SDC1_CRIGR
ID SDC1_CRIGR Reviewed; 309 AA.
AC P47951;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Syndecan-1;
DE Short=SYND1;
DE AltName: CD_antigen=CD138;
DE Flags: Precursor;
GN Name=SDC1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=7592967; DOI=10.1074/jbc.270.45.27127;
RA Zhang L., David G., Esko J.D.;
RT "Repetitive Ser-Gly sequences enhance heparan sulfate assembly in
RT proteoglycans.";
RL J. Biol. Chem. 270:27127-27135(1995).
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}.
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DR EMBL; L38991; AAC37677.1; -; mRNA.
DR PIR; I48125; I48125.
DR RefSeq; NP_001230971.1; NM_001244042.1.
DR AlphaFoldDB; P47951; -.
DR SMR; P47951; -.
DR STRING; 10029.NP_001230971.1; -.
DR Ensembl; ENSCGRT00001022644; ENSCGRP00001018400; ENSCGRG00001018173.
DR GeneID; 100689057; -.
DR KEGG; cge:100689057; -.
DR CTD; 6382; -.
DR eggNOG; ENOG502RZWT; Eukaryota.
DR GeneTree; ENSGT00940000161171; -.
DR OrthoDB; 1340825at2759; -.
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:0060140; P:modulation by virus of syncytium formation via plasma membrane fusion; IMP:CACAO.
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 Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..309
FT /note="Syndecan-1"
FT /id="PRO_0000033498"
FT TOPO_DOM 24..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 142..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 249..250
FT /note="Cleavage of ectodomain"
FT /evidence="ECO:0000255"
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; 32840 MW; B2770389570A15C3 CRC64;
MRRAALWLWL CALALRLQPV LPQIMAVNVP PEDQDGSGDD SDNFSGSGTG ALPDITLSRQ
TSSTLKDVWL LTATPTAPEP TSRDTEATFT SILPAGEKPG EGEPVLIAEV DTSSTTWDKE
LEVTTRPRET TQLLVTHRVS TARATTAQAP VTSHPHRDVQ PGLHETLAPT APGQPDHQPP
SGGTSVIKEV AEDGATNQLP TGEGSGEQDF TFETSGENTA VAAIEPDQRN QPPVDEGATG
ASQGLLDRKE VLGGVIAGGL VGLIFAVCLV GFMLYRMKKK DEGSYSLEEP KQANGGAYQK
PTKQEEFYA
