SDC3_HUMAN
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 03-AUG-2022, entry version 180.
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; 33.
DR DIP; DIP-29944N; -.
DR IntAct; O75056; 9.
DR MINT; O75056; -.
DR STRING; 9606.ENSP00000344468; -.
DR GlyGen; O75056; 9 sites, 3 O-linked glycans (3 sites).
DR iPTMnet; O75056; -.
DR PhosphoSitePlus; O75056; -.
DR BioMuta; SDC3; -.
DR EPD; O75056; -.
DR jPOST; O75056; -.
DR MassIVE; O75056; -.
DR MaxQB; O75056; -.
DR PaxDb; O75056; -.
DR PeptideAtlas; O75056; -.
DR PRIDE; O75056; -.
DR ProteomicsDB; 49730; -.
DR TopDownProteomics; O75056; -.
DR Antibodypedia; 1502; 229 antibodies from 31 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 CTD; 9672; -.
DR DisGeNET; 9672; -.
DR GeneCards; SDC3; -.
DR HGNC; HGNC:10660; SDC3.
DR HPA; ENSG00000162512; Tissue enhanced (brain).
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; MKPGPPH; -.
DR OrthoDB; 1340825at2759; -.
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; 12 hits in 1080 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 159 other tissues.
DR ExpressionAtlas; O75056; baseline and differential.
DR Genevisible; O75056; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPR031194; Syndecan-3.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR InterPro; IPR030479; Syndecan_CS.
DR PANTHER; PTHR10915; PTHR10915; 1.
DR PANTHER; PTHR10915:SF7; PTHR10915:SF7; 1.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR PROSITE; PS00964; SYNDECAN; 1.
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
