ID   NID1_HUMAN              Reviewed;        1247 AA.
AC   P14543; Q14942; Q59FL2; Q5TAF2; Q5TAF3; Q86XD7;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   27-MAR-2024, entry version 236.
DE   RecName: Full=Nidogen-1;
DE            Short=NID-1;
DE   AltName: Full=Entactin;
DE   Flags: Precursor;
GN   Name=NID1; Synonyms=NID;
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] (ISOFORM 1), AND VARIANTS ILE-246 AND ARG-1246.
RX   PubMed=2574658; DOI=10.1089/dna.1989.8.581;
RA   Nagayoshi T., Sanborn D., Hickok N.J., Olsen D.R., Fazio M.J., Chu M.-L.,
RA   Knowlton R., Mann K., Deutzmann R., Timpl R., Uitto J.;
RT   "Human nidogen: complete amino acid sequence and structural domains deduced
RT   from cDNAs, and evidence for polymorphism of the gene.";
RL   DNA 8:581-594(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-246 AND ARG-1246.
RX   PubMed=7557988; DOI=10.1006/geno.1995.1038;
RA   Zimmermann K., Hoischen S., Hafner M., Nischt R.;
RT   "Genomic sequences and structural organization of the human nidogen gene
RT   (NID).";
RL   Genomics 27:245-250(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ARG-60 AND
RP   ILE-246.
RC   TISSUE=Testis;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX   PubMed=1906509; DOI=10.1111/1523-1747.ep12480380;
RA   Fazio M.J., O'Leary J., Kahari V.M., Chen Y.Q., Saitta B., Uitto J.;
RT   "Human nidogen gene: structural and functional characterization of the 5'-
RT   flanking region.";
RL   J. Invest. Dermatol. 97:281-285(1991).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1247 (ISOFORM 2), AND VARIANTS
RP   ILE-246 AND HIS-807.
RC   TISSUE=Brain;
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 667-1247 (ISOFORM 1), AND VARIANT ARG-1246.
RC   TISSUE=Placenta;
RX   PubMed=2471408;
RA   Olsen D.R., Nagayoshi T., Fazio M., Mattei M.-G., Passage E., Weil D.,
RA   Timpl R., Chu M.-L., Uitto J.;
RT   "Human nidogen: cDNA cloning, cellular expression, and mapping of the gene
RT   to chromosome 1q43.";
RL   Am. J. Hum. Genet. 44:876-885(1989).
RN   [8]
RP   INTERACTION WITH PLXDC1.
RX   PubMed=16574105; DOI=10.1016/j.febslet.2006.03.033;
RA   Lee H.K., Seo I.A., Park H.K., Park H.T.;
RT   "Identification of the basement membrane protein nidogen as a candidate
RT   ligand for tumor endothelial marker 7 in vitro and in vivo.";
RL   FEBS Lett. 580:2253-2257(2006).
RN   [9]
RP   IDENTIFICATION BY 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   [10]
RP   VARIANT [LARGE SCALE ANALYSIS] SER-1036.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Sulfated glycoprotein widely distributed in basement
CC       membranes and tightly associated with laminin. Also binds to collagen
CC       IV and perlecan. It probably has a role in cell-extracellular matrix
CC       interactions.
CC   -!- SUBUNIT: Interacts with FBLN1 (By similarity). Interacts with LGALS3BP
CC       (By similarity). Interacts with PLXDC1 (PubMed:16574105). Interacts
CC       with SVEP1 (By similarity). {ECO:0000250|UniProtKB:P10493,
CC       ECO:0000269|PubMed:16574105}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P14543-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P14543-2; Sequence=VSP_017254;
CC   -!- PTM: N- and O-glycosylated.
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DR   EMBL; M30269; AAA59932.1; -; mRNA.
DR   EMBL; X82245; CAA57709.1; -; Genomic_DNA.
DR   EMBL; X84819; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84820; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84821; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84822; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84823; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84824; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84825; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84826; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84827; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84828; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84829; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84830; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84831; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84832; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84833; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84834; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84835; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84836; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; X84837; CAA57709.1; JOINED; Genomic_DNA.
DR   EMBL; AL122018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL139161; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC045606; AAH45606.1; -; mRNA.
DR   EMBL; AB209448; BAD92685.1; -; mRNA.
DR   EMBL; M27445; AAA57261.1; -; mRNA.
DR   CCDS; CCDS1608.1; -. [P14543-1]
DR   PIR; A33322; MMHUND.
DR   RefSeq; NP_002499.2; NM_002508.2. [P14543-1]
DR   AlphaFoldDB; P14543; -.
DR   SMR; P14543; -.
DR   BioGRID; 110876; 29.
DR   ComplexPortal; CPX-1265; Laminin111-nidogen complex.
DR   ComplexPortal; CPX-1282; Laminin211-nidogen complex.
DR   ComplexPortal; CPX-1285; Laminin221-nidogen complex.
DR   IntAct; P14543; 19.
DR   MINT; P14543; -.
DR   STRING; 9606.ENSP00000264187; -.
DR   DrugBank; DB00013; Urokinase.
DR   GlyCosmos; P14543; 9 sites, 4 glycans.
DR   GlyGen; P14543; 16 sites, 7 O-linked glycans (15 sites).
DR   iPTMnet; P14543; -.
DR   PhosphoSitePlus; P14543; -.
DR   SwissPalm; P14543; -.
DR   BioMuta; NID1; -.
DR   DMDM; 251757450; -.
DR   EPD; P14543; -.
DR   jPOST; P14543; -.
DR   MassIVE; P14543; -.
DR   MaxQB; P14543; -.
DR   PaxDb; 9606-ENSP00000264187; -.
DR   PeptideAtlas; P14543; -.
DR   ProteomicsDB; 53056; -. [P14543-1]
DR   ProteomicsDB; 53057; -. [P14543-2]
DR   Pumba; P14543; -.
DR   Antibodypedia; 4102; 479 antibodies from 34 providers.
DR   DNASU; 4811; -.
DR   Ensembl; ENST00000264187.7; ENSP00000264187.6; ENSG00000116962.15. [P14543-1]
DR   Ensembl; ENST00000366595.7; ENSP00000355554.3; ENSG00000116962.15. [P14543-2]
DR   GeneID; 4811; -.
DR   KEGG; hsa:4811; -.
DR   MANE-Select; ENST00000264187.7; ENSP00000264187.6; NM_002508.3; NP_002499.2.
DR   UCSC; uc001hxo.4; human. [P14543-1]
DR   AGR; HGNC:7821; -.
DR   CTD; 4811; -.
DR   DisGeNET; 4811; -.
DR   GeneCards; NID1; -.
DR   HGNC; HGNC:7821; NID1.
DR   HPA; ENSG00000116962; Tissue enhanced (placenta).
DR   MalaCards; NID1; -.
DR   MIM; 131390; gene.
DR   neXtProt; NX_P14543; -.
DR   OpenTargets; ENSG00000116962; -.
DR   Orphanet; 269215; Isolated Dandy-Walker malformation without hydrocephalus.
DR   PharmGKB; PA31625; -.
DR   VEuPathDB; HostDB:ENSG00000116962; -.
DR   eggNOG; KOG1214; Eukaryota.
DR   GeneTree; ENSGT00940000156318; -.
DR   HOGENOM; CLU_003163_1_0_1; -.
DR   InParanoid; P14543; -.
DR   OMA; PGTGNQF; -.
DR   OrthoDB; 25347at2759; -.
DR   PhylomeDB; P14543; -.
DR   TreeFam; TF320666; -.
DR   PathwayCommons; P14543; -.
DR   Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-HSA-3000157; Laminin interactions.
DR   SignaLink; P14543; -.
DR   SIGNOR; P14543; -.
DR   BioGRID-ORCS; 4811; 12 hits in 1161 CRISPR screens.
DR   ChiTaRS; NID1; human.
DR   GeneWiki; Entactin; -.
DR   GenomeRNAi; 4811; -.
DR   Pharos; P14543; Tbio.
DR   PRO; PR:P14543; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P14543; Protein.
DR   Bgee; ENSG00000116962; Expressed in stromal cell of endometrium and 182 other cell types or tissues.
DR   GO; GO:0005604; C:basement membrane; IDA:BHF-UCL.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; NAS:ComplexPortal.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005518; F:collagen binding; IDA:BHF-UCL.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; ISS:BHF-UCL.
DR   GO; GO:0043236; F:laminin binding; IDA:BHF-UCL.
DR   GO; GO:0043237; F:laminin-1 binding; IEA:Ensembl.
DR   GO; GO:0043394; F:proteoglycan binding; IPI:BHF-UCL.
DR   GO; GO:0042813; F:Wnt receptor activity; IBA:GO_Central.
DR   GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR   GO; GO:0071711; P:basement membrane organization; TAS:BHF-UCL.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0032836; P:glomerular basement membrane development; IEA:Ensembl.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; NAS:ComplexPortal.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR   GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; NAS:ComplexPortal.
DR   GO; GO:0051149; P:positive regulation of muscle cell differentiation; NAS:ComplexPortal.
DR   GO; GO:0110011; P:regulation of basement membrane organization; NAS:ComplexPortal.
DR   CDD; cd00054; EGF_CA; 4.
DR   CDD; cd00255; nidG2; 1.
DR   CDD; cd00191; TY; 1.
DR   Gene3D; 2.40.155.10; Green fluorescent protein; 1.
DR   Gene3D; 2.10.25.10; Laminin; 5.
DR   Gene3D; 4.10.800.10; Thyroglobulin type-1; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR006605; G2_nidogen/fibulin_G2F.
DR   InterPro; IPR009017; GFP.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR003886; NIDO_dom.
DR   InterPro; IPR000716; Thyroglobulin_1.
DR   InterPro; IPR036857; Thyroglobulin_1_sf.
DR   PANTHER; PTHR46513:SF6; NIDOGEN-1; 1.
DR   PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF12947; EGF_3; 2.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF14670; FXa_inhibition; 1.
DR   Pfam; PF07474; G2F; 1.
DR   Pfam; PF00058; Ldl_recept_b; 3.
DR   Pfam; PF06119; NIDO; 1.
DR   Pfam; PF00086; Thyroglobulin_1; 1.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 4.
DR   SMART; SM00682; G2F; 1.
DR   SMART; SM00135; LY; 5.
DR   SMART; SM00539; NIDO; 1.
DR   SMART; SM00211; TY; 1.
DR   SUPFAM; SSF54511; GFP-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 5.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS51120; LDLRB; 4.
DR   PROSITE; PS51220; NIDO; 1.
DR   PROSITE; PS50993; NIDOGEN_G2; 1.
DR   PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR   PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
DR   Genevisible; P14543; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Basement membrane; Calcium; Cell adhesion;
KW   Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW   Reference proteome; Repeat; Secreted; Signal; Sulfation.
FT   SIGNAL          1..28
FT   CHAIN           29..1247
FT                   /note="Nidogen-1"
FT                   /id="PRO_0000007669"
FT   DOMAIN          106..268
FT                   /note="NIDO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT   DOMAIN          386..426
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          430..667
FT                   /note="Nidogen G2 beta-barrel"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00348"
FT   DOMAIN          668..709
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          710..751
FT                   /note="EGF-like 3; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          758..801
FT                   /note="EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          802..840
FT                   /note="EGF-like 5; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          846..919
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT   REPEAT          990..1032
FT                   /note="LDL-receptor class B 1"
FT   REPEAT          1033..1075
FT                   /note="LDL-receptor class B 2"
FT   REPEAT          1076..1120
FT                   /note="LDL-receptor class B 3"
FT   REPEAT          1121..1162
FT                   /note="LDL-receptor class B 4"
FT   DOMAIN          1208..1244
FT                   /note="EGF-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   MOTIF           702..704
FT                   /note="Cell attachment site"
FT   MOD_RES         289
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         296
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        922
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        935
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        390..403
FT                   /evidence="ECO:0000250"
FT   DISULFID        397..412
FT                   /evidence="ECO:0000250"
FT   DISULFID        411..618
FT                   /evidence="ECO:0000250"
FT   DISULFID        414..425
FT                   /evidence="ECO:0000250"
FT   DISULFID        672..685
FT                   /evidence="ECO:0000250"
FT   DISULFID        679..695
FT                   /evidence="ECO:0000250"
FT   DISULFID        697..708
FT                   /evidence="ECO:0000250"
FT   DISULFID        714..727
FT                   /evidence="ECO:0000250"
FT   DISULFID        721..736
FT                   /evidence="ECO:0000250"
FT   DISULFID        738..750
FT                   /evidence="ECO:0000250"
FT   DISULFID        762..777
FT                   /evidence="ECO:0000250"
FT   DISULFID        769..787
FT                   /evidence="ECO:0000250"
FT   DISULFID        789..800
FT                   /evidence="ECO:0000250"
FT   DISULFID        806..817
FT                   /evidence="ECO:0000250"
FT   DISULFID        811..826
FT                   /evidence="ECO:0000250"
FT   DISULFID        828..839
FT                   /evidence="ECO:0000250"
FT   DISULFID        849..878
FT                   /evidence="ECO:0000250"
FT   DISULFID        889..896
FT                   /evidence="ECO:0000250"
FT   DISULFID        898..919
FT                   /evidence="ECO:0000250"
FT   DISULFID        1212..1223
FT                   /evidence="ECO:0000250"
FT   DISULFID        1219..1232
FT                   /evidence="ECO:0000250"
FT   DISULFID        1234..1243
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         710..842
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.6"
FT                   /id="VSP_017254"
FT   VARIANT         31
FT                   /note="R -> L (in dbSNP:rs2071529)"
FT                   /id="VAR_055760"
FT   VARIANT         60
FT                   /note="S -> R (in dbSNP:rs17857302)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_058123"
FT   VARIANT         246
FT                   /note="V -> I (in dbSNP:rs10733133)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:2574658, ECO:0000269|PubMed:7557988,
FT                   ECO:0000269|Ref.6"
FT                   /id="VAR_024264"
FT   VARIANT         302
FT                   /note="R -> H (in dbSNP:rs16833183)"
FT                   /id="VAR_055761"
FT   VARIANT         335
FT                   /note="R -> H (in dbSNP:rs34406281)"
FT                   /id="VAR_055762"
FT   VARIANT         387
FT                   /note="R -> H (in dbSNP:rs16833154)"
FT                   /id="VAR_055763"
FT   VARIANT         669
FT                   /note="Q -> R (in dbSNP:rs3738534)"
FT                   /id="VAR_021904"
FT   VARIANT         807
FT                   /note="Q -> H (in dbSNP:rs3738531)"
FT                   /evidence="ECO:0000269|Ref.6"
FT                   /id="VAR_058124"
FT   VARIANT         970
FT                   /note="K -> E (in dbSNP:rs16833060)"
FT                   /id="VAR_055764"
FT   VARIANT         1036
FT                   /note="F -> S (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035835"
FT   VARIANT         1163
FT                   /note="L -> V (in dbSNP:rs16833032)"
FT                   /id="VAR_055765"
FT   VARIANT         1226
FT                   /note="T -> I (in dbSNP:rs6662744)"
FT                   /id="VAR_055766"
FT   VARIANT         1246
FT                   /note="Q -> R (in dbSNP:rs3213190)"
FT                   /evidence="ECO:0000269|PubMed:2471408,
FT                   ECO:0000269|PubMed:2574658, ECO:0000269|PubMed:7557988"
FT                   /id="VAR_058125"
FT   CONFLICT        33..34
FT                   /note="EL -> SS (in Ref. 2; CAA57709)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        37..42
FT                   /note="FGPGQG -> SAPDR (in Ref. 2; CAA57709)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        653
FT                   /note="L -> F (in Ref. 1; AAA59932 and 2; CAA57709)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1115
FT                   /note="T -> H (in Ref. 1; AAA59932 and 2; CAA57709)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1247 AA;  136377 MW;  FCC839416525CD48 CRC64;
     MLASSSRIRA AWTRALLLPL LLAGPVGCLS RQELFPFGPG QGDLELEDGD DFVSPALELS
     GALRFYDRSD IDAVYVTTNG IIATSEPPAK ESHPGLFPPT FGAVAPFLAD LDTTDGLGKV
     YYREDLSPSI TQRAAECVHR GFPEISFQPS SAVVVTWESV APYQGPSRDP DQKGKRNTFQ
     AVLASSDSSS YAIFLYPEDG LQFHTTFSKK ENNQVPAVVA FSQGSVGFLW KSNGAYNIFA
     NDRESVENLA KSSNSGQQGV WVFEIGSPAT TNGVVPADVI LGTEDGAEYD DEDEDYDLAT
     TRLGLEDVGT TPFSYKALRR GGADTYSVPS VLSPRRAATE RPLGPPTERT RSFQLAVETF
     HQQHPQVIDV DEVEETGVVF SYNTDSRQTC ANNRHQCSVH AECRDYATGF CCSCVAGYTG
     NGRQCVAEGS PQRVNGKVKG RIFVGSSQVP IVFENTDLHS YVVMNHGRSY TAISTIPETV
     GYSLLPLAPV GGIIGWMFAV EQDGFKNGFS ITGGEFTRQA EVTFVGHPGN LVIKQRFSGI
     DEHGHLTIDT ELEGRVPQIP FGSSVHIEPY TELYHYSTSV ITSSSTREYT VTEPERDGAS
     PSRIYTYQWR QTITFQECVH DDSRPALPST QQLSVDSVFV LYNQEEKILR YALSNSIGPV
     REGSPDALQN PCYIGTHGCD TNAACRPGPR TQFTCECSIG FRGDGRTCYD IDECSEQPSV
     CGSHTICNNH PGTFRCECVE GYQFSDEGTC VAVVDQRPIN YCETGLHNCD IPQRAQCIYT
     GGSSYTCSCL PGFSGDGQAC QDVDECQPSR CHPDAFCYNT PGSFTCQCKP GYQGDGFRCV
     PGEVEKTRCQ HEREHILGAA GATDPQRPIP PGLFVPECDA HGHYAPTQCH GSTGYCWCVD
     RDGREVEGTR TRPGMTPPCL STVAPPIHQG PAVPTAVIPL PPGTHLLFAQ TGKIERLPLE
     GNTMRKTEAK AFLHVPAKVI IGLAFDCVDK MVYWTDITEP SIGRASLHGG EPTTIIRQDL
     GSPEGIAVDH LGRNIFWTDS NLDRIEVAKL DGTQRRVLFE TDLVNPRGIV TDSVRGNLYW
     TDWNRDNPKI ETSYMDGTNR RILVQDDLGL PNGLTFDAFS SQLCWVDAGT NRAECLNPSQ
     PSRRKALEGL QYPFAVTSYG KNLYFTDWKM NSVVALDLAI SKETDAFQPH KQTRLYGITT
     ALSQCPQGHN YCSVNNGGCT HLCLATPGSR TCRCPDNTLG VDCIEQK
//