SDC1_RAT
ID SDC1_RAT Reviewed; 313 AA.
AC P26260;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Syndecan-1;
DE Short=SYND1;
DE AltName: CD_antigen=CD138;
DE Flags: Precursor;
GN Name=Sdc1; Synonyms=Synd1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1537865; DOI=10.1016/s0021-9258(18)42911-0;
RA Kojima T., Shworak N.W., Rosenberg R.D.;
RT "Molecular cloning and expression of two distinct cDNA-encoding heparan
RT sulfate proteoglycan core proteins from a rat endothelial cell line.";
RL J. Biol. Chem. 267:4870-4877(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Endothelial cell;
RX PubMed=8495865; DOI=10.1159/000216925;
RA Shworak N.W., Kojima T., Rosenberg R.D.;
RT "Isolation and characterization of ryudocan and syndecan heparan sulfate
RT proteoglycans, core proteins, and cDNAs from a rat endothelial cell line.";
RL Haemostasis 23:161-176(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Aorta;
RX PubMed=1639809; DOI=10.1016/s0021-9258(19)49596-3;
RA Cizmeci-Smith G., Asundi V., Stahl R.C., Teichman L.J., Chernousov M.,
RA Cowan K., Carey D.J.;
RT "Regulated expression of syndecan in vascular smooth muscle cells and
RT cloning of rat syndecan core protein cDNA.";
RL J. Biol. Chem. 267:15729-15736(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 INTERACTION WITH MDK.
RX PubMed=9089390;
RA Nakanishi T., Kadomatsu K., Okamoto T., Ichihara-Tanaka K., Kojima T.,
RA Saito H., Tomoda Y., Muramatsu T.;
RT "Expression of syndecan-1 and -3 during embryogenesis of the central
RT nervous system in relation to binding with midkine.";
RL J. Biochem. 121:197-205(1997).
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 (PubMed:9089390).
CC {ECO:0000250|UniProtKB:P18827, ECO:0000269|PubMed:9089390}.
CC -!- INTERACTION:
CC P26260; P34900: Sdc2; NbExp=2; IntAct=EBI-1173127, EBI-1173032;
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; X60651; CAA43058.1; -; mRNA.
DR EMBL; M81785; AAA42198.1; -; mRNA.
DR EMBL; S61865; AAB26726.1; -; mRNA.
DR EMBL; BC061834; AAH61834.1; -; mRNA.
DR PIR; A42853; A42853.
DR RefSeq; NP_037158.1; NM_013026.2.
DR AlphaFoldDB; P26260; -.
DR IntAct; P26260; 4.
DR STRING; 10116.ENSRNOP00000008582; -.
DR GlyGen; P26260; 6 sites.
DR iPTMnet; P26260; -.
DR PhosphoSitePlus; P26260; -.
DR jPOST; P26260; -.
DR PaxDb; P26260; -.
DR Ensembl; ENSRNOT00000086633; ENSRNOP00000072283; ENSRNOG00000059947.
DR GeneID; 25216; -.
DR KEGG; rno:25216; -.
DR CTD; 6382; -.
DR RGD; 3648; Sdc1.
DR eggNOG; ENOG502RZWT; Eukaryota.
DR GeneTree; ENSGT00940000161171; -.
DR HOGENOM; CLU_887201_0_0_1; -.
DR InParanoid; P26260; -.
DR OMA; QPAMPQI; -.
DR OrthoDB; 1340825at2759; -.
DR PhylomeDB; P26260; -.
DR TreeFam; TF320463; -.
DR Reactome; R-RNO-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-RNO-2022928; HS-GAG biosynthesis.
DR Reactome; R-RNO-2024096; HS-GAG degradation.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-RNO-3000170; Syndecan interactions.
DR Reactome; R-RNO-449836; Other interleukin signaling.
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR PRO; PR:P26260; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000059947; Expressed in esophagus and 17 other tissues.
DR Genevisible; P26260; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
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:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0050840; F:extracellular matrix binding; TAS:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; NAS:RGD.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; NAS:RGD.
DR GO; GO:0006954; P:inflammatory response; IDA:RGD.
DR GO; GO:0048627; P:myoblast development; ISO:RGD.
DR GO; GO:0042476; P:odontogenesis; IEP:RGD.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; ISO:RGD.
DR GO; GO:1903553; P:positive regulation of extracellular exosome assembly; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0060009; P:Sertoli cell development; IEP:RGD.
DR GO; GO:0055002; P:striated muscle cell development; ISO:RGD.
DR GO; GO:0001657; P:ureteric bud development; IEP:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
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 1: Evidence at protein 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..313
FT /note="Syndecan-1"
FT /id="PRO_0000033502"
FT TOPO_DOM 23..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 27..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 253..254
FT /note="Cleavage of ectodomain"
FT /evidence="ECO:0000255"
FT MOD_RES 288
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 209
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 219
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250"
FT CONFLICT 15
FT /note="L -> V (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 33214 MW; C6EC50E8798A5218 CRC64;
MRRAALWLWL CALALRLQPA LPQIVTANVP PEDQDGSGDD SDNFSGSGTG ALPDMTLSRQ
TPSTWKDVWL LTATPTAPEP TSRDTEATLT SILPAGEKPE EGEPVAHVEA EPDFTARDKE
KEATTRPRET TQLPVTQQAS TAARATTAQA SVTSHPHGDV QPGLHETLAP TAPGQPDHQP
PSVEDGGTSV IKEVVEDETT NQLPAGEGSG EQDFTFETSG ENTAVAGVEP DLRNQSPVDE
GATGASQGLL DRKEVLGGVI AGGLVGLIFA VCLVAFMLYR MKKKDEGSYS LEEPKQANGG
AYQKPTKQEE FYA
