NEO1_HUMAN
ID NEO1_HUMAN Reviewed; 1461 AA.
AC Q92859; B7ZKM9; B7ZKN0; O00340; Q17RX1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Neogenin;
DE AltName: Full=Immunoglobulin superfamily DCC subclass member 2;
DE Flags: Precursor;
GN Name=NEO1; Synonyms=IGDCC2, NGN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Fetal brain;
RX PubMed=9121761; DOI=10.1038/sj.onc.1200935;
RA Meyerhardt J.A., Look A.T., Bigner S.H., Fearon E.R.;
RT "Identification and characterization of neogenin, a DCC-related gene.";
RL Oncogene 14:1129-1136(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Fetal brain;
RX PubMed=9169140; DOI=10.1006/geno.1997.4688;
RA Vielmetter J., Chen X.-N., Miskevich F., Lane R.P., Yamakawa K.,
RA Korenberg J.R., Dreyer W.J.;
RT "Molecular characterization of human neogenin, a DCC-related protein, and
RT the mapping of its gene (NEO1) to chromosomal position 15q22.3-q23.";
RL Genomics 41:414-421(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-210 AND ASN-489.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [6]
RP REVIEW.
RX PubMed=17204444; DOI=10.1016/j.biocel.2006.11.009;
RA Cole S.J., Bradford D., Cooper H.M.;
RT "Neogenin: A multi-functional receptor regulating diverse developmental
RT processes.";
RL Int. J. Biochem. Cell Biol. 39:1569-1575(2007).
RN [7]
RP INTERACTION WITH RBMC.
RX PubMed=18287331; DOI=10.1152/ajpcell.00563.2007;
RA Kuns-Hashimoto R., Kuninger D., Nili M., Rotwein P.;
RT "Selective binding of RGMc/hemojuvelin, a key protein in systemic iron
RT metabolism, to BMP-2 and neogenin.";
RL Am. J. Physiol. 294:C994-C1003(2008).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-210; ASN-470 AND ASN-639.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP FUNCTION, INTERACTION WITH BMP FAMILY MEMBERS, AND MISCELLANEOUS.
RX PubMed=21149453; DOI=10.1074/jbc.m110.180919;
RA Hagihara M., Endo M., Hata K., Higuchi C., Takaoka K., Yoshikawa H.,
RA Yamashita T.;
RT "Neogenin, a receptor for bone morphogenetic proteins.";
RL J. Biol. Chem. 286:5157-5165(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1198; SER-1401; THR-1404 AND
RP SER-1434, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1194, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP STRUCTURE BY NMR OF 429-1054.
RG RIKEN structural genomics initiative (RSGI);
RT "The solution structure of the six fibronectin type III domains of human
RT neogenin.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Multi-functional cell surface receptor regulating cell
CC adhesion in many diverse developmental processes, including neural tube
CC and mammary gland formation, myogenesis and angiogenesis. Receptor for
CC members of the BMP, netrin, and repulsive guidance molecule (RGM)
CC families. Netrin-Neogenin interactions result in a chemoattractive axon
CC guidance response and cell-cell adhesion, the interaction between
CC NEO1/Neogenin and RGMa and RGMb induces a chemorepulsive response.
CC {ECO:0000269|PubMed:21149453}.
CC -!- SUBUNIT: Interacts with MYO10 (By similarity). Interacts with RGMA and
CC RGMB. Interacts with BMP2, BMP4, BMP6, and BMP7. {ECO:0000250,
CC ECO:0000269|PubMed:18287331, ECO:0000269|PubMed:21149453}.
CC -!- INTERACTION:
CC Q92859; Q6ZVN8: HJV; NbExp=3; IntAct=EBI-2829116, EBI-10900704;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q92859-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92859-2; Sequence=VSP_002593;
CC Name=3;
CC IsoId=Q92859-3; Sequence=VSP_043330;
CC Name=4;
CC IsoId=Q92859-4; Sequence=VSP_047134;
CC -!- TISSUE SPECIFICITY: Widely expressed and also in cancer cell lines.
CC -!- DOMAIN: The Fibronectin repeats 5 and 6 mediate interaction with RGM
CC family molecules. {ECO:0000250}.
CC -!- MISCELLANEOUS: Knockdown of NEO1 in C2C12 cells results in the
CC enhancement of the BMP-2-induced processes of osteoblastic
CC differentiation and phosphorylation of Smad1, Smad5, and Smad8.
CC Conversely, overexpression suppresses these processes.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC {ECO:0000305}.
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DR EMBL; U61262; AAB17263.1; -; mRNA.
DR EMBL; U72391; AAC51287.1; -; mRNA.
DR EMBL; AC068397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC129980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117161; AAI17162.1; -; mRNA.
DR EMBL; BC143270; AAI43271.1; -; mRNA.
DR EMBL; BC143271; AAI43272.1; -; mRNA.
DR CCDS; CCDS10247.1; -. [Q92859-1]
DR CCDS; CCDS53957.1; -. [Q92859-3]
DR CCDS; CCDS58378.1; -. [Q92859-4]
DR RefSeq; NP_001166094.1; NM_001172623.1. [Q92859-3]
DR RefSeq; NP_001166095.1; NM_001172624.1. [Q92859-4]
DR RefSeq; NP_002490.2; NM_002499.3. [Q92859-1]
DR PDB; 1X5F; NMR; -; A=429-535.
DR PDB; 1X5G; NMR; -; A=529-631.
DR PDB; 1X5H; NMR; -; A=623-741.
DR PDB; 1X5I; NMR; -; A=719-831.
DR PDB; 1X5J; NMR; -; A=853-952.
DR PDB; 1X5K; NMR; -; A=944-1054.
DR PDB; 3P4L; X-ray; 1.80 A; A=853-1054.
DR PDBsum; 1X5F; -.
DR PDBsum; 1X5G; -.
DR PDBsum; 1X5H; -.
DR PDBsum; 1X5I; -.
DR PDBsum; 1X5J; -.
DR PDBsum; 1X5K; -.
DR PDBsum; 3P4L; -.
DR AlphaFoldDB; Q92859; -.
DR BMRB; Q92859; -.
DR SMR; Q92859; -.
DR BioGRID; 110830; 40.
DR DIP; DIP-46272N; -.
DR IntAct; Q92859; 15.
DR MINT; Q92859; -.
DR STRING; 9606.ENSP00000341198; -.
DR GlyConnect; 1539; 10 N-Linked glycans (5 sites).
DR GlyGen; Q92859; 13 sites, 9 N-linked glycans (5 sites), 3 O-linked glycans (2 sites).
DR iPTMnet; Q92859; -.
DR PhosphoSitePlus; Q92859; -.
DR BioMuta; NEO1; -.
DR DMDM; 116242676; -.
DR EPD; Q92859; -.
DR jPOST; Q92859; -.
DR MassIVE; Q92859; -.
DR MaxQB; Q92859; -.
DR PaxDb; Q92859; -.
DR PeptideAtlas; Q92859; -.
DR PRIDE; Q92859; -.
DR ProteomicsDB; 7185; -.
DR ProteomicsDB; 75552; -. [Q92859-1]
DR ProteomicsDB; 75553; -. [Q92859-2]
DR ProteomicsDB; 75554; -. [Q92859-3]
DR Antibodypedia; 3989; 199 antibodies from 28 providers.
DR DNASU; 4756; -.
DR Ensembl; ENST00000261908.11; ENSP00000261908.6; ENSG00000067141.17. [Q92859-1]
DR Ensembl; ENST00000339362.9; ENSP00000341198.5; ENSG00000067141.17. [Q92859-1]
DR Ensembl; ENST00000558964.5; ENSP00000453200.1; ENSG00000067141.17. [Q92859-4]
DR Ensembl; ENST00000560262.5; ENSP00000453317.1; ENSG00000067141.17. [Q92859-3]
DR GeneID; 4756; -.
DR KEGG; hsa:4756; -.
DR MANE-Select; ENST00000261908.11; ENSP00000261908.6; NM_002499.4; NP_002490.2.
DR UCSC; uc002avm.4; human. [Q92859-1]
DR CTD; 4756; -.
DR DisGeNET; 4756; -.
DR GeneCards; NEO1; -.
DR HGNC; HGNC:7754; NEO1.
DR HPA; ENSG00000067141; Low tissue specificity.
DR MIM; 601907; gene.
DR neXtProt; NX_Q92859; -.
DR OpenTargets; ENSG00000067141; -.
DR PharmGKB; PA31555; -.
DR VEuPathDB; HostDB:ENSG00000067141; -.
DR eggNOG; KOG4221; Eukaryota.
DR GeneTree; ENSGT00940000156684; -.
DR InParanoid; Q92859; -.
DR OMA; WINIHPG; -.
DR OrthoDB; 217780at2759; -.
DR PhylomeDB; Q92859; -.
DR TreeFam; TF321506; -.
DR PathwayCommons; Q92859; -.
DR Reactome; R-HSA-373752; Netrin-1 signaling.
DR Reactome; R-HSA-525793; Myogenesis.
DR SignaLink; Q92859; -.
DR SIGNOR; Q92859; -.
DR BioGRID-ORCS; 4756; 16 hits in 1079 CRISPR screens.
DR ChiTaRS; NEO1; human.
DR EvolutionaryTrace; Q92859; -.
DR GeneWiki; NEO1; -.
DR GenomeRNAi; 4756; -.
DR Pharos; Q92859; Tbio.
DR PRO; PR:Q92859; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q92859; protein.
DR Bgee; ENSG00000067141; Expressed in cortical plate and 192 other tissues.
DR ExpressionAtlas; Q92859; baseline and differential.
DR Genevisible; Q92859; HS.
DR GO; GO:0044295; C:axonal growth cone; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0098797; C:plasma membrane protein complex; IDA:BHF-UCL.
DR GO; GO:0039706; F:co-receptor binding; IPI:BHF-UCL.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0055072; P:iron ion homeostasis; IGI:MGI.
DR GO; GO:0001764; P:neuron migration; IBA:GO_Central.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:InterPro.
DR CDD; cd00063; FN3; 6.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR033024; Neogenin.
DR InterPro; IPR010560; Neogenin_C.
DR PANTHER; PTHR44170:SF14; PTHR44170:SF14; 1.
DR Pfam; PF00041; fn3; 6.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF06583; Neogenin_C; 1.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1461
FT /note="Neogenin"
FT /id="PRO_0000015043"
FT TOPO_DOM 34..1105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1106..1126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1127..1461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 52..141
FT /note="Ig-like C2-type 1"
FT DOMAIN 152..238
FT /note="Ig-like C2-type 2"
FT DOMAIN 243..336
FT /note="Ig-like C2-type 3"
FT DOMAIN 341..426
FT /note="Ig-like C2-type 4"
FT DOMAIN 441..535
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 541..631
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 636..731
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 741..831
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 856..952
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 957..1054
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1041..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1379
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97798"
FT MOD_RES 1194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1198
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1404
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97798"
FT MOD_RES 1434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97798"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 909
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 74..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 173..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 270..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 362..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1054..1064
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047134"
FT VAR_SEQ 1248..1301
FT /note="PVISAHPIHSLDNPHHHFHSSSLASPARSHLYHPGSPWPIGTSMSLSDRANS
FT TE -> Q (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043330"
FT VAR_SEQ 1248..1300
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9121761,
FT ECO:0000303|PubMed:9169140"
FT /id="VSP_002593"
FT VARIANT 534
FT /note="P -> L (in dbSNP:rs4467039)"
FT /id="VAR_027954"
FT CONFLICT 168
FT /note="N -> G (in Ref. 1; AAB17263)"
FT /evidence="ECO:0000305"
FT STRAND 443..450
FT /evidence="ECO:0007829|PDB:1X5F"
FT STRAND 455..460
FT /evidence="ECO:0007829|PDB:1X5F"
FT STRAND 470..479
FT /evidence="ECO:0007829|PDB:1X5F"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:1X5F"
FT STRAND 496..500
FT /evidence="ECO:0007829|PDB:1X5F"
FT STRAND 508..516
FT /evidence="ECO:0007829|PDB:1X5F"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:1X5F"
FT STRAND 528..531
FT /evidence="ECO:0007829|PDB:1X5F"
FT STRAND 546..551
FT /evidence="ECO:0007829|PDB:1X5G"
FT STRAND 554..558
FT /evidence="ECO:0007829|PDB:1X5G"
FT STRAND 570..578
FT /evidence="ECO:0007829|PDB:1X5G"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:1X5G"
FT STRAND 591..596
FT /evidence="ECO:0007829|PDB:1X5G"
FT STRAND 604..612
FT /evidence="ECO:0007829|PDB:1X5G"
FT STRAND 638..643
FT /evidence="ECO:0007829|PDB:1X5H"
FT STRAND 646..655
FT /evidence="ECO:0007829|PDB:1X5H"
FT TURN 659..661
FT /evidence="ECO:0007829|PDB:1X5H"
FT STRAND 666..670
FT /evidence="ECO:0007829|PDB:1X5H"
FT STRAND 672..675
FT /evidence="ECO:0007829|PDB:1X5H"
FT STRAND 678..683
FT /evidence="ECO:0007829|PDB:1X5H"
FT STRAND 693..697
FT /evidence="ECO:0007829|PDB:1X5H"
FT STRAND 704..708
FT /evidence="ECO:0007829|PDB:1X5H"
FT STRAND 710..713
FT /evidence="ECO:0007829|PDB:1X5H"
FT STRAND 716..720
FT /evidence="ECO:0007829|PDB:1X5H"
FT STRAND 724..727
FT /evidence="ECO:0007829|PDB:1X5H"
FT STRAND 743..750
FT /evidence="ECO:0007829|PDB:1X5I"
FT STRAND 753..759
FT /evidence="ECO:0007829|PDB:1X5I"
FT STRAND 770..775
FT /evidence="ECO:0007829|PDB:1X5I"
FT HELIX 780..782
FT /evidence="ECO:0007829|PDB:1X5I"
FT STRAND 783..786
FT /evidence="ECO:0007829|PDB:1X5I"
FT STRAND 793..796
FT /evidence="ECO:0007829|PDB:1X5I"
FT STRAND 808..812
FT /evidence="ECO:0007829|PDB:1X5I"
FT STRAND 858..864
FT /evidence="ECO:0007829|PDB:3P4L"
FT STRAND 866..868
FT /evidence="ECO:0007829|PDB:3P4L"
FT STRAND 870..875
FT /evidence="ECO:0007829|PDB:3P4L"
FT STRAND 881..883
FT /evidence="ECO:0007829|PDB:1X5J"
FT STRAND 890..897
FT /evidence="ECO:0007829|PDB:3P4L"
FT STRAND 906..917
FT /evidence="ECO:0007829|PDB:3P4L"
FT STRAND 925..934
FT /evidence="ECO:0007829|PDB:3P4L"
FT STRAND 945..948
FT /evidence="ECO:0007829|PDB:3P4L"
FT STRAND 959..966
FT /evidence="ECO:0007829|PDB:3P4L"
FT STRAND 969..978
FT /evidence="ECO:0007829|PDB:3P4L"
FT STRAND 989..996
FT /evidence="ECO:0007829|PDB:3P4L"
FT STRAND 998..1000
FT /evidence="ECO:0007829|PDB:1X5K"
FT HELIX 1002..1004
FT /evidence="ECO:0007829|PDB:3P4L"
FT STRAND 1005..1013
FT /evidence="ECO:0007829|PDB:3P4L"
FT STRAND 1015..1019
FT /evidence="ECO:0007829|PDB:3P4L"
FT STRAND 1027..1036
FT /evidence="ECO:0007829|PDB:3P4L"
FT STRAND 1047..1050
FT /evidence="ECO:0007829|PDB:3P4L"
SQ SEQUENCE 1461 AA; 160017 MW; 4AADF1EEBCAFD82C CRC64;
MAAERGARRL LSTPSFWLYC LLLLGRRAPG AAAARSGSAP QSPGASIRTF TPFYFLVEPV
DTLSVRGSSV ILNCSAYSEP SPKIEWKKDG TFLNLVSDDR RQLLPDGSLF ISNVVHSKHN
KPDEGYYQCV ATVESLGTII SRTAKLIVAG LPRFTSQPEP SSVYAGNNAI LNCEVNADLV
PFVRWEQNRQ PLLLDDRVIK LPSGMLVISN ATEGDGGLYR CVVESGGPPK YSDEVELKVL
PDPEVISDLV FLKQPSPLVR VIGQDVVLPC VASGLPTPTI KWMKNEEALD TESSERLVLL
AGGSLEISDV TEDDAGTYFC IADNGNETIE AQAELTVQAQ PEFLKQPTNI YAHESMDIVF
ECEVTGKPTP TVKWVKNGDM VIPSDYFKIV KEHNLQVLGL VKSDEGFYQC IAENDVGNAQ
AGAQLIILEH APATTGPLPS APRDVVASLV STRFIKLTWR TPASDPHGDN LTYSVFYTKE
GIARERVENT SHPGEMQVTI QNLMPATVYI FRVMAQNKHG SGESSAPLRV ETQPEVQLPG
PAPNLRAYAA SPTSITVTWE TPVSGNGEIQ NYKLYYMEKG TDKEQDVDVS SHSYTINGLK
KYTEYSFRVV AYNKHGPGVS TPDVAVRTLS DVPSAAPQNL SLEVRNSKSI MIHWQPPAPA
TQNGQITGYK IRYRKASRKS DVTETLVSGT QLSQLIEGLD RGTEYNFRVA ALTINGTGPA
TDWLSAETFE SDLDETRVPE VPSSLHVRPL VTSIVVSWTP PENQNIVVRG YAIGYGIGSP
HAQTIKVDYK QRYYTIENLD PSSHYVITLK AFNNVGEGIP LYESAVTRPH TDTSEVDLFV
INAPYTPVPD PTPMMPPVGV QASILSHDTI RITWADNSLP KHQKITDSRY YTVRWKTNIP
ANTKYKNANA TTLSYLVTGL KPNTLYEFSV MVTKGRRSST WSMTAHGTTF ELVPTSPPKD
VTVVSKEGKP KTIIVNWQPP SEANGKITGY IIYYSTDVNA EIHDWVIEPV VGNRLTHQIQ
ELTLDTPYYF KIQARNSKGM GPMSEAVQFR TPKADSSDKM PNDQASGSGG KGSRLPDLGS
DYKPPMSGSN SPHGSPTSPL DSNMLLVIIV SVGVITIVVV VIIAVFCTRR TTSHQKKKRA
ACKSVNGSHK YKGNSKDVKP PDLWIHHERL ELKPIDKSPD PNPIMTDTPI PRNSQDITPV
DNSMDSNIHQ RRNSYRGHES EDSMSTLAGR RGMRPKMMMP FDSQPPQPVI SAHPIHSLDN
PHHHFHSSSL ASPARSHLYH PGSPWPIGTS MSLSDRANST ESVRNTPSTD TMPASSSQTC
CTDHQDPEGA TSSSYLASSQ EEDSGQSLPT AHVRPSHPLK SFAVPAIPPP GPPTYDPALP
STPLLSQQAL NHHIHSVKTA SIGTLGRSRP PMPVVVPSAP EVQETTRMLE DSESSYEPDE
LTKEMAHLEG LMKDLNAITT A
