ID   SDC1_HUMAN              Reviewed;         310 AA.
AC   P18827; D6W523; Q53QV0; Q546D3; Q96HB7;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 3.
DT   27-MAR-2024, entry version 212.
DE   RecName: Full=Syndecan-1 {ECO:0000312|HGNC:HGNC:10658};
DE            Short=SYND1 {ECO:0000312|HGNC:HGNC:10658};
DE   AltName: CD_antigen=CD138;
DE   Flags: Precursor;
GN   Name=SDC1 {ECO:0000312|HGNC:HGNC:10658}; Synonyms=SDC;
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], AND VARIANT GLN-136.
RC   TISSUE=Fibroblast;
RX   PubMed=1339431; DOI=10.1016/s0021-9258(18)48404-9;
RA   Lories V., Cassiman J.-J., van de Berghe H., David G.;
RT   "Differential expression of cell surface heparan sulfate proteoglycans in
RT   human mammary epithelial cells and lung fibroblasts.";
RL   J. Biol. Chem. 267:1116-1122(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-136.
RC   TISSUE=Mammary gland;
RX   PubMed=2324102; DOI=10.1016/s0021-9258(19)39232-4;
RA   Mali M., Jaakkola P., Arvilommi A.-M., Jalkanen M.;
RT   "Sequence of human syndecan indicates a novel gene family of integral
RT   membrane proteoglycans.";
RL   J. Biol. Chem. 265:6884-6889(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-136.
RX   PubMed=15177497; DOI=10.1016/j.ejca.2004.01.038;
RA   Mennerich D., Vogel A., Klaman I., Dahl E., Lichtner R.B., Rosenthal A.,
RA   Pohlenz H.D., Thierauch K.H., Sommer A.;
RT   "Shift of syndecan-1 expression from epithelial to stromal cells during
RT   progression of solid tumours.";
RL   Eur. J. Cancer 40:1373-1382(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-136.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-136.
RC   TISSUE=Kidney;
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   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-310, AND VARIANT GLN-136.
RC   TISSUE=Placenta;
RX   PubMed=9050911; DOI=10.1007/s004390050360;
RA   Kaukonen J., Alanen-Kurki L., Jalkanen M., Palotie A.;
RT   "The mapping and visual ordering of the human syndecan-1 and N-myc genes
RT   near the telomeric region of chromosome 2p.";
RL   Hum. Genet. 99:295-297(1997).
RN   [8]
RP   SHEDDING, AND SUBCELLULAR LOCATION.
RX   PubMed=9169435; DOI=10.1074/jbc.272.23.14713;
RA   Subramanian S.V., Fitzgerald M.L., Bernfield M.;
RT   "Regulated shedding of syndecan-1 and -4 ectodomains by thrombin and growth
RT   factor receptor activation.";
RL   J. Biol. Chem. 272:14713-14720(1997).
RN   [9]
RP   INTERACTION WITH CDCP1.
RX   PubMed=16007225; DOI=10.1038/sj.onc.1208582;
RA   Bhatt A.S., Erdjument-Bromage H., Tempst P., Craik C.S., Moasser M.M.;
RT   "Adhesion signaling by a novel mitotic substrate of src kinases.";
RL   Oncogene 24:5333-5343(2005).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=22660413; DOI=10.1038/ncb2502;
RA   Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G., Geeraerts A.,
RA   Ivarsson Y., Depoortere F., Coomans C., Vermeiren E., Zimmermann P.,
RA   David G.;
RT   "Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.";
RL   Nat. Cell Biol. 14:677-685(2012).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION BY
RP   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   [13]
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   [14]
RP   TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-206.
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   [15]
RP   TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-206.
RX   PubMed=36213313; DOI=10.1007/s42485-022-00092-3;
RA   Ramarajan M.G., Saraswat M., Budhraja R., Garapati K., Raymond K.,
RA   Pandey A.;
RT   "Mass spectrometric analysis of chondroitin sulfate-linked peptides.";
RL   J. Proteins Proteom. 13:187-203(2022).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 303-310 IN COMPLEX WITH TIAM1,
RP   AND INTERACTION WITH TIAM1.
RX   PubMed=23395182; DOI=10.1016/j.str.2013.01.004;
RA   Liu X., Shepherd T.R., Murray A.M., Xu Z., Fuentes E.J.;
RT   "The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a
RT   ligand conformation that modulates protein dynamics.";
RL   Structure 21:342-354(2013).
CC   -!- FUNCTION: Cell surface proteoglycan that contains both heparan sulfate
CC       and chondroitin sulfate and that links the cytoskeleton to the
CC       interstitial matrix (By similarity). Regulates exosome biogenesis in
CC       concert with SDCBP and PDCD6IP (PubMed:22660413). Able to induce its
CC       own expression in dental mesenchymal cells and also in the neighboring
CC       dental epithelial cells via an MSX1-mediated pathway (By similarity).
CC       {ECO:0000250|UniProtKB:P18828, ECO:0000269|PubMed:22660413}.
CC   -!- SUBUNIT: Interacts with CDCP1. Interacts (via C-terminus) with TIAM1
CC       (via PDZ domain). Interacts with MDK (By similarity).
CC       {ECO:0000250|UniProtKB:P26260, ECO:0000269|PubMed:16007225,
CC       ECO:0000269|PubMed:23395182}.
CC   -!- INTERACTION:
CC       P18827; P05067: APP; NbExp=3; IntAct=EBI-2855248, EBI-77613;
CC       P18827; P18827: SDC1; NbExp=2; IntAct=EBI-2855248, EBI-2855248;
CC       P18827; P34741: SDC2; NbExp=2; IntAct=EBI-2855248, EBI-1172957;
CC       P18827; Q13009: TIAM1; NbExp=5; IntAct=EBI-2855248, EBI-1050007;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:9169435}.
CC       Secreted, extracellular exosome {ECO:0000269|PubMed:22660413}.
CC       Note=Shedding of the ectodomain produces a soluble form.
CC       {ECO:0000269|PubMed:9169435}.
CC   -!- TISSUE SPECIFICITY: Detected in placenta (at protein level)
CC       (PubMed:32337544). Detected in fibroblasts (at protein level)
CC       (PubMed:36213313). {ECO:0000269|PubMed:32337544,
CC       ECO:0000269|PubMed:36213313}.
CC   -!- PTM: Shedding is enhanced by a number of factors such as heparanase,
CC       thrombin or EGF. Also by stress and wound healing. PMA-mediated
CC       shedding is inhibited by TIMP3. {ECO:0000269|PubMed:9169435}.
CC   -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/42223/SDC1";
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DR   EMBL; X60306; CAA42851.1; -; mRNA.
DR   EMBL; J05392; AAA60605.1; -; mRNA.
DR   EMBL; AJ551176; CAD80245.1; -; mRNA.
DR   EMBL; AC104792; AAX93151.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAX00828.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAX00829.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAX00830.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAX00831.1; -; Genomic_DNA.
DR   EMBL; BC008765; AAH08765.1; -; mRNA.
DR   EMBL; Z48199; CAA88235.1; -; Genomic_DNA.
DR   CCDS; CCDS1697.1; -.
DR   PIR; A41776; A41776.
DR   RefSeq; NP_001006947.1; NM_001006946.1.
DR   RefSeq; NP_002988.3; NM_002997.4.
DR   PDB; 4GVC; X-ray; 1.54 A; B=303-310.
DR   PDB; 4GVD; X-ray; 1.85 A; C/D=303-310.
DR   PDB; 6EJE; X-ray; 2.43 A; B=201-212.
DR   PDBsum; 4GVC; -.
DR   PDBsum; 4GVD; -.
DR   PDBsum; 6EJE; -.
DR   AlphaFoldDB; P18827; -.
DR   SASBDB; P18827; -.
DR   SMR; P18827; -.
DR   BioGRID; 112284; 99.
DR   ComplexPortal; CPX-3282; Syndecan-1-syntenin-1-ALIX complex.
DR   CORUM; P18827; -.
DR   DIP; DIP-1123N; -.
DR   ELM; P18827; -.
DR   IntAct; P18827; 50.
DR   MINT; P18827; -.
DR   STRING; 9606.ENSP00000370542; -.
DR   ChEMBL; CHEMBL3712898; -.
DR   TCDB; 9.A.35.1.2; the peptide translocating syndecan (syndecan) family.
DR   GlyCosmos; P18827; 19 sites, 6 glycans.
DR   GlyGen; P18827; 48 sites, 8 O-linked glycans (43 sites).
DR   iPTMnet; P18827; -.
DR   PhosphoSitePlus; P18827; -.
DR   SwissPalm; P18827; -.
DR   BioMuta; SDC1; -.
DR   DMDM; 229463011; -.
DR   EPD; P18827; -.
DR   jPOST; P18827; -.
DR   MassIVE; P18827; -.
DR   MaxQB; P18827; -.
DR   PaxDb; 9606-ENSP00000370542; -.
DR   PeptideAtlas; P18827; -.
DR   ProteomicsDB; 53609; -.
DR   Pumba; P18827; -.
DR   ABCD; P18827; 5 sequenced antibodies.
DR   Antibodypedia; 1489; 1743 antibodies from 52 providers.
DR   DNASU; 6382; -.
DR   Ensembl; ENST00000254351.9; ENSP00000254351.4; ENSG00000115884.11.
DR   Ensembl; ENST00000381150.5; ENSP00000370542.1; ENSG00000115884.11.
DR   GeneID; 6382; -.
DR   KEGG; hsa:6382; -.
DR   MANE-Select; ENST00000254351.9; ENSP00000254351.4; NM_002997.5; NP_002988.4.
DR   UCSC; uc002rdo.2; human.
DR   AGR; HGNC:10658; -.
DR   CTD; 6382; -.
DR   DisGeNET; 6382; -.
DR   GeneCards; SDC1; -.
DR   HGNC; HGNC:10658; SDC1.
DR   HPA; ENSG00000115884; Tissue enhanced (esophagus, liver, skin).
DR   MIM; 186355; gene.
DR   neXtProt; NX_P18827; -.
DR   OpenTargets; ENSG00000115884; -.
DR   PharmGKB; PA35588; -.
DR   VEuPathDB; HostDB:ENSG00000115884; -.
DR   eggNOG; ENOG502RZWT; Eukaryota.
DR   GeneTree; ENSGT00940000161171; -.
DR   HOGENOM; CLU_887201_0_0_1; -.
DR   InParanoid; P18827; -.
DR   OMA; STWKDMA; -.
DR   OrthoDB; 5360052at2759; -.
DR   PhylomeDB; P18827; -.
DR   TreeFam; TF320463; -.
DR   PathwayCommons; P18827; -.
DR   Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR   Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR   Reactome; R-HSA-2024096; HS-GAG degradation.
DR   Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-HSA-3000170; Syndecan interactions.
DR   Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
DR   Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
DR   Reactome; R-HSA-3656237; Defective EXT2 causes exostoses 2.
DR   Reactome; R-HSA-3656253; Defective EXT1 causes exostoses 1, TRPS2 and CHDS.
DR   Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
DR   Reactome; R-HSA-449836; Other interleukin signaling.
DR   Reactome; R-HSA-9694614; Attachment and Entry.
DR   Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR   SignaLink; P18827; -.
DR   BioGRID-ORCS; 6382; 269 hits in 1149 CRISPR screens.
DR   ChiTaRS; SDC1; human.
DR   GeneWiki; Syndecan_1; -.
DR   GenomeRNAi; 6382; -.
DR   Pharos; P18827; Tbio.
DR   PRO; PR:P18827; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P18827; Protein.
DR   Bgee; ENSG00000115884; Expressed in lower esophagus mucosa and 165 other cell types or tissues.
DR   ExpressionAtlas; P18827; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0038024; F:cargo receptor activity; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0048627; P:myoblast development; ISS:UniProtKB.
DR   GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:UniProtKB.
DR   GO; GO:1903553; P:positive regulation of extracellular exosome assembly; IMP:UniProtKB.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
DR   GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR   GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR   GO; GO:0060009; P:Sertoli cell development; IEA:Ensembl.
DR   GO; GO:0055002; P:striated muscle cell development; IEP:UniProtKB.
DR   GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DR   InterPro; IPR003585; Neurexin-like.
DR   InterPro; IPR001050; Syndecan.
DR   InterPro; IPR027789; Syndecan/Neurexin_dom.
DR   InterPro; IPR030479; Syndecan_CS.
DR   PANTHER; PTHR10915; SYNDECAN; 1.
DR   PANTHER; PTHR10915:SF5; SYNDECAN-1; 1.
DR   Pfam; PF01034; Syndecan; 1.
DR   SMART; SM00294; 4.1m; 1.
DR   PROSITE; PS00964; SYNDECAN; 1.
DR   Genevisible; P18827; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Glycoprotein; Heparan sulfate; Membrane; Phosphoprotein;
KW   Proteoglycan; Reference proteome; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..310
FT                   /note="Syndecan-1"
FT                   /id="PRO_0000033499"
FT   TOPO_DOM        23..254
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        276..310
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          27..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            242..243
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CARBOHYD        37
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P18828"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        45
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        47
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        206
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000269|PubMed:32337544,
FT                   ECO:0000269|PubMed:36213313"
FT   CARBOHYD        216
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P18828"
FT   VARIANT         76
FT                   /note="T -> M (in dbSNP:rs2230922)"
FT                   /id="VAR_052242"
FT   VARIANT         136
FT                   /note="L -> Q (in dbSNP:rs10205485)"
FT                   /evidence="ECO:0000269|PubMed:1339431,
FT                   ECO:0000269|PubMed:15177497, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:2324102, ECO:0000269|PubMed:9050911,
FT                   ECO:0000269|Ref.5"
FT                   /id="VAR_052243"
FT   CONFLICT        19
FT                   /note="P -> L (in Ref. 2; AAA60605)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        259
FT                   /note="G -> V (in Ref. 6; AAH08765)"
FT                   /evidence="ECO:0000305"
FT   STRAND          305..309
FT                   /evidence="ECO:0007829|PDB:4GVC"
SQ   SEQUENCE   310 AA;  32462 MW;  8E9EF4A57F5FDBD0 CRC64;
     MRRAALWLWL CALALSLQPA LPQIVATNLP PEDQDGSGDD SDNFSGSGAG ALQDITLSQQ
     TPSTWKDTQL LTAIPTSPEP TGLEATAAST STLPAGEGPK EGEAVVLPEV EPGLTAREQE
     ATPRPRETTQ LPTTHLASTT TATTAQEPAT SHPHRDMQPG HHETSTPAGP SQADLHTPHT
     EDGGPSATER AAEDGASSQL PAAEGSGEQD FTFETSGENT AVVAVEPDRR NQSPVDQGAT
     GASQGLLDRK EVLGGVIAGG LVGLIFAVCL VGFMLYRMKK KDEGSYSLEE PKQANGGAYQ
     KPTKQEEFYA
//