NID2_HUMAN
ID NID2_HUMAN Reviewed; 1375 AA.
AC Q14112; A8K6I7; B4DU19; O43710;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Nidogen-2;
DE Short=NID-2;
DE AltName: Full=Osteonidogen;
DE Flags: Precursor;
GN Name=NID2;
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), PROTEIN SEQUENCE OF N-TERMINUS, AND
RP VARIANTS GLN-22; ASP-453; PRO-656 AND VAL-760.
RX PubMed=9733643; DOI=10.1006/jmbi.1998.2004;
RA Kohfeldt E., Sasaki T., Goehring W., Timpl R.;
RT "Nidogen-2: a new basement membrane protein with diverse binding
RT properties.";
RL J. Mol. Biol. 282:99-109(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLN-22; PRO-656 AND
RP VAL-760.
RC TISSUE=Cancellous bone;
RA Ohno I., Hashimoto J., Takaoka K., Ochi T., Okubo K., Matsubara K.;
RT "The cloning and characterization of a cDNA for the novel bone matrix
RT protein: osteonidogen.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS GLN-22; PRO-656
RP AND VAL-760.
RA Ohno I., Okubo K., Matsubara K.;
RT "Human osteonidogen gene: intron-exon junctions and chromosomal
RT localization.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP GLN-22; PRO-656; VAL-760 AND VAL-760.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
RP INTERACTION WITH COL13A1.
RX PubMed=11956183; DOI=10.1074/jbc.m107583200;
RA Tu H., Sasaki T., Snellman A., Gohring W., Pirila P., Timpl R.,
RA Pihlajaniemi T.;
RT "The type XIII collagen ectodomain is a 150-nm rod and capable of binding
RT to fibronectin, nidogen-2, perlecan, and heparin.";
RL J. Biol. Chem. 277:23092-23099(2002).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1124.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] SER-1238.
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).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-760, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Cell adhesion glycoprotein which is widely distributed in
CC basement membranes. Binds to collagens I and IV, to perlecan and to
CC laminin 1. Does not bind fibulins. It probably has a role in cell-
CC extracellular matrix interactions.
CC -!- SUBUNIT: Interacts with LAMA2 (By similarity). Interacts with COL13A1.
CC Interacts with EFEMP2 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O88322, ECO:0000269|PubMed:11956183}.
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=Q14112-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14112-2; Sequence=VSP_038779, VSP_038780;
CC -!- TISSUE SPECIFICITY: Heart, placenta and bone. Less in pancreas, kidney
CC and skeletal muscle.
CC -!- PTM: Highly N- and O-glycosylated. {ECO:0000269|PubMed:19159218}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13087.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA24112.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ223500; CAA11418.1; -; mRNA.
DR EMBL; D86425; BAA13087.1; ALT_FRAME; mRNA.
DR EMBL; AB009799; BAA24112.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AK300462; BAG62181.1; -; mRNA.
DR EMBL; AK291652; BAF84341.1; -; mRNA.
DR CCDS; CCDS9706.1; -. [Q14112-1]
DR PIR; G00043; G00043.
DR RefSeq; NP_031387.3; NM_007361.3. [Q14112-1]
DR AlphaFoldDB; Q14112; -.
DR SMR; Q14112; -.
DR BioGRID; 116476; 72.
DR IntAct; Q14112; 18.
DR MINT; Q14112; -.
DR STRING; 9606.ENSP00000216286; -.
DR GlyConnect; 1569; 8 N-Linked glycans (3 sites).
DR GlyGen; Q14112; 26 sites, 7 N-linked glycans (3 sites), 7 O-linked glycans (21 sites).
DR iPTMnet; Q14112; -.
DR PhosphoSitePlus; Q14112; -.
DR BioMuta; NID2; -.
DR DMDM; 290457669; -.
DR EPD; Q14112; -.
DR jPOST; Q14112; -.
DR MassIVE; Q14112; -.
DR MaxQB; Q14112; -.
DR PaxDb; Q14112; -.
DR PeptideAtlas; Q14112; -.
DR PRIDE; Q14112; -.
DR ProteomicsDB; 59817; -. [Q14112-1]
DR ProteomicsDB; 59818; -. [Q14112-2]
DR Antibodypedia; 10737; 174 antibodies from 30 providers.
DR DNASU; 22795; -.
DR Ensembl; ENST00000216286.10; ENSP00000216286.4; ENSG00000087303.19. [Q14112-1]
DR GeneID; 22795; -.
DR KEGG; hsa:22795; -.
DR MANE-Select; ENST00000216286.10; ENSP00000216286.4; NM_007361.4; NP_031387.3.
DR UCSC; uc001wzo.4; human. [Q14112-1]
DR CTD; 22795; -.
DR DisGeNET; 22795; -.
DR GeneCards; NID2; -.
DR HGNC; HGNC:13389; NID2.
DR HPA; ENSG00000087303; Tissue enhanced (placenta).
DR MIM; 605399; gene.
DR neXtProt; NX_Q14112; -.
DR OpenTargets; ENSG00000087303; -.
DR PharmGKB; PA31626; -.
DR VEuPathDB; HostDB:ENSG00000087303; -.
DR eggNOG; KOG1214; Eukaryota.
DR GeneTree; ENSGT00940000157901; -.
DR HOGENOM; CLU_003163_1_0_1; -.
DR InParanoid; Q14112; -.
DR OMA; VYPYCPA; -.
DR OrthoDB; 95286at2759; -.
DR PhylomeDB; Q14112; -.
DR TreeFam; TF320666; -.
DR PathwayCommons; Q14112; -.
DR Reactome; R-HSA-3000157; Laminin interactions.
DR SignaLink; Q14112; -.
DR BioGRID-ORCS; 22795; 9 hits in 1071 CRISPR screens.
DR ChiTaRS; NID2; human.
DR GeneWiki; NID2; -.
DR GenomeRNAi; 22795; -.
DR Pharos; Q14112; Tbio.
DR PRO; PR:Q14112; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q14112; protein.
DR Bgee; ENSG00000087303; Expressed in cartilage tissue and 153 other tissues.
DR ExpressionAtlas; Q14112; baseline and differential.
DR Genevisible; Q14112; 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:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005518; F:collagen binding; TAS:ProtInc.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:BHF-UCL.
DR GO; GO:0071711; P:basement membrane organization; TAS:BHF-UCL.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR CDD; cd00255; nidG2; 1.
DR CDD; cd00191; TY; 2.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 2.40.155.10; -; 1.
DR Gene3D; 4.10.800.10; -; 2.
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; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07474; G2F; 1.
DR Pfam; PF00058; Ldl_recept_b; 2.
DR Pfam; PF06119; NIDO; 1.
DR Pfam; PF00086; Thyroglobulin_1; 2.
DR SMART; SM00181; EGF; 5.
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; 2.
DR SUPFAM; SSF54511; SSF54511; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57610; SSF57610; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 4.
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; 2.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Calcium; Cell adhesion;
KW Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Methylation; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:9733643"
FT CHAIN 31..1375
FT /note="Nidogen-2"
FT /id="PRO_0000007671"
FT DOMAIN 108..273
FT /note="NIDO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT DOMAIN 484..524
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 528..758
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00348"
FT DOMAIN 759..800
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 801..843
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 848..891
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 892..930
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 937..1005
FT /note="Thyroglobulin type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 1016..1084
FT /note="Thyroglobulin type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REPEAT 1154..1197
FT /note="LDL-receptor class B 1"
FT REPEAT 1198..1240
FT /note="LDL-receptor class B 2"
FT REPEAT 1241..1285
FT /note="LDL-receptor class B 3"
FT REPEAT 1286..1327
FT /note="LDL-receptor class B 4"
FT REPEAT 1329..1373
FT /note="LDL-receptor class B 5"
FT REGION 348..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1014
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1308
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88322"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 1124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 763..776
FT /evidence="ECO:0000250"
FT DISULFID 770..786
FT /evidence="ECO:0000250"
FT DISULFID 788..799
FT /evidence="ECO:0000250"
FT DISULFID 805..818
FT /evidence="ECO:0000250"
FT DISULFID 812..827
FT /evidence="ECO:0000250"
FT DISULFID 829..842
FT /evidence="ECO:0000250"
FT DISULFID 852..867
FT /evidence="ECO:0000250"
FT DISULFID 859..877
FT /evidence="ECO:0000250"
FT DISULFID 879..890
FT /evidence="ECO:0000250"
FT DISULFID 896..907
FT /evidence="ECO:0000250"
FT DISULFID 901..916
FT /evidence="ECO:0000250"
FT DISULFID 918..929
FT /evidence="ECO:0000250"
FT DISULFID 940..963
FT /evidence="ECO:0000250"
FT DISULFID 974..981
FT /evidence="ECO:0000250"
FT DISULFID 983..1005
FT /evidence="ECO:0000250"
FT DISULFID 1019..1043
FT /evidence="ECO:0000250"
FT DISULFID 1054..1061
FT /evidence="ECO:0000250"
FT DISULFID 1063..1084
FT /evidence="ECO:0000250"
FT VAR_SEQ 7..59
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038779"
FT VAR_SEQ 844..892
FT /note="LITPPANPCEDGSHTCAPAGQARCVHHGGSTFSCACLPGYAGDGHQCTD ->
FT Y (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038780"
FT VARIANT 22
FT /note="P -> Q (in dbSNP:rs3920038)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9733643, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.3"
FT /id="VAR_062850"
FT VARIANT 313
FT /note="D -> G (in dbSNP:rs17124969)"
FT /id="VAR_055767"
FT VARIANT 354
FT /note="P -> H (in dbSNP:rs35657569)"
FT /id="VAR_055768"
FT VARIANT 453
FT /note="G -> D (in dbSNP:rs2101919)"
FT /evidence="ECO:0000269|PubMed:9733643"
FT /id="VAR_062851"
FT VARIANT 529
FT /note="P -> S (in dbSNP:rs17831525)"
FT /id="VAR_055769"
FT VARIANT 656
FT /note="S -> P (in dbSNP:rs3742536)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9733643, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.3"
FT /id="VAR_062852"
FT VARIANT 726
FT /note="V -> M (in dbSNP:rs35147930)"
FT /id="VAR_055770"
FT VARIANT 760
FT /note="G -> V (in dbSNP:rs2273430)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9733643, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.3, ECO:0007744|PubMed:24275569"
FT /id="VAR_062853"
FT VARIANT 775
FT /note="R -> Q (in dbSNP:rs10134590)"
FT /id="VAR_055771"
FT VARIANT 830
FT /note="R -> Q (in dbSNP:rs7144523)"
FT /id="VAR_055772"
FT VARIANT 866
FT /note="R -> Q (in dbSNP:rs28507587)"
FT /id="VAR_055773"
FT VARIANT 1238
FT /note="P -> S (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1305582875)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035836"
FT CONFLICT 44
FT /note="G -> W (in Ref. 2; BAA13087 and 3; BAA24112)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="I -> T (in Ref. 4; BAG62181)"
FT /evidence="ECO:0000305"
FT CONFLICT 1242
FT /note="N -> D (in Ref. 4; BAF84341)"
FT /evidence="ECO:0000305"
FT CONFLICT 1245
FT /note="W -> R (in Ref. 4; BAF84341)"
FT /evidence="ECO:0000305"
FT CONFLICT 1249
FT /note="N -> D (in Ref. 4; BAF84341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1375 AA; 151254 MW; 198D1F4E286A53E2 CRC64;
MEGDRVAGRP VLSSLPVLLL LPLLMLRAAA LHPDELFPHG ESWGDQLLQE GDDESSAVVK
LANPLHFYEA RFSNLYVGTN GIISTQDFPR ETQYVDYDFP TDFPAIAPFL ADIDTSHGRG
RVLYREDTSP AVLGLAARYV RAGFPRSARF TPTHAFLATW EQVGAYEEVK RGALPSGELN
TFQAVLASDG SDSYALFLYP ANGLQFLGTR PKESYNVQLQ LPARVGFCRG EADDLKSEGP
YFSLTSTEQS VKNLYQLSNL GIPGVWAFHI GSTSPLDNVR PAAVGDLSAA HSSVPLGRSF
SHATALESDY NEDNLDYYDV NEEEAEYLPG EPEEALNGHS SIDVSFQSKV DTKPLEESST
LDPHTKEGTS LGEVGGPDLK GQVEPWDERE TRSPAPPEVD RDSLAPSWET PPPYPENGSI
QPYPDGGPVP SEMDVPPAHP EEEIVLRSYP ASGHTTPLSR GTYEVGLEDN IGSNTEVFTY
NAANKETCEH NHRQCSRHAF CTDYATGFCC HCQSKFYGNG KHCLPEGAPH RVNGKVSGHL
HVGHTPVHFT DVDLHAYIVG NDGRAYTAIS HIPQPAAQAL LPLTPIGGLF GWLFALEKPG
SENGFSLAGA AFTHDMEVTF YPGEETVRIT QTAEGLDPEN YLSIKTNIQG QVPYVSANFT
AHISPYKELY HYSDSTVTST SSRDYSLTFG AINQTWSYRI HQNITYQVCR HAPRHPSFPT
TQQLNVDRVF ALYNDEERVL RFAVTNQIGP VKEDSDPTPG NPCYDGSHMC DTTARCHPGT
GVDYTCECAS GYQGDGRNCV DENECATGFH RCGPNSVCIN LPGSYRCECR SGYEFADDRH
TCILITPPAN PCEDGSHTCA PAGQARCVHH GGSTFSCACL PGYAGDGHQC TDVDECSENR
CHPAATCYNT PGSFSCRCQP GYYGDGFQCI PDSTSSLTPC EQQQRHAQAQ YAYPGARFHI
PQCDEQGNFL PLQCHGSTGF CWCVDPDGHE VPGTQTPPGS TPPHCGPSPE PTQRPPTICE
RWRENLLEHY GGTPRDDQYV PQCDDLGHFI PLQCHGKSDF CWCVDKDGRE VQGTRSQPGT
TPACIPTVAP PMVRPTPRPD VTPPSVGTFL LYTQGQQIGY LPLNGTRLQK DAAKTLLSLH
GSIIVGIDYD CRERMVYWTD VAGRTISRAG LELGAEPETI VNSGLISPEG LAIDHIRRTM
YWTDSVLDKI ESALLDGSER KVLFYTDLVN PRAIAVDPIR GNLYWTDWNR EAPKIETSSL
DGENRRILIN TDIGLPNGLT FDPFSKLLCW ADAGTKKLEC TLPDGTGRRV IQNNLKYPFS
IVSYADHFYH TDWRRDGVVS VNKHSGQFTD EYLPEQRSHL YGITAVYPYC PTGRK
