ID NOTC1_HUMAN Reviewed; 2555 AA.
AC P46531; Q59ED8; Q5SXM3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 4.
DT 01-MAY-2013, entry version 164.
DE RecName: Full=Neurogenic locus notch homolog protein 1;
DE Short=Notch 1;
DE Short=hN1;
DE AltName: Full=Translocation-associated notch protein TAN-1;
DE Contains:
DE RecName: Full=Notch 1 extracellular truncation;
DE Contains:
DE RecName: Full=Notch 1 intracellular domain;
DE Short=NICD;
DE Flags: Precursor;
GN Name=NOTCH1; Synonyms=TAN1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Mann R.S., Blaumueller C.M., Zagouras P.;
RT "Complete human notch 1 (hN1) cDNA sequence.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-2443.
RX PubMed=1831692; DOI=10.1016/0092-8674(91)90111-B;
RA Ellisen L.W., Bird J., West D.C., Soreng A.L., Reynolds T.C.,
RA Smith S.D., Sklar J.;
RT "TAN-1, the human homolog of the Drosophila notch gene, is broken by
RT chromosomal translocations in T lymphoblastic neoplasms.";
RL Cell 66:649-661(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 489-2555.
RC TISSUE=Aortic endothelium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 1947-1962, INTERACTION WITH HIF1AN, HYDROXYLATION
RP AT ASN-1955, AND MASS SPECTROMETRY.
RX PubMed=17573339; DOI=10.1074/jbc.M704102200;
RA Coleman M.L., McDonough M.A., Hewitson K.S., Coles C., Mecinovic J.,
RA Edelmann M., Cook K.M., Cockman M.E., Lancaster D.E., Kessler B.M.,
RA Oldham N.J., Ratcliffe P.J., Schofield C.J.;
RT "Asparaginyl hydroxylation of the Notch ankyrin repeat domain by
RT factor inhibiting hypoxia-inducible factor.";
RL J. Biol. Chem. 282:24027-24038(2007).
RN [6]
RP IDENTIFICATION OF LIGANDS.
RX PubMed=10079256;
RA Gray G.E., Mann R.S., Mitsiadis E., Henrique D., Carcangiu M.-L.,
RA Banks A., Leiman J., Ward D., Ish-Horowitz D., Artavanis-Tsakonas S.;
RT "Human ligands of the Notch receptor.";
RL Am. J. Pathol. 154:785-794(1999).
RN [7]
RP INTERACTION WITH DTX1.
RX PubMed=9590294; DOI=10.1038/ng0598-74;
RA Matsuno K., Eastman D., Mitsiades T., Quinn A.M., Carcanciu M.L.,
RA Ordentlich P., Kadesch T., Artavanis-Tsakonas S.;
RT "Human deltex is a conserved regulator of Notch signalling.";
RL Nat. Genet. 19:74-78(1998).
RN [8]
RP INTERACTION WITH SNW1.
RX PubMed=10713164; DOI=10.1128/MCB.20.7.2400-2410.2000;
RA Zhou S., Fujimuro M., Hsieh J.J., Chen L., Miyamoto A., Weinmaster G.,
RA Hayward S.D.;
RT "SKIP, a CBF1-associated protein, interacts with the ankyrin repeat
RT domain of NotchIC To facilitate NotchIC function.";
RL Mol. Cell. Biol. 20:2400-2410(2000).
RN [9]
RP INTERACTION WITH MAML1.
RX PubMed=11101851; DOI=10.1038/82644;
RA Wu L., Aster J.C., Blacklow S.C., Lake R., Artavanis-Tsakonas S.,
RA Griffin J.D.;
RT "MAML1, a human homologue of Drosophila mastermind, is a
RT transcriptional co-activator for NOTCH receptors.";
RL Nat. Genet. 26:484-489(2000).
RN [10]
RP GLYCOSYLATION.
RX PubMed=10734111; DOI=10.1074/jbc.275.13.9604;
RA Moloney D.J., Shair L.H., Lu F.M., Xia J., Locke R., Matta K.L.,
RA Haltiwanger R.S.;
RT "Mammalian Notch1 is modified with two unusual forms of O-linked
RT glycosylation found on epidermal growth factor-like modules.";
RL J. Biol. Chem. 275:9604-9611(2000).
RN [11]
RP INTERACTION WITH MAML2 AND MAML3.
RX PubMed=12370315; DOI=10.1128/MCB.22.21.7688-7700.2002;
RA Wu L., Sun T., Kobayashi K., Gao P., Griffin J.D.;
RT "Identification of a family of mastermind-like transcriptional
RT coactivators for mammalian notch receptors.";
RL Mol. Cell. Biol. 22:7688-7700(2002).
RN [12]
RP UBIQUITINATION BY ITCH.
RX PubMed=18628966; DOI=10.1371/journal.pone.0002735;
RA Chastagner P., Israel A., Brou C.;
RT "AIP4/Itch regulates Notch receptor degradation in the absence of
RT ligand.";
RL PLoS ONE 3:E2735-E2735(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP INTERACTION WITH SNAI1 AND MDM2A.
RX PubMed=22128911; DOI=10.1186/1741-7007-9-83;
RA Lim S.O., Kim H.S., Quan X., Ahn S.M., Kim H., Hsieh D., Seong J.K.,
RA Jung G.;
RT "Notch1 binds and induces degradation of Snail in hepatocellular
RT carcinoma.";
RL BMC Biol. 9:83-83(2011).
RN [15]
RP INTERACTION WITH AAK1.
RX PubMed=21464124; DOI=10.1074/jbc.M110.190769;
RA Gupta-Rossi N., Ortica S., Meas-Yedid V., Heuss S., Moretti J.,
RA Olivo-Marin J.C., Israel A.;
RT "The adaptor-associated kinase 1, AAK1, is a positive regulator of the
RT Notch pathway.";
RL J. Biol. Chem. 286:18720-18730(2011).
RN [16]
RP INTERACTION WITH SGK1 AND FBXW7.
RX PubMed=21147854; DOI=10.1242/jcs.073924;
RA Mo J.S., Ann E.J., Yoon J.H., Jung J., Choi Y.H., Kim H.Y., Ahn J.S.,
RA Kim S.M., Kim M.Y., Hong J.A., Seo M.S., Lang F., Choi E.J.,
RA Park H.S.;
RT "Serum- and glucocorticoid-inducible kinase 1 (SGK1) controls Notch1
RT signaling by downregulation of protein stability through Fbw7
RT ubiquitin ligase.";
RL J. Cell Sci. 124:100-112(2011).
RN [17]
RP INTERACTION WITH SNW1.
RX PubMed=21245387; DOI=10.1128/MCB.00360-10;
RA Vasquez-Del Carpio R., Kaplan F.M., Weaver K.L., VanWye J.D.,
RA Alves-Guerra M.C., Robbins D.J., Capobianco A.J.;
RT "Assembly of a Notch transcriptional activation complex requires
RT multimerization.";
RL Mol. Cell. Biol. 31:1396-1408(2011).
RN [18]
RP STRUCTURE BY NMR OF 1446-1480 IN COMPLEX WITH CALCIUM IONS, AND
RP DISULFIDE BONDS.
RX PubMed=12795601; DOI=10.1021/bi034156y;
RA Vardar D., North C.L., Sanchez-Irizarry C., Aster J.C., Blacklow S.C.;
RT "Nuclear magnetic resonance structure of a prototype Lin12-Notch
RT repeat module from human Notch1.";
RL Biochemistry 42:7061-7067(2003).
RN [19]
RP STRUCTURE BY NMR OF 411-526.
RX PubMed=15576031; DOI=10.1016/j.str.2004.09.012;
RA Hambleton S., Valeyev N.V., Muranyi A., Knott V., Werner J.M.,
RA McMichael A.J., Handford P.A., Downing A.K.;
RT "Structural and functional properties of the human notch-1 ligand
RT binding region.";
RL Structure 12:2173-2183(2004).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1872-2114.
RX PubMed=16011479; DOI=10.1042/BJ20050515;
RA Ehebauer M.T., Chirgadze D.Y., Hayward P., Martinez Arias A.,
RA Blundell T.L.;
RT "High-resolution crystal structure of the human Notch 1 ankyrin
RT domain.";
RL Biochem. J. 392:13-20(2005).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 1872-2126 IN COMPLEX WITH
RP RBPSUH AND MAML1.
RX PubMed=16530044; DOI=10.1016/j.cell.2005.12.037;
RA Nam Y., Sliz P., Song L., Aster J.C., Blacklow S.C.;
RT "Structural basis for cooperativity in recruitment of MAML
RT coactivators to Notch transcription complexes.";
RL Cell 124:973-983(2006).
RN [22]
RP INVOLVEMENT IN AOVD1.
RX PubMed=16025100; DOI=10.1038/nature03940;
RA Garg V., Muth A.N., Ransom J.F., Schluterman M.K., Barnes R.,
RA King I.N., Grossfeld P.D., Srivastava D.;
RT "Mutations in NOTCH1 cause aortic valve disease.";
RL Nature 437:270-274(2005).
CC -!- FUNCTION: Functions as a receptor for membrane-bound ligands
CC Jagged1, Jagged2 and Delta1 to regulate cell-fate determination.
CC Upon ligand activation through the released notch intracellular
CC domain (NICD) it forms a transcriptional activator complex with
CC RBPJ/RBPSUH and activates genes of the enhancer of split locus.
CC Affects the implementation of differentiation, proliferation and
CC apoptotic programs. May be important for normal lymphocyte
CC function. In altered form, may contribute to transformation or
CC progression in some T-cell neoplasms. Involved in the maturation
CC of both CD4+ and CD8+ cells in the thymus. May be important for
CC follicular differentiation and possibly cell fate selection within
CC the follicle. During cerebellar development, may function as a
CC receptor for neuronal DNER and may be involved in the
CC differentiation of Bergmann glia. Represses neuronal and myogenic
CC differentiation. May enhance HIF1A function by sequestering HIF1AN
CC away from HIF1A (By similarity).
CC -!- SUBUNIT: Heterodimer of a C-terminal fragment N(TM) and an N-
CC terminal fragment N(EC) which are probably linked by disulfide
CC bonds. Interacts with DNER, DTX1, DTX2 and RBPJ/RBPSUH. Also
CC interacts with MAML1, MAML2 and MAML3 which act as transcriptional
CC coactivators for NOTCH1. Notch 1 intracellular domain interacts
CC with SNW1; the interaction involves multimerized NOTCH1 NICD and
CC is implicated in a formation of an intermediate preactivation
CC complex which associates with DNA-bound CBF-1/RBPJ. The activated
CC membrane-bound form interacts with AAK1 which promotes NOTCH1
CC stabilization. Forms a trimeric complex with FBXW7 and SGK1.
CC Interacts with HIF1AN. HIF1AN negatively regulates the function of
CC notch intracellular domain (NICD), accelerating myogenic
CC differentiation (By similarity). Interacts (via NICD) with SNAI1
CC (via zinc fingers); the interaction induces SNAI1 degradation via
CC MDM2-mediated ubiquitination and inhibits SNAI1-induced cell
CC invasion. Interacts (via NICD) with MDM2A.
CC -!- INTERACTION:
CC Q13526:PIN1; NbExp=9; IntAct=EBI-636374, EBI-714158;
CC Q06330:RBPJ; NbExp=2; IntAct=EBI-636374, EBI-632552;
CC Q13573:SNW1; NbExp=3; IntAct=EBI-636374, EBI-632715;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein (By similarity).
CC -!- SUBCELLULAR LOCATION: Notch 1 intracellular domain: Nucleus (By
CC similarity). Note=Following proteolytical processing NICD is
CC translocated to the nucleus (By similarity).
CC -!- TISSUE SPECIFICITY: In fetal tissues most abundant in spleen,
CC brain stem and lung. Also present in most adult tissues where it
CC is found mainly in lymphoid tissues.
CC -!- PTM: Synthesized in the endoplasmic reticulum as an inactive form
CC which is proteolytically cleaved by a furin-like convertase in the
CC trans-Golgi network before it reaches the plasma membrane to yield
CC an active, ligand-accessible form. Cleavage results in a C-
CC terminal fragment N(TM) and a N-terminal fragment N(EC). Following
CC ligand binding, it is cleaved by TNF-alpha converting enzyme
CC (TACE) to yield a membrane-associated intermediate fragment called
CC notch extracellular truncation (NEXT). Following endocytosis, this
CC fragment is then cleaved by presenilin dependent gamma-secretase
CC to release a notch-derived peptide containing the intracellular
CC domain (NICD) from the membrane (By similarity).
CC -!- PTM: Phosphorylated (By similarity).
CC -!- PTM: O-glycosylated on the EGF-like domains. Contains both O-
CC linked fucose and O-linked glucose.
CC -!- PTM: Ubiquitinated; undergoes 'Lys-29'-linked polyubiquitination
CC catalyzed by ITCH. Monoubiquitination at Lys-1759 is required for
CC activation by gamma-secretase cleavage, it promotes interaction
CC with AAK1, which stabilizes it. Deubiquitination by EIF3F is
CC necessary for nuclear import of activated Notch.
CC -!- PTM: Hydroxylated at Asn-1955 by HIF1AN. Hydroxylated at Asn-2022
CC by HIF1AN (By similarity). Hydroxylation reduces affinity for
CC HI1AN and may thus indirectly modulate negative regulation of NICD
CC (By similarity).
CC -!- DISEASE: Aortic valve disease 1 (AOVD1) [MIM:109730]: A common
CC defect in the aortic valve in which two rather than three leaflets
CC are present. It is often associated with aortic valve
CC calcification, stenosis and insufficiency. In extreme cases, the
CC blood flow may be so restricted that the left ventricle fails to
CC grow, resulting in hypoplastic left heart syndrome. Note=The
CC disease is caused by mutations affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the NOTCH family.
CC -!- SIMILARITY: Contains 5 ANK repeats.
CC -!- SIMILARITY: Contains 36 EGF-like domains.
CC -!- SIMILARITY: Contains 3 LNR (Lin/Notch) repeats.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NOTCH1ID30ch9q34.html";
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DR EMBL; AF308602; AAG33848.1; -; mRNA.
DR EMBL; AL592301; CAI13934.1; -; Genomic_DNA.
DR EMBL; AL354671; CAI13934.1; JOINED; Genomic_DNA.
DR EMBL; AL354671; CAI16149.1; -; Genomic_DNA.
DR EMBL; AL592301; CAI16149.1; JOINED; Genomic_DNA.
DR EMBL; M73980; AAA60614.1; -; mRNA.
DR EMBL; AB209873; BAD93110.1; -; mRNA.
DR IPI; IPI00412982; -.
DR PIR; A40043; A40043.
DR RefSeq; NP_060087.3; NM_017617.3.
DR UniGene; Hs.495473; -.
DR PDB; 1PB5; NMR; -; A=1446-1480.
DR PDB; 1TOZ; NMR; -; A=411-526.
DR PDB; 1YYH; X-ray; 1.90 A; A/B=1872-2114.
DR PDB; 2F8X; X-ray; 3.25 A; K=1872-2126.
DR PDB; 2F8Y; X-ray; 1.55 A; A/B=1905-2126.
DR PDB; 2HE0; X-ray; 1.90 A; A/B=1873-2114.
DR PDB; 2VJ3; X-ray; 2.60 A; A=411-526.
DR PDB; 3ETO; X-ray; 2.00 A; A/B=1447-1733.
DR PDB; 3I08; X-ray; 3.20 A; A/C=1446-1664, B/D=1665-1733.
DR PDB; 3L95; X-ray; 2.19 A; X/Y=1448-1728.
DR PDB; 3NBN; X-ray; 3.45 A; B/E=1872-2126.
DR PDB; 3V79; X-ray; 3.85 A; K=1872-2126, R=1759-1777.
DR PDBsum; 1PB5; -.
DR PDBsum; 1TOZ; -.
DR PDBsum; 1YYH; -.
DR PDBsum; 2F8X; -.
DR PDBsum; 2F8Y; -.
DR PDBsum; 2HE0; -.
DR PDBsum; 2VJ3; -.
DR PDBsum; 3ETO; -.
DR PDBsum; 3I08; -.
DR PDBsum; 3L95; -.
DR PDBsum; 3NBN; -.
DR PDBsum; 3V79; -.
DR ProteinModelPortal; P46531; -.
DR DIP; DIP-29919N; -.
DR IntAct; P46531; 15.
DR MINT; MINT-1417018; -.
DR STRING; 9606.ENSP00000277541; -.
DR PhosphoSite; P46531; -.
DR DMDM; 206729936; -.
DR PaxDb; P46531; -.
DR PRIDE; P46531; -.
DR Ensembl; ENST00000277541; ENSP00000277541; ENSG00000148400.
DR GeneID; 4851; -.
DR KEGG; hsa:4851; -.
DR UCSC; uc004chz.3; human.
DR CTD; 4851; -.
DR GeneCards; GC09M139388; -.
DR H-InvDB; HIX0008549; -.
DR HGNC; HGNC:7881; NOTCH1.
DR HPA; CAB008112; -.
DR HPA; CAB022466; -.
DR MIM; 109730; phenotype.
DR MIM; 190198; gene.
DR neXtProt; NX_P46531; -.
DR Orphanet; 1244; Bicuspid aortic valve.
DR PharmGKB; PA31683; -.
DR eggNOG; COG0666; -.
DR HOGENOM; HOG000234369; -.
DR HOVERGEN; HBG052650; -.
DR KO; K02599; -.
DR OMA; HGGYNCV; -.
DR OrthoDB; EOG4HX504; -.
DR Pathway_Interaction_DB; ps1pathway; Presenilin action in Notch and Wnt signaling.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_2001; Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
DR Reactome; REACT_2155; NICD traffics to nucleus.
DR Reactome; REACT_691; A third proteolytic cleavage releases NICD.
DR Reactome; REACT_71; Gene Expression.
DR EvolutionaryTrace; P46531; -.
DR GenomeRNAi; 4851; -.
DR NextBio; 18684; -.
DR ArrayExpress; P46531; -.
DR Bgee; P46531; -.
DR CleanEx; HS_NOTCH1; -.
DR Genevestigator; P46531; -.
DR GermOnline; ENSG00000148400; Homo sapiens.
DR GO; GO:0009986; C:cell surface; IEA:Compara.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR GO; GO:0002193; C:MAML1-RBP-Jkappa- ICN1 complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:Compara.
DR GO; GO:0001047; F:core promoter binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB.
DR GO; GO:0004872; F:receptor activity; IEA:InterPro.
DR GO; GO:0001190; F:RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription; ISS:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:Compara.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:Compara.
DR GO; GO:0042640; P:anagen; IEA:Compara.
DR GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:0060842; P:arterial endothelial cell differentiation; ISS:BHF-UCL.
DR GO; GO:0003162; P:atrioventricular node development; IEA:Compara.
DR GO; GO:0003181; P:atrioventricular valve morphogenesis; ISS:BHF-UCL.
DR GO; GO:0009912; P:auditory receptor cell fate commitment; IEA:Compara.
DR GO; GO:0007409; P:axonogenesis; IEA:Compara.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Compara.
DR GO; GO:0003207; P:cardiac chamber formation; ISS:BHF-UCL.
DR GO; GO:0003214; P:cardiac left ventricle morphogenesis; ISS:BHF-UCL.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Compara.
DR GO; GO:0003213; P:cardiac right atrium morphogenesis; ISS:BHF-UCL.
DR GO; GO:0003219; P:cardiac right ventricle formation; IEA:Compara.
DR GO; GO:0060948; P:cardiac vascular smooth muscle cell development; ISS:BHF-UCL.
DR GO; GO:0001708; P:cell fate specification; IEA:Compara.
DR GO; GO:0003273; P:cell migration involved in endocardial cushion formation; ISS:BHF-UCL.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IDA:BHF-UCL.
DR GO; GO:0072044; P:collecting duct development; IEA:Compara.
DR GO; GO:0007386; P:compartment pattern specification; IEA:Compara.
DR GO; GO:0060982; P:coronary artery morphogenesis; ISS:BHF-UCL.
DR GO; GO:0003169; P:coronary vein morphogenesis; ISS:BHF-UCL.
DR GO; GO:0072017; P:distal tubule development; IEA:Compara.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Compara.
DR GO; GO:0060956; P:endocardial cell differentiation; ISS:BHF-UCL.
DR GO; GO:0003160; P:endocardium morphogenesis; ISS:BHF-UCL.
DR GO; GO:0007492; P:endoderm development; IEA:Compara.
DR GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL.
DR GO; GO:0030900; P:forebrain development; IEA:Compara.
DR GO; GO:0007440; P:foregut morphogenesis; IEA:Compara.
DR GO; GO:0010001; P:glial cell differentiation; IEA:Compara.
DR GO; GO:0072144; P:glomerular mesangial cell development; IEA:Compara.
DR GO; GO:0003241; P:growth involved in heart morphogenesis; ISS:BHF-UCL.
DR GO; GO:0031069; P:hair follicle morphogenesis; IEA:Compara.
DR GO; GO:0001947; P:heart looping; ISS:BHF-UCL.
DR GO; GO:0006959; P:humoral immune response; IEA:Compara.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Compara.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Compara.
DR GO; GO:0072602; P:interleukin-4 secretion; IEA:Compara.
DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Compara.
DR GO; GO:0070986; P:left/right axis specification; IEA:Compara.
DR GO; GO:0001889; P:liver development; IEA:Compara.
DR GO; GO:0030324; P:lung development; IEA:Compara.
DR GO; GO:0003192; P:mitral valve formation; IMP:BHF-UCL.
DR GO; GO:2000811; P:negative regulation of anoikis; IMP:BHF-UCL.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:BHF-UCL.
DR GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IEA:Compara.
DR GO; GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; IEA:Compara.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IDA:BHF-UCL.
DR GO; GO:0060253; P:negative regulation of glial cell proliferation; ISS:UniProtKB.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IMP:UniProtKB.
DR GO; GO:0010832; P:negative regulation of myotube differentiation; ISS:UniProtKB.
DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0030279; P:negative regulation of ossification; ISS:BHF-UCL.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:BHF-UCL.
DR GO; GO:0046533; P:negative regulation of photoreceptor cell differentiation; IEA:Compara.
DR GO; GO:2000974; P:negative regulation of pro-B cell differentiation; ISS:UniProtKB.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0021915; P:neural tube development; IEA:Compara.
DR GO; GO:0097150; P:neuronal stem cell maintenance; IEP:UniProtKB.
DR GO; GO:0007220; P:Notch receptor processing; TAS:Reactome.
DR GO; GO:0061314; P:Notch signaling involved in heart development; IMP:BHF-UCL.
DR GO; GO:0003270; P:Notch signaling pathway involved in regulation of secondary heart field cardioblast proliferation; IEA:Compara.
DR GO; GO:0003344; P:pericardium morphogenesis; ISS:BHF-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Compara.
DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISS:BHF-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:BHF-UCL.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Compara.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
DR GO; GO:0046427; P:positive regulation of JAK-STAT cascade; ISS:UniProtKB.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IEA:Compara.
DR GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISS:UniProtKB.
DR GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; ISS:BHF-UCL.
DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IEA:Compara.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:0060768; P:regulation of epithelial cell proliferation involved in prostate gland development; IEA:Compara.
DR GO; GO:1901201; P:regulation of extracellular matrix assembly; ISS:BHF-UCL.
DR GO; GO:0014807; P:regulation of somitogenesis; IEA:Compara.
DR GO; GO:0003256; P:regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation; ISS:BHF-UCL.
DR GO; GO:0032495; P:response to muramyl dipeptide; IEA:Compara.
DR GO; GO:0060528; P:secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development; IEA:Compara.
DR GO; GO:0048103; P:somatic stem cell division; IEA:Compara.
DR GO; GO:0002040; P:sprouting angiogenesis; IEA:Compara.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; ISS:BHF-UCL.
DR GO; GO:0060843; P:venous endothelial cell differentiation; ISS:BHF-UCL.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISS:BHF-UCL.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR InterPro; IPR024600; DUF3454_notch.
DR InterPro; IPR000742; EG-like_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR008297; Notch.
DR InterPro; IPR022362; Notch_1.
DR InterPro; IPR000800; Notch_dom.
DR InterPro; IPR010660; Notch_NOD_dom.
DR InterPro; IPR011656; Notch_NODP_dom.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF11936; DUF3454; 1.
DR Pfam; PF00008; EGF; 23.
DR Pfam; PF07645; EGF_CA; 5.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF06816; NOD; 1.
DR Pfam; PF07684; NODP; 1.
DR Pfam; PF00066; Notch; 3.
DR PIRSF; PIRSF002279; Notch; 1.
DR PRINTS; PR01452; LNOTCHREPEAT.
DR PRINTS; PR01984; NOTCH1.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00181; EGF; 12.
DR SMART; SM00179; EGF_CA; 24.
DR SMART; SM00004; NL; 3.
DR SUPFAM; SSF48403; ANK; 1.
DR SUPFAM; SSF90193; Notch_region; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 22.
DR PROSITE; PS00022; EGF_1; 35.
DR PROSITE; PS01186; EGF_2; 27.
DR PROSITE; PS50026; EGF_3; 36.
DR PROSITE; PS01187; EGF_CA; 20.
DR PROSITE; PS50258; LNR; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; ANK repeat; Calcium; Cell membrane;
KW Complete proteome; Developmental protein; Differentiation;
KW Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Glycoprotein; Hydroxylation; Isopeptide bond; Membrane; Metal-binding;
KW Notch signaling pathway; Nucleus; Phosphoprotein; Polymorphism;
KW Receptor; Reference proteome; Repeat; Signal; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1 18 Potential.
FT CHAIN 19 2555 Neurogenic locus notch homolog protein 1.
FT /FTId=PRO_0000007674.
FT CHAIN 1721 2555 Notch 1 extracellular truncation (By
FT similarity).
FT /FTId=PRO_0000007675.
FT CHAIN 1754 2555 Notch 1 intracellular domain (By
FT similarity).
FT /FTId=PRO_0000007676.
FT TOPO_DOM 19 1735 Extracellular (Potential).
FT TRANSMEM 1736 1756 Helical; (Potential).
FT TOPO_DOM 1757 2555 Cytoplasmic (Potential).
FT DOMAIN 20 58 EGF-like 1.
FT DOMAIN 59 99 EGF-like 2.
FT DOMAIN 102 139 EGF-like 3.
FT DOMAIN 140 176 EGF-like 4.
FT DOMAIN 178 216 EGF-like 5; calcium-binding (Potential).
FT DOMAIN 218 255 EGF-like 6.
FT DOMAIN 257 293 EGF-like 7; calcium-binding (Potential).
FT DOMAIN 295 333 EGF-like 8; calcium-binding (Potential).
FT DOMAIN 335 371 EGF-like 9; calcium-binding (Potential).
FT DOMAIN 372 410 EGF-like 10.
FT DOMAIN 412 450 EGF-like 11; calcium-binding (Potential).
FT DOMAIN 452 488 EGF-like 12; calcium-binding (Potential).
FT DOMAIN 490 526 EGF-like 13; calcium-binding (Potential).
FT DOMAIN 528 564 EGF-like 14; calcium-binding (Potential).
FT DOMAIN 566 601 EGF-like 15; calcium-binding (Potential).
FT DOMAIN 603 639 EGF-like 16; calcium-binding (Potential).
FT DOMAIN 641 676 EGF-like 17; calcium-binding (Potential).
FT DOMAIN 678 714 EGF-like 18; calcium-binding (Potential).
FT DOMAIN 716 751 EGF-like 19; calcium-binding (Potential).
FT DOMAIN 753 789 EGF-like 20.
FT DOMAIN 791 827 EGF-like 21; calcium-binding (Potential).
FT DOMAIN 829 867 EGF-like 22.
FT DOMAIN 869 905 EGF-like 23; calcium-binding (Potential).
FT DOMAIN 907 943 EGF-like 24.
FT DOMAIN 945 981 EGF-like 25; calcium-binding (Potential).
FT DOMAIN 983 1019 EGF-like 26.
FT DOMAIN 1021 1057 EGF-like 27.
FT DOMAIN 1059 1095 EGF-like 28.
FT DOMAIN 1097 1143 EGF-like 29.
FT DOMAIN 1145 1181 EGF-like 30.
FT DOMAIN 1183 1219 EGF-like 31; calcium-binding (Potential).
FT DOMAIN 1221 1265 EGF-like 32; calcium-binding (Potential).
FT DOMAIN 1267 1305 EGF-like 33.
FT DOMAIN 1307 1346 EGF-like 34.
FT DOMAIN 1348 1384 EGF-like 35.
FT DOMAIN 1387 1426 EGF-like 36.
FT REPEAT 1449 1489 LNR 1.
FT REPEAT 1490 1531 LNR 2.
FT REPEAT 1532 1571 LNR 3.
FT REPEAT 1927 1956 ANK 1.
FT REPEAT 1960 1990 ANK 2.
FT REPEAT 1994 2023 ANK 3.
FT REPEAT 2027 2056 ANK 4.
FT REPEAT 2060 2089 ANK 5.
FT REGION 1947 1955 HIF1AN-binding (By similarity).
FT REGION 2014 2022 HIF1AN-binding (By similarity).
FT COMPBIAS 1575 1578 Poly-Val.
FT COMPBIAS 1661 1664 Poly-Arg.
FT COMPBIAS 1728 1731 Poly-Pro.
FT COMPBIAS 1740 1743 Poly-Ala.
FT COMPBIAS 1901 1904 Poly-Glu.
FT COMPBIAS 2259 2262 Poly-Gly.
FT COMPBIAS 2403 2406 Poly-Gln.
FT COMPBIAS 2410 2417 Poly-Pro.
FT COMPBIAS 2521 2524 Poly-Ser.
FT METAL 1457 1457 Calcium; via carbonyl oxygen.
FT METAL 1460 1460 Calcium.
FT METAL 1475 1475 Calcium.
FT METAL 1478 1478 Calcium.
FT SITE 1664 1665 Cleavage; by furin-like protease (By
FT similarity).
FT MOD_RES 1955 1955 (3S)-3-hydroxyasparagine; by HIF1AN;
FT partial.
FT MOD_RES 2022 2022 (3S)-3-hydroxyasparagine; by HIF1AN (By
FT similarity).
FT CARBOHYD 41 41 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 959 959 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1179 1179 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1241 1241 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1489 1489 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1587 1587 N-linked (GlcNAc...) (Potential).
FT DISULFID 24 37 By similarity.
FT DISULFID 31 46 By similarity.
FT DISULFID 48 57 By similarity.
FT DISULFID 63 74 By similarity.
FT DISULFID 68 87 By similarity.
FT DISULFID 89 98 By similarity.
FT DISULFID 106 117 By similarity.
FT DISULFID 111 127 By similarity.
FT DISULFID 129 138 By similarity.
FT DISULFID 144 155 By similarity.
FT DISULFID 149 164 By similarity.
FT DISULFID 166 175 By similarity.
FT DISULFID 182 195 By similarity.
FT DISULFID 189 204 By similarity.
FT DISULFID 206 215 By similarity.
FT DISULFID 222 233 By similarity.
FT DISULFID 227 243 By similarity.
FT DISULFID 245 254 By similarity.
FT DISULFID 261 272 By similarity.
FT DISULFID 266 281 By similarity.
FT DISULFID 283 292 By similarity.
FT DISULFID 299 312 By similarity.
FT DISULFID 306 321 By similarity.
FT DISULFID 323 332 By similarity.
FT DISULFID 339 350 By similarity.
FT DISULFID 344 359 By similarity.
FT DISULFID 361 370 By similarity.
FT DISULFID 376 387 By similarity.
FT DISULFID 381 398 By similarity.
FT DISULFID 400 409 By similarity.
FT DISULFID 416 429 By similarity.
FT DISULFID 423 438 By similarity.
FT DISULFID 440 449 By similarity.
FT DISULFID 456 467 By similarity.
FT DISULFID 461 476 By similarity.
FT DISULFID 478 487 By similarity.
FT DISULFID 494 505 By similarity.
FT DISULFID 499 514 By similarity.
FT DISULFID 516 525 By similarity.
FT DISULFID 532 543 By similarity.
FT DISULFID 537 552 By similarity.
FT DISULFID 554 563 By similarity.
FT DISULFID 570 580 By similarity.
FT DISULFID 575 589 By similarity.
FT DISULFID 591 600 By similarity.
FT DISULFID 607 618 By similarity.
FT DISULFID 612 627 By similarity.
FT DISULFID 629 638 By similarity.
FT DISULFID 645 655 By similarity.
FT DISULFID 650 664 By similarity.
FT DISULFID 666 675 By similarity.
FT DISULFID 682 693 By similarity.
FT DISULFID 687 702 By similarity.
FT DISULFID 704 713 By similarity.
FT DISULFID 720 730 By similarity.
FT DISULFID 725 739 By similarity.
FT DISULFID 741 750 By similarity.
FT DISULFID 757 768 By similarity.
FT DISULFID 762 777 By similarity.
FT DISULFID 779 788 By similarity.
FT DISULFID 795 806 By similarity.
FT DISULFID 800 815 By similarity.
FT DISULFID 817 826 By similarity.
FT DISULFID 833 844 By similarity.
FT DISULFID 838 855 By similarity.
FT DISULFID 857 866 By similarity.
FT DISULFID 873 884 By similarity.
FT DISULFID 878 893 By similarity.
FT DISULFID 895 904 By similarity.
FT DISULFID 911 922 By similarity.
FT DISULFID 916 931 By similarity.
FT DISULFID 933 942 By similarity.
FT DISULFID 949 960 By similarity.
FT DISULFID 954 969 By similarity.
FT DISULFID 971 980 By similarity.
FT DISULFID 987 998 By similarity.
FT DISULFID 992 1007 By similarity.
FT DISULFID 1009 1018 By similarity.
FT DISULFID 1025 1036 By similarity.
FT DISULFID 1030 1045 By similarity.
FT DISULFID 1047 1056 By similarity.
FT DISULFID 1063 1074 By similarity.
FT DISULFID 1068 1083 By similarity.
FT DISULFID 1085 1094 By similarity.
FT DISULFID 1101 1122 By similarity.
FT DISULFID 1116 1131 By similarity.
FT DISULFID 1133 1142 By similarity.
FT DISULFID 1149 1160 By similarity.
FT DISULFID 1154 1169 By similarity.
FT DISULFID 1171 1180 By similarity.
FT DISULFID 1187 1198 By similarity.
FT DISULFID 1192 1207 By similarity.
FT DISULFID 1209 1218 By similarity.
FT DISULFID 1225 1244 By similarity.
FT DISULFID 1238 1253 By similarity.
FT DISULFID 1255 1264 By similarity.
FT DISULFID 1271 1284 By similarity.
FT DISULFID 1276 1293 By similarity.
FT DISULFID 1295 1304 By similarity.
FT DISULFID 1311 1322 By similarity.
FT DISULFID 1316 1334 By similarity.
FT DISULFID 1336 1345 By similarity.
FT DISULFID 1352 1363 By similarity.
FT DISULFID 1357 1372 By similarity.
FT DISULFID 1374 1383 By similarity.
FT DISULFID 1391 1403 By similarity.
FT DISULFID 1397 1414 By similarity.
FT DISULFID 1416 1425 By similarity.
FT DISULFID 1449 1472
FT DISULFID 1454 1467
FT DISULFID 1463 1479
FT DISULFID 1490 1514 By similarity.
FT DISULFID 1496 1509 By similarity.
FT DISULFID 1505 1521 By similarity.
FT DISULFID 1536 1549 By similarity.
FT DISULFID 1545 1561 By similarity.
FT CROSSLNK 1759 1759 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin) (By
FT similarity).
FT VARIANT 300 300 Q -> R (in dbSNP:rs11574885).
FT /FTId=VAR_034898.
FT VARIANT 879 879 R -> W (in dbSNP:rs11574895).
FT /FTId=VAR_048990.
FT VARIANT 1671 1671 V -> I (in dbSNP:rs2229968).
FT /FTId=VAR_046618.
FT CONFLICT 187 187 G -> R (in Ref. 1; AAG33848 and 3;
FT AAA60614).
FT CONFLICT 282 282 R -> P (in Ref. 1; AAG33848 and 3;
FT AAA60614).
FT CONFLICT 477 477 I -> M (in Ref. 1; AAG33848 and 3;
FT AAA60614).
FT CONFLICT 614 615 HG -> LR (in Ref. 1; AAG33848 and 3;
FT AAA60614).
FT CONFLICT 621 621 R -> P (in Ref. 1; AAG33848 and 3;
FT AAA60614).
FT CONFLICT 677 677 I -> S (in Ref. 1; AAG33848 and 3;
FT AAA60614).
FT CONFLICT 775 775 Y -> I (in Ref. 1; AAG33848 and 3;
FT AAA60614).
FT CONFLICT 803 803 Q -> K (in Ref. 1; AAG33848 and 3;
FT AAA60614).
FT CONFLICT 860 862 GWQ -> AGAK (in Ref. 1; AAG33848 and 3;
FT AAA60614).
FT CONFLICT 1021 1021 D -> V (in Ref. 1; AAG33848 and 3;
FT AAA60614).
FT CONFLICT 1028 1028 Q -> R (in Ref. 1; AAG33848 and 3;
FT AAA60614).
FT CONFLICT 1032 1032 H -> L (in Ref. 1; AAG33848 and 3;
FT AAA60614).
FT CONFLICT 1040 1043 CGSY -> RGLH (in Ref. 1; AAG33848 and 3;
FT AAA60614).
FT TURN 415 417
FT STRAND 418 420
FT STRAND 422 424
FT STRAND 428 431
FT STRAND 433 439
FT STRAND 444 446
FT TURN 455 458
FT STRAND 466 469
FT STRAND 474 477
FT STRAND 482 487
FT TURN 493 496
FT TURN 500 502
FT STRAND 504 507
FT STRAND 512 515
FT STRAND 520 525
FT HELIX 1448 1450
FT HELIX 1452 1457
FT STRAND 1460 1462
FT HELIX 1465 1467
FT HELIX 1470 1472
FT HELIX 1473 1476
FT TURN 1477 1482
FT TURN 1486 1489
FT HELIX 1492 1494
FT HELIX 1496 1498
FT TURN 1499 1501
FT STRAND 1502 1504
FT HELIX 1507 1509
FT HELIX 1512 1519
FT TURN 1530 1532
FT HELIX 1533 1539
FT STRAND 1542 1544
FT HELIX 1547 1549
FT HELIX 1552 1559
FT STRAND 1563 1565
FT STRAND 1571 1580
FT HELIX 1582 1587
FT HELIX 1589 1600
FT STRAND 1602 1606
FT STRAND 1616 1620
FT STRAND 1672 1681
FT HELIX 1685 1688
FT HELIX 1696 1708
FT STRAND 1714 1716
FT STRAND 1718 1724
FT HELIX 1884 1890
FT HELIX 1909 1914
FT TURN 1925 1927
FT HELIX 1931 1937
FT HELIX 1941 1949
FT HELIX 1964 1970
FT HELIX 1974 1982
FT STRAND 1983 1985
FT HELIX 1998 2005
FT HELIX 2008 2016
FT HELIX 2031 2037
FT HELIX 2041 2049
FT HELIX 2064 2071
FT HELIX 2074 2082
FT HELIX 2097 2103
FT HELIX 2107 2115
SQ SEQUENCE 2555 AA; 272505 MW; E173C872D195F028 CRC64;
MPPLLAPLLC LALLPALAAR GPRCSQPGET CLNGGKCEAA NGTEACVCGG AFVGPRCQDP
NPCLSTPCKN AGTCHVVDRR GVADYACSCA LGFSGPLCLT PLDNACLTNP CRNGGTCDLL
TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA NGGQCLPFEA SYICHCPPSF HGPTCRQDVN
ECGQKPGLCR HGGTCHNEVG SYRCVCRATH TGPNCERPYV PCSPSPCQNG GTCRPTGDVT
HECACLPGFT GQNCEENIDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ
LMPNACQNGG TCHNTHGGYN CVCVNGWTGE DCSENIDDCA SAACFHGATC HDRVASFYCE
CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC PSGYTGPACS QDVDECSLGA
NPCEHAGKCI NTLGSFECQC LQGYTGPRCE IDVNECVSNP CQNDATCLDQ IGEFQCICMP
GYEGVHCEVN TDECASSPCL HNGRCLDKIN EFQCECPTGF TGHLCQYDVD ECASTPCKNG
AKCLDGPNTY TCVCTEGYTG THCEVDIDEC DPDPCHYGSC KDGVATFTCL CRPGYTGHHC
ETNINECSSQ PCRHGGTCQD RDNAYLCFCL KGTTGPNCEI NLDDCASSPC DSGTCLDKID
GYECACEPGY TGSMCNINID ECAGNPCHNG GTCEDGINGF TCRCPEGYHD PTCLSEVNEC
NSNPCVHGAC RDSLNGYKCD CDPGWSGTNC DINNNECESN PCVNGGTCKD MTSGYVCTCR
EGFSGPNCQT NINECASNPC LNQGTCIDDV AGYKCNCLLP YTGATCEVVL APCAPSPCRN
GGECRQSEDY ESFSCVCPTG WQGQTCEVDI NECVLSPCRH GASCQNTHGG YRCHCQAGYS
GRNCETDIDD CRPNPCHNGG SCTDGINTAF CDCLPGFRGT FCEEDINECA SDPCRNGANC
TDCVDSYTCT CPAGFSGIHC ENNTPDCTES SCFNGGTCVD GINSFTCLCP PGFTGSYCQH
DVNECDSQPC LHGGTCQDGC GSYRCTCPQG YTGPNCQNLV HWCDSSPCKN GGKCWQTHTQ
YRCECPSGWT GLYCDVPSVS CEVAAQRQGV DVARLCQHGG LCVDAGNTHH CRCQAGYTGS
YCEDLVDECS PSPCQNGATC TDYLGGYSCK CVAGYHGVNC SEEIDECLSH PCQNGGTCLD
LPNTYKCSCP RGTQGVHCEI NVDDCNPPVD PVSRSPKCFN NGTCVDQVGG YSCTCPPGFV
GERCEGDVNE CLSNPCDARG TQNCVQRVND FHCECRAGHT GRRCESVING CKGKPCKNGG
TCAVASNTAR GFICKCPAGF EGATCENDAR TCGSLRCLNG GTCISGPRSP TCLCLGPFTG
PECQFPASSP CLGGNPCYNQ GTCEPTSESP FYRCLCPAKF NGLLCHILDY SFGGGAGRDI
PPPLIEEACE LPECQEDAGN KVCSLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF
SDGHCDSQCN SAGCLFDGFD CQRAEGQCNP LYDQYCKDHF SDGHCDQGCN SAECEWDGLD
CAEHVPERLA AGTLVVVVLM PPEQLRNSSF HFLRELSRVL HTNVVFKRDA HGQQMIFPYY
GREEELRKHP IKRAAEGWAA PDALLGQVKA SLLPGGSEGG RRRRELDPMD VRGSIVYLEI
DNRQCVQASS QCFQSATDVA AFLGALASLG SLNIPYKIEA VQSETVEPPP PAQLHFMYVA
AAAFVLLFFV GCGVLLSRKR RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA
SDGALMDDNQ NEWGDEDLET KKFRFEEPVV LPDLDDQTDH RQWTQQHLDA ADLRMSAMAP
TPPQGEVDAD CMDVNVRGPD GFTPLMIASC SGGGLETGNS EEEEDAPAVI SDFIYQGASL
HNQTDRTGET ALHLAARYSR SDAAKRLLEA SADANIQDNM GRTPLHAAVS ADAQGVFQIL
IRNRATDLDA RMHDGTTPLI LAARLAVEGM LEDLINSHAD VNAVDDLGKS ALHWAAAVNN
VDAAVVLLKN GANKDMQNNR EETPLFLAAR EGSYETAKVL LDHFANRDIT DHMDRLPRDI
AQERMHHDIV RLLDEYNLVR SPQLHGAPLG GTPTLSPPLC SPNGYLGSLK PGVQGKKVRK
PSSKGLACGS KEAKDLKARR KKSQDGKGCL LDSSGMLSPV DSLESPHGYL SDVASPPLLP
SPFQQSPSVP LNHLPGMPDT HLGIGHLNVA AKPEMAALGG GGRLAFETGP PRLSHLPVAS
GTSTVLGSSS GGALNFTVGG STSLNGQCEW LSRLQSGMVP NQYNPLRGSV APGPLSTQAP
SLQHGMVGPL HSSLAASALS QMMSYQGLPS TRLATQPHLV QTQQVQPQNL QMQQQNLQPA
NIQQQQSLQP PPPPPQPHLG VSSAASGHLG RSFLSGEPSQ ADVQPLGPSS LAVHTILPQE
SPALPTSLPS SLVPPVTAAQ FLTPPSQHSY SSPVDNTPSH QLQVPEHPFL TPSPESPDQW
SSSSPHSNVS DWSEGVSSPP TSMQSQIARI PEAFK
//
