regulation of male gonad development [GO:2000018] | extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471] | G protein-coupled receptor binding [GO:0001664]; hormone activity [GO:0005179] | PF00049; | 1.10.100.10; | Insulin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Seems to play a role in testicular function. May be a trophic hormone with a role in testicular descent in fetal life. Is a ligand for LGR8 receptor (By similarity). {ECO:0000250, ECO:0000269|PubMed:10391220, ECO:0000269|PubMed:11342953}. | Mus musculus (Mouse) |
O09110 | MP2K3_MOUSE | MESPAASPPASLPQTKGKSKRKKDLRISCVSKPPVSNPTPPRNLDSRTFITIGDRNFEVEADDLVTISELGRGAYGVVEKVRHAQSGTIMAVKRIRATVNTQEQKRLLMDLDINMRTVDCFYTVTFYGALFREGDVWICMELMDTSLDKFYRKVLEKNMKIPEDILGEIAVSIVRALEHLHSKLSVIHRDVKPSNVLINKEGHVKMCDFGISGYLVDSVAKTMDAGCKPYMAPERINPELNQKGYNVKSDVWSLGITMIEMAILRFPYESWGTPFQQLKQVVEEPSPQLPADQFSPEFVDFTSQCLRKNPAERMSYLELMEHPFFTLHKTKKTDIAAFVKEILGEDS | 2.7.12.2 | null | cardiac muscle contraction [GO:0060048]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to sorbitol [GO:0072709]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; heart development [GO:0007507]; inflammatory response [GO:0006954]; MAPK cascade [GO:0000165]; negative regulation of hippo signaling [GO:0035331]; p38MAPK cascade [GO:0038066]; phosphorylation [GO:0016310]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of nitric-oxide synthase biosynthetic process [GO:0051770]; positive regulation of protein phosphorylation [GO:0001934]; regulation of cytokine production [GO:0001817]; response to ischemia [GO:0002931]; stress-activated protein kinase signaling cascade [GO:0031098] | null | ATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily | PTM: Autophosphorylated. Phosphorylation on Ser-218 and Thr-222 by MAP kinase kinase kinases positively regulates the kinase activity. Phosphorylated by TAOK2. {ECO:0000250|UniProtKB:P46734}. | null | 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=2.7.12.2; Evidence={ECO:0000250|UniProtKB:P46734}; 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=2.7.12.2; Evidence={ECO:0000250|UniProtKB:P46734}; 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=2.7.12.2; Evidence={ECO:0000250|UniProtKB:P46734}; | null | null | null | null | FUNCTION: Dual specificity kinase. Is activated by cytokines and environmental stress in vivo. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinase p38. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. {ECO:0000250|UniProtKB:P46734}. | Mus musculus (Mouse) |
O09112 | DUS8_MOUSE | MAGDRLPRKVMDAKKLASLLRGGPGGPLVIDSRSFVEYNSCHVLSSVNICCSKLVKRRLQQGKVTIAELIQPATRSQVDATEPQDVVVYDQSTRDASVLAADSFLSILLSKLDGCFDSVAILTGGFATFSSCFPGLCEGKPATLPSMSLSQPCLPVPSVGLTRILPHLYLGSQKDVLNKDLMTQNGISYVLNASNSCPKPDFICESRFMRIPINDNYCEKLLPWLDKSIEFIDKAKLSSCQVIVHCLAGISRSATIAIAYIMKTMGMSSDDAYRFVKDRRPSISPNFNFLGQLLEYERSLKLLAALQTDGPHLGTPEPLMGPAAGIPLPRLPPSTSESAATGSEAATAAREGSPSAGGDAPIPSTAPATSALQQGLRGLHLSSDRLQDTNRLKRSFSLDIKSAYAPSRRPDFPGPPDPGEAPKLCKLDSPSGGTLGLPSPSPDSPDSVPECRPRPRRRRPPASSPARSPAHGLGLNFGDTARQTPRHGLSALSAPGLPGPGQPAGPGGWVPPLDSPGTPSPDGPWCFSPEGAQGPGAVFSAFGRVSAGAPGPGNSSSSGGGGGGGGGGGGGGGGGGSSSSNSSSSSSSSSSSSSSSSSSSDLRRRDVRTGWPEEPAADAQFKRRSCQMEFEEGMVEGRARGEELAALGKQTSFSGSVEVIEVS | 3.1.3.16; 3.1.3.48 | null | dephosphorylation [GO:0016311]; negative regulation of MAPK cascade [GO:0043409] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | MAP kinase tyrosine phosphatase activity [GO:0033550]; MAP kinase tyrosine/serine/threonine phosphatase activity [GO:0017017]; myosin phosphatase activity [GO:0017018]; phosphatase activity [GO:0016791]; protein tyrosine/threonine phosphatase activity [GO:0008330] | PF00782;PF00581; | 3.90.190.10;3.40.250.10; | Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8733137}. Nucleus {ECO:0000269|PubMed:8733137}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; | null | null | null | null | FUNCTION: Has phosphatase activity with synthetic phosphatase substrates and negatively regulates mitogen-activated protein kinase activity, presumably by catalysing their dephosphorylation (PubMed:7561881). Expected to display protein phosphatase activity toward phosphotyrosine, phosphoserine and phosphothreonine residues (Probable). {ECO:0000269|PubMed:7561881, ECO:0000305}. | Mus musculus (Mouse) |
O09113 | OTP_MOUSE | MLSHADLLDARLGMKDAAELLGHREAVKCRLGVGGSDPGGHPGDLAPNSDPVEGATLLPGEDITTVGSTPASLAVSAKDPDKQPGPQGGPNPSQAGQQQGQQKQKRHRTRFTPAQLNELERSFAKTHYPDIFMREELALRIGLTESRVQVWFQNRRAKWKKRKKTTNVFRAPGTLLPTPGLPQFPSAAAAAAAAMGDSLCSFHANDTRWAAAAMPGVSQLPLPPALGRQQAMAQSLSQCSLAAGPPPNSMGLSNSLAGSNGAGLQSHLYQPAFPGMVPASLPGPSNVSGSPQLCSSPDSSDVWRGTSIASLRRKALEHTVSMSFT | null | null | dopaminergic neuron differentiation [GO:0071542]; forebrain neuron differentiation [GO:0021879]; hypothalamus cell differentiation [GO:0021979]; neuroblast proliferation [GO:0007405]; neuroendocrine cell differentiation [GO:0061101]; neurohypophysis development [GO:0021985]; neuron differentiation [GO:0030182]; positive regulation of neuroblast proliferation [GO:0002052] | fibrillar center [GO:0001650]; nuclear body [GO:0016604] | DNA binding [GO:0003677]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF00046;PF03826; | 1.10.10.60; | Paired homeobox family, Bicoid subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}. | null | null | null | null | null | FUNCTION: Involved in the specification of hypothalamic neuroendocrine cells. Specifically required for the specification of diencephalic dopaminergic neurons of the A11 group. {ECO:0000269|PubMed:10557207, ECO:0000269|PubMed:11071765, ECO:0000269|PubMed:17481897, ECO:0000269|PubMed:7913821}. | Mus musculus (Mouse) |
O09114 | PTGDS_MOUSE | MAALRMLWMGLVLLGLLGFPQTPAQGHDTVQPNFQQDKFLGRWYSAGLASNSSWFREKKAVLYMCKTVVAPSTEGGLNLTSTFLRKNQCETKIMVLQPAGAPGHYTYSSPHSGSIHSVSVVEANYDEYALLFSRGTKGPGQDFRMATLYSRTQTLKDELKEKFTTFSKAQGLTEEDIVFLPQPDKCIQE | 5.3.99.2 | null | gene expression [GO:0010467]; mast cell degranulation [GO:0043303]; negative regulation of male germ cell proliferation [GO:2000255]; prostaglandin biosynthetic process [GO:0001516]; regulation of circadian sleep/wake cycle, sleep [GO:0045187]; response to glucocorticoid [GO:0051384] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; rough endoplasmic reticulum [GO:0005791] | fatty acid binding [GO:0005504]; prostaglandin-D synthase activity [GO:0004667]; retinoid binding [GO:0005501] | PF00061; | 2.40.128.20; | Calycin superfamily, Lipocalin family | null | SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}. | CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin D2; Xref=Rhea:RHEA:10600, ChEBI:CHEBI:57405, ChEBI:CHEBI:57406; EC=5.3.99.2; Evidence={ECO:0000269|PubMed:17715133, ECO:0000269|PubMed:19546224}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 uM for prostaglandin H2 {ECO:0000269|PubMed:19546224}; Vmax=5.9 umol/min/mg enzyme {ECO:0000269|PubMed:19546224}; | null | null | null | FUNCTION: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (PubMed:10781097, PubMed:11751991, PubMed:12077186, PubMed:17715133, PubMed:19546224, PubMed:19833210, PubMed:8922532, PubMed:9892701). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (PubMed:23624557). {ECO:0000269|PubMed:10781097, ECO:0000269|PubMed:11751991, ECO:0000269|PubMed:12077186, ECO:0000269|PubMed:17715133, ECO:0000269|PubMed:19546224, ECO:0000269|PubMed:19833210, ECO:0000269|PubMed:23624557, ECO:0000269|PubMed:8922532, ECO:0000269|PubMed:9892701}. | Mus musculus (Mouse) |
O09118 | NET1_MOUSE | MMRAVWEALAALAAVACLVGAVRGGPGLSMFAGQAAQPDPCSDENGHPRRCIPDFVNAAFGKDVRVSSTCGRPPARYCVVSERGEERLRSCHLCNSSDPKKAHPPAFLTDLNNPHNLTCWQSENYLQFPHNVTLTLSLGKKFEVTYVSLQFCSPRPESMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKQNEQEAVCTDSHTDMRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARDSYYYAVSDLQVGGRCKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKPFHYDRPWQRATAREANECVACNCNLHARRCRFNMELYKLSGRKSGGVCLNCRHNTAGRHCHYCKEGFYRDMGKPITHRKACKACDCHPVGAAGKTCNQTTGQCPCKDGVTGITCNRCAKGYQQSRSPIAPCIKIPVAPPTTAASSVEEPEDCDSYCKASKGKLKMNMKKYCRKDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDIACKCPKIKPLKKYLLLGNAEDSPDQSGIVADKSSLVIQWRDTWARRLRKFQQREKKGKCKKA | null | null | animal organ morphogenesis [GO:0009887]; anterior/posterior axon guidance [GO:0033564]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; axonogenesis [GO:0007409]; B cell mediated immunity [GO:0019724]; B cell proliferation [GO:0042100]; Cdc42 protein signal transduction [GO:0032488]; cell population proliferation [GO:0008283]; cell-cell adhesion [GO:0098609]; chemorepulsion of axon [GO:0061643]; dendrite development [GO:0016358]; glial cell proliferation [GO:0014009]; inner ear morphogenesis [GO:0042472]; mammary gland development [GO:0030879]; mammary gland duct morphogenesis [GO:0060603]; motor neuron axon guidance [GO:0008045]; motor neuron migration [GO:0097475]; negative regulation of axon extension [GO:0030517]; neuron migration [GO:0001764]; nuclear migration [GO:0007097]; positive regulation of axon extension [GO:0045773]; positive regulation of cell motility [GO:2000147]; positive regulation of glial cell proliferation [GO:0060252]; Ras protein signal transduction [GO:0007265]; regulation of cell migration [GO:0030334]; regulation of glial cell migration [GO:1903975]; regulation of synapse assembly [GO:0051963]; substrate adhesion-dependent cell spreading [GO:0034446]; substrate-dependent cell migration, cell extension [GO:0006930]; T cell mediated immunity [GO:0002456]; tissue development [GO:0009888] | actin cytoskeleton [GO:0015629]; basement membrane [GO:0005604]; cell periphery [GO:0071944]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleoplasm [GO:0005654] | cytokine activity [GO:0005125] | PF00053;PF00055;PF01759; | 2.40.50.120;2.60.120.260;2.10.25.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7604039}. Cytoplasm {ECO:0000250|UniProtKB:O95631}. Note=Mainly secreted. {ECO:0000269|PubMed:7604039}. | null | null | null | null | null | FUNCTION: Netrins control guidance of CNS commissural axons and peripheral motor axons. Its association with either DCC or some UNC5 receptors will lead to axon attraction or repulsion, respectively. Binding to UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion (PubMed:28483977). Involved in dorsal root ganglion axon projection towards the spinal cord (PubMed:28483977). It also serves as a survival factor via its association with its receptors which prevent the initiation of apoptosis. Involved in colorectal tumorigenesis by regulating apoptosis (By similarity). {ECO:0000250|UniProtKB:O95631, ECO:0000269|PubMed:10381568, ECO:0000269|PubMed:28483977, ECO:0000269|PubMed:8978605}. | Mus musculus (Mouse) |
O09126 | SEM4D_MOUSE | MRMCAPVRGLFLALVVVLRTAVAFAPVPRLTWEHGEVGLVQFHKPGIFNYSALLMSEDKDTLYVGAREAVFAVNALNISEKQHEVYWKVSEDKKSKCAEKGKSKQTECLNYIRVLQPLSSTSLYVCGTNAFQPTCDHLNLTSFKFLGKSEDGKGRCPFDPAHSYTSVMVGGELYSGTSYNFLGSEPIISRNSSHSPLRTEYAIPWLNEPSFVFADVIQKSPDGPEGEDDKVYFFFTEVSVEYEFVFKLMIPRVARVCKGDQGGLRTLQKKWTSFLKARLICSKPDSGLVFNILQDVFVLRAPGLKEPVFYAVFTPQLNNVGLSAVCAYTLATVEAVFSRGKYMQSATVEQSHTKWVRYNGPVPTPRPGACIDSEARAANYTSSLNLPDKTLQFVKDHPLMDDSVTPIDNRPKLIKKDVNYTQIVVDRTQALDGTFYDVMFISTDRGALHKAVILTKEVHVIEETQLFRDSEPVLTLLLSSKKGRKFVYAGSNSGVVQAPLAFCEKHGSCEDCVLARDPYCAWSPAIKACVTLHQEEASSRGWIQDMSGDTSSCLDKSKESFNQHFFKHGGTAELKCFQKSNLARVVWKFQNGELKAASPKYGFVGRKHLLIFNLSDGDSGVYQCLSEERVRNKTVSQLLAKHVLEVKMVPRTPPSPTSEDAQTEGSKITSKMPVASTQGSSPPTPALWATSPRAATLPPKSSSGTSCEPKMVINTVPQLHSEKTVYLKSSDNRLLMSLLLFIFVLFLCLFSYNCYKGYLPGQCLKFRSALLLGKKTPKSDFSDLEQSVKETLVEPGSFSQQNGDHPKPALDTGYETEQDTITSKVPTDREDSQRIDELSARDKPFDVKCELKFADSDADGD | null | null | axon guidance [GO:0007411]; axonogenesis [GO:0007409]; bone trabecula morphogenesis [GO:0061430]; leukocyte aggregation [GO:0070486]; negative chemotaxis [GO:0050919]; negative regulation of axon extension involved in axon guidance [GO:0048843]; negative regulation of cell adhesion [GO:0007162]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of peptidyl-tyrosine phosphorylation [GO:0050732]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural crest cell migration [GO:0001755]; ossification involved in bone maturation [GO:0043931]; positive regulation of axonogenesis [GO:0050772]; positive regulation of cell migration [GO:0030335]; positive regulation of collateral sprouting [GO:0048672]; positive regulation of inhibitory synapse assembly [GO:1905704]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of Rho protein signal transduction [GO:0035025]; regulation of cell projection organization [GO:0031344]; regulation of cell shape [GO:0008360]; regulation of dendrite morphogenesis [GO:0048814]; semaphorin-plexin signaling pathway [GO:0071526] | extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116] | chemorepellent activity [GO:0045499]; receptor ligand activity [GO:0048018]; semaphorin receptor binding [GO:0030215]; signaling receptor binding [GO:0005102]; transmembrane signaling receptor activity [GO:0004888] | PF00047;PF01437;PF01403; | 2.60.40.10;3.30.1680.10;2.130.10.10; | Semaphorin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8969198}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Cell surface receptor for PLXNB1 and PLXNB2 that plays an important role in cell-cell signaling (By similarity). Regulates GABAergic synapse development (PubMed:23699507, PubMed:29981480). Promotes the development of inhibitory synapses in a PLXNB1-dependent manner (PubMed:23699507, PubMed:29981480). Modulates the complexity and arborization of developing neurites in hippocampal neurons by activating PLXNB1 and interaction with PLXNB1 mediates activation of RHOA (By similarity). Promotes the migration of cerebellar granule cells (PubMed:17554007). Plays a role in the immune system; induces B-cells to aggregate and improves their viability (in vitro) (By similarity). Induces endothelial cell migration through the activation of PTK2B/PYK2, SRC, and the phosphatidylinositol 3-kinase-AKT pathway (By similarity). {ECO:0000250|UniProtKB:Q92854, ECO:0000269|PubMed:17554007, ECO:0000269|PubMed:23699507, ECO:0000269|PubMed:29981480}. | Mus musculus (Mouse) |
O09127 | EPHA8_MOUSE | MAPARARLSPALWVVTAAAAATCVSAGRGEVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNSIPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGACLAILSLRIYYKKCPAMVRNLAAFSEAVTGADSSSLVEVRGQCVRHSEERDTPKMYCSAEGEWLVPIGKCVCSAGYEERRDACMACELGFYKSAPGDQLCARCPPHSHSATPAAQTCRCDLSYYRAALDPPSAACTRPPSAPVNLISSVNGTSVTLEWAPPLDPGGRSDITYNAVCRRCPWALSHCEACGSGTRFVPQQTSLAQASLLVANLLAHMNYSFWIEAVNGVSNLSPEPRSAAVVNITTNQAAPSQVVVIRQERAGQTSVSLLWQEPEQPNGIILEYEIKYYEKDKEMQSYSTLKAVTTRATVSGLKPGTRYVFQVRARTSAGCGRFSQAMEVETGKPRPRYDTRTIVWICLTLITGLVVLLLLLICKKRHCGYSKAFQDSDEEKMHYQNGQAPPPVFLPLNHPPGKFPETQFSAEPHTYEEPGRAGRSFTREIEASRIHIEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALVHSPESLRATATVSRCPPPAFARSCFDLRAGGSGNGDLTVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQLSSTQGPRRHL | 2.7.10.1 | null | axon guidance [GO:0007411]; cell adhesion [GO:0007155]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; ephrin receptor signaling pathway [GO:0048013]; neuron projection development [GO:0031175]; neuron remodeling [GO:0016322]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; protein autophosphorylation [GO:0046777]; regulation of cell adhesion [GO:0030155]; regulation of cell adhesion mediated by integrin [GO:0033628]; substrate-dependent cell migration [GO:0006929] | dendrite [GO:0030425]; early endosome membrane [GO:0031901]; neuron projection [GO:0043005]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ephrin receptor activity [GO:0005003]; GPI-linked ephrin receptor activity [GO:0005004]; growth factor binding [GO:0019838]; transmembrane-ephrin receptor activity [GO:0005005] | PF14575;PF01404;PF00041;PF07714;PF00536; | 2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10; | Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily | PTM: Phosphorylated. Phosphorylation is stimulated upon binding of its ligands including EFNA2, EFNA3 and EFNA5. Autophosphorylation on Tyr-615 is critical for association with FYN. Autophosphorylation on Tyr-838 modulates tyrosine kinase activity. {ECO:0000269|PubMed:10498895, ECO:0000269|PubMed:9053851}.; PTM: Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation. ANKS1A prevents ubiquitination and degradation. {ECO:0000269|PubMed:20100865}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9053851}; Single-pass type I membrane protein {ECO:0000255}. Cell projection {ECO:0000269|PubMed:17875921}. Early endosome membrane {ECO:0000269|PubMed:20496116}. Note=Undergoes clathrin-mediated endocytosis upon EFNA5-binding and is targeted to early endosomes (PubMed:20496116). {ECO:0000269|PubMed:20496116}. | 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:0000255|PROSITE-ProRule:PRU10028}; | null | null | null | null | FUNCTION: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. The GPI-anchored ephrin-A EFNA2, EFNA3, and EFNA5 are able to activate EPHA8 through phosphorylation. With EFNA5 may regulate integrin-mediated cell adhesion and migration on fibronectin substrate but also neurite outgrowth. During development of the nervous system also plays a role in axon guidance. Downstream effectors of the EPHA8 signaling pathway include FYN which promotes cell adhesion upon activation by EPHA8 and the MAP kinases in the stimulation of neurite outgrowth. {ECO:0000269|PubMed:10498895, ECO:0000269|PubMed:11416136, ECO:0000269|PubMed:12681484, ECO:0000269|PubMed:15782114, ECO:0000269|PubMed:17875921, ECO:0000269|PubMed:9214628}. | Mus musculus (Mouse) |
O09130 | NF2IP_MOUSE | MAEPLRGRGPRSRGGRGARRARGARGRCPRARQSPARLIPDTVLVDLVSDSDEEVLEVADPVEVPVARLPAPAKPEQDSDSDSEGAAEGPAGAPRTLVRRRRRRLLDPGEAPVVPVYSGKVQSSLNLIPDNSSLLKLCPSEPEDEADLTNSGSSPSEDDALPSGSPWRKKLRKKCEKEEKKMEEFPDQDISPLPQPSSRNKSRKHTEALQKLREVNKRLQDLRSCLSPKQHQSPALQSTDDEVVLVEGPVLPQSSRLFTLKIRCRADLVRLPVRMSEPLQNVVDHMANHLGVSPNRILLLFGESELSPTATPSTLKLGVADIIDCVVLASSSEATETSQELRLRVQGKEKHQMLEISLSPDSPLKVLMSHYEEAMGLSGHKLSFFFDGTKLSGKELPADLGLESGDLIEVWG | null | null | positive regulation of transcription by RNA polymerase II [GO:0045944] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | null | PF11976; | null | null | PTM: Methylation at the N-terminus by PRMT1 modulates interaction with the NFAT complex and results in augmented cytokine production. {ECO:0000269|PubMed:15327772}. | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=TRAF1 is associated with a fraction of NFATC2IP in the cytoplasm and prevents its translocation to the nucleus. | null | null | null | null | null | FUNCTION: In T-helper 2 (Th2) cells, regulates the magnitude of NFAT-driven transcription of a specific subset of cytokine genes, including IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4 promoter; this leads to enhancement of histone H4 'Arg-3'-methylation and facilitates subsequent histone acetylation at the IL4 locus, thus promotes robust cytokine expression. Down-regulates formation of poly-SUMO chains by UBE2I/UBC9. {ECO:0000269|PubMed:20077568, ECO:0000269|PubMed:20133688}. | Mus musculus (Mouse) |
O09131 | GSTO1_MOUSE | MSGESSRSLGKGSAPPGPVPEGQIRVYSMRFCPFAQRTLMVLKAKGIRHEVININLKNKPEWFFEKNPLGLVPVLENSQGHLVTESVITCEYLDEAYPEKKLFPDDPYKKARQKMTLESFSKVPPLIASFVRSKRKEDSPNLREALENEFKKLEEGMDNYKSFLGGDSPSMVDYLTWPWFQRLEALELKECLAHTPKLKLWMAAMQQDPVASSHKIDAKTYREYLNLYLQDSPEACDYGL | 1.20.4.2; 1.8.5.1; 2.5.1.18 | null | cellular response to arsenic-containing substance [GO:0071243]; glutathione metabolic process [GO:0006749]; L-ascorbic acid biosynthetic process [GO:0019853]; L-ascorbic acid metabolic process [GO:0019852]; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0010880]; xenobiotic catabolic process [GO:0042178] | axon [GO:0030424]; basement membrane [GO:0005604]; cell body [GO:0044297]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear membrane [GO:0031965] | glutathione dehydrogenase (ascorbate) activity [GO:0045174]; glutathione transferase activity [GO:0004364]; methylarsonate reductase activity [GO:0050610]; oxidoreductase activity [GO:0016491] | PF00043;PF13409; | 1.20.1050.10;3.40.30.10; | GST superfamily, Omega family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P78417}. | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:P78417}; CATALYTIC ACTIVITY: Reaction=2 glutathione + L-dehydroascorbate = glutathione disulfide + L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1; Evidence={ECO:0000250|UniProtKB:P78417}; CATALYTIC ACTIVITY: Reaction=2 glutathione + H(+) + methylarsonate = glutathione disulfide + H2O + methylarsonous acid; Xref=Rhea:RHEA:15969, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17826, ChEBI:CHEBI:33409, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.20.4.2; Evidence={ECO:0000250|UniProtKB:P78417}; | null | null | null | null | FUNCTION: Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid. {ECO:0000250|UniProtKB:P78417}. | Mus musculus (Mouse) |
O09139 | E2F1_RAT | MAVAPAGGQHAPALEALLGAGALRLLDSSQIVIISTAPDVGAPQVPTGPAAPPAGPRDPDVLLFATPQAPRPAPSAPRPALGRPPVKRRLDLETDHQYLAGSSGPFRGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSRTMVGIGQRLEGLTQDLQQLQESEQQLDHLMHICTTQLQLLSEDSDIQRLAYVTCQDLRSIADPAEQMVIVIKAPPETQLQAVDSAETFQISLKSKQGPIDVFLCPEESAEGISPGRTSYQETSGEDRNADSGTAGPPPSPPSTSPTLDPSQSLLGLEQEAVLPRIGNLRAPMEEDRLSPLVAADSLLEHVKEDFSGLLPGEFISLSPPHEAVDYHFGLEEGEGIRDLFDCDFGDLTPLDF | null | null | anoikis [GO:0043276]; cellular response to fatty acid [GO:0071398]; cellular response to hypoxia [GO:0071456]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to xenobiotic stimulus [GO:0071466]; DNA damage checkpoint signaling [GO:0000077]; DNA-templated transcription [GO:0006351]; forebrain development [GO:0030900]; G1/S transition of mitotic cell cycle [GO:0000082]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; lens fiber cell apoptotic process [GO:1990086]; mRNA stabilization [GO:0048255]; negative regulation of DNA binding [GO:0043392]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of fat cell proliferation [GO:0070345]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of apoptotic process [GO:0043065]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of gene expression [GO:0010628]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell cycle [GO:0051726]; regulation of DNA-templated transcription [GO:0006355]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of transcription by RNA polymerase II [GO:0006357]; spermatogenesis [GO:0007283] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nuclear chromosome [GO:0000228]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; Rb-E2F complex [GO:0035189]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; molecular adaptor activity [GO:0060090]; protein dimerization activity [GO:0046983]; protein kinase binding [GO:0019901]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976] | PF16421;PF02319; | 6.10.250.540;1.10.10.10; | E2F/DP family | PTM: Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase. Phosphorylation by CHEK2 stabilizes E2F1 upon DNA damage and regulates its effect on transcription and apoptosis. Phosphorylation at Ser-398 by GSK3B promotes interaction with USP11, leading to its deubiquitination and stabilization. {ECO:0000250|UniProtKB:Q01094}.; PTM: Ubiquitinated via 'Lys-63'-linked ubiquitin, leading to its degradation. Deubiquitinated by USP11 follwong phosphorylation by GSK3B, promoting its stability. {ECO:0000250|UniProtKB:Q01094}.; PTM: Acetylation stimulates DNA-binding. Enhanced under stress conditions such as DNA damage and inhibited by retinoblastoma protein RB1. Regulated by KAP1/TRIM28 which recruits HDAC1 to E2F1 resulting in deacetylation (By similarity). {ECO:0000250|UniProtKB:Q01094}.; PTM: Methylation at Lys-183 by SETD7 promotes E2F1 ubiquitin-dependent proteasomal degradation. {ECO:0000250|UniProtKB:Q01094}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01094}. | null | null | null | null | null | FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F1 binds preferentially RB1 in a cell-cycle dependent manner. It can mediate both cell proliferation and TP53/p53-dependent apoptosis. Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters. Directly activates transcription of PEG10. Positively regulates transcription of RRP1B. {ECO:0000250|UniProtKB:Q01094}. | Rattus norvegicus (Rat) |
O09159 | MA2B1_MOUSE | MGTGPLTSGVRAGGGNTGWLWMSSCNLGSPVLPISFLFWLLLAAPGARAAGYKTCPPTKPGMLNVHLLPHTHDDVGWLKTVDQYYYGILSDVQHASVQYILDSVVSSLLEKPTRRFIYVEMAFFSRWWKQQTSATQDAVRNLVRQGRLEFVNGGWVMNDEAATHYGAIVDQMTLGLRFLQDTFGSDGLPRVAWHIDPFGHSREQASLFAQMGFDGFFLGRIDYQDKLNRKKKLRMEELWRASDSLEPPAADLFTGVLPNNYNPPKYLCWDVLCTDPPVVDNPRSPEFNAKTLVNYFLKLASSQKGFYRTNHTVMTMGSDFHYENANMWFKNMDKLIRLVNAQQVNGSLVHVLYSTPTCYLWELNKANLTWTVKEDDFFPYADGPHMFWTGYFSSRPALKRYERLSYNFLQVCNQLEALVGPEANVGPYGSGDSAPLQEAMAVLQHHDAVSGTARQNVVNDYARQLAAGWGPCEVLVSNALARLSHYKQNFSFCRELNISICPVSQTSERFQVTLYNPLGRKVDQMVRLPVYEGNFIVKDPHDKNISSNVVMVPSYYSETYQWELLFPASVPALGFSTYSVAKMSDLNHQAHNLLSRPRKHKSHHVLVIENKYMRATFDSGTGLLMKIENLEQNLSLPVSQGFFWYNASVGDEESSQASGAYIFRPNVGKPIPVSRWAQISLVKTALVQEVHQNFSAWCSQVIRLYKGQRHLELEWTVGPIPVRDDWGKEVISRFDTPMKTKGQFFTDSNGREILKRRDDYRPTWTLNQTEPVAGNYYPVNTRIYITDGQMQLTVLTDRSQGGSSLQDGSLELMVHRRLLVDDDRGVSEPLLETDTGDKVRGRHLVLLSSVSDAAARHRLLAEQEVLAPQVVLSLGGSSPYHSRATPKTQFSGLRQELPPQVHLLTLARWGPKMLLLRLEHQFALKEDSDRNLSSPVTLNVQNLFQTFTINYLQETTLAANQPLSRASRLKWMTNTGPTSYPEPSKLDPTSVTLKPMEIRTFLASVQWQEHRPA | 3.2.1.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | learning or memory [GO:0007611]; mannose metabolic process [GO:0006013]; N-glycan processing [GO:0006491]; oligosaccharide catabolic process [GO:0009313]; protein modification process [GO:0036211] | extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; nucleoplasm [GO:0005654] | alpha-mannosidase activity [GO:0004559]; mannose binding [GO:0005537]; metal ion binding [GO:0046872] | PF09261;PF07748;PF01074;PF21260; | 2.60.40.1360;3.20.110.10;1.20.1270.50;2.60.40.1180; | Glycosyl hydrolase 38 family | null | SUBCELLULAR LOCATION: Lysosome. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.; EC=3.2.1.24; | null | null | null | null | FUNCTION: Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. | Mus musculus (Mouse) |
O09160 | FUT1_MOUSE | MWTPSRRQLCLAFLLVCVLSAGSFFFHLNGGNFFRNGLTLSVLCSDYHLLKSPVAMVCLPHPLQTSNGSPSCPEQSSSLSGTWTITPGGRFGNQMGQYATLLALAQLNGRQAFIQPEMHAALAPVFRISLPVLDPEVDSLTPWQHLVLHDWMSEEYSHLEDPFLKLSGFPCSWTFFHHLREQIRREFTLHNHLREGAQYLLSGLRIGPAGIRPHTFVGVHVRRGDYLEVMPNRWKGVVGDRAYLQQAMDWFRARHKDPIFVVTSNGMKWCLENIDTSHGDVVFAGNGQEGTPGKDFALLTQCNHTIMTIGTFGFWAAYLAGGDTVYLANFTLPDSEFLKIFRPEAAFLPEWVGINADLSPLQAQFDPWKPDSLFRLV | 2.4.1.344; 2.4.1.69 | null | fucosylation [GO:0036065]; lipid metabolic process [GO:0006629]; olfactory bulb development [GO:0021772]; oligosaccharide biosynthetic process [GO:0009312]; 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]; regulation of cell adhesion [GO:0030155]; regulation of endothelial cell proliferation [GO:0001936] | Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580] | alpha-(1,2)-fucosyltransferase activity [GO:0031127]; fucosyltransferase activity [GO:0008417]; galactoside 2-alpha-L-fucosyltransferase activity [GO:0008107] | PF01531; | null | Glycosyltransferase 11 family | null | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305|PubMed:11368156}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000305}. | 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:0000269|PubMed:11368156, ECO:0000269|PubMed:14967068}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48321; Evidence={ECO:0000305|PubMed:11368156}; 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:0000269|PubMed:14967068}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32176; Evidence={ECO:0000305|PubMed:14967068}; 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:0000269|PubMed:14967068}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48305; Evidence={ECO:0000305|PubMed:14967068}; 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:0000250|UniProtKB:F6Q1T7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48293; Evidence={ECO:0000250|UniProtKB:F6Q1T7}; 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:0000250|UniProtKB:F6Q1T7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62965; Evidence={ECO:0000250|UniProtKB:F6Q1T7}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=28.85 mM for phenyl-beta-D-Galactoside {ECO:0000269|PubMed:11368156}; KM=29.09 mM for lactose {ECO:0000269|PubMed:11368156}; KM=0.24 mM for ganglioside GA1 {ECO:0000269|PubMed:11368156}; KM=22.5 uM for ganglioside GA1 {ECO:0000269|PubMed:14967068}; KM=10.8 uM for nLc4Cer {ECO:0000269|PubMed:14967068}; KM=6.2 uM for Lc4Cer {ECO:0000269|PubMed:14967068}; KM=4.3 uM for GM1 {ECO:0000269|PubMed:14967068}; | 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:11368156, PubMed:14967068, PubMed:16884711). 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 (PubMed:16884711). Preferentially fucosylates soluble lactose and to a lesser extent, fucosylates glycolipids gangliosides GA1 and GM1a (PubMed:11368156, PubMed:14967068). {ECO:0000269|PubMed:11368156, ECO:0000269|PubMed:14967068, ECO:0000269|PubMed:16884711}. | Mus musculus (Mouse) |
O09161 | CASQ2_MOUSE | MKRIYLLMVGVYLLSLSGAEEGLNFPTYDGKDRVVSLSEKNLKQMLKRYDLLCLYYHEPVSSDKVSQKQFQLKEIVLELVAQVLEHKNIGFVMVDSRKEAKLAKRLGFSEEGSLYVLKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIVNNKLEVQAFERIEDQTKLLGFFKNEDSEYYKAFQEAAEHFQPYIKFFATFDKAVAKKLSLKMNEVGFYEPFMDEPNVIPNKPYTEEELVEFVKEHQRPTLRRLRPEDMFETWEDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPDLSILWIDPDDFPLLVAYWEKTFKIDLFKPQIGVVNVTDADSIWMEIPDDDDLPTAEELEDWIEDVLSGKINTEDDDNEDEDDDGDDNDDDDDDDDDNDNSDEDNEDSDDDDDDDE | null | null | negative regulation of potassium ion transmembrane transporter activity [GO:1901017]; negative regulation of potassium ion transport [GO:0043267]; regulation of cardiac muscle cell contraction [GO:0086004]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]; regulation of heart rate [GO:0002027]; regulation of membrane repolarization [GO:0060306]; regulation of muscle contraction [GO:0006937]; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0010880]; sarcomere organization [GO:0045214] | junctional membrane complex [GO:0030314]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum lumen [GO:0033018]; Z disc [GO:0030018] | calcium ion binding [GO:0005509]; protein homodimerization activity [GO:0042803]; protein kinase C binding [GO:0005080] | PF01216; | 3.40.30.10; | Calsequestrin family | PTM: Phosphorylation in the C-terminus moderately increases calcium buffering capacity. {ECO:0000250|UniProtKB:O14958}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:O14958}. | SUBCELLULAR LOCATION: Sarcoplasmic reticulum lumen {ECO:0000269|PubMed:16932808, ECO:0000269|PubMed:19920148}. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells. {ECO:0000269|PubMed:16932808, ECO:0000269|PubMed:19920148}. | null | null | null | null | null | FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats. {ECO:0000269|PubMed:16932808, ECO:0000269|PubMed:17607358, ECO:0000269|PubMed:19920148}. | Mus musculus (Mouse) |
O09164 | SODE_MOUSE | MLAFLFYGLLLAACGSVTMSNPGESSFDLADRLDPVEKIDRLDLVEKIGDTHAKVLEIWMELGRRREVDAAEMHAICRVQPSATLPPDQPQITGLVLFRQLGPGSRLEAYFSLEGFPAEQNASNRAIHVHEFGDLSQGCDSTGPHYNPMEVPHPQHPGDFGNFVVRNGQLWRHRVGLTASLAGPHAILGRSVVVHAGEDDLGKGGNQASLQNGNAGRRLACCVVGTSSSAAWESQTKERKKRRRESECKTT | 1.15.1.1 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; Note=Binds 1 copper ion per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | blood vessel diameter maintenance [GO:0097746]; removal of superoxide radicals [GO:0019430]; response to copper ion [GO:0046688]; response to hypoxia [GO:0001666] | collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796] | copper ion binding [GO:0005507]; superoxide dismutase activity [GO:0004784] | PF00080; | 2.60.40.200; | Cu-Zn superoxide dismutase family | null | SUBCELLULAR LOCATION: Secreted, extracellular space. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:16371425}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000305|PubMed:16371425}; | null | null | null | null | FUNCTION: Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen. {ECO:0000250}. | Mus musculus (Mouse) |
O09165 | CASQ1_MOUSE | MRATDRMGARAVSELRLALLFVLVLGTPRLGVQGEDGLDFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKKLGLTEEDSVYVFKGDEVIEYDGEFSADTLVEFLLDVLEDPVELIEGERELQAFENIEDEIKLIGYFKSKDSEHYKAYEDAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPMTIPDKPNSEEEIVSFVEEHRRSTLRKLKPESMYETWEDDLDGIHIVAFAEEADPDGYEFLETLKAVAQDNTENPDLSIIWIDPDDFPLLVPYWEKTFDIDLSAPQIGVVNVTDADSIWMEMDNEEDLPSADELEDWLEDVLEGEINTEDDDDDDDDDDDDDDDDD | null | null | endoplasmic reticulum organization [GO:0007029]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of store-operated calcium channel activity [GO:1901341]; protein polymerization [GO:0051258]; regulation of muscle contraction [GO:0006937]; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0010880]; regulation of sequestering of calcium ion [GO:0051282]; regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion [GO:0014809]; regulation of store-operated calcium entry [GO:2001256]; response to denervation involved in regulation of muscle adaptation [GO:0014894]; response to heat [GO:0009408]; response to organic substance [GO:0010033]; sarcomere organization [GO:0045214]; skeletal muscle tissue development [GO:0007519] | I band [GO:0031674]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; myofibril [GO:0030016]; sarcolemma [GO:0042383]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum lumen [GO:0033018]; sarcoplasmic reticulum membrane [GO:0033017]; T-tubule [GO:0030315]; terminal cisterna [GO:0014802]; terminal cisterna lumen [GO:0014804]; Z disc [GO:0030018] | calcium ion binding [GO:0005509]; identical protein binding [GO:0042802] | PF01216; | 3.40.30.10; | Calsequestrin family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P07221}. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum lumen {ECO:0000269|PubMed:22049211, ECO:0000269|PubMed:7945294}. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P07221}. Mitochondrion matrix {ECO:0000269|PubMed:7945294}. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of fast skeletal muscle cells (PubMed:22049211). Preferentially forms linear and round aggregates in the endoplasmic reticulum (ER) of resting cells. In a minority of cells, homogeneously detected in the ER lumen. Colocalizes with STIM1 at endoplasmic reticulum in response to a depletion of intracellular calcium (By similarity). {ECO:0000250|UniProtKB:P31415, ECO:0000269|PubMed:22049211}. | null | null | null | null | null | FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions (By similarity). Regulates the release of lumenal Ca(2+) via the calcium release channel RYR1; this plays an important role in triggering muscle contraction. Negatively regulates store-operated Ca(2+) entry (SOCE) activity (By similarity). {ECO:0000250|UniProtKB:P31415, ECO:0000269|PubMed:17627988, ECO:0000269|PubMed:22049211, ECO:0000269|PubMed:7945294}. | Mus musculus (Mouse) |
O09171 | BHMT1_RAT | MAPIAGKKAKRGILERLNAGEVVIGDGGFVFALEKRGYVKAGPWTPEAAVEHPEAVRQLHREFLRAGSNVMQTFTFYASEDKLENRGNYVAEKISGQKVNEAACDIARQVADEGDALVAGGVSQTPSYLSCKSETEVKKIFHQQLEVFMKKNVDFLIAEYFEHVEEAVWAVEALKTSGKPIAATMCIGPEGDLHGVSPGECAVRLVKAGAAIVGVNCHFDPSTSLQTIKLMKEGLEAARLKAYLMSHALAYHTPDCGKQGFIDLPEFPFGLEPRVATRWDIQKYAREAYNLGVRYIGGCCGFEPYHIRAIAEELAPERGFLPPASEKHGSWGSGLDMHTKPWIRARARKEYWQNLRIASGRPYNPSMSKPDAWGVTKGAAELMQQKEATTEQQLRALFEKQKFKSAQ | 2.1.1.5 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; | 'de novo' L-methionine biosynthetic process [GO:0071266]; amino-acid betaine catabolic process [GO:0006579]; amino-acid betaine metabolic process [GO:0006577]; L-methionine salvage [GO:0071267]; methionine biosynthetic process [GO:0009086]; methylation [GO:0032259]; response to organonitrogen compound [GO:0010243] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | betaine-homocysteine S-methyltransferase activity [GO:0047150]; identical protein binding [GO:0042802]; methyltransferase activity [GO:0008168]; protein-containing complex binding [GO:0044877]; zinc ion binding [GO:0008270] | PF02574; | 3.20.20.330; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12487625, ECO:0000269|PubMed:28288879}. Nucleus {ECO:0000269|PubMed:28288879}. Note=Predominantly localized in the cytoplasm with a small fraction detected in the nucleus. Translocates into the nucleus upon oxidative stress. {ECO:0000269|PubMed:28288879}. | CATALYTIC ACTIVITY: Reaction=glycine betaine + L-homocysteine = L-methionine + N,N-dimethylglycine; Xref=Rhea:RHEA:22336, ChEBI:CHEBI:17750, ChEBI:CHEBI:57844, ChEBI:CHEBI:58199, ChEBI:CHEBI:58251; EC=2.1.1.5; Evidence={ECO:0000269|PubMed:12487625, ECO:0000269|PubMed:28288879}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22337; Evidence={ECO:0000305|PubMed:12487625, ECO:0000305|PubMed:28288879}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=106.4 uM for L-homocysteine {ECO:0000269|PubMed:12487625}; KM=333.3 uM for glycine betaine {ECO:0000269|PubMed:12487625}; Vmax=18.67 nmol/min/mg enzyme (L-methionine biosynthesis) {ECO:0000269|PubMed:12487625}; | PATHWAY: Amine and polyamine degradation; betaine degradation; sarcosine from betaine: step 1/2.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (BhmT route): step 1/1. {ECO:0000305|PubMed:12487625}. | null | null | FUNCTION: Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline. {ECO:0000269|PubMed:12487625, ECO:0000269|PubMed:28288879}. | Rattus norvegicus (Rat) |
O09172 | GSH0_MOUSE | MGTDSRAAGALLARASTLHLQTGNLLNWGRLRKKCPSTHSEELRDCIQKTLNEWSSQISPDLVREFPDVLECTMSHAVEKINPDEREEMKVSAKLFIVGSNSSSSTRSAVDMACSVLGVAQLDSVIMASPPIEDGVNLSLEHLQPYWEELENLVQSKKIVAIGTSDLDKTQLEQLYQWAQVKPNSNQVNLASCCVMPPDLTAFAKQFDIQLLTHNDPKELLSEASFQEALQESIPDIEAQDWVPLWLLRYSVIVKSRGIIKSKGYILQAKRRGS | null | null | apoptotic mitochondrial changes [GO:0008637]; blood vessel diameter maintenance [GO:0097746]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to glucose stimulus [GO:0071333]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to thyroxine stimulus [GO:0097069]; cysteine metabolic process [GO:0006534]; glutamate metabolic process [GO:0006536]; glutathione biosynthetic process [GO:0006750]; glutathione metabolic process [GO:0006749]; hepatic stellate cell activation [GO:0035733]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of mitochondrial depolarization [GO:0051900]; response to activity [GO:0014823]; response to human chorionic gonadotropin [GO:0044752]; response to nitrosative stress [GO:0051409]; response to nutrient [GO:0007584]; response to oxidative stress [GO:0006979]; response to xenobiotic stimulus [GO:0009410] | glutamate-cysteine ligase complex [GO:0017109] | enzyme regulator activity [GO:0030234]; glutamate-cysteine ligase activity [GO:0004357]; glutamate-cysteine ligase catalytic subunit binding [GO:0035226]; protein-containing complex binding [GO:0044877] | PF00248; | 3.20.20.100; | Aldo/keto reductase family, Glutamate--cysteine ligase light chain subfamily | null | null | null | null | PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2. | null | null | null | Mus musculus (Mouse) |
O09173 | HGD_MOUSE | MAELKYISGFGNECASEDPRCPGSLPKGQNNPQVCPYNLYAEQLSGSAFTCPRNTNKRSWLYRILPSVSHKPFESIDQGHVTHNWDEVGPDPNQLRWKPFEIPKASEKKVDFVSGLYTLCGAGDIKSNNGLAVHIFLCNSSMENRCFYNSDGDFLIVPQKGKLLIYTEFGKMSLQPNEICVIQRGMRFSVDVFEETRGYILEVYGVHFELPDLGPIGANGLANPRDFLIPVAWYEDRRVPGGYTVINKFQGKLFACKQDVSPFNVVAWHGNYTPYKYNLENFMVINAVAFDHADPSIFTVLTAKSLRPGVAIADFVIFPPRWGVADKTFRPPYYHRNCMSEFMGLIKGHYEAKQGGFLPGGGSLHSAMTPHGPDADCFEKASKAKLEPERIADGTMAFMFESSLSLAVTKWGLKTCSCLDENYYKCWEPLRSHFTPNSRSPTEPK | 1.13.11.5 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:7705358}; | amino acid metabolic process [GO:0006520]; L-phenylalanine catabolic process [GO:0006559]; tyrosine catabolic process [GO:0006572] | cytoplasm [GO:0005737] | homogentisate 1,2-dioxygenase activity [GO:0004411]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF04209;PF20510; | 2.60.120.10; | Homogentisate dioxygenase family | null | null | CATALYTIC ACTIVITY: Reaction=homogentisate + O2 = 4-maleylacetoacetate + H(+); Xref=Rhea:RHEA:15449, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16169, ChEBI:CHEBI:17105; EC=1.13.11.5; Evidence={ECO:0000269|PubMed:7705358}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15450; Evidence={ECO:0000269|PubMed:7705358}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=188 uM for homogentisate {ECO:0000269|PubMed:7705358}; | PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 4/6. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.1. {ECO:0000269|PubMed:7705358}; | null | FUNCTION: Catalyzes the conversion of homogentisate to maleylacetoacetate. {ECO:0000269|PubMed:7705358}. | Mus musculus (Mouse) |
O09174 | AMACR_MOUSE | MVLRGVRVVELAGLAPGPFCGMVLADFGAEVVRVNRLGSTGENFLARGKRSLALDLKRSQGVTVLRRMCARADVLLEPFRCGVMEKLQLGPETLLQDNPKLIYARLSGFGQSGIFSKVAGHDINYLALSGVLSKIGRSGENPYPPLNLLADFGGGGLMCTLGIVLALFERTRSGRGQVIDSSMVEGTAYLSSFLWKTQPMGLWKQPRGQNILDGGAPFYTTYKTADGEFMAVGAIEPQFYALLLKGLGLESEELPSQMSSADWPEMKKKFADVFAKKTKAEWCQIFDGTDACVTPVLTFEEALHHQHNRERASFITDGEQLPSPRPAPLLSRTPAVPSAKRDPSVGEHTVEVLREYGFSQEEILQLHSDRIVESDKLKANL | 5.1.99.4 | null | bile acid biosynthetic process [GO:0006699]; bile acid metabolic process [GO:0008206]; fatty acid metabolic process [GO:0006631]; isoprenoid catabolic process [GO:0008300] | mitochondrion [GO:0005739]; peroxisome [GO:0005777]; plasma membrane [GO:0005886] | alpha-methylacyl-CoA racemase activity [GO:0008111] | PF02515; | 3.30.1540.10; | CoA-transferase III family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10770938}. Mitochondrion {ECO:0000269|PubMed:10770938}. | CATALYTIC ACTIVITY: Reaction=a (2S)-2-methylacyl-CoA = a (2R)-2-methylacyl-CoA; Xref=Rhea:RHEA:12657, ChEBI:CHEBI:57313, ChEBI:CHEBI:57314; EC=5.1.99.4; Evidence={ECO:0000250|UniProtKB:Q9UHK6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12658; Evidence={ECO:0000250|UniProtKB:Q9UHK6}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12659; Evidence={ECO:0000250|UniProtKB:Q9UHK6}; CATALYTIC ACTIVITY: Reaction=(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA = (25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA; Xref=Rhea:RHEA:40455, ChEBI:CHEBI:58677, ChEBI:CHEBI:77251; Evidence={ECO:0000250|UniProtKB:Q9UHK6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40456; Evidence={ECO:0000250|UniProtKB:Q9UHK6}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:40457; Evidence={ECO:0000250|UniProtKB:Q9UHK6}; CATALYTIC ACTIVITY: Reaction=(2R,6)-dimethylheptanoyl-CoA = (2S,6)-dimethylheptanoyl-CoA; Xref=Rhea:RHEA:46732, ChEBI:CHEBI:86982, ChEBI:CHEBI:86983; Evidence={ECO:0000250|UniProtKB:Q9UHK6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46733; Evidence={ECO:0000250|UniProtKB:Q9UHK6}; | null | PATHWAY: Lipid metabolism; bile acid biosynthesis.; PATHWAY: Lipid metabolism; fatty acid metabolism. | null | null | FUNCTION: Catalyzes the interconversion of (R)- and (S)-stereoisomers of alpha-methyl-branched-chain fatty acyl-CoA esters (By similarity). Acts only on coenzyme A thioesters, not on free fatty acids, and accepts as substrates a wide range of alpha-methylacyl-CoAs, including pristanoyl-CoA, trihydroxycoprostanoyl-CoA (an intermediate in bile acid synthesis), and arylpropionic acids like the anti-inflammatory drug ibuprofen (2-(4-isobutylphenyl)propionic acid) but neither 3-methyl-branched nor linear-chain acyl-CoAs (By similarity). {ECO:0000250|UniProtKB:Q9UHK6}. | Mus musculus (Mouse) |
O09175 | AMPB_RAT | MESSGPSSCHSAARRPLHSAQAVDVASASSFRAFEILHLHLDLRAEFGPPGPGPGSRGLNGKATLELRCLLPEGASELRLDSHSCLEVMAATLLRGQPGDQQQLTEPVPFHTQPFSHYGQALCVVFPKPCCAAERFRLELTYRVGEGPGVCWLAPEQTAGKKKPFVYTQGQAVLNRAFFPCFDTPAVKCTYSALVEVPDGFTAVMSASTWERRGPNKFFFQMSQPIPSYLIALAIGDLASAEVGPRSRVWAEPCLIEAAKEEYNGVIEEFLATGEKLFGPYVWGRYDLLFMPPSFPFGGMENPCLTFVTPCLLAGDRSLADVIIHEISHSWFGNLVTNANWGEFWLNEGFTMYAQRRISTILFGAAYTCLEAATGRALLRQHMDVSGEENPLNKLRVKIEPGVDPDDTYNETPYEKGYCFVSYLAHLVGDQEQFDKFLKAYVDEFKFQSILAEDFLEFYLEYFPELKKKGVDSIPGFEFNRWLNTPGWPPYLPDLSPGDSLMKPAEELAELWAASEPDMQAIEAVAISTWKTYQLVYFLDKILQKSPLPPGNVKKLGETYPKISNAQNAELRLRWGQIILKNDHQEEFWKVKDFLQSQGKQKYTLPLYHAMMGGSEMARTLAKETFSATASQLHSNVVNYVQQILAPKGS | 3.4.11.6 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | negative regulation of blood pressure [GO:0045776]; protein processing [GO:0016485]; proteolysis [GO:0006508]; retina development in camera-type eye [GO:0060041] | external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; secretory granule [GO:0030141] | aminopeptidase activity [GO:0004177]; cobalt ion binding [GO:0050897]; copper ion binding [GO:0005507]; metalloaminopeptidase activity [GO:0070006]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270] | PF09127;PF01433;PF17900; | 3.30.2010.30;1.10.390.10;1.25.40.320;2.60.40.1730; | Peptidase M1 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.; EC=3.4.11.6; | null | null | null | null | FUNCTION: Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4). | Rattus norvegicus (Rat) |
O09185 | P53_CRIGR | MEEPQSDLSIELPLSQETFSDLWKLLPPNNVLSTLPSSDSIEELFLSENVTGWLEDSGGALQGVAAAAASTAEDPVTETPAPVASAPATPWPLSSSVPSYKTYQGDYGFRLGFLHSGTAKSVTCTYSPSLNKLFCQLAKTCPVQLWVNSTPPPGTRVRAMAIYKKLQYMTEVVRRCPHHERSSEGDSLAPPQHLIRVEGNLHAEYLDDKQTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDPSGNLLGRNSFEVRICACPGRDRRTEEKNFQKKGEPCPELPPKSAKRALPTNTSSSPPPKKKTLDGEYFTLKIRGHERFKMFQELNEALELKDAQASKGSEDNGAHSSYLKSKKGQSASRLKKLMIKREGPDSD | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | cell cycle [GO:0007049]; cellular senescence [GO:0090398]; circadian behavior [GO:0048512]; DNA damage response [GO:0006974]; entrainment of circadian clock by photoperiod [GO:0043153]; negative regulation of cell growth [GO:0030308]; negative regulation of DNA-templated transcription [GO:0045892]; nucleotide-excision repair [GO:0006289]; oligodendrocyte apoptotic process [GO:0097252]; positive regulation of apoptotic process [GO:0043065]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein tetramerization [GO:0051262] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]; PML body [GO:0016605] | ATP-dependent DNA/DNA annealing activity [GO:0036310]; copper ion binding [GO:0005507]; DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00870;PF08563;PF07710; | 2.60.40.720;6.10.50.20;4.10.170.10; | P53 family | PTM: Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylation at Ser-9 by HIPK4 increases repression activity on BIRC5 promoter (By similarity). Phosphorylated on Thr-18 by VRK1, which may prevent the interaction with MDM2. Phosphorylated on Ser-20 by CHEK2 in response to DNA damage, which prevents ubiquitination by MDM2. Phosphorylated on Ser-20 by PLK3 in response to reactive oxygen species (ROS), promoting p53/TP53-mediated apoptosis. Phosphorylated on Ser-33 by CDK7 in a CAK complex in response to DNA damage. Phosphorylated by HIPK1. Phosphorylated on Ser-392 following UV but not gamma irradiation. Stabilized by CDK5-mediated phosphorylation in response to genotoxic and oxidative stresses at Ser-15, Ser-33 and Ser-47, leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes. Phosphorylated by DYRK2 at Ser-47 in response to genotoxic stress. Phosphorylated at Ser-315 and Ser-392 by CDK2 in response to DNA-damage (By similarity). Phosphorylation at Ser-15 is required for interaction with DDX3X and gamma-tubulin (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P04637}.; PTM: Monomethylated at Lys-372 by SETD7, leading to stabilization and increased transcriptional activation. Monomethylated at Lys-370 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity. Lys-372 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-370. Dimethylated at Lys-373 by EHMT1 and EHMT2. Monomethylated at Lys-382 by KMT5A, promoting interaction with L3MBTL1 and leading to repress transcriptional activity. Demethylation of dimethylated Lys-370 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation (By similarity). Monomethylated at Arg-333 and dimethylated at Arg-337 by PRMT5; methylation is increased after DNA damage and might possibly affect TP53 target gene specificity (By similarity). {ECO:0000250|UniProtKB:P04637}.; PTM: Sumoylated with SUMO1. Sumoylated at Lys-386 by UBC9 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal degradation. Ubiquitinated by RFWD3, which works in cooperation with MDM2 and may catalyze the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome. Ubiquitinated by MKRN1, which leads to proteasomal degradation. Deubiquitinated by USP10, leading to stabilize it. Ubiquitinated by TRIM24, RFFL, RNF34 and RNF125, which leads to proteasomal degradation. Ubiquitination by TOPORS induces degradation. Deubiquitination by USP7, leading to stabilize it. Ubiquitinated by COP1, which leads to proteasomal degradation (By similarity). Ubiquitination and subsequent proteasomal degradation is negatively regulated by CCAR2 (By similarity). Polyubiquitinated by C10orf90/FATS, polyubiquitination is 'Lys-48'-linkage independent and non-proteolytic, leading to TP53 stabilization (By similarity). Polyubiquitinated by MUL1 at Lys-24 which leads to proteasomal degradation (By similarity). Deubiquitinated by USP3, leading to stabilization (By similarity). Ubiquitinated by MSL2, promoting its cytoplasmic localization (By similarity). {ECO:0000250|UniProtKB:P02340, ECO:0000250|UniProtKB:P04637}.; PTM: Acetylation of Lys-382 by CREBBP enhances transcriptional activity. Acetylation of Lys-382 by EP300. Deacetylation of Lys-382 by SIRT1 impairs its ability to induce proapoptotic program and modulate cell senescence. Deacetylation by SIRT2 impairs its ability to induce transcription activation in a AKT-dependent manner. Acetylation at Lys-381 increases stability. Deacetylation at Lys-381 by SIRT6 decreases its stability, thereby regulating cell senescence. Acetylated at Lys-120 by KAT5, KAT6A and KAT8; regulating its ability to induce proapoptotic program. {ECO:0000250|UniProtKB:P04637}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04637}. Nucleus {ECO:0000250|UniProtKB:P04637}. Nucleus, PML body {ECO:0000250|UniProtKB:P04637}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P04637}. Mitochondrion matrix {ECO:0000250|UniProtKB:P04637}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04637}. Note=Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2. Translocates to mitochondria upon oxidative stress. Translocates to mitochondria in response to mitomycin C treatment (By similarity). Competitive inhibition of TP53 interaction with HSPA9/MOT-2 by UBXN2A results in increased protein abundance and subsequent translocation of TP53 to the nucleus (By similarity). {ECO:0000250|UniProtKB:P04637}. | null | null | null | null | null | FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (By similarity). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (By similarity). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2. {ECO:0000250|UniProtKB:P02340, ECO:0000250|UniProtKB:P04637}. | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
O09198 | MAL_MOUSE | MAPAAASGGSTLPSGFSVFTTFPDLLFVCEFVFGGLVWILIASSLVPLPLAQGWVMFVSVFCFVATTSLMILYIIGTHGGETSWITLDAAYHCVAALFYLSASVLEALATISMFDGFTYKHYHENIAAVVFAYVVTLIYVVHAVFSLIRWKSS | null | null | central nervous system myelination [GO:0022010]; myelination [GO:0042552]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; protein insertion into plasma membrane [GO:0098737]; protein localization to paranode region of axon [GO:0002175] | apical plasma membrane [GO:0016324]; endoplasmic reticulum [GO:0005783]; Golgi membrane [GO:0000139]; hinge region between urothelial plaques of apical plasma membrane [GO:0120003]; membrane raft [GO:0045121]; plasma membrane raft [GO:0044853]; Schmidt-Lanterman incisure [GO:0043220] | structural constituent of myelin sheath [GO:0019911] | PF01284; | null | MAL family | PTM: Lipoprotein. {ECO:0000250}. | SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Note=Found in lipid raft. | null | null | null | null | null | FUNCTION: Could be an important component in vesicular trafficking cycling between the Golgi complex and the apical plasma membrane. Plays a role in the maintenance of the myelin sheath and in axon-glia and glia-glia interactions. {ECO:0000269|PubMed:15337780}. | Mus musculus (Mouse) |
O09232 | HBB_MELAE | MVEWTDDERAIINGIFSNLDYEEIGRKSLCRCLIVYPWTQRYFGGFGNLYNAETILCNPLIAAHGTKILHGLDRALKNMDDIKNTYAELSLLHSDKLHVDPDNFRLLADCLTVVIAAKMGAAFTVDTQVAWQKFLAVVVSALGRQYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues. | Melanogrammus aeglefinus (Haddock) (Gadus aeglefinus) |
O09460 | PCKA_ANASU | MSLSESLAKYGITGATNIVHNPSHEELFAAETQASLEGFEKGTVTEMGAVNVMTGVYTGRSPKDKFIVKNEASKEIWWTSDEFKNDNKPVTEEAWAQLKALAGKELSNKPLYVVDLFCGANENTRLKIRFVMEVAWQAHFVTNMFIRPTEEELKGFEPDFVVLNASKAKVENFKELGLNSETAVVFNLAEKMQIILNTWYGGEMKKGMFSMMNFYLPLQGIAAMHCSANTDLEGKNTAIFFGLSGTGKTTLSTDPKRLLIGDDEHGWDDDGVFNFEGGCYAKVINLSKENEPDIWGAIKRNALLENVTVDANGKVDFADKSVTENTRVSYPIFHIKNIVKPVSKAPAAKRVIFLSADAFGVLPPVSILSKEQTKYYFLSGFTAKLAGTERGITEPTPTFSSCFGAAFLTLPPTKYAEVLVKRMEASGAKAYLVNTGWNGTGKRISIKDTRGIIDAILDGSIDTANTATIPYFNFTVPTELKGVDTKILDPRNTYADASEWEVKAKDLAERFQKNFKKFESLGGDLVKAGPQL | 4.1.1.49 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:8436945}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:8436945}; | gluconeogenesis [GO:0006094] | cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphoenolpyruvate carboxykinase (ATP) activity [GO:0004612] | PF01293; | 3.90.228.20;3.40.449.10;2.170.8.10; | Phosphoenolpyruvate carboxykinase (ATP) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00453}. | CATALYTIC ACTIVITY: Reaction=ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate; Xref=Rhea:RHEA:18617, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; EC=4.1.1.49; Evidence={ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.42 mM for ADP (at 37 degrees Celsius and at pH 6.2) {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347}; KM=0.54 mM for PEP (at 37 degrees Celsius and at pH 6.2) {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347}; KM=1.2 mM for OAA (at 37 degrees Celsius and at pH 6.2) {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347}; KM=2.3 mM for ATP (at 37 degrees Celsius and at pH 6.2) {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347}; KM=17 mM for bicarbonate (at 37 degrees Celsius and at pH 6.2) {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347}; Vmax=10 umol/min/mg enzyme (at 37 degrees Celsius and at pH 6.2) {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347}; | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000255|HAMAP-Rule:MF_00453}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 6.7 and 7.1. The enzyme is stable from pH 5.0 to 9.0. It completely losing activity at pH values lower than 4.5 and retaining some activity in the pH range 9-12. {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347}; | null | FUNCTION: Involved in gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA (By similarity). {ECO:0000250, ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347}. | Anaerobiospirillum succiniciproducens |
O11436 | POLG_RGMVD | MMNFGSLNVGLKQVDGTWVPRVFEEKEMARLLAEKQHARVMRATQEMMKAPNPFAEFDEMHQRGNPFAGRVRKCETREPKSAQKPIVTVDTVPVAIYTDVIWPENGKVHALSRRRAPRKHARRSKILACDLLTQVLNISRRAGKSVEVIGKRRCCLKPRRRDGKSCFGVITKHHKGVLSSRDMVKDLFVDSIIEHIAYTGHTPLIDAADIKPGDSGLIYREKKDGYVTRVVRGRHDGDIIDARDYVRAGIHTIKHYSDDGKSLVKYAPYCQPSHHTFGHMCRVTWSDTEILQFREMLSQAIMPQRDPRCDICAEVAGQRTKDEILQHARTSQMMQMLEFGKEDERWKAPRRVMETLLEESNWPSMDYSTSSEITTICCGNNDEPFRRIYSIMKVLAEPNLADVSAWQEANSSLLQLARYMKNREMSVQAGNSATFTNPFPPTVHTFGPTNNGADILQGPWDNWGDKQPIALAFFEKHFNKWQINEFSIDRRVRKHIRGTRKLALMDLNQSRSIKDLEDHVQEEEIPYERKTESCITMYKDQYLYSCSCVTARDGKPYLSMRYLQATGLIPIARGADVQHMPNSDSWQGFYYVAPEGYCYINIFLPMLALAPYYKVGKLSELIGKLIKVLGKWPKLKDVALACLYITEYHTYAQNALLPPILVHHSTRTMHVVDTLGSLSVGYHVLKAGTVKHLVNLASRLATGEMLDYNVGGSLGGIHAYDLLIRSTFDHVLLERALETDPYYILYSALSPTVLKQMYTSKSYANALRVFVRSNQSLFQVVCTLENLARRMTRAQSIEQQIMQLQSLYPQLLDMLADNIPDSPLSWLSHHVTTDSMQRAIELNNCDIELARGGYASINTSWRKKKEQYYADLIKEYYNALSPQAKIFVSRAYIGYLHATTPLFANARKISSEIASNICTQAYSRTIGRGISIVSSGGRKGKTWLTARGDSFYKTMISRAIKLYTPEVSAVIGVATVVGILLSTMTTLHTYLVKNKQTAQKTNEKFEELMYDKVALYIPKYDAEHSHLQGKDLDFEHFARWLMARDKKLSSFVQSHLVDTVTHQAKDDTNVWIEKCIATIVLMMMAIDSNKSDKLYQILCKLRTVFSTMGQTVVTHQSIDEILDIDESKRTTIDFERVEVMQPTQPILKTTFEGFWDMQIQMGRTVAHYRTTGRLVELTRENIAEVVATISSDTANAEFIVRGGVGTGKSTSLPTALCERGRVLMLEPTRPLTENVAQQLRGEPHFKSPSVHMRGLNTFGSSRITIMTSGYALHYYANNRQLLRDFEFIMFDECHVMDSSAMAFYSLCNDAKVAAKLLKVSATPAGRECEFKPMFPVRVSEAAQLSFESFVTAQGSKSTYDIIQYGNNILVYVASYNEVDKLAAMLLEKRFRVTKVDGRTMKLNTHGIELHGTAQVKHFIVATNIIENGVTLEIDCLVDFGTKVVAQLDTEGRRIMYMKVPISYGERIQRLGRVGRTKPGARLKVGHTMRGIVEIPEVIATEAAFQCFMYDLPVMTGQVSVSLLSKCTREQARTMAAFELSPFTMSNLVAFDGTMHPAIHDLLKKFKLRDSTVVLRRTALPLRASASWYTVREYETIIGDLHIENKDVRIPFVANDLSNSLLEGLWDAIQCNRSDVSTTKLTTVSANKIAYTLKTDTSSIQRTISIIDDLLAEERKKQEMFTHHLSTTSGGYTFGLNAIAMCIKSRYAKGYCIENIATLTNVRNQLTEFSGMSEDQYTSEIIQNYPDLTLVHHQSKQEIIRNLKLKAKYDQTLIASDLLLGTAVLIGGGAMLYKTFMTETNTRVHLEGDGKRQREKLQYRAARDSKQDYEVYADEREIQENYGEAYTKHGRKGPAHEKGTGSKTREFTNFYGFDPAEYDTVRLVDPITGKTCDKAVRDLLRMRDVADTFAEIRESMDEDMILQPGVNFAPALIEAYFMNSRTNAARRVDLVPHNPMQVGRLSNNIAGFPTHDGELRQSRPSRPIQKDQVPAANEYSVQHESKSIAKGLRDYHPVSSNLCALEYYCGDMRTSIYGVCYGPYILTTAHLIKEKGGWLKIRTKHGLFKLEAMDRVQIRELCGSDIIVIKGPKDMPPAPMRLKFRAPKSGERAVLVGFVDDNLDRQLVSDSSAVYRRENTGFWKHWITTKYGNCGLPMVSVDTMDIIGLHSLGAQNSNENYFAALTDDFSKQFFEPETDVPWQRKWSYNADKVNYGTMDLTSNQPSGAFKTTKLLEDLLEAVSHQSQEYTWLTKYCGANLLVIGKCPGNLITKHVIKGKSPTFDLFLSVDAQASDFFKPLMGDYAPSRLNREAFVKDITKYDTEIPIGNLSITDFENAVEDTYYILKDSGIEQCNYITDAIPIFDSMNMKAATGALYGGKKKDYFENYTDDMKQNILKESYIRLREGKMGIWNGSLKAELRSKEKVEANKTRVFTAAPLDTLLAGKGCVDDFNNQFYAAHLKGPWTVGITKFFGRWNDFLSELPPGWDYFDADGSRFDSSLTPFLLNAVLNIRKKFMINWAFGQRCLGNLYTEIIYTPIATPDGSVVKKMRGNNSGQPSTVVDNTIMVIIAMQYAISKAEFPAGRLRDQIRYFANGDDLVVAVEPSLSDKISSFSASFAELGLSYDFSNKVNDRSELQFMSHTGKLIDGMYIPMLERERICAILEWSRSDEPQFQLDAISAAMIEAWGDDELLYQIRRYYSWLLEQEPYKSIAELGHAPYLAEAALKALYTGKDPDAELIAIYERAMLNTPPTEDRPTKVVHEANVTAASSAATQTSTTSPTVTSTSGASTSTSSGTTSAPLASTTPPVSATTTPSTGTTAPTTPTVRAANLPDIAGHRKAKANGESQLNVRGENDDEDVPAASEFALPRLPTLGAKIRVPKFKGAIVLNKDHLIKYTPDQRDLSNTRATQEQFEKWYSGVRNEVEKTDEEMALLLNGSMVWCMENGTSPDLSGSWTMMEGEEQIAYPLEPFCRHAQPTLRSIMAHFSDAATAYVVLRNQKSRYMPRYGLKRGLNDYSLAPYAFDFYEITSTSPLRARERHAQMKAAAIRGKASRMFGLDGNVSAQSENTERHTVEDVNTRVHSLSGANML | 2.7.7.48; 3.4.-.-; 3.4.22.44; 3.4.22.45; 3.6.4.- | null | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049] | helical viral capsid [GO:0019029]; host cell cytoplasmic vesicle membrane [GO:0044162]; membrane [GO:0016020] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; helicase activity [GO:0004386]; hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides [GO:0016818]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type peptidase activity [GO:0008236]; structural molecule activity [GO:0005198] | PF00270;PF00271;PF00863;PF00851;PF01577;PF00767;PF08440;PF13608;PF00680; | 3.30.70.270;3.90.70.150;3.40.50.300;2.40.10.10; | Potyviridae genome polyprotein family | PTM: [Viral genome-linked protein]: VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.; PTM: [Genome polyprotein]: Genome polyprotein of potyviruses undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle membrane. Note=Probably colocalizes with 6K2-induced vesicles associated with host chloroplasts. {ECO:0000250|UniProtKB:P13529}.; SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate with host chloroplasts. {ECO:0000250|UniProtKB:P09814}.; SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.; EC=3.4.22.44; Evidence={ECO:0000250|UniProtKB:P04517}; CATALYTIC ACTIVITY: Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.; EC=3.4.22.45; Evidence={ECO:0000250|UniProtKB:P04517}; | null | null | null | null | FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity. {ECO:0000250|UniProtKB:P04517}.; FUNCTION: [Cytoplasmic inclusion protein]: Has helicase activity. It may be involved in replication.; FUNCTION: [6 kDa protein 1]: Indispensable for virus replication. {ECO:0000250|UniProtKB:P13529}.; FUNCTION: [6 kDa protein 2]: Indispensable for virus replication. {ECO:0000250|UniProtKB:P09814}.; FUNCTION: [Viral genome-linked protein]: Mediates the cap-independent, EIF4E-dependent translation of viral genomic RNAs (By similarity). Binds to the cap-binding site of host EIF4E and thus interferes with the host EIF4E-dependent mRNA export and translation (By similarity). VPg-RNA directly binds EIF4E and is a template for transcription (By similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are templates for translation (By similarity). {ECO:0000250|UniProtKB:P18247}.; FUNCTION: [Nuclear inclusion protein A]: Has RNA-binding and proteolytic activities. {ECO:0000250|UniProtKB:P04517}.; FUNCTION: [Nuclear inclusion protein B]: An RNA-dependent RNA polymerase that plays an essential role in the virus replication.; FUNCTION: [Capsid protein]: Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification. {ECO:0000250|UniProtKB:P04517}. | Ryegrass mosaic virus (isolate Denmark/Danish) (RGMV) |
O11457 | VGP_EBOG4 | MGVTGILQLPRDRFKRTSFFLWVIILFQRTFSIPLGVIHNSTLQVSDVDKLVCRDKLSSTNQLRSVGLNLEGNGVATDVPSATKRWGFRSGVPPKVVNYEAGEWAENCYNLEIKKPDGSECLPAAPDGIRGFPRCRYVHKVSGTGPCAGDFAFHKEGAFFLYDRLASTVIYRGTTFAEGVVAFLILPQAKKDFFSSHPLREPVNATEDPSSGYYSTTIRYQATGFGTNETEYLFEVDNLTYVQLESRFTPQFLLQLNETRYTSGKRSNTTGKLIWKVNPEIDTTIGEWAFWETKKNLTRKIRSEELSFTAVSNRAKNISGQSPARTSSDPGTNTTTEDHKIMASENSSAMVQVHSQGREAAVSHLTTLATISTSLRPPITKPGPDNSTHNTPVYKLDISEATQVEQHHRRTDNASTTSDTPPATTAAGPLKAENTNTSKGTDLLDPATTTSPQNHSETAGNNNTHHQDTGEESASSGKLGLITNTIAGVAGLITGGRRTRREAIVNAQPKCNPNLHYWTTQDEGAAIGLAWIPYFGPAAEGIYIEGLMHNQDGLICGLRQLANETTQALQLFLRATTELRTFSILNRKAIDFLLQRWGGTCHILGPDCCIEPHDWTKNITDKIDQIIHDFVDKTLPDQGDNDNWWTGWRQWIPAGIGVTGVIIAVIALFCICKFVF | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; entry receptor-mediated virion attachment to host cell [GO:0098670]; fusion of virus membrane with host endosome membrane [GO:0039654]; suppression by virus of host tetherin activity [GO:0039587] | extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF01611; | 1.10.287.210; | Filoviruses glycoprotein family | PTM: The signal peptide region modulates GP's high mannose glycosylation, thereby determining the efficiency of the interactions with DC-SIGN(R). {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}.; PTM: O-glycosylated in the mucin-like region. {ECO:0000250}.; PTM: Palmitoylation of GP2 is not required for its function. {ECO:0000250}.; PTM: Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into GP1 and GP2 by host cell furin in the trans Golgi, and maybe by other host proteases, to yield the mature GP1 and GP2 proteins. The cleavage site corresponds to the furin optimal cleavage sequence [KR]-X-[KR]-R. This cleavage does not seem to be required for function. After the internalization of the virus into cell endosomes, GP1 C-terminus is removed by the endosomal proteases cathepsin B, cathepsin L, or both, leaving a 19-kDa N-terminal fragment which is further digested by cathepsin B. Proteolytic processing of GP1,2 by host ADAM17 can remove the transmembrane anchor of GP2 and leads to shedding of complexes consisting in GP1 and truncated GP2 (GP1,2delta) (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: [GP2]: Virion membrane {ECO:0000250|UniProtKB:Q05320}; Single-pass type I membrane protein {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:Q05320}; Single-pass type I membrane protein {ECO:0000255}. Note=In the cell, localizes to the plasma membrane lipid rafts, which probably represent the assembly and budding site. {ECO:0000250|UniProtKB:Q05320}.; SUBCELLULAR LOCATION: [GP1]: Virion membrane {ECO:0000250|UniProtKB:Q05320}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q05320}. Host cell membrane {ECO:0000250|UniProtKB:Q05320}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q05320}. Note=GP1 is not anchored to the viral envelope, but forms a disulfid-linked complex with the extravirion surface GP2. In the cell, both GP1 and GP2 localize to the plasma membrane lipid rafts, which probably represent the assembly and budding site. GP1 can also be shed after proteolytic processing. {ECO:0000250|UniProtKB:Q05320}.; SUBCELLULAR LOCATION: [Shed GP]: Secreted {ECO:0000250|UniProtKB:Q05320}. Note=GP2-delta bound to GP1 (GP1,2-delta) is produced by proteolytic cleavage of GP1,2 by host ADAM17 and shed by the virus. {ECO:0000250|UniProtKB:Q05320}. | null | null | null | null | null | FUNCTION: [Envelope glycoprotein]: Trimeric GP1,2 complexes form the virion surface spikes and mediate the viral entry processes, with GP1 acting as the receptor-binding subunit and GP2 as the membrane fusion subunit. At later times of infection, down-regulates the expression of various host cell surface molecules that are essential for immune surveillance and cell adhesion. Down-modulates several integrins including ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6, ITGAV and ITGB1. This decrease in cell adhesion molecules may lead to cell detachment, contributing to the disruption of blood vessel integrity and hemorrhages developed during infection (cytotoxicity). Interacts with host TLR4 and thereby stimulates the differentiation and activation of monocytes leading to bystander death of T-lymphocytes. Down-regulates as well the function of host natural killer cells. Counteracts the antiviral effect of host BST2/tetherin that restricts release of progeny virions from infected cells. However, cooperates with VP40 and host BST2 to activate canonical NF-kappa-B pathway in a manner dependent on neddylation. {ECO:0000250|UniProtKB:Q05320}.; FUNCTION: [Shed GP]: Functions as a decoy for anti-GP1,2 antibodies thereby contributing to viral immune evasion. Interacts and activates host macrophages and dendritic cells inducing up-regulation of cytokine transcription. This effect is mediated throught activation of host TLR4. {ECO:0000250|UniProtKB:Q05320}.; FUNCTION: [GP1]: Responsible for binding to the receptor(s) on target cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as cofactors for virus entry into dendritic cells (DCs) and endothelial cells (By similarity). Binding to the macrophage specific lectin CLEC10A also seems to enhance virus infectivity (By similarity). Interaction with FOLR1/folate receptor alpha may be a cofactor for virus entry in some cell types, although results are contradictory (By similarity). Members of the Tyro3 receptor tyrosine kinase family also seem to be cell entry factors in filovirus infection (PubMed:17005688). Once attached, the virions are internalized through clathrin-dependent endocytosis and/or macropinocytosis. After internalization of the virus into the endosomes of the host cell, proteolysis of GP1 by two cysteine proteases, CTSB/cathepsin B and CTSL/cathepsin L removes the glycan cap and allows GP1 binding to the host entry receptor NPC1. NPC1-binding, Ca(2+) and acidic pH induce a conformational change of GP2, which unmasks its fusion peptide and permit membranes fusion (By similarity). {ECO:0000250|UniProtKB:Q05320, ECO:0000250|UniProtKB:Q66814, ECO:0000269|PubMed:17005688}.; FUNCTION: [GP2]: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in GP2, releasing the fusion hydrophobic peptide. {ECO:0000250|UniProtKB:Q05320}. | Zaire ebolavirus (strain Gabon-94) (ZEBOV) (Zaire Ebola virus) |
O12157 | GAG_HV192 | MGARASILRGGKLDAWERIKLKPGGKKHYMMKHLVWASRELERFALDPGLLETSEGCKQIMKQLQPALQTGTKELISLHNTVATLYCVHEKIDVRDTKEALDKIKEEQNKSQQKTQQAEAADKGKVSQNYPIVQNLQGQMVHQPISARTLNAWVKVVEEKAFSPEVIPMFTALSEGATPQDLNTMLNTVGGHQAAMQMLKDTINEEAAEWDRLHPVHAGPVAPGQMREPRGSDIAGTTSTLQEQITWMTNNPPVPVGDIYKRWIILGLNKIVRMYSPVSILDIKQGPKEPFRDYVDRFFKTLRAEQATQDVKNWMTDTLLVQNANPDCKTILRALGPGASLEEMMTACQGVGGPGHKARVLAEAMSKVNNTNIMMQRSNCKGPKRTIKCFNCGKEGHLARNCRAPRKKGCWKCGKEGHQVKDCTERQANFLGKIWPSHRGRPGNLLQNRTEPTAPPEESFRFGEETTTPSRKQETIDKELPLTSLKSLFGSDPLST | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|UniProtKB:P04591}.; PTM: Capsid protein p24 is phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating. {ECO:0000250|UniProtKB:P12493}.; PTM: Nucleocapsid protein p7 is methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription. {ECO:0000250|UniProtKB:P03347}. | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000250|UniProtKB:P12493}. | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). {ECO:0000250|UniProtKB:P04591}.; FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12493}.; FUNCTION: [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). The capsid promotes immune invasion by cloaking viral DNA from CGAS detection (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (By similarity). {ECO:0000250|UniProtKB:P04591, ECO:0000250|UniProtKB:P12493}.; FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly. {ECO:0000250|UniProtKB:P04591}.; FUNCTION: [p6-gag]: Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1. {ECO:0000250|UniProtKB:P12493}. | Human immunodeficiency virus type 1 group M subtype C (isolate 92BR025) (HIV-1) |
O12158 | POL_HV192 | MGARASILRGGKLDAWERIKLKPGGKKHYMMKHLVWASRELERFALDPGLLETSEGCKQIMKQLQPALQTGTKELISLHNTVATLYCVHEKIDVRDTKEALDKIKEEQNKSQQKTQQAEAADKGKVSQNYPIVQNLQGQMVHQPISARTLNAWVKVVEEKAFSPEVIPMFTALSEGATPQDLNTMLNTVGGHQAAMQMLKDTINEEAAEWDRLHPVHAGPVAPGQMREPRGSDIAGTTSTLQEQITWMTNNPPVPVGDIYKRWIILGLNKIVRMYSPVSILDIKQGPKEPFRDYVDRFFKTLRAEQATQDVKNWMTDTLLVQNANPDCKTILRALGPGASLEEMMTACQGVGGPGHKARVLAEAMSKVNNTNIMMQRSNCKGPKRTIKCFNCGKEGHLARNCRAPRKKGCWKCGKEGHQVKDCTERQANFFRENLAFPQGEARKSSSEQNRANSPTRRELQVWGRDNNSLSEAGDDRQGTALNFPQITLWQRPLVNIKVGGQLKEALLDTGADDTVLEEIKLPGNWKPKMIGGIGGFIKVRQYDQILIEICGKKAIGTVLVGPTPVNIIGRNMLTQLGCTLNFPISPIETVPVKLKPGMDGPKVKQWLLTEEKIKALTAICDEMEREGKITKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTWDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEGFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPSIFQSSTTKILEPFRAQNPEIIIYQYMDDLYVGSDLEIGQHRAKIEELREHLLKWGFTTPDKKHQKEPPFLWMGYELHPDKWTVQPIQLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGAKALTDIVPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQNQWTYQIYQEPFKNLKTGKYAKMRTAHTNDVRQLTEAVQKIALESIIIWGKTPKFRLPIQKETWEAWWTDYWQATWIPEWEFVNTPPLVKLWYQLEKEPIAGAETFYVDGAANREIKMGKAGYVTDRGRQKIVSITETTNQKTELQAIQLALQDSGSEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKERVYLSWVPAHKGIGGNEQVDKLVSSGIRKVLFLDGINKAQEEHEKYHSNWRAMASEFNLPPIVAKEIVASCDKCQLKGEATHGQVDCSPGIWQLDCTHLEGKIILVAVHVASGYIEAEVIPAETGQETAYFILKLAGRWPVKVIHTDNGSNFISNTVKAACWWAGIQQEFGIPYNPQSQGVVESMNKELKKIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIIDIIATDIQTKELQKQIMKIQNFRVYYRDSRDPIWKGPAKLLWKGEGAVVLQDNSDIKVVPRRKVKIIKDYGKQMAGADCMASRQDED | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions. {ECO:0000250}; | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral penetration into host nucleus [GO:0075732] | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. Nucleocapsid protein p7 might be further cleaved after virus entry. {ECO:0000250|UniProtKB:P04585, ECO:0000255|PROSITE-ProRule:PRU00405}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|UniProtKB:P04585}.; PTM: [Capsid protein p24]: Phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating. {ECO:0000250|UniProtKB:P12493}.; PTM: [Nucleocapsid protein p7]: Methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription. {ECO:0000250|UniProtKB:P03347}. | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. {ECO:0000250|UniProtKB:P12497}.; SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane; Lipid-anchor {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Reverse transcriptase/ribonuclease H]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Integrase]: Virion {ECO:0000305}. Host nucleus {ECO:0000305}. Host cytoplasm {ECO:0000305}. Note=Nuclear at initial phase, cytoplasmic at assembly. {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.; EC=3.1.26.13; Evidence={ECO:0000250}; CATALYTIC ACTIVITY: Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.; EC=3.1.13.2; Evidence={ECO:0000250}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation. {ECO:0000250}.; FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA. {ECO:0000250|UniProtKB:P12497}.; FUNCTION: [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating. On the other hand, interactions with PDZD8 or CYPA stabilize the capsid. {ECO:0000250|UniProtKB:P04585, ECO:0000250|UniProtKB:P12497}.; FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly. {ECO:0000250|UniProtKB:P04585}.; FUNCTION: [Protease]: Aspartyl protease that mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response. Also mediates cleavage of host YTHDF3. Mediates cleavage of host CARD8, thereby activating the CARD8 inflammasome, leading to the clearance of latent HIV-1 in patient CD4(+) T-cells after viral reactivation; in contrast, HIV-1 can evade CARD8-sensing when its protease remains inactive in infected cells prior to viral budding (By similarity). {ECO:0000250|UniProtKB:P04585, ECO:0000255|PROSITE-ProRule:PRU00275}.; FUNCTION: [Reverse transcriptase/ribonuclease H]: Multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends. {ECO:0000250|UniProtKB:P04585}.; FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration. {ECO:0000250|UniProtKB:P04585}. | Human immunodeficiency virus type 1 group M subtype C (isolate 92BR025) (HIV-1) |
O12161 | TAT_HV192 | MEPVDPNLEPWNHPGSQPKTACNNCYCKRCSYHCLVCFQTKGLGISYGRKKRRQRRSAPPSSEDHQNPIPKQPLPQTRGDQTGSEESKKKVESKTETDPFD | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; symbiont-mediated suppression of host translation initiation [GO:0039606]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049] | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of Lys-50 promotes dissociation of Tat from the TAR RNA through the competitive binding to PCAF's bromodomain. In addition, the non-acetylated Tat's N-terminus can also interact with PCAF. PCAF-mediated acetylation of Lys-28 enhances Tat's binding to CCNT1. Lys-50 is deacetylated by SIRT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Polyubiquitination by host MDM2 does not target Tat to degradation, but activates its transactivation function and fosters interaction with CCNT1 and TAR RNA. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Phosphorylated by EIF2AK2 on serine and threonine residues adjacent to the basic region important for TAR RNA binding and function. Phosphorylation of Tat by EIF2AK2 is dependent on the prior activation of EIF2AK2 by dsRNA. {ECO:0000255|HAMAP-Rule:MF_04079}. | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type. {ECO:0000255|HAMAP-Rule:MF_04079}. | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TEFb complex) that will in turn hyperphosphorylate the RNA polymerase II to allow efficient elongation. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs. {ECO:0000255|HAMAP-Rule:MF_04079}.; FUNCTION: Extracellular circulating Tat can be endocytosed by surrounding uninfected cells via the binding to several surface receptors such as CD26, CXCR4, heparan sulfate proteoglycans (HSPG) or LDLR. Neurons are rarely infected, but they internalize Tat via their LDLR. Through its interaction with nuclear HATs, Tat is potentially able to control the acetylation-dependent cellular gene expression. Modulates the expression of many cellular genes involved in cell survival, proliferation or in coding for cytokines or cytokine receptors. Tat plays a role in T-cell and neurons apoptosis. Tat induced neurotoxicity and apoptosis probably contribute to neuroAIDS. Circulating Tat also acts as a chemokine-like and/or growth factor-like molecule that binds to specific receptors on the surface of the cells, affecting many cellular pathways. In the vascular system, Tat binds to ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of endothelial cells and competes with bFGF for heparin-binding sites, leading to an excess of soluble bFGF. {ECO:0000255|HAMAP-Rule:MF_04079}. | Human immunodeficiency virus type 1 group M subtype C (isolate 92BR025) (HIV-1) |
O12164 | ENV_HV192 | MRVEGIQRNWKQWWIWGILGFWMVMIYNVRGNLWVTVYYGVPVWKEAKTTLFCASDAKAYDAEVHNVWATHACVPTDPNPQEMVLENVTENFNMWENDMVEQMHQDIISLWDQSLKPCVKLTPLCVTLHCSNRTIDYNNRTDNMGGEIKNCSFNMTTEVRDKREKVHALFYRLDIVPLKNESSNTSGDYRLINCNTSAITQACPKVSFDPIPIHYCAPAGYAILKCNNKTFNGTGPCNNVSTIQCTHGTKPVVSTQLLLNGSLAEEEIIIRSKNLTDNVKTIIVHLNESVEINCTRPNNNTRKSIRIGPGQAFYATGEIIGDIRQAHCNISRTAWNKTLQEVGKKLAEHFPNKAIKFAKHSGGDLEITTHSFNCRGEFFYCNTSSLFNSTYTPNSTENITGTENSIITIPCRIKQIINMWQGVGRAMYAPPIEGILTCRSNITGLLLTRDGGTGMHDTEIFRPEGGDMRDNWRSELYKYKVVEIKPLGIAPTKAKRRVVEREKRAVGIGAVFLGFLGAAGSTMGAASITLTVQVRQLLSGIVQQQSNLLRAIEAQQHMLQLTVWGIKQLQTRVLAIERYLRDQQLLGIWGCSGKLICTTAVPWNSSWSNRSQEDIWNNMTWMQWDREISNYTNTIYRLLEDSQNQQEKNEQDLLALDKWQNLWTWFGITNWLWYIKIFIKIVGGLIGLRIIFAVLSIVNRVRQGYSPLSFQTLTPNPRGPDRLGGIEEEGGEQDRDRSIRLVSGFLALAWDDLRSLCLFSYHRLRDLILIAARAVELLGRSSLRGIQRGWEILKYLGGLVQYWSLELKKSAISLFDTIAIAVAEGTDRIIEVIQGIWRAICNIPRRIRQGFEAALQ | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polarization [GO:1903908]; positive regulation of receptor clustering [GO:1903911]; viral protein processing [GO:0019082]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049] | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic cleavage) is essential for their association with host cell membrane lipid rafts. Palmitoylation is therefore required for envelope trafficking to classical lipid rafts, but not for viral replication. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. About 2 of the 9 disulfide bonds of gp41 are reduced by P4HB/PDI, following binding to CD4 receptor. {ECO:0000255|HAMAP-Rule:MF_04083}. | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.; SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}. | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41. {ECO:0000255|HAMAP-Rule:MF_04083}.; FUNCTION: [Surface protein gp120]: Attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. {ECO:0000255|HAMAP-Rule:MF_04083}.; FUNCTION: [Transmembrane protein gp41]: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04083}. | Human immunodeficiency virus type 1 group M subtype C (isolate 92BR025) (HIV-1) |
O12165 | NEF_HV192 | MGNKWSKCSTVGRPAIRERMRRAPAAEGVGPASQDSDKYGALTSSSTPANNADCAWLEAQQEEEEVGFPVRPQVPLRPMTYKAVVDLSFFLEEKGGLEGLIYSKKRQDILDLWVYNTQGYFPDWQNYTPGPGVRFPLTFGWCFKLVPVDPREVEEANTGENNSLLHPMSLHGMEDSHREVLQWKFDSLLARRHMARELHPEYYKDC | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated perturbation of host defense response [GO:0019049] | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Phosphorylated on serine residues, probably by host PKCdelta and theta. {ECO:0000255|HAMAP-Rule:MF_04078}. | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04078}. Note=TGN localization requires PACS1. Associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved. {ECO:0000255|HAMAP-Rule:MF_04078}. | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network-associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase-ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impair the membrane fusion event necessary for subsequent virion penetration. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T-lymphocytes into apoptosis. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR-mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of host BAD. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. {ECO:0000255|HAMAP-Rule:MF_04078}. | Human immunodeficiency virus type 1 group M subtype C (isolate 92BR025) (HIV-1) |
O12940 | TOM1_CHICK | MDFLLGNPFSSPVGQRIERATDGSLRGEDWSLNMEICDIINETEEGPKDAFRAIKKRIVGNKNFHEVMLALTVLETCVKNCGHRFHILVASQDFVESVLVRTILPKNNPPAIVHDKVLTLIQSWADAFRSSPDLTGVVAVYEDLRRKGLEFPMTDLDMLSPIHTPRRSVYSSNSQSGQNSPAVNSPQQMESILHPVTLPSGRDTSSNVPITPTQEQIKKLRSELEVVNGNVKVMSEMLTELVPSQAETSDLELLQELNRTCRAMQQRVLELIPRVQHEQLTEELLLINDNLNNVFLRHERFERVRTGQPVKAPSEAENNLIDLRPSTPPAVRQPEVTNNLSSQLAGMTLGSRSVSAGLHSLDTSGKLEEEFDMFAVTRGSSLAEQRREVKYEDPQATKGLAGALDARQQNTGAEESSASSDGAQLTNWMMRQGMVPVPQANFMEDIEKWLSTDVGESEDGKGVTSEEFDKFLEERAKVADRLPTLSSSSAGTPVSPAAASRHQKQAKEDDAMFAL | null | null | autophagosome-lysosome fusion [GO:0061909]; endosomal transport [GO:0016197]; positive regulation of autophagosome maturation [GO:1901098]; protein transport [GO:0015031]; regulation of endosome organization [GO:1904978]; signal transduction [GO:0007165]; substrate localization to autophagosome [GO:0061753] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; endosome membrane [GO:0010008]; membrane [GO:0016020] | clathrin binding [GO:0030276]; clathrin heavy chain binding [GO:0032050]; myosin VI binding [GO:0070853]; phosphatidylinositol-5-phosphate binding [GO:0010314]; polyubiquitin modification-dependent protein binding [GO:0031593]; ubiquitin binding [GO:0043130] | PF03127;PF00790; | 1.20.58.160;1.25.40.90; | TOM1 family | PTM: Monoubiquitinated. {ECO:0000250|UniProtKB:O60784}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60784}. Endosome membrane {ECO:0000250|UniProtKB:O60784}; Peripheral membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000250|UniProtKB:O60784}; Peripheral membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Adapter protein that plays a role in the intracellular membrane trafficking of ubiquitinated proteins, thereby participating in autophagy, ubiquitination-dependent signaling and receptor recycling pathways (By similarity). Acts as a MYO6/Myosin VI adapter protein that targets MYO6 to endocytic structures (By similarity). Together with MYO6, required for autophagosomal delivery of endocytic cargo, the maturation of autophagosomes and their fusion with lysosomes (By similarity). MYO6 links TOM1 with autophagy receptors, such as TAX1BP1; CALCOCO2/NDP52 and OPTN (By similarity). Binds to polyubiquitinated proteins via its GAT domain (By similarity). In a complex with TOLLIP, recruits ubiquitin-conjugated proteins onto early endosomes (By similarity). The Tom1-Tollip complex may regulate endosomal trafficking by linking polyubiquitinated proteins to clathrin (By similarity). Mediates clathrin recruitment to early endosomes (By similarity). Modulates binding of TOLLIP to phosphatidylinositol 3-phosphate (PtdIns(3)P) via binding competition; the association with TOLLIP may favor the release of TOLLIP from endosomal membranes, allowing TOLLIP to commit to cargo trafficking (By similarity). Acts as a phosphatidylinositol 5-phosphate (PtdIns(5)P) effector by binding to PtdIns(5)P, thereby regulating endosomal maturation (By similarity). PtdIns(5)P-dependent recruitment to signaling endosomes may block endosomal maturation (By similarity). Also inhibits Toll-like receptor (TLR) signaling and participates in immune receptor recycling (By similarity). {ECO:0000250|UniProtKB:O60784}. | Gallus gallus (Chicken) |
O12971 | LFNG_CHICK | MLKSCGRKLLLSLVGSMFTCLLVLMVEPPGRPGLARGEAGGAQRALQSLGAARAAGQGAPGLRSFADYFGRLSRARRELPAAPPSPPRPPAEDITPRDVFIAVKTTKKFHKARLELLLDTWISRNRDMTFIFTDGEDEELKKQARNVINTNCSAAHSRQALSCKMAVEYDKFIESGRKWFCHVDDDNYVNVRTLVKLLSSYPHTQDIYIGKPSLDRPIQATERISENKMHPVHFWFATGGAGFCISRGLALKMSPWASGGHFMSTAEKIRLPDDCTIGYIIESVLGVKLIRSNLFHSHLENLHQVPKTEIHKQVTLSYGMFENKRNSIHMKGAFSVEEDPSRFRSVHCLLYPDTPWCPSNVVY | 2.4.1.222 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O09010}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250|UniProtKB:O09010}; Note=Manganese is the most effective. Can also use cobalt with lower efficiency. Has some activity with magnesium and calcium, but not zinc. {ECO:0000250|UniProtKB:O09010}; | compartment pattern specification [GO:0007386]; marginal zone B cell differentiation [GO:0002315]; negative regulation of Notch signaling pathway involved in somitogenesis [GO:1902367]; ovarian follicle development [GO:0001541]; positive regulation of meiotic cell cycle [GO:0051446]; positive regulation of Notch signaling pathway [GO:0045747]; regulation of Notch signaling pathway [GO:0008593]; regulation of somitogenesis [GO:0014807]; somitogenesis [GO:0001756]; T cell differentiation [GO:0030217] | Golgi membrane [GO:0000139] | metal ion binding [GO:0046872]; O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity [GO:0033829] | PF02434; | 3.90.550.50; | Glycosyltransferase 31 family | PTM: A soluble form may be derived from the membrane form by proteolytic processing. {ECO:0000305}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70531, Rhea:RHEA-COMP:17922, Rhea:RHEA-COMP:17923, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:189631, ChEBI:CHEBI:189634; EC=2.4.1.222; Evidence={ECO:0000250|UniProtKB:O09010}; CATALYTIC ACTIVITY: Reaction=3-O-(alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70511, Rhea:RHEA-COMP:17919, Rhea:RHEA-COMP:17920, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:189632, ChEBI:CHEBI:189633; EC=2.4.1.222; Evidence={ECO:0000250|UniProtKB:O09010}; | null | null | null | null | FUNCTION: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Essential mediator of somite segmentation and patterning. {ECO:0000250|UniProtKB:O09010}. | Gallus gallus (Chicken) |
O12976 | PSN1_XENLA | MNDTSERRSNENSESQSNGQTQSSSQQVLEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRFDGQLIYTPFTEDTESVGQRALNSILNATIMISVIIVMTILLVVLYKYRCYKVIHGWLIISSLLLLFFFSYIYLGEVFKTYNVAVDYITLALLIWNFGVVGMICIHWKGPLLLQQAYLIMISALMALVFIKYLPEWTTWLILAVISVYDLVAVLSPKGPLRMLVETAQERNETLFPALIYSSTMIWLVNMADGDPGLKQSASTKTYNTQAPTAHPRSDSAASDDNGGFDTTWEDHRNAQIGPINSTPESRVAVQALPSNSPPSEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTLACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI | 3.4.23.- | null | amyloid precursor protein metabolic process [GO:0042982]; amyloid-beta formation [GO:0034205]; membrane protein ectodomain proteolysis [GO:0006509]; Notch signaling pathway [GO:0007219]; positive regulation of catalytic activity [GO:0043085]; protein processing [GO:0016485]; regulation of canonical Wnt signaling pathway [GO:0060828]; smooth endoplasmic reticulum calcium ion homeostasis [GO:0051563] | axon [GO:0030424]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; gamma-secretase complex [GO:0070765]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synapse [GO:0045202] | aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296] | PF01080; | 1.10.472.100; | Peptidase A22A family | PTM: Heterogeneous proteolytic processing generates N-terminal (NTF) and C-terminal (CTF) fragments of approximately 35 and 20 kDa, respectively. During apoptosis, the C-terminal fragment (CTF) is further cleaved by a caspase. {ECO:0000250|UniProtKB:P49768}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P49768}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49768}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P49768}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49768}. Cytoplasmic granule {ECO:0000250|UniProtKB:P49768}. Cell membrane {ECO:0000250|UniProtKB:P49768}. Cell projection, axon {ECO:0000250|UniProtKB:Q4JIM4}. Synapse {ECO:0000250|UniProtKB:Q4JIM4}. Cell projection, neuron projection {ECO:0000250|UniProtKB:P49768}. | null | null | null | null | null | FUNCTION: Catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the presence of the other members of the gamma-secretase complex for protease activity. Plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins. {ECO:0000250|UniProtKB:P49768}. | Xenopus laevis (African clawed frog) |
O12977 | PSN2_XENLA | MIKLSDSEDEECNERTSLITSESPPLPSYQDGVQASEGLETSYHRERQPDSTQNNEDVPNGRTSGADAYNSETTVENEEEELTLKYGARHVIMLFVPVTLCMVVVVATIKSVSFYTEKDGQLIYTPFSEDTTSVGERLLNSVLNTLIMISVILVMTIFLVLLYKYRCYKFIHGWLILSSLMLLFMFTYIYLSEVFKTYNIAMDYPTLFMVIWNFGAVGMICIHWKGPLQLQQAYLIMISALMALVFIKYLPEWSAWVILGAISVYDLLAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMMWTVGMADSATADGRMNQQVQHIDRNTPEGANSTVEDAAETRIQTQSNLSSEDPDEERGVKLGLGDFIFYSVLVGKAAATASGDWNTTLACFVAILIGLCLTLLLLAVFKKALPALPISITFGLIFYFSTDNIVRPFMDTLASHQMYI | 3.4.23.- | null | amyloid precursor protein catabolic process [GO:0042987]; amyloid-beta metabolic process [GO:0050435]; calcium ion transport [GO:0006816]; membrane protein ectodomain proteolysis [GO:0006509]; negative regulation of apoptotic process [GO:0043066]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; protein processing [GO:0016485] | apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; cell surface [GO:0009986]; ciliary rootlet [GO:0035253]; dendritic shaft [GO:0043198]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; growth cone [GO:0030426]; lysosomal membrane [GO:0005765]; membrane raft [GO:0045121]; mitochondrial inner membrane [GO:0005743]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; Z disc [GO:0030018] | aspartic endopeptidase activity, intramembrane cleaving [GO:0042500] | PF01080; | 1.10.472.100; | Peptidase A22A family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors (By similarity). May play a role in negative regulation of apoptotic cascades during oogenesis and embryogenesis, and in developmentally matured tissues such as brain tissue. {ECO:0000250}. | Xenopus laevis (African clawed frog) |
O12990 | JAK1_DANRE | MPELAVMDLGRQLCVKMKKQRKAEMTIPTAMKGLEIHFYLADTHQLEFFKACYTAEDLCVEAAKRCRISPLCHNLFALYEESQDLWYAPNHVFKVTDETSIKLHYRMRFYFTNWHGTSEIESPVWRHTLSKQKSVLNSQKTTEGTPLLDAASLDYLFAQGQYDFLRGLSPVRPTQTDEEHHEIENECLGMAVLAITHHAKSNNLPLSGAGAETSYKRFIPDSLNRTIKQRNFLTRIRISNVFKNFLNEFNSKTIQDSNIGLYDLKVKYLSTLETLTQGVGREIFKPKNLKVTGESEGSPAQMLPLGDNGMGYEVQVYGTTGISWRRKPAPNQLILKDKPKSKKIKGDKQWNDKKKDSGWTLFSDFHEITHIVIKDCCVTIYRQDNKTMELDLFYRDAALSFAALVDGYFRLTVDAHHYLCTDVAPSSVVQNLENGCHGPICTEYAIHKLRQEGNEEGTYVLRWSCTEYNFIIMTVVCIELDLCESRPVPQYKNFQIETSPQGYRLYGTDTFRPTLKELLEHLQGQLLRTDNLRFQLRRCCPPQPREISNLLVMTTDREPVPQKKTQVSQLSFDRILKEEIVQGEHLGRGTRTNIYAGILKPKSDDEDDLGGYSQEVKVVLKVLGSGHRDISLAFFETASMMRQISHKHTALLYGVCVRHQENIMVEEFVQYGPLDLFMRRQTTPLSTAWKFQVAKQLASALSYLEDKKMVHGYVCSKNILVARDGLDGEGGPFIKLSDPGIPITVLSREECVDRIPWIAPECVKDTANLTIAADKWSFGTTLWEICYNGEIPLKDKKLSEKERFYAAQCQLATPDCDELAKLMTHCMTYDPRQRLFFRAIVRDIVMVEKQNPSIQPVPMLEVDPTVFEKRFLKKIRDLGEGHFGKVELCRYDPRGDRTGELVAVKSLKPENREEQSNNLWREIHILRELYHENIVKYKGICNEEGGRSIKLIMEFLPAGSLKEYLPRNKAHINLKTLHNYSVQICQGMDYLGSRNYIHRDLAARNVLVENEGTVKIGDFGLTKSIKDNEGYYTVKDDLDSPVFWYAPECLIHCKFYRASDVWSFGVTMYELLTYCDASCSPMSVFLKLIGPTHGQMTVTRLVKVLEEGKRLPRPDDCSEQLYNLMRRCWEATPEKRIDFKSLIANFQQMLDNL | 2.7.10.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P23458}; Note=Mn(2+) was used in the in vitro kinase assay but Mg(2+) is likely to be the in vivo cofactor. {ECO:0000250|UniProtKB:P23458}; | cell differentiation [GO:0030154]; cytokine-mediated signaling pathway [GO:0019221]; growth hormone receptor signaling pathway via JAK-STAT [GO:0060397]; intracellular signal transduction [GO:0035556]; protein phosphorylation [GO:0006468]; receptor signaling pathway via JAK-STAT [GO:0007259]; T cell differentiation in thymus [GO:0033077] | cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; membrane [GO:0016020] | ATP binding [GO:0005524]; growth hormone receptor binding [GO:0005131]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715] | PF18379;PF18377;PF17887;PF07714; | 3.30.505.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, JAK subfamily | null | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Wholly intracellular, possibly membrane associated. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; | null | null | null | null | FUNCTION: Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway (By similarity). Appears to be required in early development for specific cell migrations (epiboly), expression of homeobox protein goosecoid and formation of anterior structures (PubMed:9096349). {ECO:0000250|UniProtKB:P23458, ECO:0000269|PubMed:9096349}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
O13010 | PI42A_PIG | MATPGNLGSSVLASKTKTKKKHFVAQKVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSXARSGARFHTSYDRRYVIKTITSEDVAEMHNILKNYHQHIVECHGITLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNXKKVFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVECEENDGEEEGESDGTHPVGTPPDSPGNTLNSSPPLAPGEFDPNIDVYGIKCHENSPRKEVYFMAIIDILTHYDAKKKAAHAAKXVKHGAGAEISTVNPEQYSKRFLDFIGHILT | 2.7.1.149 | null | 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process [GO:1902635]; autophagosome-lysosome fusion [GO:0061909]; negative regulation of insulin receptor signaling pathway [GO:0046627]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation [GO:0016310]; regulation of autophagy [GO:0010506]; vesicle-mediated cholesterol transport [GO:0090119] | cytosol [GO:0005829]; lysosome [GO:0005764]; nucleus [GO:0005634]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886] | 1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; 1-phosphatidylinositol-5-phosphate 4-kinase activity [GO:0016309]; ATP binding [GO:0005524]; protein homodimerization activity [GO:0042803] | PF01504; | 3.30.810.10;3.30.800.10; | null | PTM: Phosphorylated in tyrosines. Phosphorylation is induced by light and increases kinase activity. {ECO:0000250|UniProtKB:Q9R0I8}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O70172}. Nucleus {ECO:0000250|UniProtKB:P48426}. Lysosome {ECO:0000250|UniProtKB:O70172}. Cytoplasm {ECO:0000250|UniProtKB:P48426}. Photoreceptor inner segment {ECO:0000250|UniProtKB:O70172}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:O70172}. Note=May translocate from the cytosol to the cell membrane upon activation of tyrosine phosphorylation. May translocate from the inner to the outer segments of the rod photoreceptor cells in response to light (By similarity). Localization to the nucleus is modulated by the interaction with PIP4K2B (By similarity). {ECO:0000250|UniProtKB:O70172, ECO:0000250|UniProtKB:P48426}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:12280, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57795, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.149; Evidence={ECO:0000250|UniProtKB:P48426}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12281; Evidence={ECO:0000250|UniProtKB:P48426}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + ATP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:55992, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:83423, ChEBI:CHEBI:84968, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P48426}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55993; Evidence={ECO:0000250|UniProtKB:P48426}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + GTP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + GDP + H(+); Xref=Rhea:RHEA:55964, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:83423, ChEBI:CHEBI:84968; Evidence={ECO:0000250|UniProtKB:P48426}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55965; Evidence={ECO:0000250|UniProtKB:P48426}; | null | null | null | null | FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Has both ATP- and GTP-dependent kinase activities. May exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2 (By similarity). May regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation (By similarity). May be involved in thrombopoiesis, and the terminal maturation of megakaryocytes and regulation of their size (By similarity). May negatively regulate insulin-stimulated glucose uptake by lowering the levels of PtdIns5P (By similarity). {ECO:0000250|UniProtKB:O70172, ECO:0000250|UniProtKB:P48426, ECO:0000250|UniProtKB:Q9R0I8}. | Sus scrofa (Pig) |
O13012 | ESR2_ANGJA | MAGSPGNELPLLQLQEVDSSKVGESGGSSGLLPTMYNGALPALSMESHAVCIPSPYTDSSHDYAALTFYSPPILSHGGPAVPESPAARQSLSPSLFWPAHGHHGHVSPLALHFQQPLVYREPAHSPWAEPKPLEHGQAQTSKLAGKRMAESEEGTSSVGGCFAGKGDMHFCAVCHDYASGYHYGVWSCEGCKAFFKRSIQGHNGYICPATNQCTIDKNRRKSCQACRLRKCYEVGMMKCGVRRERCTYRGARHRRMPHIRELAGTGGGARTQRRGEGVVPQTQEAQSSALTPEQLINRIIEAEPPEIYLMKELKKPFTEDSMMMSLTNLADKELVLMISWAKKIPGFVELDLSDQVHLLECCWLEVLMLGLMWRSVDHPGKLIFSPDLKLNRDEGSCVEGILEIFDMVLAATSRFRELKLQREEYVCLKAIILLNPNLCTTSSENREELESRNKLLHMLDSVTDALVWTIAKKGLTFQQQSARLAHLLMLLAHIRHLSNKGMEHLSNMKRKNVVPLYDLLLEMLDANTMHSSRMSASYSSQPSPWSQAAQSQPGPPPSCSGECPCPPKESSTI | null | null | cellular response to estradiol stimulus [GO:0071392]; cellular response to estrogen stimulus [GO:0071391]; intracellular estrogen receptor signaling pathway [GO:0030520] | nucleus [GO:0005634] | estrogen response element binding [GO:0034056]; hormone binding [GO:0042562]; nuclear estrogen receptor activity [GO:0030284]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; zinc ion binding [GO:0008270] | PF12497;PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Binds estrogens with an affinity similar to that of ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. | Anguilla japonica (Japanese eel) |
O13016 | PTN1_CHICK | MEIEKEFHRLDQAASWAAIYQDIRHEASDFPCKVAKHPRNKNRNRYRDVSPFDHSRIKLNQGDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSIKCAQYWPRKEEKEMFFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPEYGPVVVHCSAGIGRSGTFCLVDTCLLLMDKRKDPSSVDVKQVLLEMRKYRMGLIQTADQLRFSYLAVIEGAKFIMGDASVQEQWKELSNEDLDPPPEHTPPPPRPPKRTSEMHNGRMHEHAEFFPKHQVVEEEIRCSVSTAEETVSDGRVFSSVPLITDSTSQDTEIRRRTVGENLHVTAHKEESKSESVEEDDENMMTTWKPFLVNICMFTFLTAGAYLCYRVCFH | 3.1.3.48 | null | actin cytoskeleton organization [GO:0030036]; endoplasmic reticulum unfolded protein response [GO:0030968]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of PERK-mediated unfolded protein response [GO:1903898]; peptidyl-tyrosine dephosphorylation [GO:0035335]; regulation of endocytosis [GO:0030100]; regulation of signal transduction [GO:0009966] | cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | non-membrane spanning protein tyrosine phosphatase activity [GO:0004726]; protein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725] | PF00102; | 3.90.190.10; | Protein-tyrosine phosphatase family, Non-receptor class 1 subfamily | PTM: Phosphorylated on serine and threonine residues near the N-terminus by casein kinase II (CK2). | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; | null | null | null | null | FUNCTION: May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET (By similarity). {ECO:0000250}. | Gallus gallus (Chicken) |
O13023 | HHEX_XENLA | MQYQHPSSSALGLSVPLFAPTPLQHPTPFYIDDILGRNSASNGTPALPTPTLPSPNSSFTSLVATYRTPIYEPTPIHPAFTHPGAALAASYGASTYASPLYPFSRPVSDYTHALIRHDSLGKPLLWSPFIQRPLHKRKGGQVRFSNDQTIELEKKFETQKYLSPPERKRLAKMLQLSERQVKTWFQNRRAKWRRLKQENPQGNKKDETESLENICEESQERCLSAEQKSRESSLDDPTSSPTSQGNLDSEVSDDSDQEVDIEGDKGYYNCAH | null | null | anterior/posterior pattern specification [GO:0009952]; embryonic hemopoiesis [GO:0035162]; heart development [GO:0007507]; liver development [GO:0001889]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of Wnt signaling pathway [GO:0030177]; vasculogenesis [GO:0001570]; Wnt signaling pathway [GO:0016055] | 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]; sequence-specific DNA binding [GO:0043565] | PF00046; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}. | null | null | null | null | null | FUNCTION: Recognizes the DNA sequence 5'-ATTAA-3'. Transcriptional repressor. Regulates the differentiation of both endothelial and blood cells (By similarity). Probably plays a role in the proliferation of vascular endothelial cells during blood vessel development. Establishes anterior identity at two levels; acts early to enhance canonical wnt-signaling by repressing expression of tle4, and acts later to inhibit nodal-signaling by directly targeting nodal/nr1 and nodal2/nr2. May play a role in liver development. Induces heart development. {ECO:0000250|UniProtKB:Q05502, ECO:0000250|UniProtKB:Q9IAV3, ECO:0000269|PubMed:10328921, ECO:0000269|PubMed:10508583, ECO:0000269|PubMed:12464432, ECO:0000269|PubMed:15687261, ECO:0000269|PubMed:16936074, ECO:0000269|PubMed:9376326}. | Xenopus laevis (African clawed frog) |
O13024 | INCEA_XENLA | MNDAECLSHLLQVCARKTEEFVRTLDSKHMVWLLEIEEEARKMFSSDFNAEPELMPKTPSQKRRRKKRTSILPDENRDPSGRRISRRQSNASWSSSVRRLSVRNQNKANDDSIQEEPAQLKRMTRARAQASIKSTPVLETALPESPSQICQKNAQVKISEQERRSAEQKLIESDFELKTVPEITKDNVSETVNSAVPAVPVTPENKSRAAGKLKIAASSTPEQKAEMVDLTCESPRPANEQQLNLSNQSATPTGSKSDRRSVRRSLVVRKSSSRRASLASQFSLASKRESMTREAVRKSIRQSISQKKAAMEISSTSSQRSYQSSIEMVDDEITIKIRPETVPSETVSEEAPAAESPRRSLRSRAFKKIAISNLPDSEEPPRKVTRQMVAGNAEPTPETTEDAQNIRRKSYKRAVDELSDDERPSEEERSPPRKKTPSPPCPPSKIVRPPPHMKSFLHTVQKNQLLMMTPGSIGKNIIMKSFIKRNTPLKTDPKTEEKERQRLDALRKKEEAELQRKQKIEEGKKRKQEELKVRREERLRKVLQARERVEQLEEEKKKKIEQKFAQIDEKSEKVREDRMAEEKAKKKMTAKKQEEVECRRKQEEEARRLKVKQMEEEERRHQELLQKKREEEELERQKKIAEAKRLAEQERERQLLAEKERLRAEREKERIEKEKALQLQRELERAAQEKEQQRREAEERKKREQQERLEQERLRKEQEAKRLQEEEQRKAKEQAAVAASAPVMNVTVDMQNSPACESYEMTPKSCKVPSVKVNEDNYGMDLNSDDSTDDESQPRKPIPAWASGNLLTQAIRQQYYKPIDVDRMYGTIDSPKLEELFNKSKPRYFKRTSSAVWHSPPLSSNRHHLAVGYGLKY | null | null | chromosome segregation [GO:0007059]; meiotic spindle midzone assembly [GO:0051257]; metaphase chromosome alignment [GO:0051310]; mitotic cytokinesis [GO:0000281]; spindle assembly [GO:0051225] | chromosome [GO:0005694]; chromosome passenger complex [GO:0032133]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; meiotic spindle midzone [GO:1990385]; microtubule [GO:0005874]; midbody [GO:0030496]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; spindle [GO:0005819] | protein kinase binding [GO:0019901] | PF03941;PF12178; | 1.20.5.3600;6.10.250.2990; | INCENP family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NQS7}. Chromosome {ECO:0000269|PubMed:12464631}. Chromosome, centromere {ECO:0000269|PubMed:10996078}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10996078}. Midbody {ECO:0000250|UniProtKB:Q9NQS7}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9NQS7}. Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis (PubMed:10996078). Colocalizes to the equatorial cell cortex at anaphase (PubMed:10996078). Colocalizes with AURKB at mitotic chromosomes (PubMed:10996078). {ECO:0000269|PubMed:10996078}. | null | null | null | null | null | FUNCTION: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Acts as a scaffold regulating CPC localization and activity. The C-terminus associates with aurkb/aurora-B, the N-terminus associated with cdca8/borealin and/or cdca9/dasra-A tethers the CPC to the inner centromere, and the microtubule binding activity within the central SAH domain directs aurkb/aurora-B toward substrates near microtubules. Activates aurkb. {ECO:0000250|UniProtKB:P53352, ECO:0000269|PubMed:12221116, ECO:0000269|PubMed:17199039}. | Xenopus laevis (African clawed frog) |
O13033 | RAG1_DANRE | MEKGRWSSEDAPRASMPDELSHPKFSEWKFKLFRVRSMEKAPVQNETPVEKENQPELAMEKTSSQGSVMRLCFGGKSKENVESARGRVDLKLQEIDTHMNLLKNMCRLCGIAIQKAKGPSHEVQGVLEESSRCALRRMGCKLVTWPEVILKVFKVDVTTDMETVHPSLFCHRCWTAAIRGGGFCSFTNTRIPDWKPHTSQCNLCFPKKSSFQRVGRKRTKPLKSAHILPKRFRRDSSESSRVWRQTTENPDGKEWLKLSVQRGQWVKNITRCQRDHLSTKLIPTEVPADLIRAVTCQVCDHLLSDPVQSPCRHLFCRLCIIRYTHALGPNCPTCNQHLNPSHLIKPAKFFLATLSSLPLLCPSEECSDWVRLDSFREHCLNHYREKESQEEQTPSEQNLDGYLPVNKGGRPRQHLLSLTRRAQKHRLRDLKNQVKTFAEKEEGGDVKSVCLTLFLLALRAGNEHKQADELEAMMQGRGFGLHPAVCLAIRVNTFLSCSQYHKMYRTVKATSGRQIFQPLHTLRNAEKELLPGFHQFEWQPALKNVSTSWDVGIIDGLSGWTVSVDDVPADTISRRFRYDVALVSALKDLEEDIMEGLRERALDDSMCTSGFTVVVKESCDGMGDVSEKHGSGPAVPEKAVRFSFTIMSISIRLEGEDDGITIFQEQKPNSELSCRPLCLMFVDESDHETLTAILGPVVAERKAMMESRLIISVGGLLRSFRFFFRGTGYDEKMVREMEGLEASGSTYICTLCDSTRAEASQNMVLHSITRSHDENLERYEIWRKNPFSESADELRDRVKGVSAKPFMETQPTLDALHCDIGNATEFYKIFQDEIGEVYQKPNPSREERRRWRSTLDKQLRKKMKLKPVMRMNGNYARRLMTREAVEAVCELVPSEERREALLKLMDLYLQMKPVWRSTCPSRDCPDQLCQYSYNSQQFADLLSSMFKYRYDGKITNYLHKTLAHVPEIVERDGSIGAWASEGNESGNKLFRRFRKMNARQSKTFELEDILKHHWLYTSKYLQKFMEAHKNSVKAMQATFNPEETPEEADNSLDVPDF | 2.3.2.27; 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 1 divalent metal cation per subunit. Mg(2+) or Mn(2+). {ECO:0000250}; | adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; chromatin organization [GO:0006325]; pre-B cell allelic exclusion [GO:0002331]; protein-DNA complex assembly [GO:0065004]; somatic diversification of immune receptors via germline recombination within a single locus [GO:0002562]; T cell differentiation in thymus [GO:0033077]; V(D)J recombination [GO:0033151] | DNA recombinase complex [GO:0097519]; endodeoxyribonuclease complex [GO:1905347]; nucleus [GO:0005634] | double-stranded DNA endonuclease activity [GO:1990238]; endonuclease activity [GO:0004519]; histone binding [GO:0042393]; magnesium ion binding [GO:0000287]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; sequence-specific DNA binding [GO:0043565]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF12940;PF12560;PF00097; | 6.10.140.510;3.30.40.10; | RAG1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00820}. | 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 | null | null | null | FUNCTION: Catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. In the RAG complex, RAG1 mediates the DNA-binding to the conserved recombination signal sequences (RSS) and catalyzes the DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. RAG2 is not a catalytic component but is required for all known catalytic activities. DNA cleavage occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. In addition to its endonuclease activity, RAG1 also acts as an E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3. Histone H3 monoubiquitination is required for the joining step of V(D)J recombination (By similarity). {ECO:0000250}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
O13034 | RAG2_DANRE | MSLQPLTAVNCGSLVQPGFSLLDLEGDVYLFGQKGWPKRSCPTGIFGVRIKKGELKLRAISFSNNSSYLPPLRCPAIAHFEAQDGKPECYLIHGGRTPNNELSSSLYMLSVDSRGCNRKVTLRCEEKELVGDVPSARYGHTLSVINSRGKTACVLFGGRSYMPPTERTTQNWNSVGDCPPQVYLIDLEFGCCTAHTLPELTDGQSFHVALARQDCVYFLGGHILSSDCRPSRLIRLHVELLLGSPVLTCTILHEGLTITSAIASPIGYHEYIIFGGYQSETQKRMECTYVGLDDVGVHMESREPPQWTSEISHSRTWFGGSLGKGTALVAIPSEGNPTPPEAYHFYQVSFQKEQDGEATAQGCSQESTDFEDSAPLEDSEELYFGREPHELEYSSDVEGDTYNEEDEEDESQTGYWIKCCLSCQVDPNIWEPYYSTELTRPAMIFCSRGEGGHWVHAQCMELPESLLLQLSQDNSKYFCLDHGGLPKQEMTPPKQMLPVKRVPMKMTHRKAPVSLKMTPAKKTFLRRLFD | null | null | B cell differentiation [GO:0030183]; chromatin organization [GO:0006325]; hematopoietic or lymphoid organ development [GO:0048534]; immunoglobulin V(D)J recombination [GO:0033152]; lymphocyte differentiation [GO:0030098]; protein-DNA complex assembly [GO:0065004]; T cell differentiation [GO:0030217]; T cell differentiation in thymus [GO:0033077]; thymus development [GO:0048538]; V(D)J recombination [GO:0033151] | DNA recombinase complex [GO:0097519]; endodeoxyribonuclease complex [GO:1905347]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; methylated histone binding [GO:0035064]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270] | PF03089;PF13341; | 2.120.10.80;3.30.160.290; | RAG2 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Core component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. DNA cleavage by the RAG complex occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. In the RAG complex, rag2 is not the catalytic component but is required for all known catalytic activities mediated by RAG1. It probably acts as a sensor of chromatin state that recruits the RAG complex to H3K4me3 (By similarity). {ECO:0000250}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
O13065 | MMP18_XENLA | MNSLLLKLLLCVAITAAFPADKQDEPPATKEEMAENYLKRFYSLGTDGGPVGRKKHIQPFTEKLEQMQKFFGLKVTGTLDPKTVEVMEKPRCGVYDVGQYSTVAKSSAWQKKDLTYRILNFTPDLPQADVETAIQRAFKVWSDVTPLTFTRIYNEVSDIEISFTAGDHKDNSPFDGSGGILAHAFQPGNGIGGDAHFDEDETWTKTSEIYNLFLVAAHEFGHSLGLSHSTDQGALMYPTYSNTDPKTFQLPQDDINAIQYLYGKSSNPVQPTGPSTPSRCDPNVVFNAVTTMRGELIFFVKRFLWRKHPQASEAELMFVQAFWPSLPTNIDAAYENPITEQILVFKGSKYTALDGFDVVQGYPRNIYSLGFPKTVKRIDAAVHIEQLGKTYFFAAKKYWSYDEDKKQMDKGFPKQISNDFPGIPDKIDAAFYYRGRLYFFIGRSQFEYNINSKRIVQVLRSNSWLGC | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270] | PF00045;PF00413;PF01471; | 3.40.390.10;2.110.10.10; | Peptidase M10A family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: Cleaves collagen type I. May play a role in larval tissue degeneration and adult organogenesis during amphibian metamorphosis. May be involved in tail resorption. | Xenopus laevis (African clawed frog) |
O13076 | AA2BR_CHICK | MNTMKTTYIVLELIIAVLSIAGNVLVCWAVAINSTLKNATNYFLVSLAVADIAVGLLAIPFAITISIGFQVDFHSCLFFACFVLVLTQSSIFSLLAVAIDRYLAIKIPLRYNSLVTGKRARGLIAVLWLLSFVIGLTPLMGWNKAMSGCPNSTNETGADHGAGHHGCFISCLFENVVTMSYMVYFNFFGCVLLPLIIMLGIYIKIFMVACKQLHQIELMGNSRTTLQKEVHAAKSLAIIVGLFAFCWLPLHILNCITHFHEEFSKSKPEWVMYVAIILSHANSVINPIIYAYRIRDFRYTFHKIISKILCKTDDFPKCTTDNNQHLTVTNVNAPAASVTI | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cellular response to extracellular stimulus [GO:0031668]; cGMP-mediated signaling [GO:0019934]; mast cell degranulation [GO:0043303]; positive regulation of cGMP-mediated signaling [GO:0010753]; positive regulation of chemokine production [GO:0032722]; positive regulation of chronic inflammatory response to non-antigenic stimulus [GO:0002882]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of mast cell degranulation [GO:0043306]; positive regulation of vascular endothelial growth factor production [GO:0010575]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; relaxation of vascular associated smooth muscle [GO:0060087]; vasodilation [GO:0042311] | glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; Schaffer collateral - CA1 synapse [GO:0098685] | G protein-coupled adenosine receptor activity [GO:0001609]; G protein-coupled receptor activity [GO:0004930] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. | Gallus gallus (Chicken) |
O13078 | HBB_MERMR | MVEWTDDERAIINSIFSTLDYEEIGRKSLCRCLIVYPWTQRYFGGFGNLYNAETILCNPLIAAHGTKILHGLDRALKNMDDIKNTYAELSQLHSDKLHVDPDNFRLLADCLTVVIAAKMGTAFTVETQVAWQKFLAVVVSALGRQYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues. | Merlangius merlangus (Whiting) (Gadus merlangus) |
O13097 | EFNB1_XENLA | MEGLRRLLGLLLVLYRLCSALGKNLEPVTWNSQNPRFISGKGLVLYPEIGDRLDIICPKGDSSQPYEYYKLYMVRRDQLEACSTVIDPNVLVTCNQPGKEYRFTIKFQEFSPNYMGLEFRRNQDYYITSTSNSTLQGLENREGGVCQTRSMKIIMKVGQDPNAVPPEQLTTTRPSKEADNTGKIATFGPWNGPVENPGKSDTNLSDKPTAGGGVDGFFNSKIAVFAAIGAGCVIFILIIIFLVVLLIKIRKRHRKHTQQRAAALSLSTLASPKCSGNAGSEPSDIIIPLRTTENNYCPHYEKVSGDYGHPVYIVQEMPPQSPANIYYKV | null | null | axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013] | plasma membrane [GO:0005886] | ephrin receptor binding [GO:0046875] | PF00812; | 2.60.40.420; | Ephrin family | PTM: Inducible phosphorylation of tyrosine residues in the cytoplasmic domain. Tyrosine phosphorylation inhibits TLE4-binding. {ECO:0000269|PubMed:21429299}. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling (By similarity). May have a role in the developing mesenchymal and nervous tissue. {ECO:0000250}. | Xenopus laevis (African clawed frog) |
O13146 | EPHA3_DANRE | MALFRIYSFLAPFHILVLCQALRNYPDNEVTLLDSMSAPGDLGWEAYPSEGWEEISVMDERNIPMRTYQVCNVMEANQNNWLRTGLIQREGAQRVYVEIKFTLRDCNSLPGVPGTCKETFNVYYHESNNAVAAPLRHIRESQYIKIDTIAADESFTQTDVGDRVMKLNTEVRDISGLSKRGLYLAFQDLGACIALVSVRVFYKRCPLAVLNLARFPDTVTGGDSALVEVRGTCVEDAEELEGPRMFCSADGGWLVPIGRCVCRPGFEEVDGHCQPCRSGFYKASAMDAYCVKCPPHSYSHQDKASECVCERGFYRAESDPRSMACTRPPSAPGNPISMVNETAVTLEWSPPRDSGGRGDVSYSVHCRKCSGETGASERCVPCGSGAHFNPRQFGLTHPRVLVTELQPHTNYTFSVEALNGVSDLSPSPRQLVSVNVTTSQTVSVILKERKGTDSVTLAWQGPEPVDGTVVEYEVTYYEKNQQDQNYTVLKTKSNSMTVDGLKPGTTYIFRVRARTDGGYGNYKGEIELETSHEDMLAVGDPNQQTILAISVAGGAVLLVLLVACFIVSGRRCGYIKAKQDPEEEKMQFQHGRVKLPETRTYIHPHTYEDPNQAVRDFAKEIEVSNIRIERVIGAGEFGEVCSGRLRLPSKREIQVAIKSLKAGYSEHQRRDFLSEASIMGQFDHPNIIRLEGVVTRCKPVMIVTEYMENGSLDTFLKKHDGQFTVIQLLGMLRGIAAGMQYLSEMNYVHRDLAARNILVNRNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTAPEAITYRKFTSASDVWSYGIVMWEVISYGERPYWEMSNQDVIKAVDEGYRLPAPMDCPVVLHQLMLDCWEKNRSDRPKFGQIVNTLDRLIRNPSSLKQLANSAVWEDPVTPEAAVNTVEDWLDLIKMGQYKEHFSSAGYVTLDSVLYVSSSELDKMGVELAGHQKKILSSIQCLQAHHGTQVQV | 2.7.10.1 | null | axon guidance [GO:0007411]; cell migration [GO:0016477]; ephrin receptor signaling pathway [GO:0048013]; fasciculation of motor neuron axon [GO:0097156]; fasciculation of sensory neuron axon [GO:0097155]; phosphorylation [GO:0016310]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of focal adhesion assembly [GO:0051893]; regulation of GTPase activity [GO:0043087]; regulation of microtubule cytoskeleton organization [GO:0070507] | dendrite [GO:0030425]; early endosome [GO:0005769]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; GPI-linked ephrin receptor activity [GO:0005004]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; transmembrane-ephrin receptor activity [GO:0005005] | PF14575;PF01404;PF00041;PF07714;PF00536; | 2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10; | Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily | PTM: Autophosphorylates upon activation by efna5. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P29320}; 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:0000255|PROSITE-ProRule:PRU10028}; | null | null | null | null | FUNCTION: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially efna5. Upon activation by efna5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation probably through activation by efna1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development (By similarity). {ECO:0000250}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
O13147 | EPHB3_DANRE | PLLVLDLIIQERGESFSHTVTAQHTSAKVEGLKAGTVYSVQVRARTVAGYGRYSNPVDFSTSLYVCPVSSSSTSMHLRRREELTTTTTGLKSREERFQKSDDPERSVQDLLPLIVGSASAGFVVILAMIVIAVVCLRRQRTGSELEYTEKLQQYVSPGVKVYIDPFTYEDPNEAVHEFAREIDISCVKIEEVIGAGEFGEVCRGRLKQAGRKETTVAIKTLKAGYTEHQRRDFLSEASIMGQFDHPNVIHLEGVLTRSCPVLIVTEFMENGALDSFLRLNDGRFTVTQLVGMLRGIAAGMKYLSDMNYVHRDLAARNVLVNSNLVCKVSDFGLSRFLDDNSSDPTYTSSLGGKIPIRWTAPEAIAFRKFTSASDVWSYGIVMWEVMSFGERPYWDMSNQDVMNAVEQDYRLPPPMDCPAVLHQLMLECWVKERNMRPRFGQIVSTLDKFLRNAASLKVLTSTHSGDLCRIGGTLPGHQRKSIGDAQDIKQQMSQTLPIRV | 2.7.10.1 | null | angiogenesis [GO:0001525]; axon guidance [GO:0007411]; axonal fasciculation [GO:0007413]; cell migration [GO:0016477]; dendritic spine development [GO:0060996]; dendritic spine morphogenesis [GO:0060997]; ephrin receptor signaling pathway [GO:0048013]; positive regulation of synapse assembly [GO:0051965]; protein autophosphorylation [GO:0046777]; regulation of axonogenesis [GO:0050770]; regulation of cell-cell adhesion [GO:0022407]; regulation of GTPase activity [GO:0043087]; substrate adhesion-dependent cell spreading [GO:0034446] | dendrite [GO:0030425]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; ephrin receptor activity [GO:0005003]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; transmembrane-ephrin receptor activity [GO:0005005] | PF14575;PF00041;PF07714; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily | PTM: Phosphorylated. Autophosphorylates upon ligand-binding. Autophosphorylation on Tyr-168 is required for interaction with SH2 domain-containing proteins (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; | null | null | null | null | FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Generally has an overlapping and redundant function with EPHB2. Like EPHB2, functions in axon guidance during development. In addition to its role in axon guidance also plays an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and the formation of excitatory synapses. May control other aspects of development through regulation of cell migration and positioning (By similarity). May play a role in early pattern formation within the developing nervous system. {ECO:0000250}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
O13148 | EPA4A_DANRE | IGIGEFGEVCSGRLKMPGKREICVAIKTLKAGYTDKQRRDFLSEASIMGQFDHPNIIRLEGVVTKCKPVMIITEYMENGSLDAFLRKNDGRFTVIQLVGILRGIASGMKYLSDMSYVHRDLAARNILVNSNLVCKVSDFGMSRVLEEDPDAAYTTREITGTYQSQGGKIPIRWTAPEAITYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPPPMDCPVSLHQLMLDCWQKERAERPKFSQIVNMLDKLIRNPNSLKRTGGEIARPNTTLLEPSSPE | 2.7.10.1 | null | anterior/posterior pattern specification [GO:0009952]; axon guidance [GO:0007411]; cell-cell recognition [GO:0009988]; forebrain development [GO:0030900]; negative regulation of axon extension [GO:0030517]; negative regulation of collateral sprouting of intact axon in response to injury [GO:0048685]; optic vesicle morphogenesis [GO:0003404]; phosphorylation [GO:0016310]; regulation of myelination [GO:0031641]; rhombomere boundary formation [GO:0021654]; somite development [GO:0061053] | dendrite [GO:0030425]; early endosome [GO:0005769]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; transmembrane-ephrin receptor activity [GO:0005005] | PF07714; | 1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q03137}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q03137}. Early endosome {ECO:0000250|UniProtKB:Q03137}. Note=Clustered upon activation and targeted to early endosome. {ECO:0000250|UniProtKB:Q03137}. | 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:0000255|PROSITE-ProRule:PRU10028}; | null | null | null | null | FUNCTION: Receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including efna1 and efnb3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections (By similarity). {ECO:0000250|UniProtKB:Q03137}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
O13154 | PACN2_CHICK | MSGSYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCNDLMNCIHERARIEKVYAQQLTEWAKRWKQLVEKGPQYGTVERAWCAFMSEAEKVSELHLEVKGSLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHAACKEEKLAISRETNSKADPALNPEQLKKLQDKVERSKQDVLKTKAKYEKSLKELDNATPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKNIYRELEQNIKTADAVEDLRWFRANQGPGMSMNWPQFEDDEWSADLNRTLSRREKKKASDGVTLTGINQTGDQVSQPNKHSSVSSYEKNQSYPTDWSDEESNNPFSSTDAKGDTNPFDEDTSPVMEVRVRALYDYEGQEQDELSFKAGDELTKMENEDEQGWCKGRLDNGQVGLYPANYVEPIQ | null | null | actin cytoskeleton organization [GO:0030036]; caveola assembly [GO:0070836]; cytoskeleton organization [GO:0007010]; endocytosis [GO:0006897]; negative regulation of endocytosis [GO:0045806]; plasma membrane tubulation [GO:0097320]; regulation of endocytosis [GO:0030100] | caveola [GO:0005901]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; early endosome [GO:0005769]; endosome [GO:0005768]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]; ruffle membrane [GO:0032587] | cytoskeletal protein binding [GO:0008092]; phosphatidic acid binding [GO:0070300]; phospholipid binding [GO:0005543] | PF00611;PF14604; | 1.20.1270.60;2.30.30.40; | PACSIN family | PTM: Phosphorylated on serine residues. {ECO:0000269|PubMed:9287337}. | SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:9287337}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome membrane {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection {ECO:0000250}. Membrane, caveola {ECO:0000250}. Note=Detected at the neck of flask-shaped caveolae. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Regulates the morphogenesis and endocytosis of caveolae (By similarity). Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus. {ECO:0000250, ECO:0000250|UniProtKB:Q9WVE8}. | Gallus gallus (Chicken) |
O13163 | HBB_SILAS | MVXWTDXERHVIADVWGKINPDEIGPHALARLLIVYPWTQRYFSSFGNLSNAAAILGNPKVAAHGKVVVGGLDKAVKHLDNVKGTYAKLSELHSEKLHVDPSNFTLLADCLTITLAAKFGPSVFTPEVHEVWQKFLNVAVAALGKQYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues. | Silurus asotus (Amur catfish) (Parasilurus asotus) |
O13186 | GCR_SAIBB | MDSKESLTPGKEENPSSVLTQERGNVMDFCKILRGGATLKVSVSSTSLAAASQSDSKQQRLLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLQLLEESIANLNRSTSVPENPKSSASSSVSAAPKEKEFPKTHSDVSSEQQNLKGQTGSNGGNVKLYTADQSTFDILQDLEFSSGSPGKETNQSPWKSDLLIDENCLLSPLAGEEDSFLLEGNSNEDCKPLILPDTKPKIKDNGDLVLSSSSNVTLPQVKTEKEDFIELCTPGVIKQEKLSTVYCQASFPGANIIGNKMSAISIHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVGSENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQATTGVSQETSENPANKTIVPATLPQLTPTLVSLLEVIEPEVLYAGYDSTVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQASSNLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSYEEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQLPKYSNGNIKKLLFHQK | null | null | cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to steroid hormone stimulus [GO:0071383]; chromatin organization [GO:0006325]; positive regulation of transcription by RNA polymerase II [GO:0045944] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; spindle [GO:0005819] | DNA-binding transcription factor activity [GO:0003700]; estrogen response element binding [GO:0034056]; nuclear glucocorticoid receptor activity [GO:0004883]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239]; zinc ion binding [GO:0008270] | PF02155;PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Acetylation by CLOCK reduces its binding to glucocorticoid response elements and its transcriptional activity. {ECO:0000250}.; PTM: Increased proteasome-mediated degradation in response to glucocorticoids. {ECO:0000250|UniProtKB:P04150}.; PTM: Phosphorylated in the absence of hormone; becomes hyperphosphorylated in the presence of glucocorticoid. The Ser-203, Ser-226 and Ser-404-phosphorylated forms are mainly cytoplasmic, and the Ser-211-phosphorylated form is nuclear. Phosphorylation at Ser-211 increases transcriptional activity. Phosphorylation at Ser-203, Ser-226 and Ser-404 decreases signaling capacity. Phosphorylation at Ser-404 may protect from glucocorticoid-induced apoptosis. Phosphorylation at Ser-203 and Ser-211 is not required in regulation of chromosome segregation. May be dephosphorylated by PPP5C, attenuates NR3C1 action. {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537}.; PTM: Ubiquitinated; restricts glucocorticoid-mediated transcriptional signaling. {ECO:0000250|UniProtKB:P06537}.; PTM: Sumoylation at Lys-277 and Lys-293 negatively regulates its transcriptional activity. Sumoylation at Lys-703 positively regulates its transcriptional activity in the presence of RWDD3. Sumoylation at Lys-277 and Lys-293 is dispensable whereas sumoylation at Lys-703 is critical for the stimulatory effect of RWDD3 on its transcriptional activity. Heat shock increases sumoylation in a RWDD3-dependent manner. {ECO:0000250|UniProtKB:P06536}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04150}. Nucleus {ECO:0000250|UniProtKB:P04150}. Mitochondrion {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04150}. Note=After ligand activation, translocates from the cytoplasm to the nucleus (By similarity). In the presence of NR1D1 shows a time-dependent subcellular localization, localizing to the cytoplasm at ZT8 and to the nucleus at ZT20 (By similarity). Lacks this diurnal pattern of localization in the absence of NR1D1, localizing to both nucleus and the cytoplasm at ZT8 and ZT20 (By similarity). {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537}. | null | null | null | null | null | FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling. Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth. Mediates glucocorticoid-induced apoptosis. Promotes accurate chromosome segregation during mitosis. May act as a tumor suppressor. May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression. {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537}. | Saimiri boliviensis boliviensis (Bolivian squirrel monkey) |
O13282 | TAF5_SCHPO | MSATNGPQPQDLNRIVLDYLAKKGYSRTEAMLRLEASGSGVSVEEKLKSIEETPDAYTHTYTILRDWVDSSLELYKAELHRILFPIFVHSYLNLLSQDHYEAAKQFYELFKDDHTDLHDFDVKNLKSLSLPSHVAEDRTAQQYRQNKYQLHFSRITFDLLLHFLFENVSNGGSIIIKLINQHIDIHIVPGRPTVLENAKVINEQEGITGQSFERGDAQLQPVKLQQMPMDKEMEKIVEMDLEEEDMMHQNDPNNQSPKLLKEFRKLHEPNAEDAPSRDYIPLPPHKGVDILSEVEAVKDWSKRLHLGPRASLPSVCMYTFHHTNNNMNCAEFSPDSTMIACGFQESYIRLWSIKADKKSLPKSTSVEDSDGSVRLLSHSGPVYGTTFSPDNKYLLSCSEDASARLWSVDTKTALVAYKGHTGPVWDVAFGPFGHYFATASHDQTAQLWSCDHIYPLRVFAGHLSDVDCVTFHPNSAYVLTGSSDKTCRLWDVHRGHSVRVFNGHTQPVTAVAIAPDGHTMASADSEGLIHLWDIGTGRRIKTMRGHRGNIYSLSFSRESTVLVSGGSDCTVRAWDVFKTNYNNPVSSSLTGSVVTPFSAKTSTFNEVNWSTSPDQMVALYTKQTPIFNVSFTRRNLCLAISVS | null | null | positive regulation of DNA-templated transcription [GO:0045893]; transcription initiation at RNA polymerase II promoter [GO:0006367]; transcription initiation-coupled chromatin remodeling [GO:0045815] | cytosol [GO:0005829]; nucleus [GO:0005634]; SAGA complex [GO:0000124]; transcription factor TFIID complex [GO:0005669] | RNA polymerase II general transcription initiation factor activity [GO:0016251] | PF08513;PF04494;PF00400; | 1.25.40.500;2.130.10.10; | WD repeat TAF5 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex that are essential for mediating regulation of RNA polymerase transcription. Regulates the genes involved in ubiquitin-dependent proteolysis during the progression of M-phase of mitosis. {ECO:0000269|PubMed:11279037}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13286 | SRW1_SCHPO | MDEFDGFTRPTSSNSSANRNSNNSMNRVENNNSNSDSANTVDSRGDAHTRMRQGFEKSFPSSPNKKRPRTNEGDRFIPSRDASTELWTGFTKVEGPLTPVKKKQSVADRNFTTLLRSELFGSNDETFNNSPIATPNTTIGVSTPRTDSGIDDIELTQRTPPSSSHTSSSILQNTPVTPSRKIFHYLSPRDRNKSSYGKKAQYQDNPNRTIYSLSPVRSITKDLISASRLEGRELPSIPYRVLDAPGLAGDFYLNLLDWGQCNMLAVALASRVYLWSGISSEVTVMHNFYPTDTVTSLRWVQRGTHLAVGTHNGSVEIWDAATCKKTRTMSGHTERVGALSWNDHVLSSGGRDNHILHRDVRAPEHYFRVLTAHRQEVCGLEWNSNENLLASGGNDNALMVWDKFEEKPLYSFHNHIAAVKAITWSPHQRGILASGGGTADRTIKLWNTQRGSMLHNIDTGSQVCNLLWSKQTNEFISTHGFMENEVALWNYPSVSRVGTLKGHTDRVLYLAMSPNGENIVTGAADETLRFWKLFDSKSKHSASTMSSPFDPTMKIR | null | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; mitotic G1 cell size control checkpoint signaling [GO:0031568]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; positive regulation of anaphase-promoting complex-dependent catabolic process [GO:1905786] | anaphase-promoting complex [GO:0005680]; nucleus [GO:0005634] | anaphase-promoting complex binding [GO:0010997]; ubiquitin ligase activator activity [GO:1990757] | PF12894;PF00400; | 2.130.10.10; | WD repeat CDC20/Fizzy family | PTM: Phosphorylated by cdc2-cdc13-CDK complex. This targets srw1 for proteolysis which in turn promotes cdc13 turnover. Dephosphorylated during G1 arrest. {ECO:0000269|PubMed:10921878, ECO:0000269|PubMed:18257517}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: Has a role in cell differentiation and cell cycling by negatively regulating cig2 and cdc12-associated cdc2. Down-regulates the level of cdc13, particularly in a nitrogen deprived environment. Regulator of cell cycle G1 phase progression. Prevents onset of mitosis during the pre-Start G1 period. Required for degradation of cdc13 mitotic cyclin B during G1 arrest but not during mitotic exit. {ECO:0000269|PubMed:10921878, ECO:0000269|PubMed:9398669, ECO:0000269|PubMed:9571240, ECO:0000269|PubMed:9736616}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13289 | CATA_CANAL | MAPTFTNSNGQPIPEPFATQRVGQHGPLLLQDFNLIDSLAHFDRERIPERVVHAKGSGAYGVFEVTDDITDICAAKFLDTVGKKTRIFTRFSTVGGELGSADTARDPRGFATKFYTEEGNLDLVYNNTPVFFIRDPSKFPHFIHTQKRNPETHLKDANMFWDYLTSNEESIHQVMVLFSDRGTPASYREMNGYSGHTYKWSNKKGEWFYVQVHFISDQGIKTLTNEEAGALAGSNPDYAQEDLFKNIAAGNYPSWTAYIQTMTEAEAKEAEFSVFDLTKVWPHKKYPLRRFGKFTLNENPKNYFAEVEQAAFSPAHTVPYMEPSADPVLQSRLFSYADTHRHRLGTNYTQIPVNCPVTGAVFNPHMRDGAMTVNGNLGSHPNYLASDKPVEFKQFSLQEDQEVWNGAATPFHWKATPADFKQAQELWKVLKRYPNQQEHLAHNIAVHAAGADAAIQDRVFAYFGKVSQDLADAIKKEVLELSPRK | 1.11.1.6 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P15202}; | biological process involved in interaction with host [GO:0051701]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to starvation [GO:0009267]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to chemical stimulus [GO:0036171]; filamentous growth of a population of unicellular organisms in response to starvation [GO:0036170]; hydrogen peroxide catabolic process [GO:0042744]; hydrogen peroxide metabolic process [GO:0042743]; response to hydrogen peroxide [GO:0042542] | cytoplasm [GO:0005737]; fungal-type cell wall [GO:0009277]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777] | catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00199;PF06628; | 2.40.180.10; | Catalase family | null | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:P15202}. | CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013}; | null | null | null | null | FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide. {ECO:0000269|PubMed:18352908}. | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
O13290 | DYHC_SCHPO | MDKNDNSQCQLSTVSDEILIFLKKLLSLSVSDNLDDICETIALQSTFVDTFRSFINDEYYTVIYLYGSPCLTSSPTSPDSCTFGNMTFQWTSLLQDVFSGTSAFAIFKRFPLTDTPLTLQNMLYINQLPILKGGHKSNEIPERPINAIFLYTKYVMSCYFTAYLAMESVDDRSTIDLNSPSKGKELELTCQKFADFERSFTFFCREYQNSDTILQHHPLILSTIKHAEENNLDLSVRLLPSKVLSDSEFYKSLSNLVNVWLKTTRSLIKLFHDQISKTALEEFNFWQFYYRSLSRLNDQLHSRPVLFVLDILAFGKRFHTIASFNSETNIQCFVDKVGKIDALFKEISLDIFLSSSTLESLQLSAALLYSTFSKKWRNTGYPETRVLDFINFITEDLLKLISRLLPALGALSLSNVDFSHRTAVSSDILSLCYIRLKDFLRISGSLKEEQSYYGLKNSIKQIKAFENKLKYIQSFHEKHQQLIGALSEVYGLTHLTELEILEHLNKKEHVFNILTVFKDLQSLNVLDISLKGVNAWNSLETSYYNCMTVLEDEVIAQLKSLLQYSKTSSQMFTTLMRFQPLFFRTRVRTSISDCLHLLVNRIKQELDLLKTRFTEDVSDTELIAMNELRNLPMASSAIIWATQLKNRLHEYTKNINIIFGEDWNNFPDGFELKVECITLQKRLDTNLIFTNWINDVSSRNLNFDFDSKIFYLTQSESAESPLRLSVSIDFDPCSFCKEIRTLAHLGYNIPSQLMELASCLQRIQLIAMCLIDSVQSFNDVSFEISKTEEERFLLQEYELAVRQHIVTGLFISWNDFIVGNLSTPPKCAIGKRNFLKNIHPNVENYAYQFSSLTSLLMNKRNAISHTYMQIQEQLFQLDICEYSGDIFLTIQRKLQDLIDLLYVNGYSNLPPFVRALNLRFQDLLISRCRKFLSFFKTTILTSGNENNDLKSKFSSDMYEKLRGFLKPTNLTIQRNIIEFDPPVYRKKEDSIYLLDMCLQSVVNIPLLSIKTTAQRNCTLIGFFPVINRLESEILGIFESLLFHFDSILGYQNYWKKVEPFLNLNSLNLLLKSELFQLDQCYSLSLYLIHLKSEVDEIGKVTDFKIFSVNNTEFKSQVYLYLREWINALFDRFTFLLGKESEHLLNELDDTHSSLSTVDFTVNNTESLINSLKIFKKAGCYKLNVEHKIITYQNYEMTFNDCDAFSEFNFSLLKDITSKWKDLLESFECRRLKLENNKDEILRNFSEFAKRVNTETLSLISEWCASSLSLIKANYDEFSSTVDDFLFRFSKATEQCLMVKYIKKDLEIEIEESCDFSIQTEEIHLYKKFKDVISSNLEFIVEIKNTRWKLFDTATLSVQTTHQINALESVHTSFQHFKLFTNTKQSLNQLKDCTLLLQKLKSCPLKPVHWISLFEITKSTEQLDFEKLLVSDILGIDLQAHESFITTLLNSAVVEANLENQFNEVHSFWKNSYFSFKSFKGRNYIVVGCQELIDAVEKNMDSLNLIKTSRHFKDGDMNITDLQSKMKIIVKFLNIWKEIQQIWTHLSAIFYESTYIQQLLPELAASFFNSSKTYMHLVTLLKERSYLYKVSNIPSLLESAAKLSTTLEDSKKSLLKYFELQRHKISRLYFLGDDDLMELISNPCDPFVINKQIIKLYPGIRSLIVDTENTNINGCTTNEGNELLFDNPICLLDNTQPLHWISSLEPFLKATLFQLFSTSFQQIRDFYYNKSRNVFCKEWFLRYPSQITLLSLRCTLCHEIETGIADCCLDAVFNFINDGISSLVLLADENELSIKKKVTLMFNELLHFKETVGLLCKNSFNNYFWSREVKAFYREDHDDEAVVIKMFSLEFIYAFEYSELDDPIVYTDLTRNCFSVLLHSIASNLGGSPIGPAGTGKTETVKAVSAYLGKNVFVFNCDNAFNYKTIQRILSGLAQIGTYICFDEFNRLDSGTLSAISYDIQRIQSLVSHSDGLCQSPILLDAPTIFVTMNPGYLGRFKLPSNLKKLFRPIWMGSPDNKKICEILFLSFGFKESSLLSQVLDSFFLCCSGSLSNCLHYDFGLRAMKVVIKAAKRIKGFLKKKNTICQELEILWYAIREVLYPSLIYQDIPLFFKAEESYFNFPAVKANAFIDPDNFEVNIEQTLSKNFFGNNQYLKLKIMQLYQMSEAYNGIILLGKTGSGKSQIFRILQSALLNIGIDCIVYVISPKALTKESLFGSMNMDTREWTDGVFTKLLRKTRDSCYYKRYMFVFDDELSPEWVEAMNSLLDDNKTLTLSNGERIALQPYVKIFFEADSVASLTRATISRCGLICISNIDDNILSSTDKMLSFTSGATNYPLGSSNDEFSTVFSKVLTDEVMMNLISSCYKFSVDLQHIMNFTKQRFFTTFYSLLDQTKLFTRSSNITESLSFKELCNYLKKKICYILAWCCTGDTDAKSRERFTHWLMQNASVDLPEIKDFEHVSILDFDVSLETQSWYPIAGKTLKSSALKYAGNTVIPTLDTVRYAEFLNFSLTKNRCVIFCGPPGSGKSMLMLGTLRSRQDVEVIALNFSISTSSKSVVSFLEQSTVYYRSTGMTIMCPKNHEKVLVLFCDEINLPRSRNCLAEDVICFLRHMLEHQGFWHPLHKEWVTIKNIFVCGACNPSTDIGRNDFPERFLRRTVLIFVDYPESYSLVTIYNALLEKSALINQYKTIILNIVKASVKFYQVLRENFKSSTQGYVYTPRDLTRWLISFKNYAESYAETNNLSLIKVWYHEACRVLLDRLVSQKECSWGMTELQKVIVTDFGEFEVSVIFEKQIIFTDILKNGLEFLDFASLRPKLESLYKKFYSSHPNNTLVFVDETITHILRFHRILNNSGMHALLQGSVGLGQKAVVEFVCWLNSFSLFELQKNQTYSIEDFEDNLKSILILAGTTNCKACLAINESIAGVPGFLDLLNNLLTNSEVSNFFDQNDWAEIKKNLNKLNEFQPLKFDSEESVTEIFMNNVFQNLCVVFYVYTSADVDFQTNSLSPALLNRCTIDYYHSWDYHSMLQIANEVLQETISLNALDHDNPNLKNIKGSSIYDAVAQAVVNTHTSIVWEFKHLGKTSYFSCLHFIRFLNTFCLIFGRDANKLSKEKSRIENGFKKIKETSQGIDKFKEALSDQQNVLFSKTKTANDRLQCIIQTKQAVEAKKVYSLQAEASLQKKSFLLNEKKNSVMKEVSYAKPAVIEARKSVSDIKKAHLIELRSLSRPPMAIRITMEVVCKLLGFSATDWKNVQQLLKRDDFIPKILNYNLEKELSINLRRKIEQDYFSNPIFTFDSVNRASKACGPLLLWIKSICNYSKVLEKLEPLNSEVDRLKLEQKNAEECIQETIAACKDLDEKLLQLQEEYASMISEIHSMELQMDEVKCKMQRSIEVITDLSIERNEWSGFLNLYPKRMWNLVGESLMEASFVVYAGNLDPSMRIFLRNKCEPIISSFGFPISKSAVRTNIERCVQTSIESKYYKNLTDYSLENIYIIQENKSPLLIIDPSSQILDILPSLYKGKASDLISFSNKSFQNQIKLALLSGSAIIIKDAELWDVSIEPLLKPEFFTGSGEVQTTFAKDTITITLPLNIIFFSEVQSNELENKASKFMNVVNFTLSISLLETQMLKSVISVQEPGVFKQKDNCFTLKLSIERQIRSLQEQLLKTLCSSNENIVGTDEIVVLLKNLKEKHETIRLAYSESQSINRKVDELIRRYKLSIKSFLSVVVVFQHFISLKKSYSFSFNFIWSTFHQMLNVVLENRNQDFKSLIMDALRDLIRRCFLYIFPEDRVLFLFLLMFFFFPKETESLRKLLIVNGKTLELEQSYLNFFETCSDSNERGGLESLFFKTHASNIQNFCTEVLANTHCEEDCLKLLYDLWSSAFKVEFSNIKYDFLKIINDESESRMPTIVYLMENCEIDSLLQNAKIPQNIKKLTVSLGSAENESLADSYLKLASTEPLWLFINNIHLSTPWAEKLPSKMSNHLHKNSRIVCLSEIHNQLPHQLLCISRSIVFNKQTSFKNNLLNLLELLPTMTHTLPHNRFRLFFFLSWLHATLAEIYCFTCSSWKEPCYFDDSDFYFGTKILCNILYRNVHLEEFSWGTFKDLLLNVVYGPKVSASSDFIALDKILKRLIAQFKTQISSNILLTDNFKFILPYEITFSSAKEVIGQLPDEIPPGWLDIPENSKRKRTDIYFSMCI | null | null | attachment of mitotic spindle microtubules to kinetochore [GO:0051315]; cytoplasmic microtubule organization [GO:0031122]; dynein-driven meiotic oscillatory nuclear movement [GO:0030989]; homologous chromosome pairing at meiosis [GO:0007129]; karyogamy involved in conjugation with cellular fusion [GO:0000742]; mitotic spindle organization [GO:0007052]; nuclear migration [GO:0007097]; nuclear migration involved in conjugation with cellular fusion [GO:0000743]; retrograde axonal transport [GO:0008090] | cell cortex [GO:0005938]; cortical microtubule cytoskeleton [GO:0030981]; cytoplasmic dynein complex [GO:0005868]; cytoplasmic microtubule [GO:0005881]; meiotic spindle astral microtubule [GO:1990574]; meiotic spindle pole body [GO:0035974]; spindle pole body [GO:0005816] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; dynein intermediate chain binding [GO:0045505]; dynein light intermediate chain binding [GO:0051959]; minus-end-directed microtubule motor activity [GO:0008569] | PF12774;PF12775;PF12780;PF12781;PF18198;PF08385;PF08393;PF17852;PF03028;PF12777; | 1.10.287.2620;1.10.472.130;1.10.8.710;1.20.58.1120;1.20.920.20;1.20.920.30;6.10.140.1060;1.20.140.100;3.20.180.20;3.40.50.300;1.10.8.720; | Dynein heavy chain family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10366596}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:10366596}. Note=Localized at the astral microtubules and the spindle pole body (SPB) during nuclear movements associated with meiotic prophase. | null | null | null | null | null | FUNCTION: Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required for nuclear movement during meiotic prophase. {ECO:0000269|PubMed:10366596}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13297 | CET1_YEAST | MSYTDNPPQTKRALSLDDLVNHDENEKVKLQKLSEAANGSRPFAENLESDINQTETGQAAPIDNYKESTGHGSHSQKPKSRKSSNDDEETDTDDEMGASGEINFDSEMDFDYDKQHRNLLSNGSPPMNDGSDANAKLEKPSDDSIHQNSKSDEEQRIPKQGNEGNIASNYITQVPLQKQKQTEKKIAGNAVGSVVKKEEEANAAVDNIFEEKATLQSKKNNIKRDLEVLNEISASSKPSKYRNVPIWAQKWKPTIKALQSINVKDLKIDPSFLNIIPDDDLTKSVQDWVYATIYSIAPELRSFIELEMKFGVIIDAKGPDRVNPPVSSQCVFTELDAHLTPNIDASLFKELSKYIRGISEVTENTGKFSIIESQTRDSVYRVGLSTQRPRFLRMSTDIKTGRVGQFIEKRHVAQLLLYSPKDSYDVKISLNLELPVPDNDPPEKYKSQSPISERTKDRVSYIHNDSCTRIDITKVENHNQNSKSRQSETTHEVELEINTPALLNAFDNITNDSKEYASLIRTFLNNGTIIRRKLSSLSYEIFEGSKKVM | 3.6.1.74 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:6094533}; | 7-methylguanosine mRNA capping [GO:0006370]; polynucleotide 5' dephosphorylation [GO:0098507]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968] | mRNA capping enzyme complex [GO:0031533] | mRNA 5'-phosphatase activity [GO:0140818]; polynucleotide 5'-phosphatase activity [GO:0004651] | PF02940; | 3.20.100.10; | Fungal TPase family | null | SUBCELLULAR LOCATION: Nucleus. | CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate; Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74; Evidence={ECO:0000269|PubMed:6094533}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67005; Evidence={ECO:0000269|PubMed:6094533}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 uM for pppA-poly(A) {ECO:0000269|PubMed:6094533}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-8.5. {ECO:0000269|PubMed:6094533}; | null | FUNCTION: First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end. {ECO:0000269|PubMed:12788946, ECO:0000269|PubMed:3029058, ECO:0000269|PubMed:6094533}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
O13298 | PHD1_SCHPO | MDTPETSTPYEQVEKGSFFSFRPQKKRVTYHLDEQVGNYHYGDKHPMKPHRITITNHLVMGYGLHNKMSVFSPRMATFGEMSEFHREDYLDFLKRVTPDNAEQFADKFQQFNIGDDCPVFDGTYEFSQRSAGASLDASRKLVQGQTDIAINWSGGLHHAKRGEASGFCYVNDIVLAILNMLRFFPRVLYIDIDIHHGDGVQQAFYESDRVLTVSFHKYNGDFFPATGNFDENGVKGGKYFALNVPLEDGIGDEQYTSLFKSIIEPTINTFQPSAIVLQCGADSLGYDRLGVFNLSIHAHGECVRFTRSFNIPMLVVGGGGYTLRNVARAWCYETSICVNEQIPSELPRETLYYEFFAPDYTLHPRLTTKIENKNTPKALEDLRIRALEQLRYLGGAPSVQMQQIPPDLTGHLEEEDERLNDEYLDKAVDVRVRG | 3.5.1.98 | null | epigenetic regulation of gene expression [GO:0040029]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression, epigenetic [GO:0045814] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; Rpd3L-Expanded complex [GO:0070210]; Set3 complex [GO:0034967] | histone deacetylase activity [GO:0004407]; histone H4K16 deacetylase activity [GO:0034739] | PF00850; | 3.40.800.20; | Histone deacetylase family, HD type 1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9781677}. | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Evidence={ECO:0000269|PubMed:9781677}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197; Evidence={ECO:0000269|PubMed:9781677}; | null | null | null | null | FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:9781677). Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Is not essential (PubMed:9781677). {ECO:0000250, ECO:0000269|PubMed:9781677}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13310 | ORB6_SCHPO | MDKNDYLHFERNPSLFPKSTLDKVQKTKKYIEHYYKVAVDHAVERNQRRINLEQRLATERGSEERKNRQLRASGEKESQFLRFRRTRLSLEDFSTIKVIGKGAFGEVRLVQKLDTGKIYAMKSLLKTEMFKRDQLAHVKAERDLLVESDSPWVVSLYYAFQDSLYLYLIMEFLPGGDLMTMLINYDTFSEDVTRFYMAECVLAIADVHRMGYIHRDIKPDNILIDRDGHIKLSDFGLSTGFYKQDQSASYMKPRTGNTVKRGQMVDAIWLTMSSKDKMATWKKNRRVMAYSTVGTPDYIAPEIFLQQGYGQDCDWWSLGAIMFECLIGWPPFCSENSHETYRKIINWRETLTFPNDIHLSIEARDLMDRLMTDSEHRLGRGGAIEIMQHPFFTGIDWDHIRETAAPFIPNLKSITDTHYFPVDELEQVPEQPVTQQPASVDPQTLEQTNLAFLGYTYKKFNYLTMKGAL | 2.7.11.1 | null | cellular response to salt stress [GO:0071472]; cortical actin cytoskeleton organization [GO:0030866]; establishment or maintenance of actin cytoskeleton polarity [GO:0030950]; intracellular signal transduction [GO:0035556]; maintenance of protein location in cell cortex of cell tip [GO:0097248]; phosphorylation [GO:0016310]; positive regulation of establishment or maintenance of bipolar cell polarity regulating cell shape [GO:2000247]; positive regulation of exocytosis [GO:0045921]; RAM/MOR signaling [GO:0062200]; regulation of establishment or maintenance of bipolar cell polarity regulating cell shape [GO:2000100]; regulation of fungal-type cell wall biogenesis [GO:0032995] | cell cortex of cell tip [GO:0051285]; cell division site [GO:0032153]; cytosol [GO:0005829]; growing cell tip [GO:0035838]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; | null | null | null | null | FUNCTION: Interacts with pak1/shk1 and coordinates cell morphogenesis with the cell cycle. It is essential for maintenance of cell polarity and is involved in mitotic control. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13318 | PHR2_CANAL | MLLKSLFPSILAATSFVSSVAAEDLPAIEIVGNKFFYSNNGSQFYIKGIAYQQNNLDSNESFVDPLANPEHCKRDIPYLEAVDTNVIRVYALDTSQDHTECMQMLQDAGIYVIADLSQPDESINRDDPSWDLDLFERYTSVVDLFHNYTNILGFFAGNEVTNKKSNTDASAFVKAAIRDTKAYIKSKGYRSIPVGYSANDDSAIRVSLADYFACGDEDEAADFFGINMYEWCGDSSYKASGYESATNDYKNLGIPIFFSEYGCNEVRPRKFTEVATLFGDQMTPVWSGGIVYMYFEEENNYGLVSIKDNTVSTLKDYSYYSSEIKDIHPSSAKASAESASSISRTTCPTNTNNWEASTNLPPTPDKEVCECMSASLKCVVDDKVDSDDYSDLFSYICAKIDCDGINANGTTGEYGAYSPCHSKDKLSFVMNLYYEQNKESKSACDFGGSASLQSAKTASSCSAYLSSAGSSGLGTVSGTVRTDTSQSTSDSGSGSSSSSSSSSSSSSSGSSGSKSAASIVSVNLLTKIATIGISIVVGFGLITM | null | null | fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process [GO:0071970]; fungal-type cell wall organization [GO:0031505] | cell surface [GO:0009986]; extracellular vesicle [GO:1903561]; fungal-type cell wall [GO:0009277]; hyphal cell wall [GO:0030446]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; yeast-form cell wall [GO:0030445] | 1,3-beta-glucanosyltransferase activity [GO:0042124]; glucanosyltransferase activity [GO:0042123] | PF03198;PF07983; | 1.20.58.1040;3.20.20.80; | Glycosyl hydrolase 72 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. | null | null | null | null | null | FUNCTION: Required for apical cell growth and plays an essential role in morphogenesis. May be integral to the pathogenic ability of the organism (By similarity). {ECO:0000250}. | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
O13326 | CYSD_SCHPO | MPVESEHFETLQLHAGQEPDAATSSRAVPIYATTSYVFRDCDHGGRLFGLQEPGYIYSRMMNPTADVFEKRIAALEHGAAAIATSSGTSALFMALTTLAKAGDNIVSTSYLYGGTYNLFKVTLPRLGITTKFVNGDDPNDLAAQIDENTKAVYVESIGNPMYNVPDFERIAEVAHAAGVPLMVDNTFGGGGYLVRPIDHGADIVTHSATKWIGGHGTTIGGVIVDSGKFDWKKNSKRFPEFNEPHPGYHGMVFTETFGNLAYAFACRTQTLRDVGGNANPFGVFLLLQGLETLSLRMERHVQNAFALAKYLEKHPKVNWVSYPGLESHVSHKLAKKYLKNGYGAVLSFGAKGGPDQSRKVVNALKLASQLANVGDAKTLVIAPAYTTHLQLTDEEQISAGVTKDLIRVAVGIEHIDDIIADFAQALEVA | 2.5.1.49 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:6526818}; | cysteine biosynthetic process from serine [GO:0006535]; L-homocysteine biosynthetic process [GO:0071269]; methionine metabolic process [GO:0006555]; transsulfuration [GO:0019346] | cytosol [GO:0005829]; nucleus [GO:0005634] | cysteine synthase activity [GO:0004124]; O-acetylhomoserine aminocarboxypropyltransferase activity [GO:0003961]; O-acetylhomoserine sulfhydrylase activity [GO:0051009]; pyridoxal phosphate binding [GO:0030170] | PF01053; | 3.90.1150.10;3.40.640.10; | Trans-sulfuration enzymes family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=methanethiol + O-acetyl-L-homoserine = acetate + H(+) + L-methionine; Xref=Rhea:RHEA:10048, ChEBI:CHEBI:15378, ChEBI:CHEBI:16007, ChEBI:CHEBI:30089, ChEBI:CHEBI:57716, ChEBI:CHEBI:57844; EC=2.5.1.49; Evidence={ECO:0000269|PubMed:11754480, ECO:0000269|PubMed:6526818}; CATALYTIC ACTIVITY: Reaction=hydrogen sulfide + O-acetyl-L-homoserine = acetate + L-homocysteine; Xref=Rhea:RHEA:27822, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, ChEBI:CHEBI:57716, ChEBI:CHEBI:58199; EC=2.5.1.49; Evidence={ECO:0000250|UniProtKB:P06106}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.5 mM for O-acetyl-L-homoserine {ECO:0000269|PubMed:6526818}; KM=11.1 mM for O-succinyl-L-homoserine {ECO:0000269|PubMed:6526818}; KM=10.4 mM for L-homoserine {ECO:0000269|PubMed:6526818}; KM=0.053 mM for H(2)S {ECO:0000269|PubMed:6526818}; Vmax=15.5 umol/min/mg enzyme for O-acetyl-L-homoserine {ECO:0000269|PubMed:6526818}; Vmax=6.2 umol/min/mg enzyme for O-succinyl-L-homoserinee {ECO:0000269|PubMed:6526818}; Vmax=2.5 umol/min/mg enzyme for L-homoserine {ECO:0000269|PubMed:6526818}; | PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from O-acetyl-L-homoserine. {ECO:0000305|PubMed:11754480}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:6526818}; | null | FUNCTION: Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway (PubMed:11754480, PubMed:6526818). Can also use O-succinyl-L-homoserine and L-homoserine as substrates (PubMed:6526818). Has also cysteine synthase (O-acetylserine sulfhydrylase) activity in vitro, but in S.pombe, it seems only to be involved in the alternative pathway of methionine biosynthesis under cysteine deficiency conditions (PubMed:11754480). {ECO:0000269|PubMed:11754480, ECO:0000269|PubMed:6526818, ECO:0000305|PubMed:11754480}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13329 | FOB1_YEAST | MTKPRYNDVLFDDDDSVPSESVTRKSQRRKATSPGESRESSKDRLLILPSMGESYTEYVDSYLNLELLERGERETPIFLESLTRQLTQKIYELIKTKSLTADTLQQISDKYDGVVAENKLLFLQRQYYVDDEGNVRDGRNNDKIYCEPKHVYDMVMATHLMNKHLRGKTLHSFLFSHFANISHAIIDWVQQFCSKCNKKGKIKPLKEYKRPDMYDKLLPMERIHIEVFEPFNGEAIEGKYSYVLLCRDYRSSFMWLLPLKSTKFKHLIPVVSSLFLTFARVPIFVTSSTLDKDDLYDICEEIASKYGLRIGLGLKSSARFHTGGILCIQYALNSYKKECLADWGKCLRYGPYRFNRRRNKRTKRKPVQVLLSEVPGHNAKFETKRERVIENTYSRNMFKMAGGKGLIYLEDVNTFALANEADNSCNNNGILHNNNIGNDNFEEEVQKQFDLTEKNYIDEYDDLAHDSSEGEFEPNTLTPEEKPPHNVDEDRIESTGVAAPMQGTEEPEKGDQKESDGASQVDQSVEITRPETSYYQTLESPSTKRQKLDQQGNGDQTRDFGTSMEL | null | null | chromatin organization [GO:0006325]; chromosome segregation [GO:0007059]; DNA recombination [GO:0006310]; maintenance of DNA repeat elements [GO:0043570]; maintenance of rDNA [GO:0043007]; negative regulation of DNA replication [GO:0008156]; positive regulation of DNA recombination [GO:0045911]; protein localization to nucleolar rDNA repeats [GO:0034503]; rDNA chromatin condensation [GO:0070550]; rDNA heterochromatin formation [GO:0000183]; replication fork arrest at rDNA repeats [GO:0031582] | nucleolus [GO:0005730]; rDNA heterochromatin [GO:0033553] | metal ion binding [GO:0046872]; rDNA spacer replication fork barrier binding [GO:0043110] | null | null | null | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10230397, ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: Required for replication fork blocking activity at the replication fork barrier (RFB) site in rDNA and for recombination hot-spot (HOT1) activity, regulating the recombination rate and the number of rDNA copies. Binds directly to two separated sequences in the RFB. {ECO:0000269|PubMed:14645529, ECO:0000269|PubMed:9078378, ECO:0000269|PubMed:9869636}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
O13339 | TERT_SCHPO | MTEHHTPKSRILRFLENQYVYLCTLNDYVQLVLRGSPASSYSNICERLRSDVQTSFSIFLHSTVVGFDSKPDEGVQFSSPKCSQSELIANVVKQMFDESFERRRNLLMKGFSMNHEDFRAMHVNGVQNDLVSTFPNYLISILESKNWQLLLEIIGSDAMHYLLSKGSIFEALPNDNYLQISGIPLFKNNVFEETVSKKRKRTIETSITQNKSARKEVSWNSISISRFSIFYRSSYKKFKQDLYFNLHSICDRNTVHMWLQWIFPRQFGLINAFQVKQLHKVIPLVSQSTVVPKRLLKVYPLIEQTAKRLHRISLSKVYNHYCPYIDTHDDEKILSYSLKPNQVFAFLRSILVRVFPKLIWGNQRIFEIILKDLETFLKLSRYESFSLHYLMSNIKISEIEWLVLGKRSNAKMCLSDFEKRKQIFAEFIYWLYNSFIIPILQSFFYITESSDLRNRTVYFRKDIWKLLCRPFITSMKMEAFEKINENNVRMDTQKTTLPPAVIRLLPKKNTFRLITNLRKRFLIKMGSNKKMLVSTNQTLRPVASILKHLINEESSGIPFNLEVYMKLLTFKKDLLKHRMFGRKKYFVRIDIKSCYDRIKQDLMFRIVKKKLKDPEFVIRKYATIHATSDRATKNFVSEAFSYFDMVPFEKVVQLLSMKTSDTLFVDFVDYWTKSSSEIFKMLKEHLSGHIVKIGNSQYLQKVGIPQGSILSSFLCHFYMEDLIDEYLSFTKKKGSVLLRVVDDFLFITVNKKDAKKFLNLSLRGFEKHNFSTSLEKTVINFENSNGIINNTFFNESKKRMPFFGFSVNMRSLDTLLACPKIDEALFNSTSVELTKHMGKSFFYKILRSSLASFAQVFIDITHNSKFNSCCNIYRLGYSMCMRAQAYLKRMKDIFIPQRMFITDLLNVIGRKIWKKLAEILGYTSRRFLSSAEVKWLFCLGMRDGLKPSFKYHPCFEQLIYQFQSLTDLIKPLRPVLRQVLFLHRRIAD | 2.7.7.49 | null | DNA strand elongation [GO:0022616]; telomerase catalytic core complex assembly [GO:1904868]; telomere maintenance [GO:0000723]; telomere maintenance via telomerase [GO:0007004] | chromosome, telomeric repeat region [GO:0140445]; nucleus [GO:0005634]; telomerase catalytic core complex [GO:0000333]; telomere cap complex [GO:0000782] | enzyme activator activity [GO:0008047]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; telomerase RNA binding [GO:0070034]; telomerase RNA reverse transcriptase activity [GO:0003721]; telomeric DNA binding [GO:0042162] | PF00078;PF12009; | 1.10.132.70;3.30.70.2630; | Reverse transcriptase family, Telomerase subfamily | null | SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000269|PubMed:24793650}; | null | null | null | null | FUNCTION: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. {ECO:0000269|PubMed:24793650, ECO:0000269|PubMed:9252327}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13345 | AFLQ_ASPPU | MIYSIIICAGALLGFLILQKLLAPKDTRPPLPPGPWRKPIIGNLTDFPPKGTPEWLFWAKHHERYGPMSSLEVMGQTIIMINDAHLGIEIMHKKSALSQMIPDAPFAHMAGWGMSLATERNKQAWKTIRANMKQEIGTRRAIATFHPKMEIGIRRFLLRTLDNPDDLRFHIRKEANAFMMDVAYGYTIAPHGKDELYDLTQQSVRQFSHIFSPGEWSVNFFPILRYVPSWFPGASFQIKAAEYKRTIERMTMVPYLWIKDQVARGCTRPSILLRLLQKGHYESGSHQEQVLVWTNAEFVMGGSDTTVSAVSSFFVAMALYPEVQHQAREELDRVVGPTTLATFEHRSQLPFIDALVKEVFRWHPASPLGAPHITQEDQIWDGYLLPKGALLLPNIWTFTHDPSVYHDPMVFKPERFLERQSSPPETDPMKFVFGFGRRICPGRFVTDEKLFLIACHAISCFLISPKDPGAPEPDWLPGVISQPGPFDLNVVPRSPAHEELIRSIETDHPWKNADATDISQFMARNQMI | 1.14.14.117 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | aflatoxin biosynthetic process [GO:0045122] | null | aflatoxin B synthase activity [GO:0140399]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | null | CATALYTIC ACTIVITY: Reaction=8-O-methylsterigmatocystin + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = aflatoxin B1 + CO2 + 2 H(+) + H2O + methanol + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:35759, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:2504, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:17790, ChEBI:CHEBI:18171, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.117; Evidence={ECO:0000269|PubMed:11996570}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35760; Evidence={ECO:0000269|PubMed:11996570}; CATALYTIC ACTIVITY: Reaction=8-O-methyldihydrosterigmatocystin + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = aflatoxin B2 + CO2 + 2 H(+) + H2O + methanol + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:35763, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:17790, ChEBI:CHEBI:48209, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:72678; EC=1.14.14.117; Evidence={ECO:0000269|PubMed:11996570}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35764; Evidence={ECO:0000269|PubMed:11996570}; | null | PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis. {ECO:0000305|PubMed:15006741}. | null | null | FUNCTION: O-methylsterigmatocystin oxidoreductase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:11996570, PubMed:15006741). The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) (PubMed:15006741). Within the aflatoxin pathway, the O-methylsterigmatocystin oxidoreductase aflQ is involved in the last steps in which OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2 (PubMed:11996570, PubMed:15006741). The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 (PubMed:15006741). {ECO:0000269|PubMed:11996570, ECO:0000305|PubMed:15006741}. | Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1) |
O13351 | PMT3_SCHPO | MSESPSANISDADKSAITPTTGDTSQQDVKPSTEHINLKVVGQDNNEVFFKIKKTTEFSKLMKIYCARQGKSMNSLRFLVDGERIRPDQTPAELDMEDGDQIEAVLEQLGGCTHLCL | null | null | mitotic recombination-dependent replication fork processing [GO:1990426]; protein sumoylation [GO:0016925]; stalled replication fork localization to nuclear periphery [GO:0120290]; telomere maintenance [GO:0000723] | linear element [GO:0030998]; mitotic spindle pole body [GO:0044732]; nucleus [GO:0005634]; PML body [GO:0016605]; septin ring [GO:0005940] | protein tag activity [GO:0031386]; ubiquitin-like protein ligase binding [GO:0044389] | PF11976; | null | Ubiquitin family, SUMO subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10567589}. | null | null | null | null | null | FUNCTION: Required for chromosome segregation where it may be involved in microtubule assembly. Loss of smt3 leads to an increase in telomere length. {ECO:0000269|PubMed:10567589}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13370 | DED1_SCHPO | MSDNVQQQVDSVGSVTEKLQKTNISRPRKYIPPFARDKPSAGAAPAVGDDESVSSRGSSRSQTPSEFSSNYGGRREYNRGGHYGGGEGRQNNYRGGREGGYSNGGGYRNNRGFGQWRDGQHVIGARNTLLERQLFGAVADGTKVSTGINFEKYDDIPVEVSGGDIEPVNEFTSPPLNSHLLQNIKLSGYTQPTPVQKNSIPIVTSGRDLMACAQTGSGKTAGFLFPILSLAFDKGPAAVPVDQDAGMGYRPRKAYPTTLILAPTRELVCQIHEESRKFCYRSWVRPCAVYGGADIRAQIRQIDQGCDLLSATPGRLVDLIDRGRISLANIKFLVLDEADRMLDMGFEPQIRHIVEGADMTSVEERQTLMFSATFPRDIQLLARDFLKDYVFLSVGRVGSTSENITQKVVHVEDSEKRSYLLDILHTLPPEGLTLIFVETKRMADTLTDYLLNSNFPATSIHGDRTQRERERALELFRSGRTSIMVATAVASRGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGQAVAFFNRNNKGIAKELIELLQEANQECPSFLIAMARESSFGGNGRGGRYSGRGGRGGNAYGARDFRRPTNSSSGYSSGPSYSGYGGFESRTPHHGNTYNSGSAQSWW | 3.6.4.13 | null | cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cell division [GO:0051301]; cytoplasmic translational initiation [GO:0002183]; negative regulation of cytoplasmic translational initiation in response to stress [GO:1990625]; regulatory ncRNA-mediated gene silencing [GO:0031047] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA binding [GO:0003729]; RNA helicase activity [GO:0003724]; translation initiation factor activity [GO:0003743] | PF00270;PF00271; | 3.40.50.300; | DEAD box helicase family, DDX3/DED1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; | null | null | null | null | FUNCTION: ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes (By similarity). Inactivation of ded1 blocks mitotic cell cycle progression at G1 and G2/M. Induces sexual development and ascus formation. {ECO:0000250, ECO:0000269|PubMed:10725227, ECO:0000269|PubMed:11711540, ECO:0000269|PubMed:16273369}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
O13397 | ATN1_SCHOC | MTPSIGYVDEDENGQKSKFLRSSDDPYRLSIEEVIEKFETHLENGLSDEQAKSKLAKVGLNNLGADEKISISKILAHQIFNAMVLVLIISLIIALAIKDWISGGVIGFVVFINIFVGFIQELKAEKTMGSLRSLSSPMARALRNGVDSNINAEEVVPGDIIHIKVGDTIPADLRLVDCMNLETDEALLTGESLPVAKDHEEIYDYGAPIPVGDRLNMAFSSSIVAKGRGTGIVVATGLDTEIGKIAKSLKNNDDAVVVKVDKSLNPSTKDYLIAVIKTTKNIIFNVLGTNVGTPLQRKLSWLAILLFWVAVLFAIVVMASQEMRVNRNVAIYAICVALSMIPSSLVVVLTITMAIGAQVMVTKNVIVRKLDSLEALGGINDICSDKTGTLTMGKMIARKVWIPNVGSYLVQNSNEPFNPTVGDISFNENSPKFIKETDDELDFIPHLPSPTPILFEKWLHIATLANIASLNQIQNEMDGSIEWEAHGDATEIAINVFTTRLGYTRDKLIGDSLEHLNEFPFDSSIKRMSTVYKDKDGNSTVYTKGAVERVLSCCKYWYNPELTALSEEDKLLIESNMNALSSEGLRVLAFAQREINISKENVSNREVVESNLIFLGLIGIYDPPRPESAKSVKLCHKAGINVHMLTGDHPGTAKAIAQEVGILPHNLYHYREEVVKVMVMIANEFDSLSDDEIDNLPVLPLVIARCAPQTKVRMIEALHRRGKFVAMTGDGVNDSPSLKKADVGIAMGLNGSDVAKDASDIVLTDDNFASILNAIEEGRRMSSNIQKFVLQLLAENVAQALYLMIGLAFIDKSGYSVFPLSPVEVLWIIVVTSCFPAMGLGQEKASHDILEQPPNATIFTWEVIIDMIAYGFWMAVCCLVCFVCIVYGKGDGSLGENCNEGSDTGCNLVFRGRSGAFAAFTWCALLLAWECIHLRLSFFKMRPELENPWWKQLAIDLWDNQFLFWSVMGAIVSVFPVVYIPVINNKVFLHAPIGYEWGLAVAFTILFLIGAEGWKWFKRVYYRKSNANNPEYDLERNDPFKEYSSFSKSNTMEIV | 7.2.2.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P04191}; | intracellular calcium ion homeostasis [GO:0006874]; intracellular sodium ion homeostasis [GO:0006883]; sodium ion export across plasma membrane [GO:0036376] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type potassium transmembrane transporter activity [GO:0008556]; P-type sodium transporter activity [GO:0008554]; salt transmembrane transporter activity [GO:1901702] | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IID subfamily | PTM: The active site is phosphorylated in presence of sodium or potassium and in conditions of higher pH. Not phosphorylated in presence of calcium ions. {ECO:0000250|UniProtKB:P13587}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9430707}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + Na(+)(in) = ADP + H(+) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:14633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.3; Evidence={ECO:0000305|PubMed:9430707}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14634; Evidence={ECO:0000305|PubMed:9430707}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(in) = ADP + H(+) + K(+)(out) + phosphate; Xref=Rhea:RHEA:75815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O13398}; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of ATP coupled with the export of sodium and potassium from the cell (PubMed:9430707). May be an inefficient potassium exporter (PubMed:9430707). May transport other cations such as lithium (By similarity). Sodium/potassium efflux ATPases are involved in salt tolerance and maintaining the membrane potential across the plasma membrane in high salinity (Na+) or alkaline (K+) environments (PubMed:9430707). {ECO:0000250|UniProtKB:P13587, ECO:0000269|PubMed:9430707}. | Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis) |
O13398 | ATN2_SCHOC | MSSINTNVAEKHSYKERVNTDASSLSADGSVEAHRLTIEQVAKIFNTDIINGLSTSQANQTLKDFGANTLGDGDKISLTKIIAHQVCNAMILVLIISMVIALAIKDWISGGVIGFVVLINISVGFVQEYKAEKTMGSLRSLSSPTARVTRNGDDTTIPAEEVVPGDIVHIKVGDTVPADLRLIDLMNLETDEALLTGESLPITKNHLDVYDDYSVPIPVGDRLNLAYSSSVVSKGRGTGIVIATALDTQIGQIAKSLRNNNSVIRKVDKSNGKPKKREYSKAFCGTIKDIFYNILGINVGTPLQRKLSWLAIFLFWGCRYFCNYCNGIPKNRVNKEVAIYAICVALSMIPSALIVVLTITMAVGAQVMVMKHVIVRKLDSLEALGGINDICSDKTGTLTQGKMIARKTWIPNVGTFNVGNSNDPFNPKAGEVSFVNLSPKFIEETDEEIDFKQKLPSPFPENFNNWLLTATLANIATLNQSRDEETGELVWKAHGDATEIAIQVFTSRLNYGRDSLIENYEHLAEFPFDSSIKRMSAVYQSLQTNQIKVYTKGAVERVLNCCTHWYGHEENDELYDNQQLKELTDDDKHLIESNMNALSTQGLRVLAFATKDITNSSIDLSNRESIESNLIFQGLIGIYDPPRPETAGSVKSCHNAGINVHMLTGDHPGTAKAIAQEVGILPHNLYHYSEEVVKAMCMTANEFDSLSDDEIDKLPVLPLVIARCAPQTKVRMIEALHRRGKFVAMTGDGVNDSPSLKKADVGIAMGLNGSDVAKDASDIVLTDDNFASILNAIEEGRRMSSNIQKFVLQLLAENVAQALYLMVGLAFIDDSGLSVFPLSPVEVLWILVVTSCFPAMDLGQERASDDILEESPNSTIFTWEVIIDMIVYGFWMAVCCLVCFVIIVYGEGDPYLGVNCNKSSSSNSDVCELVFRGRSASFATMTWCALILAWECIHPYNSLFYMRQDTDHPWWKQTVIDLWDNQFLFWSVAIGFISVFPVVYIPVINTKVFLHGPIGYEWGLAVGFSILFLAGSELWKWIKRIHKRKANKKAKNPEYELERSDPFKKYASFSRSNTMDRPELMV | 7.2.2.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P04191}; | intracellular calcium ion homeostasis [GO:0006874]; intracellular pH reduction [GO:0051452]; potassium ion export across plasma membrane [GO:0097623] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type potassium:proton transporter activity [GO:0008900]; P-type sodium transporter activity [GO:0008554]; salt transmembrane transporter activity [GO:1901702] | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IID subfamily | PTM: The active site is phosphorylated in presence of sodium or potassium and in conditions of higher pH. Not phosphorylated in presence of calcium ions. {ECO:0000250|UniProtKB:P13587}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9430707}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + Na(+)(in) = ADP + H(+) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:14633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.3; Evidence={ECO:0000250|UniProtKB:P13587}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14634; Evidence={ECO:0000250|UniProtKB:P13587}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(in) = ADP + H(+) + K(+)(out) + phosphate; Xref=Rhea:RHEA:75815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:9430707}; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of ATP coupled with the export of sodium and potassium from the cell (PubMed:9430707). May be an inefficient sodium exporter (PubMed:9430707). May transport other cations such as lithium (By similarity). Sodium/potassium efflux ATPases are involved in salt tolerance and maintaining the membrane potential across the plasma membrane in high salinity (Na+) or alkaline (K+) environments (PubMed:9430707). {ECO:0000250|UniProtKB:P13587, ECO:0000269|PubMed:9430707}. | Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis) |
O13426 | GLYC_CANAL | MSAYALSQSHRQLTEGHLKDTDPEVDQIIKDEIDRQQHSIVLIASENFTTTAVFDALGTPMCNKYSEGYPGARYYGGNEHIDRMELLCQERALKAFGLTPDKWGVNVQTLSGSPANLQVYQAIMKPHERLMGLDLPHGGHLSHGYQTDSRKISAVSTYFETMPYRVDLETGLIDYDMLEKTAVLYRPKVLVAGTSAYCRLIDYKRMREIADKVGAYLVVDMAHISGLIAAGVIPSPFEYADIVTTTTHKSLRGPRGAMIFFRRGVRSVNPKTGQEILYDLENPINFSVFPGHQGGPHNHTIAALATALKQANTPEFKEYQEQVLKNAKALESEFTKKGYKLVSDGTDSHMVLVSLKDKQIDGARVETVCEKINIALNKNSIPGDKSALVPGGVRIGAPAMTTRGLGEEDFKKIVSYIDFAVNYAKEVQSQLPKDANKLKDFKNAVSGDSEKLKAVRDEIYQWAGSFPLAV | 2.1.2.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; | folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; L-serine catabolic process [GO:0006565]; tetrahydrofolate interconversion [GO:0035999]; tetrahydrofolate metabolic process [GO:0046653] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739] | cobalt ion binding [GO:0050897]; glycine hydroxymethyltransferase activity [GO:0004372]; pyridoxal phosphate binding [GO:0030170]; serine binding [GO:0070905]; zinc ion binding [GO:0008270] | PF00464; | 3.90.1150.10;3.40.640.10; | SHMT family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15378761}. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1; | null | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. | null | null | FUNCTION: Interconversion of serine and glycine. | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
O13437 | FDH_CANBO | MKIVLVLYDAGKHAADEEKLYGCTENKLGIANWLKDQGHELITTSDKEGETSELDKHIPDADIIITTPFHPAYITKERLDKAKNLKLVVVAGVGSDHIDLDYINQTGKKISVLEVTGSNVVSVAEHVVMTMLVLVRNFVPAHEQIINHDWEVAAIAKDAYDIEGKTIATIGAGRIGYRVLERLLPFNPKELLYYDYQALPKEAEEKVGARRVENIEELVAQADIVTVNAPLHAGTKGLINKELLSKFKKGAWLVNTARGAICVAEDVAAALESGQLRGYGGDVWFPQPAPKDHPWRDMRNKYGAGNAMTPHYSGTTLDAQTRYAEGTKNILESFFTGKFDYRPQDIILLNGEYVTKAYGKHDKK | 1.17.1.9 | null | choline catabolic process [GO:0042426]; formate catabolic process [GO:0042183]; methanol oxidation [GO:0015946]; methylamine metabolic process [GO:0030416]; NADH metabolic process [GO:0006734]; NADH regeneration [GO:0006735] | cytosol [GO:0005829]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; formate dehydrogenase (NAD+) activity [GO:0008863]; NAD+ binding [GO:0070403]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]; protein homodimerization activity [GO:0042803] | PF00389;PF02826; | 3.40.50.720; | D-isomer specific 2-hydroxyacid dehydrogenase family, FDH subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03210}. | CATALYTIC ACTIVITY: Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985, ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.17.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|PubMed:10691964, ECO:0000269|PubMed:11171126, ECO:0000269|PubMed:1248477, ECO:0000269|PubMed:17525463, ECO:0000269|PubMed:9226256}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 mM for formate (at 30 degrees Celsius and at pH 7.5) {ECO:0000269|PubMed:1248477}; KM=0.09 mM for NAD (at 30 degrees Celsius and at pH 7.5) {ECO:0000269|PubMed:1248477}; KM=5.6 mM for formate (at 30 degrees Celsius and at pH 7.5) {ECO:0000269|PubMed:10691964}; KM=0.045 mM for NAD (at 30 degrees Celsius and at pH 7.5) {ECO:0000269|PubMed:10691964}; KM=2.42 mM for formate (at 25 degrees Celsius and at pH 7.5) {ECO:0000269|PubMed:11171126}; KM=0.04 mM for NAD (at 25 degrees Celsius and at pH 7.5) {ECO:0000269|PubMed:11171126}; KM=2.4 mM for formate (at 25 degrees Celsius and at pH 7.6) {ECO:0000269|PubMed:11054119}; KM=0.04 mM for NAD (at 25 degrees Celsius and at pH 7.6) {ECO:0000269|PubMed:11054119}; KM=20 mM for formate (at 20 degrees Celsius, at pH 7.5 and after 2 weeks of storage at 4 degrees Celsius in GF buffer) {ECO:0000269|PubMed:17525463}; KM=0.05 mM for NAD (at 20 degrees Celsius, at pH 7.5 and after 2 weeks of storage at 4 degrees Celsius in GF buffer) {ECO:0000269|PubMed:17525463}; KM=35 mM for formate (at 20 degrees Celsius, at pH 7.5 and after 4 months of storage at 4 degrees Celsius in GF buffer) {ECO:0000269|PubMed:17525463}; KM=0.09 mM for NAD (at 20 degrees Celsius, at pH 7.5 and after 4 months of storage at 4 degrees Celsius in GF buffer) {ECO:0000269|PubMed:17525463}; Vmax=6 uM/min/mg enzyme {ECO:0000269|PubMed:10691964}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:10691964, ECO:0000269|PubMed:11054119, ECO:0000269|PubMed:11171126, ECO:0000269|PubMed:1248477, ECO:0000269|PubMed:17525463}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Broad temperature optima between 45 and 55 degrees Celsius. Reaction rate increases steeply up to 55 degrees Celsius. 50% of activity lost after incubation for 20 minutes at 57 degrees Celsius. Thermal stability increases in the presence of glycerol. {ECO:0000269|PubMed:10691964, ECO:0000269|PubMed:11054119, ECO:0000269|PubMed:11171126, ECO:0000269|PubMed:1248477, ECO:0000269|PubMed:17525463}; | FUNCTION: Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms. {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|PubMed:1248477, ECO:0000269|PubMed:9226256}. | Candida boidinii (Yeast) |
O13516 | RS9A_YEAST | MPRAPRTYSKTYSTPKRPYESSRLDAELKLAGEFGLKNKKEIYRISFQLSKIRRAARDLLTRDEKDPKRLFEGNALIRRLVRVGVLSEDKKKLDYVLALKVEDFLERRLQTQVYKLGLAKSVHHARVLITQRHIAVGKQIVNIPSFMVRLDSEKHIDFAPTSPFGGARPGRVARRNAARKAEASGEAADEADEADEE | null | null | maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; ribosomal small subunit biogenesis [GO:0042274]; translation [GO:0006412] | 90S preribosome [GO:0030686]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small-subunit processome [GO:0032040] | rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735] | PF00163;PF01479; | 3.10.290.10; | Universal ribosomal protein uS4 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus, nucleolus {ECO:0000269|PubMed:15590835}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). uS4 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835). {ECO:0000269|PubMed:15590835, ECO:0000305|PubMed:22096102}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
O13527 | YA11B_YEAST | METFTGYLKSTCFHQISPYPPSIMSIQVKVHANILILSFIECLRMPMHRQIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKLRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMNTWDTDKYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMEKSLTEKLPKLNVPLNPKGKKLRAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH | 2.7.7.49; 2.7.7.7; 3.1.26.4 | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; retrotransposition [GO:0032197] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; retrotransposon nucleocapsid [GO:0000943] | DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523] | PF00665;PF07727; | 3.30.420.10; | null | PTM: Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; | null | null | null | null | FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity). {ECO:0000250}.; FUNCTION: Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity). {ECO:0000250}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
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