SDC1_MESAU
ID SDC1_MESAU Reviewed; 309 AA.
AC P34740;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Syndecan-1;
DE Short=SYND1;
DE AltName: CD_antigen=CD138;
DE Flags: Precursor;
GN Name=SDC1;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2144898; DOI=10.1073/pnas.87.18.6985;
RA Kiefer M.C., Stephans J.C., Crawford K., Okino K., Barr P.J.;
RT "Ligand-affinity cloning and structure of a cell surface heparan sulfate
RT proteoglycan that binds basic fibroblast growth factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6985-6989(1990).
CC -!- FUNCTION: Cell surface proteoglycan that bears both heparan sulfate and
CC chondroitin sulfate and that links the cytoskeleton to the interstitial
CC matrix. Regulates exosome biogenesis in concert with SDCBP and PDCD6IP.
CC {ECO:0000250|UniProtKB:P18827}.
CC -!- SUBUNIT: Interacts with CDCP1. Interacts (via C-terminus) with TIAM1
CC (via PDZ domain) (By similarity). Interacts with MDK (By similarity).
CC {ECO:0000250|UniProtKB:P18827, ECO:0000250|UniProtKB:P26260}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}. Secreted
CC {ECO:0000250|UniProtKB:P18827}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:P18827}. Note=Shedding of the ectodomain
CC produces a soluble form. {ECO:0000250|UniProtKB:P18827}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P18827}.
CC -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M29967; AAA37087.1; -; mRNA.
DR PIR; A36064; A36064.
DR RefSeq; XP_005079125.1; XM_005079068.2.
DR AlphaFoldDB; P34740; -.
DR SMR; P34740; -.
DR STRING; 10036.XP_005079125.1; -.
DR GeneID; 101836998; -.
DR CTD; 6382; -.
DR eggNOG; ENOG502RZWT; Eukaryota.
DR OrthoDB; 1340825at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0048627; P:myoblast development; IEA:Ensembl.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; IEA:Ensembl.
DR GO; GO:1903553; P:positive regulation of extracellular exosome assembly; IEA:Ensembl.
DR GO; GO:0055002; P:striated muscle cell development; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:InterPro.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR001050; Syndecan.
DR InterPro; IPR031190; Syndecan-1.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR InterPro; IPR030479; Syndecan_CS.
DR PANTHER; PTHR10915; PTHR10915; 1.
DR PANTHER; PTHR10915:SF5; PTHR10915:SF5; 1.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR PROSITE; PS00964; SYNDECAN; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Heparan sulfate; Membrane; Phosphoprotein; Proteoglycan;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..309
FT /note="Syndecan-1"
FT /id="PRO_0000033500"
FT TOPO_DOM 23..253
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 28..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 241..242
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18827"
FT CARBOHYD 37
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250"
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 205
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 215
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 309 AA; 32678 MW; B759CB36670290A2 CRC64;
MRRAALWLWL CALALRLQPV LPQIVTVNVP PEDQDGSGDD SDNFSGSGTG ALPDITLSRQ
ASPTLKDVWL LTATPTAPEP TSRDAQATTT SILPAAEKPG EGEPVLTAEV DPGFTARDKE
SEVTTRPRET TQLLITHWVS TARATTAQAP VTSHPHRDVQ PGLHETSAPT APGQPDQQPP
SGGTSVIKEV AEDGATNQLP TGEGSGEQDF TFETSGENTA VAAVEPDQRN QPPVDEGATG
ASQGLLDRKE VLGGVIAGGL VGLIFAVCLV GFMLYRMKKK DEGSYSLEEP KQANGGAYQK
PTKQEEFYA
