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   27-MAR-2024, entry version 215.
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   TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-452.
RX   PubMed=32337544; DOI=10.1093/glycob/cwaa039;
RA   Toledo A.G., Pihl J., Spliid C.B., Persson A., Nilsson J., Pereira M.A.,
RA   Gustavsson T., Choudhary S., Oo H.Z., Black P.C., Daugaard M., Esko J.D.,
RA   Larson G., Salanti A., Clausen T.M.;
RT   "An affinity chromatography and glycoproteomics workflow to profile the
RT   chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in
RT   the placenta and in cancer.";
RL   Glycobiology 30:989-1002(2020).
RN   [10]
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   [11]
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: Detected in placenta (at protein level)
CC       (PubMed:32337544). Heart and bone. Less in pancreas, kidney and
CC       skeletal muscle. {ECO:0000269|PubMed:32337544}.
CC   -!- PTM: Highly N-glycosylated. {ECO:0000269|PubMed:19159218}.
CC   -!- PTM: Highly O-glycosylated (PubMed:19159218). Contains chondroitin
CC       sulfate which is attached at Ser-452 and at either Ser-358 or Ser-359
CC       (PubMed:32337544). {ECO:0000269|PubMed:19159218,
CC       ECO:0000269|PubMed:32337544}.
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; 74.
DR   IntAct; Q14112; 19.
DR   MINT; Q14112; -.
DR   STRING; 9606.ENSP00000216286; -.
DR   GlyConnect; 1569; 8 N-Linked glycans (3 sites).
DR   GlyCosmos; Q14112; 26 sites, 14 glycans.
DR   GlyGen; Q14112; 34 sites, 7 N-linked glycans (3 sites), 10 O-linked glycans (29 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; 9606-ENSP00000216286; -.
DR   PeptideAtlas; Q14112; -.
DR   ProteomicsDB; 59817; -. [Q14112-1]
DR   ProteomicsDB; 59818; -. [Q14112-2]
DR   Antibodypedia; 10737; 198 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   AGR; HGNC:13389; -.
DR   CTD; 22795; -.
DR   DisGeNET; 22795; -.
DR   GeneCards; NID2; -.
DR   HGNC; HGNC:13389; NID2.
DR   HPA; ENSG00000087303; Tissue enhanced (ovary, 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; TCEHNHG; -.
DR   OrthoDB; 25347at2759; -.
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 1151 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 155 other cell types or tissues.
DR   ExpressionAtlas; Q14112; baseline and differential.
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; cd00054; EGF_CA; 2.
DR   CDD; cd00255; nidG2; 1.
DR   CDD; cd00191; TY; 2.
DR   Gene3D; 2.40.155.10; Green fluorescent protein; 1.
DR   Gene3D; 2.10.25.10; Laminin; 4.
DR   Gene3D; 4.10.800.10; Thyroglobulin type-1; 2.
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:SF15; NIDOGEN-2 ISOFORM X1; 1.
DR   PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
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; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF54511; GFP-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57610; Thyroglobulin type-1 domain; 2.
DR   SUPFAM; SSF63825; YWTD domain; 1.
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.
DR   Genevisible; Q14112; HS.
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; Proteoglycan;
KW   Reference proteome; 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        358
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        359
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        417
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        452
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000269|PubMed:32337544"
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
//