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Q07008 (NOTC1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurogenic locus notch homolog protein 1

Short name=Notch 1

Cleaved into the following 2 chains:

  1. Notch 1 extracellular truncation
    Short name=NEXT
  2. Notch 1 intracellular domain
    Short name=NICD
Gene names
Name:Notch1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length2531 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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. 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. May enhance HIF1A function by sequestering HIF1AN away from HIF1A. Required for the THBS4 function in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury. 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. Ref.5

Subunit structure

Heterodimer of a C-terminal fragment N(TM) and an N-terminal fragment N(EC) which are probably linked by disulfide bonds. Interacts with DNER, DTX1, DTX2 and RBPJ/RBPSUH. Also interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH1. Notch 1 intracellular domain interacts with SNW1; the interaction involves multimerized NOTCH1 NICD and is implicated in a formation of an intermediate preactivation complex which associates with DNA-bound CBF-1/RBPJ. The activated membrane-bound form interacts with AAK1 which promotes NOTCH1 stabilization. Forms a trimeric complex with FBXW7 and SGK1. Interacts with HIF1AN. HIF1AN negatively regulates the function of notch intracellular domain (NICD), accelerating myogenic differentiation. Interacts (via NICD) with SNAI1 (via zinc fingers); the interaction induces SNAI1 degradation via MDM2-mediated ubiquitination and inhibits SNAI1-induced cell invasion. Interacts (via NICD) with MDM2A. Interacts (via NICD) with BCL6; the interaction decreases MAML1 recruitment by NOTCH1 NICD on target genes DNA and inhibits NOTCH1 transcractivation activity By similarity. Interacts with THBS4 By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Notch 1 intracellular domain: Nucleus By similarity. Note: Following proteolytical processing NICD is translocated to the nucleus By similarity.

Tissue specificity

Expressed in the brain, kidney and spleen. Expressed in postnatal central nervous system (CNS) germinal zones and, in early postnatal life, within numerous cells throughout the CNS. Found in both subventricular and ventricular germinal zones. Ref.6 Ref.7

Developmental stage

In the embryo, highest levels occur between days 12 and 14 and decrease rapidly to much lower levels in the adult.

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.

Phosphorylated 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.

Ubiquitinated; undergoes 'Lys-29'-linked polyubiquitination catalyzed by ITCH. Monoubiquitination at Lys-1749 is required for activation by gamma-secretase cleavage, it promotes interaction with AAK1, which stabilizes it. Deubiquitination by EIF3F is necessary for nuclear import of activated Notch By similarity.

Hydroxylated at Asn-1945 and Asn-2012 by HIF1AN. Hydroxylation reduces affinity for HI1AN and may thus indirectly modulate negative regulation of NICD By similarity.

Sequence similarities

Belongs to the NOTCH family.

Contains 5 ANK repeats.

Contains 36 EGF-like domains.

Contains 3 LNR (Lin/Notch) repeats.

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
Notch signaling pathway
Transcription
Transcription regulation
   Cellular componentCell membrane
Membrane
Nucleus
   DomainANK repeat
EGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionActivator
Developmental protein
Receptor
   PTMDisulfide bond
Glycoprotein
Hydroxylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling involved in heart development

Inferred from sequence or structural similarity. Source: UniProtKB

Notch signaling pathway

Inferred from mutant phenotype PubMed 15057910. Source: RGD

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

astrocyte differentiation

Inferred from direct assay PubMed 19378247. Source: RGD

cell differentiation in spinal cord

Inferred from expression pattern PubMed 20195794. Source: RGD

cellular response to vascular endothelial growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cilium morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of catalytic activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell migration involved in sprouting angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of endothelial cell chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of glial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of myotube differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neurogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron differentiation

Inferred from mutant phenotype PubMed 19109527. Source: RGD

negative regulation of oligodendrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of pro-B cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

oligodendrocyte differentiation

Inferred from expression pattern PubMed 12876431. Source: RGD

organ regeneration

Inferred from expression pattern PubMed 18781453. Source: RGD

positive regulation of BMP signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of JAK-STAT cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of astrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of endothelial cell differentiation

Inferred from mutant phenotype PubMed 19109527. Source: RGD

positive regulation of glial cell differentiation

Inferred from mutant phenotype PubMed 12853432. Source: RGD

positive regulation of neuroblast proliferation

Inferred from mutant phenotype PubMed 19109527. Source: RGD

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 12853432. Source: RGD

positive regulation of transcription from RNA polymerase II promoter in response to hypoxia

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription of Notch receptor target

Inferred from mutant phenotype PubMed 12853432. Source: RGD

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cardioblast proliferation

Inferred from mutant phenotype PubMed 18824567. Source: RGD

regulation of cell proliferation

Inferred from mutant phenotype PubMed 15057910. Source: RGD

response to corticosteroid

Inferred from expression pattern PubMed 19481784. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 18449946. Source: RGD

spermatogenesis

Inferred from mutant phenotype PubMed 11700865. Source: RGD

tissue regeneration

Inferred from expression pattern PubMed 15057910PubMed 16048523. Source: RGD

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

tube formation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 11700865. Source: RGD

acrosomal vesicle

Inferred from direct assay PubMed 11700865. Source: RGD

cytoskeleton

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 15057910. Source: RGD

plasma membrane

Inferred from direct assay PubMed 15057910. Source: RGD

ruffle

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

core promoter binding

Inferred from sequence or structural similarity. Source: UniProtKB

enzyme binding

Inferred from sequence or structural similarity. Source: UniProtKB

enzyme inhibitor activity

Inferred from sequence or structural similarity. Source: UniProtKB

receptor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 25312513Neurogenic locus notch homolog protein 1
PRO_0000007680
Chain1711 – 2531821Notch 1 extracellular truncation By similarity
PRO_0000007681
Chain1744 – 2531788Notch 1 intracellular domain By similarity
PRO_0000007682

Regions

Topological domain19 – 17231705Extracellular Potential
Transmembrane1724 – 174623Helical; Potential
Topological domain1747 – 2531785Cytoplasmic Potential
Domain20 – 5839EGF-like 1
Domain59 – 9941EGF-like 2
Domain102 – 13938EGF-like 3
Domain140 – 17637EGF-like 4
Domain178 – 21639EGF-like 5; calcium-binding Potential
Domain218 – 25538EGF-like 6
Domain257 – 29337EGF-like 7; calcium-binding Potential
Domain295 – 33339EGF-like 8; calcium-binding Potential
Domain335 – 37137EGF-like 9; calcium-binding Potential
Domain372 – 41039EGF-like 10
Domain412 – 45039EGF-like 11; calcium-binding Potential
Domain452 – 48837EGF-like 12; calcium-binding Potential
Domain490 – 52637EGF-like 13; calcium-binding Potential
Domain528 – 56437EGF-like 14; calcium-binding Potential
Domain566 – 60136EGF-like 15; calcium-binding Potential
Domain603 – 63937EGF-like 16; calcium-binding Potential
Domain641 – 67636EGF-like 17; calcium-binding Potential
Domain678 – 71437EGF-like 18; calcium-binding Potential
Domain716 – 75136EGF-like 19; calcium-binding Potential
Domain753 – 78937EGF-like 20; calcium-binding Potential
Domain791 – 82737EGF-like 21; calcium-binding Potential
Domain829 – 86739EGF-like 22
Domain869 – 90537EGF-like 23; calcium-binding Potential
Domain907 – 94337EGF-like 24
Domain945 – 98137EGF-like 25; calcium-binding Potential
Domain983 – 101937EGF-like 26
Domain1021 – 105737EGF-like 27; calcium-binding Potential
Domain1059 – 109537EGF-like 28
Domain1097 – 114347EGF-like 29
Domain1145 – 118137EGF-like 30; calcium-binding Potential
Domain1183 – 121937EGF-like 31; calcium-binding Potential
Domain1221 – 126545EGF-like 32; calcium-binding Potential
Domain1267 – 130539EGF-like 33
Domain1307 – 134640EGF-like 34
Domain1348 – 138437EGF-like 35
Domain1387 – 142640EGF-like 36
Repeat1449 – 148941LNR 1
Repeat1490 – 153142LNR 2
Repeat1532 – 157140LNR 3
Repeat1917 – 194630ANK 1
Repeat1950 – 198031ANK 2
Repeat1984 – 201330ANK 3
Repeat2017 – 204630ANK 4
Repeat2050 – 207930ANK 5
Region1937 – 19459HIF1AN-binding By similarity
Region2004 – 20129HIF1AN-binding By similarity
Compositional bias1730 – 17334Poly-Ala
Compositional bias1891 – 18944Poly-Glu
Compositional bias2258 – 22614Poly-Pro
Compositional bias2497 – 25004Poly-Ser

Sites

Metal binding14571Calcium; via carbonyl oxygen By similarity
Metal binding14601Calcium By similarity
Metal binding14751Calcium By similarity
Metal binding14781Calcium By similarity
Site1654 – 16552Cleavage; by furin-like protease By similarity
Site1710 – 17112Cleavage; by ADAM17 By similarity

Amino acid modifications

Modified residue19451(3S)-3-hydroxyasparagine; by HIF1AN By similarity
Modified residue20121(3S)-3-hydroxyasparagine; by HIF1AN By similarity
Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation651O-linked (Glc...) By similarity
Glycosylation731O-linked (Fuc...) By similarity
Glycosylation1161O-linked (Fuc...) By similarity
Glycosylation1461O-linked (Glc...) By similarity
Glycosylation1941O-linked (Fuc...) By similarity
Glycosylation2321O-linked (Fuc...); alternate By similarity
Glycosylation2321O-linked (GalNAc...); alternate By similarity
Glycosylation3411O-linked (Glc...) By similarity
Glycosylation3781O-linked (Glc...) By similarity
Glycosylation4581O-linked (Glc...) By similarity
Glycosylation4661O-linked (Fuc...) By similarity
Glycosylation4961O-linked (Glc...) By similarity
Glycosylation5341O-linked (Glc...) By similarity
Glycosylation6091O-linked (Glc...) By similarity
Glycosylation6471O-linked (Glc...) By similarity
Glycosylation7221O-linked (Glc...) By similarity
Glycosylation7591O-linked (Glc...) By similarity
Glycosylation7671O-linked (Fuc...) By similarity
Glycosylation7971O-linked (Glc...) By similarity
Glycosylation8051O-linked (Fuc...) By similarity
Glycosylation8881N-linked (GlcNAc...) Potential
Glycosylation9511O-linked (Glc...) By similarity
Glycosylation9591N-linked (GlcNAc...) Potential
Glycosylation10271O-linked (Glc...) By similarity
Glycosylation10351O-linked (Fuc...) By similarity
Glycosylation10651O-linked (Glc...) By similarity
Glycosylation11791N-linked (GlcNAc...) Potential
Glycosylation11891O-linked (Glc...) By similarity
Glycosylation11971O-linked (Fuc...) By similarity
Glycosylation12411N-linked (GlcNAc...) Potential
Glycosylation12731O-linked (Glc...) By similarity
Glycosylation13621O-linked (Fuc...) By similarity
Glycosylation14021O-linked (Fuc...); alternate By similarity
Glycosylation14021O-linked (GalNAc...); alternate By similarity
Glycosylation14891N-linked (GlcNAc...) Potential
Glycosylation15871N-linked (GlcNAc...) Potential
Glycosylation17151O-linked (GalNAc...) By similarity
Disulfide bond24 ↔ 37 By similarity
Disulfide bond31 ↔ 46 By similarity
Disulfide bond48 ↔ 57 By similarity
Disulfide bond63 ↔ 74 By similarity
Disulfide bond68 ↔ 87 By similarity
Disulfide bond89 ↔ 98 By similarity
Disulfide bond106 ↔ 117 By similarity
Disulfide bond111 ↔ 127 By similarity
Disulfide bond129 ↔ 138 By similarity
Disulfide bond144 ↔ 155 By similarity
Disulfide bond149 ↔ 164 By similarity
Disulfide bond166 ↔ 175 By similarity
Disulfide bond182 ↔ 195 By similarity
Disulfide bond189 ↔ 204 By similarity
Disulfide bond206 ↔ 215 By similarity
Disulfide bond222 ↔ 233 By similarity
Disulfide bond227 ↔ 243 By similarity
Disulfide bond245 ↔ 254 By similarity
Disulfide bond261 ↔ 272 By similarity
Disulfide bond266 ↔ 281 By similarity
Disulfide bond283 ↔ 292 By similarity
Disulfide bond299 ↔ 312 By similarity
Disulfide bond306 ↔ 321 By similarity
Disulfide bond323 ↔ 332 By similarity
Disulfide bond339 ↔ 350 By similarity
Disulfide bond344 ↔ 359 By similarity
Disulfide bond361 ↔ 370 By similarity
Disulfide bond376 ↔ 387 By similarity
Disulfide bond381 ↔ 398 By similarity
Disulfide bond400 ↔ 409 By similarity
Disulfide bond416 ↔ 429 By similarity
Disulfide bond423 ↔ 438 By similarity
Disulfide bond440 ↔ 449 By similarity
Disulfide bond456 ↔ 467 By similarity
Disulfide bond461 ↔ 476 By similarity
Disulfide bond478 ↔ 487 By similarity
Disulfide bond494 ↔ 505 By similarity
Disulfide bond499 ↔ 514 By similarity
Disulfide bond516 ↔ 525 By similarity
Disulfide bond532 ↔ 543 By similarity
Disulfide bond537 ↔ 552 By similarity
Disulfide bond554 ↔ 563 By similarity
Disulfide bond570 ↔ 580 By similarity
Disulfide bond575 ↔ 589 By similarity
Disulfide bond591 ↔ 600 By similarity
Disulfide bond607 ↔ 618 By similarity
Disulfide bond612 ↔ 627 By similarity
Disulfide bond629 ↔ 638 By similarity
Disulfide bond645 ↔ 655 By similarity
Disulfide bond650 ↔ 664 By similarity
Disulfide bond666 ↔ 675 By similarity
Disulfide bond682 ↔ 693 By similarity
Disulfide bond687 ↔ 702 By similarity
Disulfide bond704 ↔ 713 By similarity
Disulfide bond720 ↔ 730 By similarity
Disulfide bond725 ↔ 739 By similarity
Disulfide bond741 ↔ 750 By similarity
Disulfide bond757 ↔ 768 By similarity
Disulfide bond762 ↔ 777 By similarity
Disulfide bond779 ↔ 788 By similarity
Disulfide bond795 ↔ 806 By similarity
Disulfide bond800 ↔ 815 By similarity
Disulfide bond817 ↔ 826 By similarity
Disulfide bond833 ↔ 844 By similarity
Disulfide bond838 ↔ 855 By similarity
Disulfide bond857 ↔ 866 By similarity
Disulfide bond873 ↔ 884 By similarity
Disulfide bond878 ↔ 893 By similarity
Disulfide bond895 ↔ 904 By similarity
Disulfide bond911 ↔ 922 By similarity
Disulfide bond916 ↔ 931 By similarity
Disulfide bond933 ↔ 942 By similarity
Disulfide bond949 ↔ 960 By similarity
Disulfide bond954 ↔ 969 By similarity
Disulfide bond971 ↔ 980 By similarity
Disulfide bond987 ↔ 998 By similarity
Disulfide bond992 ↔ 1007 By similarity
Disulfide bond1009 ↔ 1018 By similarity
Disulfide bond1025 ↔ 1036 By similarity
Disulfide bond1030 ↔ 1045 By similarity
Disulfide bond1047 ↔ 1056 By similarity
Disulfide bond1063 ↔ 1074 By similarity
Disulfide bond1068 ↔ 1083 By similarity
Disulfide bond1085 ↔ 1094 By similarity
Disulfide bond1101 ↔ 1122 By similarity
Disulfide bond1116 ↔ 1131 By similarity
Disulfide bond1133 ↔ 1142 By similarity
Disulfide bond1149 ↔ 1160 By similarity
Disulfide bond1154 ↔ 1169 By similarity
Disulfide bond1171 ↔ 1180 By similarity
Disulfide bond1187 ↔ 1198 By similarity
Disulfide bond1192 ↔ 1207 By similarity
Disulfide bond1209 ↔ 1218 By similarity
Disulfide bond1225 ↔ 1244 By similarity
Disulfide bond1238 ↔ 1253 By similarity
Disulfide bond1255 ↔ 1264 By similarity
Disulfide bond1271 ↔ 1284 By similarity
Disulfide bond1276 ↔ 1293 By similarity
Disulfide bond1295 ↔ 1304 By similarity
Disulfide bond1311 ↔ 1322 By similarity
Disulfide bond1316 ↔ 1334 By similarity
Disulfide bond1336 ↔ 1345 By similarity
Disulfide bond1352 ↔ 1363 By similarity
Disulfide bond1357 ↔ 1372 By similarity
Disulfide bond1374 ↔ 1383 By similarity
Disulfide bond1391 ↔ 1403 By similarity
Disulfide bond1397 ↔ 1414 By similarity
Disulfide bond1416 ↔ 1425 By similarity
Disulfide bond1449 ↔ 1472 By similarity
Disulfide bond1454 ↔ 1467 By similarity
Disulfide bond1463 ↔ 1479 By similarity
Disulfide bond1490 ↔ 1514 By similarity
Disulfide bond1496 ↔ 1509 By similarity
Disulfide bond1505 ↔ 1521 By similarity
Disulfide bond1536 ↔ 1549 By similarity
Disulfide bond1545 ↔ 1561 By similarity
Cross-link1749Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict3091G → A in CAA40667. Ref.1
Sequence conflict3341E → D in CAA40667. Ref.1
Sequence conflict4021S → R in CAA40667. Ref.1
Sequence conflict5771Y → I in CAA40667. Ref.1
Sequence conflict9511S → T in CAA40667. Ref.1
Sequence conflict13391G → R in CAA40667. Ref.1
Sequence conflict14351G → A in CAA40667. Ref.1
Sequence conflict1595 – 15962EL → DV in CAA40667. Ref.1
Sequence conflict25011P → R in CAA40667. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q07008 [UniParc].

Last modified October 16, 2013. Version 3.
Checksum: 3E61AE863AA237F2

FASTA2,531270,822
        10         20         30         40         50         60 
MPRLLAPLLC LTLLPALAAR GLRCSQPSGT CLNGGRCEVA NGTEACVCSG AFVGQRCQDP 

        70         80         90        100        110        120 
SPCLSTPCKN AGTCYVVDHG GIVDYACSCP LGFSGPLCLT PLANACLANP CRNGGTCDLL 

       130        140        150        160        170        180 
TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA NGGQCLPFES SYICGCPPGF HGPTCRQDVN 

       190        200        210        220        230        240 
ECSQNPGLCR HGGTCHNEIG SYRCACRATH TGPHCELPYV PCSPSPCQNG GTCRPTGDTT 

       250        260        270        280        290        300 
HECACLPGFA GQNCEENVDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ 

       310        320        330        340        350        360 
LMPNACQNGG TCHNSHGGYN CVCVNGWTGE DCSENIDDCA SAACFQGATC HDRVASFYCE 

       370        380        390        400        410        420 
CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC PSGYTGPACS QDVDECALGA 

       430        440        450        460        470        480 
NPCEHAGKCL NTLGSFECQC LQGYTGPRCE IDVNECISNP CQNDATCLDQ IGEFQCICMP 

       490        500        510        520        530        540 
GYEGVYCEIN TDECASSPCL HNGRCVDKIN EFLCQCPKGF SGHLCQYDVD ECASTPCKNG 

       550        560        570        580        590        600 
AKCLDGPNTY TCVCTEGYTG THCEVDIDEC DPDPCHYGLC KDGVATFTCL CQPGYTGHHC 

       610        620        630        640        650        660 
ETNINECHSQ PCRHGGTCQD RDNYYLCLCL KGTTGPNCEI NLDDCASNPC DSGTCLDKID 

       670        680        690        700        710        720 
GYECACEPGY TGSMCNVNID ECAGSPCHNG GTCEDGIAGF TCRCPEGYHD PTCLSEVNEC 

       730        740        750        760        770        780 
NSNPCIHGAC RDGLNGYKCD CAPGWSGTNC DINNNECESN PCVNGGTCKD MTSGYVCTCR 

       790        800        810        820        830        840 
EGFSGPNCQT NINECASNPC LNQGTCIDDV AGYKCNCPLP YTGATCEVVL APCATSPCKN 

       850        860        870        880        890        900 
SGVCKESEDY ESFSCVCPTG WQGQTCEIDI NECVKSPCRH GASCQNTNGS YRCLCQAGYT 

       910        920        930        940        950        960 
GRNCESDIDD CRPNPCHNGG SCTDGVNAAF CDCLPGFQGA FCEEDINECA SNPCQNGANC 

       970        980        990       1000       1010       1020 
TDCVDSYTCT CPTGFNGIHC ENNTPDCTES SCFNGGTCVD GINSFTCLCP PGFTGSYCQY 

      1030       1040       1050       1060       1070       1080 
DVNECDSRPC LHGGTCQDSY GTYKCTCPQG YTGLNCQNLV RWCDSAPCKN GGKCWQTNTQ 

      1090       1100       1110       1120       1130       1140 
YHCECRSGWT GFNCDVLSVS CEVAAQKRGI DVTLLCQHGG LCVDEEDKHY CHCQAGYTGS 

      1150       1160       1170       1180       1190       1200 
YCEDEVDECS PNPCQNGATC TDYLGGFSCK CVAGYHGSNC SEEINECLSQ PCQNGGTCID 

      1210       1220       1230       1240       1250       1260 
LTNTYKCSCP RGTQGVHCEI NVDDCHPPLD PASRSPKCFN NGTCVDQVGG YTCTCPPGFV 

      1270       1280       1290       1300       1310       1320 
GERCEGDVNE CLSNPCDPRG TQNCVQRVND FHCECRAGHT GRRCESVING CRGKPCRNGG 

      1330       1340       1350       1360       1370       1380 
VCAVASNTAR GFICRCPAGF EGATCENDAR TCGSLRCLNG GTCISGPRSP TCLCLGSFTG 

      1390       1400       1410       1420       1430       1440 
PECQFPASSP CVGSNPCYNQ GTCEPTSESP FYRCLCPAKF NGLLCHILDY SFTGGAGRDI 

      1450       1460       1470       1480       1490       1500 
PPPQIEEACE LPECQEDAGN KVCNLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF 

      1510       1520       1530       1540       1550       1560 
SDGHCDSQCN SAGCLFDGFD CQLTEGQCNP LYDQYCKDHF SDGHCDQGCN SAECEWDGLD 

      1570       1580       1590       1600       1610       1620 
CAEHVPERLA AGTLVLVVLL PPDQLRNNSF HFLRELSHVL HTNVVFKRDA QGQQMIFPYY 

      1630       1640       1650       1660       1670       1680 
GREEELRKHP IKRSAVGWAT TSLLPGTNGG RQRRELDPMD IHGSIVYLEI DNRQCVQSSS 

      1690       1700       1710       1720       1730       1740 
QCFQSATDVA AFLGALASLG SLNIPYKIEA VKSETVEPPL PSQLHLMYVA AAAFVLLFFV 

      1750       1760       1770       1780       1790       1800 
GCGVLLSRKR RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA SDGALMDDNQ 

      1810       1820       1830       1840       1850       1860 
NEWGDEDLET KKFRFEEPVV LPDLDDQTDH RQWTQQHLDA ADLRVSAMAP TPPQGEVDAD 

      1870       1880       1890       1900       1910       1920 
CMDVNVRGPD GFTPLMIASC SGGGLETGNS EEEEDAPAVI SDFIYQGASL HNQTDRTGET 

      1930       1940       1950       1960       1970       1980 
ALHLAARYSR SDAAKRLLEA SADANIQDNM GRTPLHAAVS ADAQGVFQIL LRNRATDLDA 

      1990       2000       2010       2020       2030       2040 
RMHDGTTPLI LAARLAVEGM LEDLINSHAD VNAVDDLGKS ALHWAAAVNN VDAAVVLLKN 

      2050       2060       2070       2080       2090       2100 
GANKDMQNNK EETPLFLAAR EGSYETAKVL LDHFANRDIT DHMDRLPRDI AQERMHHDIV 

      2110       2120       2130       2140       2150       2160 
RLLDEYNLVR SPQLHGTALG GTPTLSPTLC SPNGYLGNLK SATQGKKARK PSTKGLACSS 

      2170       2180       2190       2200       2210       2220 
KEAKDLKARR KKSQDGKGCL LDSSSMLSPV DSLESPHGYL SDVASPPLLP SPFQQSPSMP 

      2230       2240       2250       2260       2270       2280 
LSHLPGMPDT HLGISHLNVA AKPEMAALAG GSRLAFEPPP PRLSHLPVAS SASTVLSTNG 

      2290       2300       2310       2320       2330       2340 
TGAMNFTVGA PASLNGQCEW LPRLQNGMVP SQYNPLRPGV TPGTLSTQAA GLQHGMMGPI 

      2350       2360       2370       2380       2390       2400 
HSSLSTNTLS PIIYQGLPNT RLATQPHLVQ TQQVQPQNLQ IQPQNLQPPS QPHLSVSSAA 

      2410       2420       2430       2440       2450       2460 
NGHLGRSFLS GEPSQADVQP LGPSSLPVHT ILPQESQALP TSLPSSMVPP MTTTQFLTPP 

      2470       2480       2490       2500       2510       2520 
SQHSYSSSPV DNTPSHQLQV PEHPFLTPSP ESPDQWSSSS PHSNISDWSE GISSPPTSMP 

      2530 
SQITHIPEAF K 

« Hide

References

« Hide 'large scale' references
[1]"A homolog of Drosophila Notch expressed during mammalian development."
Weinmaster G., Roberts V.J., Lemke G.
Development 113:199-205(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Schwann cell.
[2]Weinmaster G.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 1652-1653.
[3]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Notch1 and Notch3 instructively restrict bFGF-responsive multipotent neural progenitor cells to an astroglial fate."
Tanigaki K., Nogaki F., Takahashi J., Tashiro K., Kurooka H., Honjo T.
Neuron 29:45-55(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Notch2: a second mammalian Notch gene."
Weinmaster G., Roberts V.J., Lemke G.
Development 116:931-941(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Expression patterns of Notch1, Notch2, and Notch3 suggest multiple functional roles for the Notch-DSL signaling system during brain development."
Irvin D.K., Zurcher S.D., Nguyen T., Weinmaster G., Kornblum H.I.
J. Comp. Neurol. 436:167-181(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57405 mRNA. Translation: CAA40667.1.
AABR06021907 Genomic DNA. No translation available.
AABR06021908 Genomic DNA. No translation available.
CH474001 Genomic DNA. Translation: EDL93491.1.
PIRS18188.
RefSeqNP_001099191.1. NM_001105721.1.
UniGeneRn.25046.

3D structure databases

ProteinModelPortalQ07008.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000026212.

Proteomic databases

PaxDbQ07008.
PRIDEQ07008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026212; ENSRNOP00000026212; ENSRNOG00000019322.
GeneID25496.
KEGGrno:25496.
UCSCRGD:3187. rat.

Organism-specific databases

CTD4851.
RGD3187. Notch1.

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00730000110611.
HOGENOMHOG000234369.
HOVERGENHBG052650.
InParanoidQ07008.
KOK02599.
OMAGASCQNT.
OrthoDBEOG7992RD.
TreeFamTF351641.

Enzyme and pathway databases

ReactomeREACT_206767. Disease.
REACT_212996. Signal Transduction.

Gene expression databases

GenevestigatorQ07008.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR008297. Notch.
IPR022362. Notch_1.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 21 hits.
PF07645. EGF_CA. 5 hits.
PF12661. hEGF. 2 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PIRSFPIRSF002279. Notch. 1 hit.
PRINTSPR01452. LNOTCHREPEAT.
PR01984. NOTCH1.
SMARTSM00248. ANK. 6 hits.
SM00181. EGF. 11 hits.
SM00179. EGF_CA. 25 hits.
SM00004. NL. 3 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 5 hits.
SSF90193. SSF90193. 3 hits.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS00010. ASX_HYDROXYL. 22 hits.
PS00022. EGF_1. 35 hits.
PS01186. EGF_2. 27 hits.
PS50026. EGF_3. 36 hits.
PS01187. EGF_CA. 21 hits.
PS50258. LNR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio35582897.
PROQ07008.

Entry information

Entry nameNOTC1_RAT
AccessionPrimary (citable) accession number: Q07008
Secondary accession number(s): F1M9E7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 16, 2013
Last modified: July 9, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families