NID1_HUMAN
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 03-AUG-2022, entry version 227.
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 and LGALS3BP (By similarity). Interacts
CC with PLXDC1. {ECO:0000250, 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; 26.
DR ComplexPortal; CPX-1265; Laminin111-nidogen complex.
DR ComplexPortal; CPX-1282; Laminin211-nidogen complex.
DR ComplexPortal; CPX-1285; Laminin221-nidogen complex.
DR IntAct; P14543; 18.
DR MINT; P14543; -.
DR STRING; 9606.ENSP00000264187; -.
DR DrugBank; DB00013; Urokinase.
DR GlyGen; P14543; 10 sites, 4 O-linked glycans (9 sites).
DR iPTMnet; P14543; -.
DR PhosphoSitePlus; P14543; -.
DR BioMuta; NID1; -.
DR DMDM; 251757450; -.
DR EPD; P14543; -.
DR jPOST; P14543; -.
DR MassIVE; P14543; -.
DR MaxQB; P14543; -.
DR PaxDb; P14543; -.
DR PeptideAtlas; P14543; -.
DR PRIDE; P14543; -.
DR ProteomicsDB; 53056; -. [P14543-1]
DR ProteomicsDB; 53057; -. [P14543-2]
DR Antibodypedia; 4102; 425 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 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; HVSRLQF; -.
DR OrthoDB; 95286at2759; -.
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 1074 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 180 other tissues.
DR Genevisible; P14543; HS.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; IC: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:0071711; P:basement membrane organization; TAS:BHF-UCL.
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; IC: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; IC:ComplexPortal.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IC:ComplexPortal.
DR GO; GO:0110011; P:regulation of basement membrane organization; IC:ComplexPortal.
DR CDD; cd00255; nidG2; 1.
DR CDD; cd00191; TY; 1.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 2.40.155.10; -; 1.
DR Gene3D; 4.10.800.10; -; 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 Pfam; PF12662; cEGF; 1.
DR Pfam; PF12947; EGF_3; 2.
DR Pfam; PF07645; EGF_CA; 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; SSF54511; 1.
DR SUPFAM; SSF57184; SSF57184; 2.
DR SUPFAM; SSF57610; SSF57610; 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.
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
