Q61982 · NOTC3_MOUSE

  • Protein
    Neurogenic locus notch homolog protein 3
  • Gene
    Notch3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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

Features

Showing features for site.

123182004006008001,0001,2001,4001,6001,8002,0002,200
TypeIDPosition(s)Description
Site1572-1573Cleavage; by furin-like protease

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell surface
Cellular Componentcytosol
Cellular Componentnucleoplasm
Cellular Componentplasma membrane
Cellular Componentreceptor complex
Molecular Functioncalcium ion binding
Molecular Functionenzyme binding
Molecular Functionidentical protein binding
Molecular Functionsignaling receptor activity
Biological Processartery morphogenesis
Biological Processaxon guidance
Biological Processforebrain development
Biological Processglomerular capillary formation
Biological Processnegative regulation of cell differentiation
Biological Processnegative regulation of neuron differentiation
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processneuroblast differentiation
Biological Processneuron differentiation
Biological Processneuron fate commitment
Biological ProcessNotch signaling pathway
Biological Processpositive regulation of miRNA transcription
Biological Processpositive regulation of smooth muscle cell proliferation
Biological Processpositive regulation of transcription by RNA polymerase II
Biological Processregulation of DNA-templated transcription

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      Notch3

Organism names

  • Taxonomic identifier
  • Strain
    • ICR X Swiss Webster
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q61982

Proteomes

Organism-specific databases

Subcellular Location

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.

TypeIDPosition(s)Description
Topological domain40-1643Extracellular
Transmembrane1644-1664Helical
Topological domain1665-2318Cytoplasmic

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis1664No effect on NICD processing.

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.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, modified residue.

TypeIDPosition(s)Description
Signal1-39
ChainPRO_000000769540-2318Neurogenic locus notch homolog protein 3
Disulfide bond43↔55
Disulfide bond49↔66
Disulfide bond68↔77
Disulfide bond83↔94
Disulfide bond88↔107
Disulfide bond109↔118
Disulfide bond124↔135
Disulfide bond129↔145
Disulfide bond147↔156
Disulfide bond163↔175
Disulfide bond169↔184
Disulfide bond186↔195
Disulfide bond202↔213
Disulfide bond207↔223
Disulfide bond225↔234
Disulfide bond241↔252
Disulfide bond246↔261
Disulfide bond263↔272
Disulfide bond279↔292
Disulfide bond286↔301
Disulfide bond303↔312
Disulfide bond319↔330
Disulfide bond324↔339
Disulfide bond341↔350
Disulfide bond356↔367
Disulfide bond361↔378
Disulfide bond380↔389
Disulfide bond396↔409
Disulfide bond403↔418
Disulfide bond420↔429
Disulfide bond436↔447
Disulfide bond441↔456
Disulfide bond458↔467
Disulfide bond474↔485
Disulfide bond479↔494
Disulfide bond496↔505
Disulfide bond512↔523
Disulfide bond517↔532
Disulfide bond534↔543
Disulfide bond550↔560
Disulfide bond555↔569
Disulfide bond571↔580
Disulfide bond587↔598
Disulfide bond592↔607
Disulfide bond609↔618
Disulfide bond625↔635
Disulfide bond630↔644
Disulfide bond646↔655
Disulfide bond662↔673
Disulfide bond667↔682
Disulfide bond684↔693
Disulfide bond700↔710
Disulfide bond705↔719
Disulfide bond721↔730
Disulfide bond739↔750
Disulfide bond744↔759
Disulfide bond761↔770
Disulfide bond776↔787
Disulfide bond781↔797
Disulfide bond799↔808
Disulfide bond815↔827
Disulfide bond821↔836
Disulfide bond838↔847
Disulfide bond854↔865
Disulfide bond859↔874
Disulfide bond876↔885
Disulfide bond892↔902
Disulfide bond897↔911
Disulfide bond913↔922
Disulfide bond929↔940
Disulfide bond934↔949
Disulfide bond951↔960
Disulfide bond967↔978
Disulfide bond972↔987
Disulfide bond989↔998
Disulfide bond1005↔1016
Disulfide bond1010↔1023
Disulfide bond1025↔1034
Disulfide bond1041↔1062
Disulfide bond1056↔1071
Disulfide bond1073↔1082
Disulfide bond1089↔1100
Disulfide bond1094↔1109
Disulfide bond1111↔1120
Disulfide bond1127↔1138
Disulfide bond1132↔1147
Disulfide bond1149↔1158
Disulfide bond1165↔1183
Disulfide bond1177↔1192
Glycosylation1180N-linked (GlcNAc...) asparagine
Disulfide bond1194↔1203
Disulfide bond1210↔1223
Disulfide bond1215↔1233
Disulfide bond1235↔1244
Disulfide bond1251↔1262
Disulfide bond1256↔1276
Disulfide bond1278↔1287
Disulfide bond1294↔1305
Disulfide bond1299↔1314
Disulfide bond1316↔1325
Glycosylation1337N-linked (GlcNAc...) asparagine
Disulfide bond1340↔1351
Disulfide bond1345↔1362
Disulfide bond1364↔1373
Disulfide bond1388↔1411
Disulfide bond1393↔1406
Disulfide bond1402↔1418
Disulfide bond1429↔1452
Disulfide bond1434↔1447
Glycosylation1439N-linked (GlcNAc...) asparagine
Disulfide bond1443↔1459
Disulfide bond1468↔1494
Disulfide bond1476↔1489
Disulfide bond1485↔1501
ChainPRO_00000076961630-2318Notch 3 extracellular truncation
ChainPRO_00000076971663-2318Notch 3 intracellular domain
Modified residue2174Omega-N-methylarginine

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

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

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
XENO PRO_0000007697LRORF2 Q77CA83EBI-11292908, EBI-11292862

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain, repeat.

TypeIDPosition(s)Description
Compositional bias1-15Basic residues
Region1-20Disordered
Domain40-78EGF-like 1
Domain79-119EGF-like 2
Domain120-157EGF-like 3
Domain159-196EGF-like 4; calcium-binding
Domain198-235EGF-like 5
Domain237-273EGF-like 6; calcium-binding
Domain275-313EGF-like 7
Domain315-351EGF-like 8; calcium-binding
Domain352-390EGF-like 9
Domain392-430EGF-like 10; calcium-binding
Domain432-468EGF-like 11; calcium-binding
Domain470-506EGF-like 12; calcium-binding
Domain508-544EGF-like 13; calcium-binding
Domain546-581EGF-like 14; calcium-binding
Domain583-619EGF-like 15; calcium-binding
Domain621-656EGF-like 16; calcium-binding
Domain658-694EGF-like 17; calcium-binding
Domain696-731EGF-like 18
Domain735-771EGF-like 19
Domain772-809EGF-like 20
Domain811-848EGF-like 21; calcium-binding
Domain850-886EGF-like 22; calcium-binding
Domain888-923EGF-like 23; calcium-binding
Domain925-961EGF-like 24
Domain963-999EGF-like 25
Domain1001-1035EGF-like 26
Domain1037-1083EGF-like 27
Domain1085-1121EGF-like 28
Domain1123-1159EGF-like 29; calcium-binding
Domain1161-1204EGF-like 30; calcium-binding
Domain1206-1245EGF-like 31
Domain1247-1288EGF-like 32
Domain1290-1326EGF-like 33
Domain1336-1374EGF-like 34
Repeat1388-1428LNR 1
Repeat1429-1466LNR 2
Repeat1468-1506LNR 3
Repeat1839-1868ANK 1
Repeat1872-1902ANK 2
Repeat1906-1935ANK 3
Repeat1939-1968ANK 4
Repeat1972-2001ANK 5
Region2025-2045Disordered
Region2058-2126Disordered
Compositional bias2184-2211Pro residues
Region2184-2318Disordered
Region2242-2261PEST-like
Compositional bias2257-2284Polar residues
Compositional bias2294-2309Polar residues

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    2,318
  • Mass (Da)
    244,248
  • Last updated
    1997-11-01 v1
  • Checksum
    A80D1F75AFF0185A
MGLGARGRRRRRRLMALPPPPPPMRALPLLLLLAGLGAAAPPCLDGSPCANGGRCTHQQPSLEAACLCLPGWVGERCQLEDPCHSGPCAGRGVCQSSVVAGTARFSCRCLRGFQGPDCSQPDPCVSRPCVHGAPCSVGPDGRFACACPPGYQGQSCQSDIDECRSGTTCRHGGTCLNTPGSFRCQCPLGYTGLLCENPVVPCAPSPCRNGGTCRQSSDVTYDCACLPGFEGQNCEVNVDDCPGHRCLNGGTCVDGVNTYNCQCPPEWTGQFCTEDVDECQLQPNACHNGGTCFNLLGGHSCVCVNGWTGESCSQNIDDCATAVCFHGATCHDRVASFYCACPMGKTGLLCHLDDACVSNPCHEDAICDTNPVSGRAICTCPPGFTGGACDQDVDECSIGANPCEHLGRCVNTQGSFLCQCGRGYTGPRCETDVNECLSGPCRNQATCLDRIGQFTCICMAGFTGTYCEVDIDECQSSPCVNGGVCKDRVNGFSCTCPSGFSGSMCQLDVDECASTPCRNGAKCVDQPDGYECRCAEGFEGTLCERNVDDCSPDPCHHGRCVDGIASFSCACAPGYTGIRCESQVDECRSQPCRYGGKCLDLVDKYLCRCPPGTTGVNCEVNIDDCASNPCTFGVCRDGINRYDCVCQPGFTGPLCNVEINECASSPCGEGGSCVDGENGFHCLCPPGSLPPLCLPANHPCAHKPCSHGVCHDAPGGFRCVCEPGWSGPRCSQSLAPDACESQPCQAGGTCTSDGIGFRCTCAPGFQGHQCEVLSPCTPSLCEHGGHCESDPDRLTVCSCPPGWQGPRCQQDVDECAGASPCGPHGTCTNLPGNFRCICHRGYTGPFCDQDIDDCDPNPCLHGGSCQDGVGSFSCSCLDGFAGPRCARDVDECLSSPCGPGTCTDHVASFTCACPPGYGGFHCEIDLPDCSPSSCFNGGTCVDGVSSFSCLCRPGYTGTHCQYEADPCFSRPCLHGGICNPTHPGFECTCREGFTGSQCQNPVDWCSQAPCQNGGRCVQTGAYCICPPGWSGRLCDIQSLPCTEAAAQMGVRLEQLCQEGGKCIDKGRSHYCVCPEGRTGSHCEHEVDPCTAQPCQHGGTCRGYMGGYVCECPAGYAGDSCEDNIDECASQPCQNGGSCIDLVARYLCSCPPGTLGVLCEINEDDCDLGPSLDSGVQCLHNGTCVDLVGGFRCNCPPGYTGLHCEADINECRPGACHAAHTRDCLQDPGGHFRCVCHPGFTGPRCQIALSPCESQPCQHGGQCRHSLGRGGGLTFTCHCVPPFWGLRCERVARSCRELQCPVGIPCQQTARGPRCACPPGLSGPSCRVSRASPSGATNASCASAPCLHGGSCLPVQSVPFFRCVCAPGWGGPRCETPSAAPEVPEEPRCPRAACQAKRGDQNCDRECNTPGCGWDGGDCSLNVDDPWRQCEALQCWRLFNNSRCDPACSSPACLYDNFDCYSGGRDRTCNPVYEKYCADHFADGRCDQGCNTEECGWDGLDCASEVPALLARGVLVLTVLLPPEELLRSSADFLQRLSAILRTSLRFRLDARGQAMVFPYHRPSPGSESRVRRELGPEVIGSVVMLEIDNRLCLQSAENDHCFPDAQSAADYLGALSAVERLDFPYPLRDVRGEPLEAPEQSVPLLPLLVAGAVFLLIIFILGVMVARRKREHSTLWFPEGFALHKDIAAGHKGRREPVGQDALGMKNMAKGESLMGEVVTDLNDSECPEAKRLKVEEPGMGAEEPEDCRQWTQHHLVAADIRVAPATALTPPQGDADADGVDVNVRGPDGFTPLMLASFCGGALEPMPAEEDEADDTSASIISDLICQGAQLGARTDRTGETALHLAARYARADAAKRLLDAGADTNAQDHSGRTPLHTAVTADAQGVFQILIRNRSTDLDARMADGSTALILAARLAVEGMVEELIASHADVNAVDELGKSALHWAAAVNNVEATLALLKNGANKDMQDSKEETPLFLAAREGSYEAAKLLLDHLANREITDHLDRLPRDVAQERLHQDIVRLLDQPSGPRSPSGPHGLGPLLCPPGAFLPGLKAVQSGTKKSRRPPGKTGLGPQGTRGRGKKLTLACPGPLADSSVTLSPVDSLDSPRPFSGPPASPGGFPLEGPYATTATAVSLAQLGASRAGPLGRQPPGGCVLSFGLLNPVAVPLDWARLPPPAPPGPSFLLPLAPGPQLLNPGAPVSPQERPPPYLAAPGHGEEYPAAGTRSSPTKARFLRVPSEHPYLTPSPESPEHWASPSPPSLSDWSDSTPSPATATNATASGALPAQPHPISVPSLPQSQTQLGPQPEVTPKRQVMA

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A494BAZ6A0A494BAZ6_MOUSENotch3239

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-15Basic residues
Compositional bias2184-2211Pro residues
Compositional bias2257-2284Polar residues
Compositional bias2294-2309Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X74760
EMBL· GenBank· DDBJ
CAA52776.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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