Q61982 · NOTC3_MOUSE
- ProteinNeurogenic locus notch homolog protein 3
- GeneNotch3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2318 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 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 (By similarity).
May play a role during CNS development
May play a role during CNS development
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 1572-1573 | Cleavage; by furin-like protease | ||||
Sequence: RE |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNeurogenic locus notch homolog protein 3
- Short namesNotch 3
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ61982
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Notch 3 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 | 40-1643 | Extracellular | ||||
Sequence: APPCLDGSPCANGGRCTHQQPSLEAACLCLPGWVGERCQLEDPCHSGPCAGRGVCQSSVVAGTARFSCRCLRGFQGPDCSQPDPCVSRPCVHGAPCSVGPDGRFACACPPGYQGQSCQSDIDECRSGTTCRHGGTCLNTPGSFRCQCPLGYTGLLCENPVVPCAPSPCRNGGTCRQSSDVTYDCACLPGFEGQNCEVNVDDCPGHRCLNGGTCVDGVNTYNCQCPPEWTGQFCTEDVDECQLQPNACHNGGTCFNLLGGHSCVCVNGWTGESCSQNIDDCATAVCFHGATCHDRVASFYCACPMGKTGLLCHLDDACVSNPCHEDAICDTNPVSGRAICTCPPGFTGGACDQDVDECSIGANPCEHLGRCVNTQGSFLCQCGRGYTGPRCETDVNECLSGPCRNQATCLDRIGQFTCICMAGFTGTYCEVDIDECQSSPCVNGGVCKDRVNGFSCTCPSGFSGSMCQLDVDECASTPCRNGAKCVDQPDGYECRCAEGFEGTLCERNVDDCSPDPCHHGRCVDGIASFSCACAPGYTGIRCESQVDECRSQPCRYGGKCLDLVDKYLCRCPPGTTGVNCEVNIDDCASNPCTFGVCRDGINRYDCVCQPGFTGPLCNVEINECASSPCGEGGSCVDGENGFHCLCPPGSLPPLCLPANHPCAHKPCSHGVCHDAPGGFRCVCEPGWSGPRCSQSLAPDACESQPCQAGGTCTSDGIGFRCTCAPGFQGHQCEVLSPCTPSLCEHGGHCESDPDRLTVCSCPPGWQGPRCQQDVDECAGASPCGPHGTCTNLPGNFRCICHRGYTGPFCDQDIDDCDPNPCLHGGSCQDGVGSFSCSCLDGFAGPRCARDVDECLSSPCGPGTCTDHVASFTCACPPGYGGFHCEIDLPDCSPSSCFNGGTCVDGVSSFSCLCRPGYTGTHCQYEADPCFSRPCLHGGICNPTHPGFECTCREGFTGSQCQNPVDWCSQAPCQNGGRCVQTGAYCICPPGWSGRLCDIQSLPCTEAAAQMGVRLEQLCQEGGKCIDKGRSHYCVCPEGRTGSHCEHEVDPCTAQPCQHGGTCRGYMGGYVCECPAGYAGDSCEDNIDECASQPCQNGGSCIDLVARYLCSCPPGTLGVLCEINEDDCDLGPSLDSGVQCLHNGTCVDLVGGFRCNCPPGYTGLHCEADINECRPGACHAAHTRDCLQDPGGHFRCVCHPGFTGPRCQIALSPCESQPCQHGGQCRHSLGRGGGLTFTCHCVPPFWGLRCERVARSCRELQCPVGIPCQQTARGPRCACPPGLSGPSCRVSRASPSGATNASCASAPCLHGGSCLPVQSVPFFRCVCAPGWGGPRCETPSAAPEVPEEPRCPRAACQAKRGDQNCDRECNTPGCGWDGGDCSLNVDDPWRQCEALQCWRLFNNSRCDPACSSPACLYDNFDCYSGGRDRTCNPVYEKYCADHFADGRCDQGCNTEECGWDGLDCASEVPALLARGVLVLTVLLPPEELLRSSADFLQRLSAILRTSLRFRLDARGQAMVFPYHRPSPGSESRVRRELGPEVIGSVVMLEIDNRLCLQSAENDHCFPDAQSAADYLGALSAVERLDFPYPLRDVRGEPLEAPEQSVP | ||||||
Transmembrane | 1644-1664 | Helical | ||||
Sequence: LLPLLVAGAVFLLIIFILGVM | ||||||
Topological domain | 1665-2318 | Cytoplasmic | ||||
Sequence: VARRKREHSTLWFPEGFALHKDIAAGHKGRREPVGQDALGMKNMAKGESLMGEVVTDLNDSECPEAKRLKVEEPGMGAEEPEDCRQWTQHHLVAADIRVAPATALTPPQGDADADGVDVNVRGPDGFTPLMLASFCGGALEPMPAEEDEADDTSASIISDLICQGAQLGARTDRTGETALHLAARYARADAAKRLLDAGADTNAQDHSGRTPLHTAVTADAQGVFQILIRNRSTDLDARMADGSTALILAARLAVEGMVEELIASHADVNAVDELGKSALHWAAAVNNVEATLALLKNGANKDMQDSKEETPLFLAAREGSYEAAKLLLDHLANREITDHLDRLPRDVAQERLHQDIVRLLDQPSGPRSPSGPHGLGPLLCPPGAFLPGLKAVQSGTKKSRRPPGKTGLGPQGTRGRGKKLTLACPGPLADSSVTLSPVDSLDSPRPFSGPPASPGGFPLEGPYATTATAVSLAQLGASRAGPLGRQPPGGCVLSFGLLNPVAVPLDWARLPPPAPPGPSFLLPLAPGPQLLNPGAPVSPQERPPPYLAAPGHGEEYPAAGTRSSPTKARFLRVPSEHPYLTPSPESPEHWASPSPPSLSDWSDSTPSPATATNATASGALPAQPHPISVPSLPQSQTQLGPQPEVTPKRQVMA |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 1664 | No effect on NICD processing. | ||||
Sequence: M → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 134 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-39 | |||||
Sequence: MGLGARGRRRRRRLMALPPPPPPMRALPLLLLLAGLGAA | ||||||
Chain | PRO_0000007695 | 40-2318 | Neurogenic locus notch homolog protein 3 | |||
Sequence: APPCLDGSPCANGGRCTHQQPSLEAACLCLPGWVGERCQLEDPCHSGPCAGRGVCQSSVVAGTARFSCRCLRGFQGPDCSQPDPCVSRPCVHGAPCSVGPDGRFACACPPGYQGQSCQSDIDECRSGTTCRHGGTCLNTPGSFRCQCPLGYTGLLCENPVVPCAPSPCRNGGTCRQSSDVTYDCACLPGFEGQNCEVNVDDCPGHRCLNGGTCVDGVNTYNCQCPPEWTGQFCTEDVDECQLQPNACHNGGTCFNLLGGHSCVCVNGWTGESCSQNIDDCATAVCFHGATCHDRVASFYCACPMGKTGLLCHLDDACVSNPCHEDAICDTNPVSGRAICTCPPGFTGGACDQDVDECSIGANPCEHLGRCVNTQGSFLCQCGRGYTGPRCETDVNECLSGPCRNQATCLDRIGQFTCICMAGFTGTYCEVDIDECQSSPCVNGGVCKDRVNGFSCTCPSGFSGSMCQLDVDECASTPCRNGAKCVDQPDGYECRCAEGFEGTLCERNVDDCSPDPCHHGRCVDGIASFSCACAPGYTGIRCESQVDECRSQPCRYGGKCLDLVDKYLCRCPPGTTGVNCEVNIDDCASNPCTFGVCRDGINRYDCVCQPGFTGPLCNVEINECASSPCGEGGSCVDGENGFHCLCPPGSLPPLCLPANHPCAHKPCSHGVCHDAPGGFRCVCEPGWSGPRCSQSLAPDACESQPCQAGGTCTSDGIGFRCTCAPGFQGHQCEVLSPCTPSLCEHGGHCESDPDRLTVCSCPPGWQGPRCQQDVDECAGASPCGPHGTCTNLPGNFRCICHRGYTGPFCDQDIDDCDPNPCLHGGSCQDGVGSFSCSCLDGFAGPRCARDVDECLSSPCGPGTCTDHVASFTCACPPGYGGFHCEIDLPDCSPSSCFNGGTCVDGVSSFSCLCRPGYTGTHCQYEADPCFSRPCLHGGICNPTHPGFECTCREGFTGSQCQNPVDWCSQAPCQNGGRCVQTGAYCICPPGWSGRLCDIQSLPCTEAAAQMGVRLEQLCQEGGKCIDKGRSHYCVCPEGRTGSHCEHEVDPCTAQPCQHGGTCRGYMGGYVCECPAGYAGDSCEDNIDECASQPCQNGGSCIDLVARYLCSCPPGTLGVLCEINEDDCDLGPSLDSGVQCLHNGTCVDLVGGFRCNCPPGYTGLHCEADINECRPGACHAAHTRDCLQDPGGHFRCVCHPGFTGPRCQIALSPCESQPCQHGGQCRHSLGRGGGLTFTCHCVPPFWGLRCERVARSCRELQCPVGIPCQQTARGPRCACPPGLSGPSCRVSRASPSGATNASCASAPCLHGGSCLPVQSVPFFRCVCAPGWGGPRCETPSAAPEVPEEPRCPRAACQAKRGDQNCDRECNTPGCGWDGGDCSLNVDDPWRQCEALQCWRLFNNSRCDPACSSPACLYDNFDCYSGGRDRTCNPVYEKYCADHFADGRCDQGCNTEECGWDGLDCASEVPALLARGVLVLTVLLPPEELLRSSADFLQRLSAILRTSLRFRLDARGQAMVFPYHRPSPGSESRVRRELGPEVIGSVVMLEIDNRLCLQSAENDHCFPDAQSAADYLGALSAVERLDFPYPLRDVRGEPLEAPEQSVPLLPLLVAGAVFLLIIFILGVMVARRKREHSTLWFPEGFALHKDIAAGHKGRREPVGQDALGMKNMAKGESLMGEVVTDLNDSECPEAKRLKVEEPGMGAEEPEDCRQWTQHHLVAADIRVAPATALTPPQGDADADGVDVNVRGPDGFTPLMLASFCGGALEPMPAEEDEADDTSASIISDLICQGAQLGARTDRTGETALHLAARYARADAAKRLLDAGADTNAQDHSGRTPLHTAVTADAQGVFQILIRNRSTDLDARMADGSTALILAARLAVEGMVEELIASHADVNAVDELGKSALHWAAAVNNVEATLALLKNGANKDMQDSKEETPLFLAAREGSYEAAKLLLDHLANREITDHLDRLPRDVAQERLHQDIVRLLDQPSGPRSPSGPHGLGPLLCPPGAFLPGLKAVQSGTKKSRRPPGKTGLGPQGTRGRGKKLTLACPGPLADSSVTLSPVDSLDSPRPFSGPPASPGGFPLEGPYATTATAVSLAQLGASRAGPLGRQPPGGCVLSFGLLNPVAVPLDWARLPPPAPPGPSFLLPLAPGPQLLNPGAPVSPQERPPPYLAAPGHGEEYPAAGTRSSPTKARFLRVPSEHPYLTPSPESPEHWASPSPPSLSDWSDSTPSPATATNATASGALPAQPHPISVPSLPQSQTQLGPQPEVTPKRQVMA | ||||||
Disulfide bond | 43↔55 | |||||
Sequence: CLDGSPCANGGRC | ||||||
Disulfide bond | 49↔66 | |||||
Sequence: CANGGRCTHQQPSLEAAC | ||||||
Disulfide bond | 68↔77 | |||||
Sequence: CLPGWVGERC | ||||||
Disulfide bond | 83↔94 | |||||
Sequence: CHSGPCAGRGVC | ||||||
Disulfide bond | 88↔107 | |||||
Sequence: CAGRGVCQSSVVAGTARFSC | ||||||
Disulfide bond | 109↔118 | |||||
Sequence: CLRGFQGPDC | ||||||
Disulfide bond | 124↔135 | |||||
Sequence: CVSRPCVHGAPC | ||||||
Disulfide bond | 129↔145 | |||||
Sequence: CVHGAPCSVGPDGRFAC | ||||||
Disulfide bond | 147↔156 | |||||
Sequence: CPPGYQGQSC | ||||||
Disulfide bond | 163↔175 | |||||
Sequence: CRSGTTCRHGGTC | ||||||
Disulfide bond | 169↔184 | |||||
Sequence: CRHGGTCLNTPGSFRC | ||||||
Disulfide bond | 186↔195 | |||||
Sequence: CPLGYTGLLC | ||||||
Disulfide bond | 202↔213 | |||||
Sequence: CAPSPCRNGGTC | ||||||
Disulfide bond | 207↔223 | |||||
Sequence: CRNGGTCRQSSDVTYDC | ||||||
Disulfide bond | 225↔234 | |||||
Sequence: CLPGFEGQNC | ||||||
Disulfide bond | 241↔252 | |||||
Sequence: CPGHRCLNGGTC | ||||||
Disulfide bond | 246↔261 | |||||
Sequence: CLNGGTCVDGVNTYNC | ||||||
Disulfide bond | 263↔272 | |||||
Sequence: CPPEWTGQFC | ||||||
Disulfide bond | 279↔292 | |||||
Sequence: CQLQPNACHNGGTC | ||||||
Disulfide bond | 286↔301 | |||||
Sequence: CHNGGTCFNLLGGHSC | ||||||
Disulfide bond | 303↔312 | |||||
Sequence: CVNGWTGESC | ||||||
Disulfide bond | 319↔330 | |||||
Sequence: CATAVCFHGATC | ||||||
Disulfide bond | 324↔339 | |||||
Sequence: CFHGATCHDRVASFYC | ||||||
Disulfide bond | 341↔350 | |||||
Sequence: CPMGKTGLLC | ||||||
Disulfide bond | 356↔367 | |||||
Sequence: CVSNPCHEDAIC | ||||||
Disulfide bond | 361↔378 | |||||
Sequence: CHEDAICDTNPVSGRAIC | ||||||
Disulfide bond | 380↔389 | |||||
Sequence: CPPGFTGGAC | ||||||
Disulfide bond | 396↔409 | |||||
Sequence: CSIGANPCEHLGRC | ||||||
Disulfide bond | 403↔418 | |||||
Sequence: CEHLGRCVNTQGSFLC | ||||||
Disulfide bond | 420↔429 | |||||
Sequence: CGRGYTGPRC | ||||||
Disulfide bond | 436↔447 | |||||
Sequence: CLSGPCRNQATC | ||||||
Disulfide bond | 441↔456 | |||||
Sequence: CRNQATCLDRIGQFTC | ||||||
Disulfide bond | 458↔467 | |||||
Sequence: CMAGFTGTYC | ||||||
Disulfide bond | 474↔485 | |||||
Sequence: CQSSPCVNGGVC | ||||||
Disulfide bond | 479↔494 | |||||
Sequence: CVNGGVCKDRVNGFSC | ||||||
Disulfide bond | 496↔505 | |||||
Sequence: CPSGFSGSMC | ||||||
Disulfide bond | 512↔523 | |||||
Sequence: CASTPCRNGAKC | ||||||
Disulfide bond | 517↔532 | |||||
Sequence: CRNGAKCVDQPDGYEC | ||||||
Disulfide bond | 534↔543 | |||||
Sequence: CAEGFEGTLC | ||||||
Disulfide bond | 550↔560 | |||||
Sequence: CSPDPCHHGRC | ||||||
Disulfide bond | 555↔569 | |||||
Sequence: CHHGRCVDGIASFSC | ||||||
Disulfide bond | 571↔580 | |||||
Sequence: CAPGYTGIRC | ||||||
Disulfide bond | 587↔598 | |||||
Sequence: CRSQPCRYGGKC | ||||||
Disulfide bond | 592↔607 | |||||
Sequence: CRYGGKCLDLVDKYLC | ||||||
Disulfide bond | 609↔618 | |||||
Sequence: CPPGTTGVNC | ||||||
Disulfide bond | 625↔635 | |||||
Sequence: CASNPCTFGVC | ||||||
Disulfide bond | 630↔644 | |||||
Sequence: CTFGVCRDGINRYDC | ||||||
Disulfide bond | 646↔655 | |||||
Sequence: CQPGFTGPLC | ||||||
Disulfide bond | 662↔673 | |||||
Sequence: CASSPCGEGGSC | ||||||
Disulfide bond | 667↔682 | |||||
Sequence: CGEGGSCVDGENGFHC | ||||||
Disulfide bond | 684↔693 | |||||
Sequence: CPPGSLPPLC | ||||||
Disulfide bond | 700↔710 | |||||
Sequence: CAHKPCSHGVC | ||||||
Disulfide bond | 705↔719 | |||||
Sequence: CSHGVCHDAPGGFRC | ||||||
Disulfide bond | 721↔730 | |||||
Sequence: CEPGWSGPRC | ||||||
Disulfide bond | 739↔750 | |||||
Sequence: CESQPCQAGGTC | ||||||
Disulfide bond | 744↔759 | |||||
Sequence: CQAGGTCTSDGIGFRC | ||||||
Disulfide bond | 761↔770 | |||||
Sequence: CAPGFQGHQC | ||||||
Disulfide bond | 776↔787 | |||||
Sequence: CTPSLCEHGGHC | ||||||
Disulfide bond | 781↔797 | |||||
Sequence: CEHGGHCESDPDRLTVC | ||||||
Disulfide bond | 799↔808 | |||||
Sequence: CPPGWQGPRC | ||||||
Disulfide bond | 815↔827 | |||||
Sequence: CAGASPCGPHGTC | ||||||
Disulfide bond | 821↔836 | |||||
Sequence: CGPHGTCTNLPGNFRC | ||||||
Disulfide bond | 838↔847 | |||||
Sequence: CHRGYTGPFC | ||||||
Disulfide bond | 854↔865 | |||||
Sequence: CDPNPCLHGGSC | ||||||
Disulfide bond | 859↔874 | |||||
Sequence: CLHGGSCQDGVGSFSC | ||||||
Disulfide bond | 876↔885 | |||||
Sequence: CLDGFAGPRC | ||||||
Disulfide bond | 892↔902 | |||||
Sequence: CLSSPCGPGTC | ||||||
Disulfide bond | 897↔911 | |||||
Sequence: CGPGTCTDHVASFTC | ||||||
Disulfide bond | 913↔922 | |||||
Sequence: CPPGYGGFHC | ||||||
Disulfide bond | 929↔940 | |||||
Sequence: CSPSSCFNGGTC | ||||||
Disulfide bond | 934↔949 | |||||
Sequence: CFNGGTCVDGVSSFSC | ||||||
Disulfide bond | 951↔960 | |||||
Sequence: CRPGYTGTHC | ||||||
Disulfide bond | 967↔978 | |||||
Sequence: CFSRPCLHGGIC | ||||||
Disulfide bond | 972↔987 | |||||
Sequence: CLHGGICNPTHPGFEC | ||||||
Disulfide bond | 989↔998 | |||||
Sequence: CREGFTGSQC | ||||||
Disulfide bond | 1005↔1016 | |||||
Sequence: CSQAPCQNGGRC | ||||||
Disulfide bond | 1010↔1023 | |||||
Sequence: CQNGGRCVQTGAYC | ||||||
Disulfide bond | 1025↔1034 | |||||
Sequence: CPPGWSGRLC | ||||||
Disulfide bond | 1041↔1062 | |||||
Sequence: CTEAAAQMGVRLEQLCQEGGKC | ||||||
Disulfide bond | 1056↔1071 | |||||
Sequence: CQEGGKCIDKGRSHYC | ||||||
Disulfide bond | 1073↔1082 | |||||
Sequence: CPEGRTGSHC | ||||||
Disulfide bond | 1089↔1100 | |||||
Sequence: CTAQPCQHGGTC | ||||||
Disulfide bond | 1094↔1109 | |||||
Sequence: CQHGGTCRGYMGGYVC | ||||||
Disulfide bond | 1111↔1120 | |||||
Sequence: CPAGYAGDSC | ||||||
Disulfide bond | 1127↔1138 | |||||
Sequence: CASQPCQNGGSC | ||||||
Disulfide bond | 1132↔1147 | |||||
Sequence: CQNGGSCIDLVARYLC | ||||||
Disulfide bond | 1149↔1158 | |||||
Sequence: CPPGTLGVLC | ||||||
Disulfide bond | 1165↔1183 | |||||
Sequence: CDLGPSLDSGVQCLHNGTC | ||||||
Disulfide bond | 1177↔1192 | |||||
Sequence: CLHNGTCVDLVGGFRC | ||||||
Glycosylation | 1180 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1194↔1203 | |||||
Sequence: CPPGYTGLHC | ||||||
Disulfide bond | 1210↔1223 | |||||
Sequence: CRPGACHAAHTRDC | ||||||
Disulfide bond | 1215↔1233 | |||||
Sequence: CHAAHTRDCLQDPGGHFRC | ||||||
Disulfide bond | 1235↔1244 | |||||
Sequence: CHPGFTGPRC | ||||||
Disulfide bond | 1251↔1262 | |||||
Sequence: CESQPCQHGGQC | ||||||
Disulfide bond | 1256↔1276 | |||||
Sequence: CQHGGQCRHSLGRGGGLTFTC | ||||||
Disulfide bond | 1278↔1287 | |||||
Sequence: CVPPFWGLRC | ||||||
Disulfide bond | 1294↔1305 | |||||
Sequence: CRELQCPVGIPC | ||||||
Disulfide bond | 1299↔1314 | |||||
Sequence: CPVGIPCQQTARGPRC | ||||||
Disulfide bond | 1316↔1325 | |||||
Sequence: CPPGLSGPSC | ||||||
Glycosylation | 1337 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1340↔1351 | |||||
Sequence: CASAPCLHGGSC | ||||||
Disulfide bond | 1345↔1362 | |||||
Sequence: CLHGGSCLPVQSVPFFRC | ||||||
Disulfide bond | 1364↔1373 | |||||
Sequence: CAPGWGGPRC | ||||||
Disulfide bond | 1388↔1411 | |||||
Sequence: CPRAACQAKRGDQNCDRECNTPGC | ||||||
Disulfide bond | 1393↔1406 | |||||
Sequence: CQAKRGDQNCDREC | ||||||
Disulfide bond | 1402↔1418 | |||||
Sequence: CDRECNTPGCGWDGGDC | ||||||
Disulfide bond | 1429↔1452 | |||||
Sequence: CEALQCWRLFNNSRCDPACSSPAC | ||||||
Disulfide bond | 1434↔1447 | |||||
Sequence: CWRLFNNSRCDPAC | ||||||
Glycosylation | 1439 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1443↔1459 | |||||
Sequence: CDPACSSPACLYDNFDC | ||||||
Disulfide bond | 1468↔1494 | |||||
Sequence: CNPVYEKYCADHFADGRCDQGCNTEEC | ||||||
Disulfide bond | 1476↔1489 | |||||
Sequence: CADHFADGRCDQGC | ||||||
Disulfide bond | 1485↔1501 | |||||
Sequence: CDQGCNTEECGWDGLDC | ||||||
Chain | PRO_0000007696 | 1630-2318 | Notch 3 extracellular truncation | |||
Sequence: VRGEPLEAPEQSVPLLPLLVAGAVFLLIIFILGVMVARRKREHSTLWFPEGFALHKDIAAGHKGRREPVGQDALGMKNMAKGESLMGEVVTDLNDSECPEAKRLKVEEPGMGAEEPEDCRQWTQHHLVAADIRVAPATALTPPQGDADADGVDVNVRGPDGFTPLMLASFCGGALEPMPAEEDEADDTSASIISDLICQGAQLGARTDRTGETALHLAARYARADAAKRLLDAGADTNAQDHSGRTPLHTAVTADAQGVFQILIRNRSTDLDARMADGSTALILAARLAVEGMVEELIASHADVNAVDELGKSALHWAAAVNNVEATLALLKNGANKDMQDSKEETPLFLAAREGSYEAAKLLLDHLANREITDHLDRLPRDVAQERLHQDIVRLLDQPSGPRSPSGPHGLGPLLCPPGAFLPGLKAVQSGTKKSRRPPGKTGLGPQGTRGRGKKLTLACPGPLADSSVTLSPVDSLDSPRPFSGPPASPGGFPLEGPYATTATAVSLAQLGASRAGPLGRQPPGGCVLSFGLLNPVAVPLDWARLPPPAPPGPSFLLPLAPGPQLLNPGAPVSPQERPPPYLAAPGHGEEYPAAGTRSSPTKARFLRVPSEHPYLTPSPESPEHWASPSPPSLSDWSDSTPSPATATNATASGALPAQPHPISVPSLPQSQTQLGPQPEVTPKRQVMA | ||||||
Chain | PRO_0000007697 | 1663-2318 | Notch 3 intracellular domain | |||
Sequence: VMVARRKREHSTLWFPEGFALHKDIAAGHKGRREPVGQDALGMKNMAKGESLMGEVVTDLNDSECPEAKRLKVEEPGMGAEEPEDCRQWTQHHLVAADIRVAPATALTPPQGDADADGVDVNVRGPDGFTPLMLASFCGGALEPMPAEEDEADDTSASIISDLICQGAQLGARTDRTGETALHLAARYARADAAKRLLDAGADTNAQDHSGRTPLHTAVTADAQGVFQILIRNRSTDLDARMADGSTALILAARLAVEGMVEELIASHADVNAVDELGKSALHWAAAVNNVEATLALLKNGANKDMQDSKEETPLFLAAREGSYEAAKLLLDHLANREITDHLDRLPRDVAQERLHQDIVRLLDQPSGPRSPSGPHGLGPLLCPPGAFLPGLKAVQSGTKKSRRPPGKTGLGPQGTRGRGKKLTLACPGPLADSSVTLSPVDSLDSPRPFSGPPASPGGFPLEGPYATTATAVSLAQLGASRAGPLGRQPPGGCVLSFGLLNPVAVPLDWARLPPPAPPGPSFLLPLAPGPQLLNPGAPVSPQERPPPYLAAPGHGEEYPAAGTRSSPTKARFLRVPSEHPYLTPSPESPEHWASPSPPSLSDWSDSTPSPATATNATASGALPAQPHPISVPSLPQSQTQLGPQPEVTPKRQVMA | ||||||
Modified residue | 2174 | Omega-N-methylarginine | ||||
Sequence: R |
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 TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). This fragment is then cleaved by presenilin dependent gamma-secretase to release a notch-derived peptide containing the intracellular domain (NICD) from the membrane.
Phosphorylated.
Hydroxylated by HIF1AN.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Proliferating neuroepithelium.
Developmental stage
CNS development.
Gene expression databases
Interaction
Subunit
Interacts with PSMA1 (By similarity).
Heterodimer of a C-terminal fragment N(TM) and a N-terminal fragment N(EC) which are probably linked by disulfide bonds. Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH3. Interacts with HIF1AN
Heterodimer of a C-terminal fragment N(TM) and a N-terminal fragment N(EC) which are probably linked by disulfide bonds. Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH3. Interacts with HIF1AN
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | PRO_0000007697 | LRORF2 Q77CA8 | 3 | EBI-11292908, EBI-11292862 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic residues | ||||
Sequence: MGLGARGRRRRRRLM | ||||||
Region | 1-20 | Disordered | ||||
Sequence: MGLGARGRRRRRRLMALPPP | ||||||
Domain | 40-78 | EGF-like 1 | ||||
Sequence: APPCLDGSPCANGGRCTHQQPSLEAACLCLPGWVGERCQ | ||||||
Domain | 79-119 | EGF-like 2 | ||||
Sequence: LEDPCHSGPCAGRGVCQSSVVAGTARFSCRCLRGFQGPDCS | ||||||
Domain | 120-157 | EGF-like 3 | ||||
Sequence: QPDPCVSRPCVHGAPCSVGPDGRFACACPPGYQGQSCQ | ||||||
Domain | 159-196 | EGF-like 4; calcium-binding | ||||
Sequence: DIDECRSGTTCRHGGTCLNTPGSFRCQCPLGYTGLLCE | ||||||
Domain | 198-235 | EGF-like 5 | ||||
Sequence: PVVPCAPSPCRNGGTCRQSSDVTYDCACLPGFEGQNCE | ||||||
Domain | 237-273 | EGF-like 6; calcium-binding | ||||
Sequence: NVDDCPGHRCLNGGTCVDGVNTYNCQCPPEWTGQFCT | ||||||
Domain | 275-313 | EGF-like 7 | ||||
Sequence: DVDECQLQPNACHNGGTCFNLLGGHSCVCVNGWTGESCS | ||||||
Domain | 315-351 | EGF-like 8; calcium-binding | ||||
Sequence: NIDDCATAVCFHGATCHDRVASFYCACPMGKTGLLCH | ||||||
Domain | 352-390 | EGF-like 9 | ||||
Sequence: LDDACVSNPCHEDAICDTNPVSGRAICTCPPGFTGGACD | ||||||
Domain | 392-430 | EGF-like 10; calcium-binding | ||||
Sequence: DVDECSIGANPCEHLGRCVNTQGSFLCQCGRGYTGPRCE | ||||||
Domain | 432-468 | EGF-like 11; calcium-binding | ||||
Sequence: DVNECLSGPCRNQATCLDRIGQFTCICMAGFTGTYCE | ||||||
Domain | 470-506 | EGF-like 12; calcium-binding | ||||
Sequence: DIDECQSSPCVNGGVCKDRVNGFSCTCPSGFSGSMCQ | ||||||
Domain | 508-544 | EGF-like 13; calcium-binding | ||||
Sequence: DVDECASTPCRNGAKCVDQPDGYECRCAEGFEGTLCE | ||||||
Domain | 546-581 | EGF-like 14; calcium-binding | ||||
Sequence: NVDDCSPDPCHHGRCVDGIASFSCACAPGYTGIRCE | ||||||
Domain | 583-619 | EGF-like 15; calcium-binding | ||||
Sequence: QVDECRSQPCRYGGKCLDLVDKYLCRCPPGTTGVNCE | ||||||
Domain | 621-656 | EGF-like 16; calcium-binding | ||||
Sequence: NIDDCASNPCTFGVCRDGINRYDCVCQPGFTGPLCN | ||||||
Domain | 658-694 | EGF-like 17; calcium-binding | ||||
Sequence: EINECASSPCGEGGSCVDGENGFHCLCPPGSLPPLCL | ||||||
Domain | 696-731 | EGF-like 18 | ||||
Sequence: ANHPCAHKPCSHGVCHDAPGGFRCVCEPGWSGPRCS | ||||||
Domain | 735-771 | EGF-like 19 | ||||
Sequence: APDACESQPCQAGGTCTSDGIGFRCTCAPGFQGHQCE | ||||||
Domain | 772-809 | EGF-like 20 | ||||
Sequence: VLSPCTPSLCEHGGHCESDPDRLTVCSCPPGWQGPRCQ | ||||||
Domain | 811-848 | EGF-like 21; calcium-binding | ||||
Sequence: DVDECAGASPCGPHGTCTNLPGNFRCICHRGYTGPFCD | ||||||
Domain | 850-886 | EGF-like 22; calcium-binding | ||||
Sequence: DIDDCDPNPCLHGGSCQDGVGSFSCSCLDGFAGPRCA | ||||||
Domain | 888-923 | EGF-like 23; calcium-binding | ||||
Sequence: DVDECLSSPCGPGTCTDHVASFTCACPPGYGGFHCE | ||||||
Domain | 925-961 | EGF-like 24 | ||||
Sequence: DLPDCSPSSCFNGGTCVDGVSSFSCLCRPGYTGTHCQ | ||||||
Domain | 963-999 | EGF-like 25 | ||||
Sequence: EADPCFSRPCLHGGICNPTHPGFECTCREGFTGSQCQ | ||||||
Domain | 1001-1035 | EGF-like 26 | ||||
Sequence: PVDWCSQAPCQNGGRCVQTGAYCICPPGWSGRLCD | ||||||
Domain | 1037-1083 | EGF-like 27 | ||||
Sequence: QSLPCTEAAAQMGVRLEQLCQEGGKCIDKGRSHYCVCPEGRTGSHCE | ||||||
Domain | 1085-1121 | EGF-like 28 | ||||
Sequence: EVDPCTAQPCQHGGTCRGYMGGYVCECPAGYAGDSCE | ||||||
Domain | 1123-1159 | EGF-like 29; calcium-binding | ||||
Sequence: NIDECASQPCQNGGSCIDLVARYLCSCPPGTLGVLCE | ||||||
Domain | 1161-1204 | EGF-like 30; calcium-binding | ||||
Sequence: NEDDCDLGPSLDSGVQCLHNGTCVDLVGGFRCNCPPGYTGLHCE | ||||||
Domain | 1206-1245 | EGF-like 31 | ||||
Sequence: DINECRPGACHAAHTRDCLQDPGGHFRCVCHPGFTGPRCQ | ||||||
Domain | 1247-1288 | EGF-like 32 | ||||
Sequence: ALSPCESQPCQHGGQCRHSLGRGGGLTFTCHCVPPFWGLRCE | ||||||
Domain | 1290-1326 | EGF-like 33 | ||||
Sequence: VARSCRELQCPVGIPCQQTARGPRCACPPGLSGPSCR | ||||||
Domain | 1336-1374 | EGF-like 34 | ||||
Sequence: TNASCASAPCLHGGSCLPVQSVPFFRCVCAPGWGGPRCE | ||||||
Repeat | 1388-1428 | LNR 1 | ||||
Sequence: CPRAACQAKRGDQNCDRECNTPGCGWDGGDCSLNVDDPWRQ | ||||||
Repeat | 1429-1466 | LNR 2 | ||||
Sequence: CEALQCWRLFNNSRCDPACSSPACLYDNFDCYSGGRDR | ||||||
Repeat | 1468-1506 | LNR 3 | ||||
Sequence: CNPVYEKYCADHFADGRCDQGCNTEECGWDGLDCASEVP | ||||||
Repeat | 1839-1868 | ANK 1 | ||||
Sequence: TGETALHLAARYARADAAKRLLDAGADTNA | ||||||
Repeat | 1872-1902 | ANK 2 | ||||
Sequence: SGRTPLHTAVTADAQGVFQILIRNRSTDLDA | ||||||
Repeat | 1906-1935 | ANK 3 | ||||
Sequence: DGSTALILAARLAVEGMVEELIASHADVNA | ||||||
Repeat | 1939-1968 | ANK 4 | ||||
Sequence: LGKSALHWAAAVNNVEATLALLKNGANKDM | ||||||
Repeat | 1972-2001 | ANK 5 | ||||
Sequence: KEETPLFLAAREGSYEAAKLLLDHLANREI | ||||||
Region | 2025-2045 | Disordered | ||||
Sequence: LDQPSGPRSPSGPHGLGPLLC | ||||||
Region | 2058-2126 | Disordered | ||||
Sequence: QSGTKKSRRPPGKTGLGPQGTRGRGKKLTLACPGPLADSSVTLSPVDSLDSPRPFSGPPASPGGFPLEG | ||||||
Compositional bias | 2184-2211 | Pro residues | ||||
Sequence: SFLLPLAPGPQLLNPGAPVSPQERPPPY | ||||||
Region | 2184-2318 | Disordered | ||||
Sequence: SFLLPLAPGPQLLNPGAPVSPQERPPPYLAAPGHGEEYPAAGTRSSPTKARFLRVPSEHPYLTPSPESPEHWASPSPPSLSDWSDSTPSPATATNATASGALPAQPHPISVPSLPQSQTQLGPQPEVTPKRQVMA | ||||||
Region | 2242-2261 | PEST-like | ||||
Sequence: HPYLTPSPESPEHWASPSPP | ||||||
Compositional bias | 2257-2284 | Polar residues | ||||
Sequence: SPSPPSLSDWSDSTPSPATATNATASGA | ||||||
Compositional bias | 2294-2309 | Polar residues | ||||
Sequence: VPSLPQSQTQLGPQPE |
Domain
The EGF-like domains 10 and 11 are required for binding the ligands JAG1 and DLL1.
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.
- Length2,318
- Mass (Da)244,248
- Last updated1997-11-01 v1
- ChecksumA80D1F75AFF0185A
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A494BAZ6 | A0A494BAZ6_MOUSE | Notch3 | 239 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic residues | ||||
Sequence: MGLGARGRRRRRRLM | ||||||
Compositional bias | 2184-2211 | Pro residues | ||||
Sequence: SFLLPLAPGPQLLNPGAPVSPQERPPPY | ||||||
Compositional bias | 2257-2284 | Polar residues | ||||
Sequence: SPSPPSLSDWSDSTPSPATATNATASGA | ||||||
Compositional bias | 2294-2309 | Polar residues | ||||
Sequence: VPSLPQSQTQLGPQPE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X74760 EMBL· GenBank· DDBJ | CAA52776.1 EMBL· GenBank· DDBJ | mRNA |