ID   SDC3_HUMAN              Reviewed;         442 AA.
AC   O75056; Q5T1Z6; Q5T1Z7; Q96CT3; Q96PR8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   24-JAN-2024, entry version 188.
DE   RecName: Full=Syndecan-3;
DE            Short=SYND3;
GN   Name=SDC3; Synonyms=KIAA0468;
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], FUNCTION, TISSUE SPECIFICITY, AND VARIANT
RP   ASN-303.
RX   PubMed=11527150; DOI=10.1002/jcb.1119;
RA   Berndt C., Casaroli-Marano R.P., Vilaro S., Reina M.;
RT   "Cloning and characterization of human syndecan-3.";
RL   J. Cell. Biochem. 82:246-259(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA   Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA   Nomura N., Ohara O.;
RT   "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT   human brain.";
RL   DNA Res. 4:345-349(1997).
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].
RC   TISSUE=Muscle;
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   PHOSPHORYLATION AT TYR-409; TYR-419; TYR-431 AND TYR-441.
RX   PubMed=9388509; DOI=10.1006/bbrc.1997.7684;
RA   Asundi V.K., Carey D.J.;
RT   "Phosphorylation of recombinant N-syndecan (syndecan 3) core protein.";
RL   Biochem. Biophys. Res. Commun. 240:502-506(1997).
RN   [6]
RP   GLYCOSYLATION AT SER-108; THR-109; THR-110; SER-160; THR-161; THR-162;
RP   THR-169; SER-170 AND THR-171.
RX   PubMed=12407114; DOI=10.1074/jbc.m203094200;
RA   Zhang Y., Iwasaki H., Wang H., Kudo T., Kalka T.B., Hennet T., Kubota T.,
RA   Cheng L., Inaba N., Gotoh M., Togayachi A., Guo J.-M., Hisatomi H.,
RA   Nakajima K., Nishihara S., Nakamura M., Marth J.D., Narimatsu H.;
RT   "Cloning and characterization of a new human UDP-N-acetyl-alpha-D-
RT   galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-
RT   GalNAc-T13, that is specifically expressed in neurons and synthesizes
RT   GalNAc alpha-serine/threonine antigen.";
RL   J. Biol. Chem. 278:573-584(2003).
RN   [7]
RP   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 may bear heparan sulfate (By
CC       similarity). May have a role in the organization of cell shape by
CC       affecting the actin cytoskeleton, possibly by transferring signals from
CC       the cell surface in a sugar-dependent mechanism. {ECO:0000250,
CC       ECO:0000269|PubMed:11527150}.
CC   -!- SUBUNIT: Interacts with TIAM1 (PubMed:23395182). Interacts with PTN
CC       (via heparan sulfate chains); this interaction mediates the neurite
CC       outgrowth-promoting signal from PTN to the cytoskeleton of growing
CC       neurites; this interaction mediates osteoblast recruitment (By
CC       similarity). Interacts with MDK; this interaction induces SDC3
CC       clustering; this interaction induces neuronal cell adhesion and neurite
CC       outgrowth (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P33671,
CC       ECO:0000250|UniProtKB:Q64519, ECO:0000269|PubMed:23395182}.
CC   -!- INTERACTION:
CC       O75056; P34741: SDC2; NbExp=2; IntAct=EBI-1642090, EBI-1172957;
CC       O75056; O75056: SDC3; NbExp=3; IntAct=EBI-1642090, EBI-1642090;
CC       O75056; P31431: SDC4; NbExp=2; IntAct=EBI-1642090, EBI-3913237;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed in the nervous system, the adrenal gland,
CC       and the spleen. {ECO:0000269|PubMed:11527150}.
CC   -!- PTM: O-glycosylated within the Thr/Ser-rich region which could interact
CC       with lectin domains on other molecules. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA32313.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; AF248634; AAK39969.1; -; mRNA.
DR   EMBL; AB007937; BAA32313.2; ALT_SEQ; mRNA.
DR   EMBL; AL445235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC013974; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS30661.1; -.
DR   RefSeq; NP_055469.3; NM_014654.3.
DR   AlphaFoldDB; O75056; -.
DR   SASBDB; O75056; -.
DR   SMR; O75056; -.
DR   BioGRID; 115027; 35.
DR   DIP; DIP-29944N; -.
DR   IntAct; O75056; 10.
DR   MINT; O75056; -.
DR   STRING; 9606.ENSP00000344468; -.
DR   GlyCosmos; O75056; 18 sites, 3 glycans.
DR   GlyGen; O75056; 30 sites, 4 O-linked glycans (15 sites).
DR   iPTMnet; O75056; -.
DR   PhosphoSitePlus; O75056; -.
DR   BioMuta; SDC3; -.
DR   EPD; O75056; -.
DR   jPOST; O75056; -.
DR   MassIVE; O75056; -.
DR   MaxQB; O75056; -.
DR   PaxDb; 9606-ENSP00000344468; -.
DR   PeptideAtlas; O75056; -.
DR   ProteomicsDB; 49730; -.
DR   Pumba; O75056; -.
DR   TopDownProteomics; O75056; -.
DR   Antibodypedia; 1502; 258 antibodies from 32 providers.
DR   DNASU; 9672; -.
DR   Ensembl; ENST00000339394.7; ENSP00000344468.6; ENSG00000162512.16.
DR   GeneID; 9672; -.
DR   KEGG; hsa:9672; -.
DR   MANE-Select; ENST00000339394.7; ENSP00000344468.6; NM_014654.4; NP_055469.3.
DR   UCSC; uc001bse.3; human.
DR   AGR; HGNC:10660; -.
DR   CTD; 9672; -.
DR   DisGeNET; 9672; -.
DR   GeneCards; SDC3; -.
DR   HGNC; HGNC:10660; SDC3.
DR   HPA; ENSG00000162512; Low tissue specificity.
DR   MalaCards; SDC3; -.
DR   MIM; 186357; gene.
DR   neXtProt; NX_O75056; -.
DR   OpenTargets; ENSG00000162512; -.
DR   PharmGKB; PA35590; -.
DR   VEuPathDB; HostDB:ENSG00000162512; -.
DR   eggNOG; ENOG502QTD2; Eukaryota.
DR   GeneTree; ENSGT00940000160209; -.
DR   HOGENOM; CLU_047258_0_0_1; -.
DR   InParanoid; O75056; -.
DR   OMA; EMQPSES; -.
DR   OrthoDB; 5360052at2759; -.
DR   PhylomeDB; O75056; -.
DR   TreeFam; TF320463; -.
DR   PathwayCommons; O75056; -.
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-9694614; Attachment and Entry.
DR   Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR   SignaLink; O75056; -.
DR   SIGNOR; O75056; -.
DR   BioGRID-ORCS; 9672; 14 hits in 1159 CRISPR screens.
DR   ChiTaRS; SDC3; human.
DR   GeneWiki; SDC3; -.
DR   GenomeRNAi; 9672; -.
DR   Pharos; O75056; Tbio.
DR   PRO; PR:O75056; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O75056; Protein.
DR   Bgee; ENSG00000162512; Expressed in right adrenal gland cortex and 160 other cell types or tissues.
DR   ExpressionAtlas; O75056; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0044393; C:microspike; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
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:SF7; SYNDECAN-3; 1.
DR   Pfam; PF01034; Syndecan; 1.
DR   SMART; SM00294; 4.1m; 1.
DR   PROSITE; PS00964; SYNDECAN; 1.
DR   Genevisible; O75056; HS.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Heparan sulfate; Membrane; Phosphoprotein;
KW   Proteoglycan; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..442
FT                   /note="Syndecan-3"
FT                   /id="PRO_0000183989"
FT   TOPO_DOM        1..387
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        409..442
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          57..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            383..384
FT                   /note="Cleavage of ectodomain"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         409
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:9388509"
FT   MOD_RES         419
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:9388509"
FT   MOD_RES         431
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:9388509"
FT   MOD_RES         441
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:9388509"
FT   CARBOHYD        80
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        82
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        91
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        108
FT                   /note="O-linked (GalNAc) serine; by GALNT13"
FT                   /evidence="ECO:0000269|PubMed:12407114"
FT   CARBOHYD        109
FT                   /note="O-linked (GalNAc) threonine; by GALNT13"
FT                   /evidence="ECO:0000269|PubMed:12407114"
FT   CARBOHYD        110
FT                   /note="O-linked (GalNAc) threonine; by GALNT13"
FT                   /evidence="ECO:0000269|PubMed:12407114"
FT   CARBOHYD        160
FT                   /note="O-linked (GalNAc) serine; by GALNT13"
FT                   /evidence="ECO:0000269|PubMed:12407114"
FT   CARBOHYD        161
FT                   /note="O-linked (GalNAc) threonine; by GALNT13"
FT                   /evidence="ECO:0000269|PubMed:12407114"
FT   CARBOHYD        162
FT                   /note="O-linked (GalNAc) threonine; by GALNT13"
FT                   /evidence="ECO:0000269|PubMed:12407114"
FT   CARBOHYD        169
FT                   /note="O-linked (GalNAc) threonine; by GALNT13"
FT                   /evidence="ECO:0000269|PubMed:12407114"
FT   CARBOHYD        170
FT                   /note="O-linked (GalNAc) serine; by GALNT13"
FT                   /evidence="ECO:0000269|PubMed:12407114"
FT   CARBOHYD        171
FT                   /note="O-linked (GalNAc) threonine; by GALNT13"
FT                   /evidence="ECO:0000269|PubMed:12407114"
FT   CARBOHYD        314
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        367
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         208
FT                   /note="V -> I (in dbSNP:rs2491132)"
FT                   /id="VAR_027251"
FT   VARIANT         303
FT                   /note="D -> N (in dbSNP:rs4949184)"
FT                   /evidence="ECO:0000269|PubMed:11527150"
FT                   /id="VAR_027252"
FT   VARIANT         329
FT                   /note="T -> I (in dbSNP:rs2282440)"
FT                   /id="VAR_027253"
SQ   SEQUENCE   442 AA;  45497 MW;  D4C284CBC36A92E2 CRC64;
     MKPGPPHRAG AAHGAGAGAG AAAGPGARGL LLPPLLLLLL AGRAAGAQRW RSENFERPVD
     LEGSGDDDSF PDDELDDLYS GSGSGYFEQE SGIETAMRFS PDVALAVSTT PAVLPTTNIQ
     PVGTPFEELP SERPTLEPAT SPLVVTEVPE EPSQRATTVS TTMATTAATS TGDPTVATVP
     ATVATATPST PAAPPFTATT AVIRTTGVRR LLPLPLTTVA TARATTPEAP SPPTTAAVLD
     TEAPTPRLVS TATSRPRALP RPATTQEPDI PERSTLPLGT TAPGPTEVAQ TPTPETFLTT
     IRDEPEVPVS GGPSGDFELP EEETTQPDTA NEVVAVGGAA AKASSPPGTL PKGARPGPGL
     LDNAIDSGSS AAQLPQKSIL ERKEVLVAVI VGGVVGALFA AFLVTLLIYR MKKKDEGSYT
     LEEPKQASVT YQKPDKQEEF YA
//