P46530 · NOTC1_DANRE
- ProteinNeurogenic locus notch homolog protein 1
- Genenotch1a
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids2437 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4+ and CD8+ cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis (By similarity).
Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO) (By similarity).
Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO) (By similarity).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 1656-1657 | Cleavage; by furin-like protease | ||||
Sequence: RE | ||||||
Site | 1712-1713 | Cleavage; by adam17 | ||||
Sequence: AV |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNeurogenic locus notch homolog protein 1
- Short namesNotch 1
- Cleaved into 2 chains
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionP46530
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Notch 1 intracellular domain
Note: Following proteolytical processing NICD is translocated to the nucleus.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 21-1726 | Extracellular | ||||
Sequence: QGQRCSEYCQNGGICEYKPSGEASCRCPADFVGAQCQFPNPCNPSPCRNGGVCRPQMQGNEVGVKCDCVLGFSDRLCLTPVNHACMNSPCRNGGTCSLLTLDTFTCRCQPGWSGKTCQLADPCASNPCANGGQCSAFESHYICTCPPNFHGQTCRQDVNECAVSPSPCRNGGTCINEVGSYLCRCPPEYTGPHCQRLYQPCLPSPCRSGGTCVQTSDTTHTCSCLPGFTGQTCEHNVDDCTQHACENGGPCIDGINTYNCHCDKHWTGQYCTEDVDECELSPNACQNGGTCHNTIGGFHCVCVNGWTGDDCSENIDDCASAACSHGATCHDRVASFFCECPHGRTGLLCHLDDACISNPCQKGSNCDTNPVSGKAICTCPPGYTGSACNQDIDECSLGANPCEHGGRCLNTKGSFQCKCLQGYEGPRCEMDVNECKSNPCQNDATCLDQIGGFHCICMPGYEGVFCQINSDDCASQPCLNGKCIDKINSFHCECPKGFSGSLCQVDVDECASTPCKNGAKCTDGPNKYTCECTPGFSGIHCELDINECASSPCHYGVCRDGVASFTCDCRPGYTGRLCETNINECLSQPCRNGGTCQDRENAYICTCPKGTTGVNCEINIDDCKRKPCDYGKCIDKINGYECVCEPGYSGSMCNINIDDCALNPCHNGGTCIDGVNSFTCLCPDGFRDATCLSQHNECSSNPCIHGSCLDQINSYRCVCEAGWMGRNCDININECLSNPCVNGGTCKDMTSGYLCTCRAGFSGPNCQMNINECASNPCLNQGSCIDDVAGFKCNCMLPYTGEVCENVLAPCSPRPCKNGGVCRESEDFQSFSCNCPAGWQGQTCEVDINECVRNPCTNGGVCENLRGGFQCRCNPGFTGALCENDIDDCEPNPCSNGGVCQDRVNGFVCVCLAGFRGERCAEDIDECVSAPCRNGGNCTDCVNSYTCSCPAGFSGINCEINTPDCTESSCFNGGTCVDGISSFSCVCLPGFTGNYCQHDVNECDSRPCQNGGSCQDGYGTYKCTCPHGYTGLNCQSLVRWCDSSPCKNGGSCWQQGASFTCQCASGWTGIYCDVPSVSCEVAARQQGVSVAVLCRHAGQCVDAGNTHLCRCQAGYTGSYCQEQVDECQPNPCQNGATCTDYLGGYSCECVPGYHGMNCSKEINECLSQPCQNGGTCIDLVNTYKCSCPRGTQGVHCEIDIDDCSPSVDPLTGEPRCFNGGRCVDRVGGYGCVCPAGFVGERCEGDVNECLSDPCDPSGSYNCVQLINDFRCECRTGYTGKRCETVFNGCKDTPCKNGGTCAVASNTKHGYICKCQPGYSGSSCEYDSQSCGSLRCRNGATCVSGHLSPRCLCAPGFSGHECQTRMDSPCLVNPCYNGGTCQPISDAPFYRCSCPANFNGLLCHILDYSFSGGQGRDIAPPVEVEIRCEIAQCEGRGGNAICDTQCNNHACGWDGGDCSLNFDDPWQNCSAALQCWRYFNDGKCDEQCATAGCLYDGFDCQRLEGQCNPLYDQYCRDHYADGHCDQGCNNAECEWDGLDCADDVPQKLAVGSLVLVVHIPPDELRNRSSSFLRELSSLLHTNVVFRRDANGEALIFPYYGSEHELSKHKRSDWTDPGQLMQRARRSLTSFLKPRTRRELDHMEVKGSIVYLEIDNRQCFQQSDECFQSATDVAAFLGALASSGNLNVPYIIEAVTSEGGPPKTGEMY | ||||||
Transmembrane | 1727-1747 | Helical | ||||
Sequence: PMFLVLLALAVLALAAVGVVV | ||||||
Topological domain | 1748-2437 | Cytoplasmic | ||||
Sequence: SRKRKREHGQLWFPEGFKVNEPKKKRREPVGEDSVGLKPLKNSDSSLMDEQLSEWAEDDTNKRFRFEGQSILEMSGQLDHRQWTQQHLDAADLRLNSMAPTPPQGQIENDCMDVNVRGPDGFTPLMIASCSGGGLENENGEAEEDPSADVITDFIYHGANLHNQTDRTGETALHLAARYARSDAAKRLLESCADANVQDNMGRTPLHAAVAADAQGVFQILIRNRATDLDARMHDGTTPLILATRLAVEGMVEELINCHADPNAVDDSGKSALHWAAAVNNVDAAVVLLKNGANKDLQNNKEETPLFLAAREGSYETAKVLLDHLANRDIADHLDQLPRDIAHERMHHDIVRLLEEYNLVRSPPLPLSPPLCCPNTYLGIKPSPGNNNNTAKKTRKPGGKGVGGKDSGKDIRTKKKKSGDGKNGGIMEVGVLSPVDSLESPHGYLSDVSSPPMMTSPFQQSPPISLNQLQGLADSHMGGALQGLGKPFDSAPRLSHLPVANNVGGAQAGACDWLQRVQQQQQQQQQQQQAGMLMPTMLSATNMPQVMGYPTMQSSHLGAPSHMIAHQNMAPMQHQNISHHFLGDLSGLDLQSSSGHAPIQTILPQDSQRMAPPISSTQFLTPPSQHSYSNPMDNTPNHQQVPDHPFLTPSAGSPDQWSSSSPHSNLSDWSEGISSPPTSMQMNHIPEAFK |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MNRFLVKLTLLTAASLATVA | ||||||
Chain | PRO_0000007708 | 21-2437 | Neurogenic locus notch homolog protein 1 | |||
Sequence: QGQRCSEYCQNGGICEYKPSGEASCRCPADFVGAQCQFPNPCNPSPCRNGGVCRPQMQGNEVGVKCDCVLGFSDRLCLTPVNHACMNSPCRNGGTCSLLTLDTFTCRCQPGWSGKTCQLADPCASNPCANGGQCSAFESHYICTCPPNFHGQTCRQDVNECAVSPSPCRNGGTCINEVGSYLCRCPPEYTGPHCQRLYQPCLPSPCRSGGTCVQTSDTTHTCSCLPGFTGQTCEHNVDDCTQHACENGGPCIDGINTYNCHCDKHWTGQYCTEDVDECELSPNACQNGGTCHNTIGGFHCVCVNGWTGDDCSENIDDCASAACSHGATCHDRVASFFCECPHGRTGLLCHLDDACISNPCQKGSNCDTNPVSGKAICTCPPGYTGSACNQDIDECSLGANPCEHGGRCLNTKGSFQCKCLQGYEGPRCEMDVNECKSNPCQNDATCLDQIGGFHCICMPGYEGVFCQINSDDCASQPCLNGKCIDKINSFHCECPKGFSGSLCQVDVDECASTPCKNGAKCTDGPNKYTCECTPGFSGIHCELDINECASSPCHYGVCRDGVASFTCDCRPGYTGRLCETNINECLSQPCRNGGTCQDRENAYICTCPKGTTGVNCEINIDDCKRKPCDYGKCIDKINGYECVCEPGYSGSMCNINIDDCALNPCHNGGTCIDGVNSFTCLCPDGFRDATCLSQHNECSSNPCIHGSCLDQINSYRCVCEAGWMGRNCDININECLSNPCVNGGTCKDMTSGYLCTCRAGFSGPNCQMNINECASNPCLNQGSCIDDVAGFKCNCMLPYTGEVCENVLAPCSPRPCKNGGVCRESEDFQSFSCNCPAGWQGQTCEVDINECVRNPCTNGGVCENLRGGFQCRCNPGFTGALCENDIDDCEPNPCSNGGVCQDRVNGFVCVCLAGFRGERCAEDIDECVSAPCRNGGNCTDCVNSYTCSCPAGFSGINCEINTPDCTESSCFNGGTCVDGISSFSCVCLPGFTGNYCQHDVNECDSRPCQNGGSCQDGYGTYKCTCPHGYTGLNCQSLVRWCDSSPCKNGGSCWQQGASFTCQCASGWTGIYCDVPSVSCEVAARQQGVSVAVLCRHAGQCVDAGNTHLCRCQAGYTGSYCQEQVDECQPNPCQNGATCTDYLGGYSCECVPGYHGMNCSKEINECLSQPCQNGGTCIDLVNTYKCSCPRGTQGVHCEIDIDDCSPSVDPLTGEPRCFNGGRCVDRVGGYGCVCPAGFVGERCEGDVNECLSDPCDPSGSYNCVQLINDFRCECRTGYTGKRCETVFNGCKDTPCKNGGTCAVASNTKHGYICKCQPGYSGSSCEYDSQSCGSLRCRNGATCVSGHLSPRCLCAPGFSGHECQTRMDSPCLVNPCYNGGTCQPISDAPFYRCSCPANFNGLLCHILDYSFSGGQGRDIAPPVEVEIRCEIAQCEGRGGNAICDTQCNNHACGWDGGDCSLNFDDPWQNCSAALQCWRYFNDGKCDEQCATAGCLYDGFDCQRLEGQCNPLYDQYCRDHYADGHCDQGCNNAECEWDGLDCADDVPQKLAVGSLVLVVHIPPDELRNRSSSFLRELSSLLHTNVVFRRDANGEALIFPYYGSEHELSKHKRSDWTDPGQLMQRARRSLTSFLKPRTRRELDHMEVKGSIVYLEIDNRQCFQQSDECFQSATDVAAFLGALASSGNLNVPYIIEAVTSEGGPPKTGEMYPMFLVLLALAVLALAAVGVVVSRKRKREHGQLWFPEGFKVNEPKKKRREPVGEDSVGLKPLKNSDSSLMDEQLSEWAEDDTNKRFRFEGQSILEMSGQLDHRQWTQQHLDAADLRLNSMAPTPPQGQIENDCMDVNVRGPDGFTPLMIASCSGGGLENENGEAEEDPSADVITDFIYHGANLHNQTDRTGETALHLAARYARSDAAKRLLESCADANVQDNMGRTPLHAAVAADAQGVFQILIRNRATDLDARMHDGTTPLILATRLAVEGMVEELINCHADPNAVDDSGKSALHWAAAVNNVDAAVVLLKNGANKDLQNNKEETPLFLAAREGSYETAKVLLDHLANRDIADHLDQLPRDIAHERMHHDIVRLLEEYNLVRSPPLPLSPPLCCPNTYLGIKPSPGNNNNTAKKTRKPGGKGVGGKDSGKDIRTKKKKSGDGKNGGIMEVGVLSPVDSLESPHGYLSDVSSPPMMTSPFQQSPPISLNQLQGLADSHMGGALQGLGKPFDSAPRLSHLPVANNVGGAQAGACDWLQRVQQQQQQQQQQQQAGMLMPTMLSATNMPQVMGYPTMQSSHLGAPSHMIAHQNMAPMQHQNISHHFLGDLSGLDLQSSSGHAPIQTILPQDSQRMAPPISSTQFLTPPSQHSYSNPMDNTPNHQQVPDHPFLTPSAGSPDQWSSSSPHSNLSDWSEGISSPPTSMQMNHIPEAFK | ||||||
Disulfide bond | 25↔35 | |||||
Sequence: CSEYCQNGGIC | ||||||
Disulfide bond | 29↔45 | |||||
Sequence: CQNGGICEYKPSGEASC | ||||||
Disulfide bond | 47↔56 | |||||
Sequence: CPADFVGAQC | ||||||
Disulfide bond | 62↔73 | |||||
Sequence: CNPSPCRNGGVC | ||||||
Disulfide bond | 67↔86 | |||||
Sequence: CRNGGVCRPQMQGNEVGVKC | ||||||
Disulfide bond | 88↔97 | |||||
Sequence: CVLGFSDRLC | ||||||
Disulfide bond | 105↔116 | |||||
Sequence: CMNSPCRNGGTC | ||||||
Disulfide bond | 110↔126 | |||||
Sequence: CRNGGTCSLLTLDTFTC | ||||||
Disulfide bond | 128↔137 | |||||
Sequence: CQPGWSGKTC | ||||||
Disulfide bond | 143↔154 | |||||
Sequence: CASNPCANGGQC | ||||||
Disulfide bond | 148↔163 | |||||
Sequence: CANGGQCSAFESHYIC | ||||||
Disulfide bond | 165↔174 | |||||
Sequence: CPPNFHGQTC | ||||||
Disulfide bond | 181↔194 | |||||
Sequence: CAVSPSPCRNGGTC | ||||||
Disulfide bond | 188↔203 | |||||
Sequence: CRNGGTCINEVGSYLC | ||||||
Disulfide bond | 205↔214 | |||||
Sequence: CPPEYTGPHC | ||||||
Disulfide bond | 221↔232 | |||||
Sequence: CLPSPCRSGGTC | ||||||
Disulfide bond | 226↔242 | |||||
Sequence: CRSGGTCVQTSDTTHTC | ||||||
Glycosylation | 231 | O-linked (Fuc...) threonine; alternate | ||||
Sequence: T | ||||||
Glycosylation | 231 | O-linked (GalNAc...) threonine; alternate | ||||
Sequence: T | ||||||
Disulfide bond | 244↔253 | |||||
Sequence: CLPGFTGQTC | ||||||
Disulfide bond | 260↔271 | |||||
Sequence: CTQHACENGGPC | ||||||
Disulfide bond | 265↔280 | |||||
Sequence: CENGGPCIDGINTYNC | ||||||
Disulfide bond | 282↔291 | |||||
Sequence: CDKHWTGQYC | ||||||
Disulfide bond | 298↔311 | |||||
Sequence: CELSPNACQNGGTC | ||||||
Disulfide bond | 305↔320 | |||||
Sequence: CQNGGTCHNTIGGFHC | ||||||
Disulfide bond | 322↔331 | |||||
Sequence: CVNGWTGDDC | ||||||
Disulfide bond | 338↔349 | |||||
Sequence: CASAACSHGATC | ||||||
Disulfide bond | 343↔358 | |||||
Sequence: CSHGATCHDRVASFFC | ||||||
Disulfide bond | 360↔369 | |||||
Sequence: CPHGRTGLLC | ||||||
Disulfide bond | 375↔386 | |||||
Sequence: CISNPCQKGSNC | ||||||
Disulfide bond | 380↔397 | |||||
Sequence: CQKGSNCDTNPVSGKAIC | ||||||
Disulfide bond | 399↔408 | |||||
Sequence: CPPGYTGSAC | ||||||
Disulfide bond | 415↔428 | |||||
Sequence: CSLGANPCEHGGRC | ||||||
Disulfide bond | 422↔437 | |||||
Sequence: CEHGGRCLNTKGSFQC | ||||||
Disulfide bond | 439↔448 | |||||
Sequence: CLQGYEGPRC | ||||||
Disulfide bond | 455↔466 | |||||
Sequence: CKSNPCQNDATC | ||||||
Disulfide bond | 460↔475 | |||||
Sequence: CQNDATCLDQIGGFHC | ||||||
Disulfide bond | 477↔486 | |||||
Sequence: CMPGYEGVFC | ||||||
Disulfide bond | 493↔503 | |||||
Sequence: CASQPCLNGKC | ||||||
Disulfide bond | 498↔512 | |||||
Sequence: CLNGKCIDKINSFHC | ||||||
Disulfide bond | 514↔523 | |||||
Sequence: CPKGFSGSLC | ||||||
Disulfide bond | 530↔541 | |||||
Sequence: CASTPCKNGAKC | ||||||
Disulfide bond | 535↔550 | |||||
Sequence: CKNGAKCTDGPNKYTC | ||||||
Disulfide bond | 552↔561 | |||||
Sequence: CTPGFSGIHC | ||||||
Disulfide bond | 568↔578 | |||||
Sequence: CASSPCHYGVC | ||||||
Disulfide bond | 573↔587 | |||||
Sequence: CHYGVCRDGVASFTC | ||||||
Disulfide bond | 589↔598 | |||||
Sequence: CRPGYTGRLC | ||||||
Disulfide bond | 605↔616 | |||||
Sequence: CLSQPCRNGGTC | ||||||
Disulfide bond | 610↔625 | |||||
Sequence: CRNGGTCQDRENAYIC | ||||||
Disulfide bond | 627↔636 | |||||
Sequence: CPKGTTGVNC | ||||||
Disulfide bond | 643↔653 | |||||
Sequence: CKRKPCDYGKC | ||||||
Disulfide bond | 648↔662 | |||||
Sequence: CDYGKCIDKINGYEC | ||||||
Disulfide bond | 664↔673 | |||||
Sequence: CEPGYSGSMC | ||||||
Disulfide bond | 680↔691 | |||||
Sequence: CALNPCHNGGTC | ||||||
Disulfide bond | 685↔700 | |||||
Sequence: CHNGGTCIDGVNSFTC | ||||||
Disulfide bond | 702↔711 | |||||
Sequence: CPDGFRDATC | ||||||
Disulfide bond | 718↔728 | |||||
Sequence: CSSNPCIHGSC | ||||||
Disulfide bond | 723↔737 | |||||
Sequence: CIHGSCLDQINSYRC | ||||||
Disulfide bond | 739↔748 | |||||
Sequence: CEAGWMGRNC | ||||||
Disulfide bond | 755↔766 | |||||
Sequence: CLSNPCVNGGTC | ||||||
Disulfide bond | 760↔775 | |||||
Sequence: CVNGGTCKDMTSGYLC | ||||||
Disulfide bond | 777↔786 | |||||
Sequence: CRAGFSGPNC | ||||||
Disulfide bond | 793↔804 | |||||
Sequence: CASNPCLNQGSC | ||||||
Disulfide bond | 798↔813 | |||||
Sequence: CLNQGSCIDDVAGFKC | ||||||
Disulfide bond | 815↔824 | |||||
Sequence: CMLPYTGEVC | ||||||
Disulfide bond | 831↔842 | |||||
Sequence: CSPRPCKNGGVC | ||||||
Disulfide bond | 836↔853 | |||||
Sequence: CKNGGVCRESEDFQSFSC | ||||||
Disulfide bond | 855↔864 | |||||
Sequence: CPAGWQGQTC | ||||||
Disulfide bond | 871↔882 | |||||
Sequence: CVRNPCTNGGVC | ||||||
Disulfide bond | 876↔891 | |||||
Sequence: CTNGGVCENLRGGFQC | ||||||
Disulfide bond | 893↔902 | |||||
Sequence: CNPGFTGALC | ||||||
Disulfide bond | 909↔920 | |||||
Sequence: CEPNPCSNGGVC | ||||||
Disulfide bond | 914↔929 | |||||
Sequence: CSNGGVCQDRVNGFVC | ||||||
Disulfide bond | 931↔940 | |||||
Sequence: CLAGFRGERC | ||||||
Disulfide bond | 947↔958 | |||||
Sequence: CVSAPCRNGGNC | ||||||
Disulfide bond | 952↔967 | |||||
Sequence: CRNGGNCTDCVNSYTC | ||||||
Glycosylation | 957 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 969↔978 | |||||
Sequence: CPAGFSGINC | ||||||
Disulfide bond | 985↔996 | |||||
Sequence: CTESSCFNGGTC | ||||||
Disulfide bond | 990↔1005 | |||||
Sequence: CFNGGTCVDGISSFSC | ||||||
Disulfide bond | 1007↔1016 | |||||
Sequence: CLPGFTGNYC | ||||||
Disulfide bond | 1023↔1034 | |||||
Sequence: CDSRPCQNGGSC | ||||||
Disulfide bond | 1028↔1043 | |||||
Sequence: CQNGGSCQDGYGTYKC | ||||||
Disulfide bond | 1045↔1054 | |||||
Sequence: CPHGYTGLNC | ||||||
Disulfide bond | 1061↔1072 | |||||
Sequence: CDSSPCKNGGSC | ||||||
Disulfide bond | 1066↔1081 | |||||
Sequence: CKNGGSCWQQGASFTC | ||||||
Disulfide bond | 1083↔1092 | |||||
Sequence: CASGWTGIYC | ||||||
Disulfide bond | 1099↔1120 | |||||
Sequence: CEVAARQQGVSVAVLCRHAGQC | ||||||
Disulfide bond | 1114↔1129 | |||||
Sequence: CRHAGQCVDAGNTHLC | ||||||
Disulfide bond | 1131↔1140 | |||||
Sequence: CQAGYTGSYC | ||||||
Disulfide bond | 1147↔1158 | |||||
Sequence: CQPNPCQNGATC | ||||||
Disulfide bond | 1152↔1167 | |||||
Sequence: CQNGATCTDYLGGYSC | ||||||
Disulfide bond | 1169↔1178 | |||||
Sequence: CVPGYHGMNC | ||||||
Glycosylation | 1177 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1185↔1196 | |||||
Sequence: CLSQPCQNGGTC | ||||||
Disulfide bond | 1190↔1205 | |||||
Sequence: CQNGGTCIDLVNTYKC | ||||||
Disulfide bond | 1207↔1216 | |||||
Sequence: CPRGTQGVHC | ||||||
Disulfide bond | 1223↔1242 | |||||
Sequence: CSPSVDPLTGEPRCFNGGRC | ||||||
Disulfide bond | 1236↔1251 | |||||
Sequence: CFNGGRCVDRVGGYGC | ||||||
Disulfide bond | 1253↔1262 | |||||
Sequence: CPAGFVGERC | ||||||
Disulfide bond | 1269↔1282 | |||||
Sequence: CLSDPCDPSGSYNC | ||||||
Disulfide bond | 1274↔1291 | |||||
Sequence: CDPSGSYNCVQLINDFRC | ||||||
Disulfide bond | 1293↔1302 | |||||
Sequence: CRTGYTGKRC | ||||||
Disulfide bond | 1309↔1320 | |||||
Sequence: CKDTPCKNGGTC | ||||||
Disulfide bond | 1314↔1332 | |||||
Sequence: CKNGGTCAVASNTKHGYIC | ||||||
Disulfide bond | 1334↔1343 | |||||
Sequence: CQPGYSGSSC | ||||||
Disulfide bond | 1350↔1361 | |||||
Sequence: CGSLRCRNGATC | ||||||
Disulfide bond | 1355↔1370 | |||||
Sequence: CRNGATCVSGHLSPRC | ||||||
Disulfide bond | 1372↔1381 | |||||
Sequence: CAPGFSGHEC | ||||||
Disulfide bond | 1389↔1400 | |||||
Sequence: CLVNPCYNGGTC | ||||||
Disulfide bond | 1394↔1411 | |||||
Sequence: CYNGGTCQPISDAPFYRC | ||||||
Glycosylation | 1399 | O-linked (Fuc...) threonine; alternate | ||||
Sequence: T | ||||||
Glycosylation | 1399 | O-linked (GalNAc...) threonine; alternate | ||||
Sequence: T | ||||||
Disulfide bond | 1413↔1422 | |||||
Sequence: CPANFNGLLC | ||||||
Disulfide bond | 1447↔1470 | |||||
Sequence: CEIAQCEGRGGNAICDTQCNNHAC | ||||||
Disulfide bond | 1452↔1465 | |||||
Sequence: CEGRGGNAICDTQC | ||||||
Disulfide bond | 1461↔1477 | |||||
Sequence: CDTQCNNHACGWDGGDC | ||||||
Glycosylation | 1487 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1488↔1512 | |||||
Sequence: CSAALQCWRYFNDGKCDEQCATAGC | ||||||
Disulfide bond | 1494↔1507 | |||||
Sequence: CWRYFNDGKCDEQC | ||||||
Disulfide bond | 1503↔1519 | |||||
Sequence: CDEQCATAGCLYDGFDC | ||||||
Disulfide bond | 1526↔1552 | |||||
Sequence: CNPLYDQYCRDHYADGHCDQGCNNAEC | ||||||
Disulfide bond | 1534↔1547 | |||||
Sequence: CRDHYADGHCDQGC | ||||||
Disulfide bond | 1543↔1559 | |||||
Sequence: CDQGCNNAECEWDGLDC | ||||||
Glycosylation | 1585 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000425200 | 1713-2437 | Notch 1 extracellular truncation | |||
Sequence: VTSEGGPPKTGEMYPMFLVLLALAVLALAAVGVVVSRKRKREHGQLWFPEGFKVNEPKKKRREPVGEDSVGLKPLKNSDSSLMDEQLSEWAEDDTNKRFRFEGQSILEMSGQLDHRQWTQQHLDAADLRLNSMAPTPPQGQIENDCMDVNVRGPDGFTPLMIASCSGGGLENENGEAEEDPSADVITDFIYHGANLHNQTDRTGETALHLAARYARSDAAKRLLESCADANVQDNMGRTPLHAAVAADAQGVFQILIRNRATDLDARMHDGTTPLILATRLAVEGMVEELINCHADPNAVDDSGKSALHWAAAVNNVDAAVVLLKNGANKDLQNNKEETPLFLAAREGSYETAKVLLDHLANRDIADHLDQLPRDIAHERMHHDIVRLLEEYNLVRSPPLPLSPPLCCPNTYLGIKPSPGNNNNTAKKTRKPGGKGVGGKDSGKDIRTKKKKSGDGKNGGIMEVGVLSPVDSLESPHGYLSDVSSPPMMTSPFQQSPPISLNQLQGLADSHMGGALQGLGKPFDSAPRLSHLPVANNVGGAQAGACDWLQRVQQQQQQQQQQQQAGMLMPTMLSATNMPQVMGYPTMQSSHLGAPSHMIAHQNMAPMQHQNISHHFLGDLSGLDLQSSSGHAPIQTILPQDSQRMAPPISSTQFLTPPSQHSYSNPMDNTPNHQQVPDHPFLTPSAGSPDQWSSSSPHSNLSDWSEGISSPPTSMQMNHIPEAFK | ||||||
Chain | PRO_0000425201 | 1745-2437 | Notch 1 intracellular domain | |||
Sequence: VVVSRKRKREHGQLWFPEGFKVNEPKKKRREPVGEDSVGLKPLKNSDSSLMDEQLSEWAEDDTNKRFRFEGQSILEMSGQLDHRQWTQQHLDAADLRLNSMAPTPPQGQIENDCMDVNVRGPDGFTPLMIASCSGGGLENENGEAEEDPSADVITDFIYHGANLHNQTDRTGETALHLAARYARSDAAKRLLESCADANVQDNMGRTPLHAAVAADAQGVFQILIRNRATDLDARMHDGTTPLILATRLAVEGMVEELINCHADPNAVDDSGKSALHWAAAVNNVDAAVVLLKNGANKDLQNNKEETPLFLAAREGSYETAKVLLDHLANRDIADHLDQLPRDIAHERMHHDIVRLLEEYNLVRSPPLPLSPPLCCPNTYLGIKPSPGNNNNTAKKTRKPGGKGVGGKDSGKDIRTKKKKSGDGKNGGIMEVGVLSPVDSLESPHGYLSDVSSPPMMTSPFQQSPPISLNQLQGLADSHMGGALQGLGKPFDSAPRLSHLPVANNVGGAQAGACDWLQRVQQQQQQQQQQQQAGMLMPTMLSATNMPQVMGYPTMQSSHLGAPSHMIAHQNMAPMQHQNISHHFLGDLSGLDLQSSSGHAPIQTILPQDSQRMAPPISSTQFLTPPSQHSYSNPMDNTPNHQQVPDHPFLTPSAGSPDQWSSSSPHSNLSDWSEGISSPPTSMQMNHIPEAFK |
Post-translational modification
Synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase in the trans-Golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Following ligand binding, it is cleaved by adam17 to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). Following endocytosis, this fragment is then cleaved by presenilin dependent gamma-secretase to release a Notch-derived peptide containing the intracellular domain (NICD) from the membrane (By similarity).
O-glycosylated on the EGF-like domains. Contains both O-linked fucose and O-linked glucose. O-linked glycosylation by galnt11 is involved in determination of left/right symmetry: glycosylation promotes activation of notch1, possibly by promoting cleavage by adam17, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO) (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Expressed in all cells in pregastrulation stages. During gastrulation is differentially expressed, accumulating predominantly in the prechordal mesoderm and notochord. At the end of gastrulation, expressed along the anterior-posterior axis including the developing neural plate and differentiating mesoderm. Also present in the developing brain and head regions.
Structure
Family & Domains
Features
Showing features for domain, repeat, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 21-57 | EGF-like 1 | ||||
Sequence: QGQRCSEYCQNGGICEYKPSGEASCRCPADFVGAQCQ | ||||||
Domain | 58-98 | EGF-like 2 | ||||
Sequence: FPNPCNPSPCRNGGVCRPQMQGNEVGVKCDCVLGFSDRLCL | ||||||
Domain | 101-138 | EGF-like 3 | ||||
Sequence: VNHACMNSPCRNGGTCSLLTLDTFTCRCQPGWSGKTCQ | ||||||
Domain | 139-175 | EGF-like 4 | ||||
Sequence: LADPCASNPCANGGQCSAFESHYICTCPPNFHGQTCR | ||||||
Domain | 177-215 | EGF-like 5; calcium-binding | ||||
Sequence: DVNECAVSPSPCRNGGTCINEVGSYLCRCPPEYTGPHCQ | ||||||
Domain | 217-254 | EGF-like 6 | ||||
Sequence: LYQPCLPSPCRSGGTCVQTSDTTHTCSCLPGFTGQTCE | ||||||
Domain | 256-292 | EGF-like 7; calcium-binding | ||||
Sequence: NVDDCTQHACENGGPCIDGINTYNCHCDKHWTGQYCT | ||||||
Domain | 294-332 | EGF-like 8; calcium-binding | ||||
Sequence: DVDECELSPNACQNGGTCHNTIGGFHCVCVNGWTGDDCS | ||||||
Domain | 334-370 | EGF-like 9; calcium-binding | ||||
Sequence: NIDDCASAACSHGATCHDRVASFFCECPHGRTGLLCH | ||||||
Domain | 371-409 | EGF-like 10 | ||||
Sequence: LDDACISNPCQKGSNCDTNPVSGKAICTCPPGYTGSACN | ||||||
Domain | 411-449 | EGF-like 11; calcium-binding | ||||
Sequence: DIDECSLGANPCEHGGRCLNTKGSFQCKCLQGYEGPRCE | ||||||
Domain | 451-487 | EGF-like 12; calcium-binding | ||||
Sequence: DVNECKSNPCQNDATCLDQIGGFHCICMPGYEGVFCQ | ||||||
Domain | 489-524 | EGF-like 13; calcium-binding | ||||
Sequence: NSDDCASQPCLNGKCIDKINSFHCECPKGFSGSLCQ | ||||||
Domain | 526-562 | EGF-like 14; calcium-binding | ||||
Sequence: DVDECASTPCKNGAKCTDGPNKYTCECTPGFSGIHCE | ||||||
Domain | 564-599 | EGF-like 15; calcium-binding | ||||
Sequence: DINECASSPCHYGVCRDGVASFTCDCRPGYTGRLCE | ||||||
Domain | 601-637 | EGF-like 16; calcium-binding | ||||
Sequence: NINECLSQPCRNGGTCQDRENAYICTCPKGTTGVNCE | ||||||
Domain | 639-674 | EGF-like 17; calcium-binding | ||||
Sequence: NIDDCKRKPCDYGKCIDKINGYECVCEPGYSGSMCN | ||||||
Domain | 676-712 | EGF-like 18; calcium-binding | ||||
Sequence: NIDDCALNPCHNGGTCIDGVNSFTCLCPDGFRDATCL | ||||||
Domain | 714-749 | EGF-like 19; calcium-binding | ||||
Sequence: QHNECSSNPCIHGSCLDQINSYRCVCEAGWMGRNCD | ||||||
Domain | 751-787 | EGF-like 20; calcium-binding | ||||
Sequence: NINECLSNPCVNGGTCKDMTSGYLCTCRAGFSGPNCQ | ||||||
Domain | 789-825 | EGF-like 21; calcium-binding | ||||
Sequence: NINECASNPCLNQGSCIDDVAGFKCNCMLPYTGEVCE | ||||||
Domain | 827-865 | EGF-like 22 | ||||
Sequence: VLAPCSPRPCKNGGVCRESEDFQSFSCNCPAGWQGQTCE | ||||||
Domain | 867-903 | EGF-like 23; calcium-binding | ||||
Sequence: DINECVRNPCTNGGVCENLRGGFQCRCNPGFTGALCE | ||||||
Domain | 905-941 | EGF-like 24; calcium-binding | ||||
Sequence: DIDDCEPNPCSNGGVCQDRVNGFVCVCLAGFRGERCA | ||||||
Domain | 943-979 | EGF-like 25; calcium-binding | ||||
Sequence: DIDECVSAPCRNGGNCTDCVNSYTCSCPAGFSGINCE | ||||||
Domain | 981-1017 | EGF-like 26 | ||||
Sequence: NTPDCTESSCFNGGTCVDGISSFSCVCLPGFTGNYCQ | ||||||
Domain | 1019-1055 | EGF-like 27; calcium-binding | ||||
Sequence: DVNECDSRPCQNGGSCQDGYGTYKCTCPHGYTGLNCQ | ||||||
Domain | 1057-1093 | EGF-like 28 | ||||
Sequence: LVRWCDSSPCKNGGSCWQQGASFTCQCASGWTGIYCD | ||||||
Domain | 1095-1141 | EGF-like 29 | ||||
Sequence: PSVSCEVAARQQGVSVAVLCRHAGQCVDAGNTHLCRCQAGYTGSYCQ | ||||||
Domain | 1143-1179 | EGF-like 30; calcium-binding | ||||
Sequence: QVDECQPNPCQNGATCTDYLGGYSCECVPGYHGMNCS | ||||||
Domain | 1181-1217 | EGF-like 31; calcium-binding | ||||
Sequence: EINECLSQPCQNGGTCIDLVNTYKCSCPRGTQGVHCE | ||||||
Domain | 1219-1263 | EGF-like 32; calcium-binding | ||||
Sequence: DIDDCSPSVDPLTGEPRCFNGGRCVDRVGGYGCVCPAGFVGERCE | ||||||
Domain | 1265-1303 | EGF-like 33 | ||||
Sequence: DVNECLSDPCDPSGSYNCVQLINDFRCECRTGYTGKRCE | ||||||
Domain | 1305-1344 | EGF-like 34 | ||||
Sequence: VFNGCKDTPCKNGGTCAVASNTKHGYICKCQPGYSGSSCE | ||||||
Domain | 1346-1382 | EGF-like 35 | ||||
Sequence: DSQSCGSLRCRNGATCVSGHLSPRCLCAPGFSGHECQ | ||||||
Domain | 1385-1423 | EGF-like 36 | ||||
Sequence: MDSPCLVNPCYNGGTCQPISDAPFYRCSCPANFNGLLCH | ||||||
Repeat | 1447-1487 | LNR 1 | ||||
Sequence: CEIAQCEGRGGNAICDTQCNNHACGWDGGDCSLNFDDPWQN | ||||||
Repeat | 1488-1525 | LNR 2 | ||||
Sequence: CSAALQCWRYFNDGKCDEQCATAGCLYDGFDCQRLEGQ | ||||||
Repeat | 1526-1566 | LNR 3 | ||||
Sequence: CNPLYDQYCRDHYADGHCDQGCNNAECEWDGLDCADDVPQK | ||||||
Region | 1770-1790 | Disordered | ||||
Sequence: KKKRREPVGEDSVGLKPLKNS | ||||||
Repeat | 1867-1910 | ANK 1 | ||||
Sequence: DGFTPLMIASCSGGGLENENGEAEEDPSADVITDFIYHGANLHN | ||||||
Repeat | 1915-1944 | ANK 2 | ||||
Sequence: TGETALHLAARYARSDAAKRLLESCADANV | ||||||
Repeat | 1948-1978 | ANK 3 | ||||
Sequence: MGRTPLHAAVAADAQGVFQILIRNRATDLDA | ||||||
Repeat | 1982-2011 | ANK 4 | ||||
Sequence: DGTTPLILATRLAVEGMVEELINCHADPNA | ||||||
Repeat | 2015-2044 | ANK 5 | ||||
Sequence: SGKSALHWAAAVNNVDAAVVLLKNGANKDL | ||||||
Repeat | 2048-2077 | ANK 6 | ||||
Sequence: KEETPLFLAAREGSYETAKVLLDHLANRDI | ||||||
Compositional bias | 2127-2141 | Polar residues | ||||
Sequence: IKPSPGNNNNTAKKT | ||||||
Region | 2127-2174 | Disordered | ||||
Sequence: IKPSPGNNNNTAKKTRKPGGKGVGGKDSGKDIRTKKKKSGDGKNGGIM | ||||||
Compositional bias | 2146-2169 | Basic and acidic residues | ||||
Sequence: GKGVGGKDSGKDIRTKKKKSGDGK | ||||||
Compositional bias | 2356-2429 | Polar residues | ||||
Sequence: RMAPPISSTQFLTPPSQHSYSNPMDNTPNHQQVPDHPFLTPSAGSPDQWSSSSPHSNLSDWSEGISSPPTSMQM | ||||||
Region | 2356-2437 | Disordered | ||||
Sequence: RMAPPISSTQFLTPPSQHSYSNPMDNTPNHQQVPDHPFLTPSAGSPDQWSSSSPHSNLSDWSEGISSPPTSMQMNHIPEAFK |
Sequence similarities
Belongs to the NOTCH family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length2,437
- Mass (Da)262,308
- Last updated1995-11-01 v1
- ChecksumD8C21012AA4CA8FC
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 2127-2141 | Polar residues | ||||
Sequence: IKPSPGNNNNTAKKT | ||||||
Compositional bias | 2146-2169 | Basic and acidic residues | ||||
Sequence: GKGVGGKDSGKDIRTKKKKSGDGK | ||||||
Compositional bias | 2356-2429 | Polar residues | ||||
Sequence: RMAPPISSTQFLTPPSQHSYSNPMDNTPNHQQVPDHPFLTPSAGSPDQWSSSSPHSNLSDWSEGISSPPTSMQM |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X69088 EMBL· GenBank· DDBJ | CAA48831.1 EMBL· GenBank· DDBJ | mRNA |