SDC1_MOUSE
ID SDC1_MOUSE Reviewed; 311 AA.
AC P18828; Q62278; Q9WVD2;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Syndecan-1;
DE Short=SYND1;
DE AltName: CD_antigen=CD138;
DE Flags: Precursor;
GN Name=Sdc1; Synonyms=Synd-1, Synd1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
RX PubMed=2494194; DOI=10.1083/jcb.108.4.1547;
RA Saunders S., Jalkanen M., O'Farrell S., Bernfield M.;
RT "Molecular cloning of syndecan, an integral membrane proteoglycan.";
RL J. Cell Biol. 108:1547-1556(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8349612; DOI=10.1016/s0021-9258(19)85331-0;
RA Vihinen T., Auvinen P., Alanen-Kurki L., Jalkanen M.;
RT "Structural organization and genomic sequence of mouse syndecan-1 gene.";
RL J. Biol. Chem. 268:17261-17269(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=NMRI; TISSUE=Embryo;
RX PubMed=10373479; DOI=10.1074/jbc.274.26.18667;
RA Romaris M., Coomans C., Ceulemans H., Bruystens A.-M., Vekemans S.,
RA David G.;
RT "Molecular polymorphism of the syndecans. Identification of a hypo-
RT glycanated murine syndecan-1 splice variant.";
RL J. Biol. Chem. 274:18667-18674(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8496192; DOI=10.1016/s0021-9258(18)82143-3;
RA Hinkes M.T., Goldberger O., Neumann P., Kokenyeji R., Bernfield M.;
RT "Organization and promoter activity of the mouse syndecan-1 gene.";
RL J. Biol. Chem. 268:11440-11448(1993).
RN [6]
RP GLYCOSYLATION AT SER-37; SER-207 AND SER-217.
RX PubMed=8163535; DOI=10.1016/s0021-9258(17)32716-3;
RA Kokenyesi R., Bernfield M.;
RT "Core protein structure and sequence determine the site and presence of
RT heparan sulfate and chondroitin sulfate on syndecan-1.";
RL J. Biol. Chem. 269:12304-12309(1994).
RN [7]
RP SHEDDING, AND SUBCELLULAR LOCATION.
RX PubMed=10684261; DOI=10.1083/jcb.148.4.811;
RA Fitzgerald M.L., Wang Z., Park P.W., Murphy G., Bernfield M.;
RT "Shedding of syndecan-1 and -4 ectodomains is regulated by multiple
RT signaling pathways and mediated by a TIMP-3-sensitive metalloproteinase.";
RL J. Cell Biol. 148:811-824(2000).
RN [8]
RP PROTEOLYTIC CLEAVAGE AT ALA-243, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16156648; DOI=10.1021/bi050620i;
RA Wang Z., Gotte M., Bernfield M., Reizes O.;
RT "Constitutive and accelerated shedding of murine syndecan-1 is mediated by
RT cleavage of its core protein at a specific juxtamembrane site.";
RL Biochemistry 44:12355-12361(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH TIAM1.
RX PubMed=20361982; DOI=10.1016/j.jmb.2010.03.047;
RA Shepherd T.R., Klaus S.M., Liu X., Ramaswamy S., DeMali K.A., Fuentes E.J.;
RT "The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix
RT adhesion.";
RL J. Mol. Biol. 398:730-746(2010).
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 (By similarity). Interacts (via C-
CC terminus) with TIAM1 (via PDZ domain) (PubMed:20361982). Interacts with
CC MDK (By similarity). {ECO:0000250|UniProtKB:P18827,
CC ECO:0000250|UniProtKB:P26260, ECO:0000269|PubMed:20361982}.
CC -!- INTERACTION:
CC P18828; Q15113: PCOLCE; Xeno; NbExp=4; IntAct=EBI-9985816, EBI-8869614;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:10684261}.
CC Secreted, extracellular exosome {ECO:0000250|UniProtKB:P18827}.
CC Note=Shedding of the ectodomain produces a soluble form.
CC {ECO:0000269|PubMed:10684261}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P18828-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P18828-2; Sequence=VSP_007542;
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. {ECO:0000269|PubMed:10684261}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform.
CC -!- MISCELLANEOUS: [Isoform 2]: Minor isoform. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
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DR EMBL; X15487; CAA33514.1; -; mRNA.
DR EMBL; Z22532; CAA80254.1; -; Genomic_DNA.
DR EMBL; AF134897; AAD42345.1; -; mRNA.
DR EMBL; BC010560; AAH10560.1; -; mRNA.
DR EMBL; L11565; AAA40159.1; -; Genomic_DNA.
DR CCDS; CCDS25803.1; -. [P18828-1]
DR PIR; S06619; S06619.
DR RefSeq; NP_035649.1; NM_011519.2. [P18828-1]
DR AlphaFoldDB; P18828; -.
DR BioGRID; 203602; 2.
DR ComplexPortal; CPX-3283; Syndecan-1-syntenin-1-ALIX complex.
DR IntAct; P18828; 1.
DR STRING; 10090.ENSMUSP00000020911; -.
DR GlyGen; P18828; 6 sites.
DR iPTMnet; P18828; -.
DR PhosphoSitePlus; P18828; -.
DR CPTAC; non-CPTAC-4060; -.
DR MaxQB; P18828; -.
DR PaxDb; P18828; -.
DR PeptideAtlas; P18828; -.
DR PRIDE; P18828; -.
DR ProteomicsDB; 256716; -. [P18828-1]
DR ProteomicsDB; 256717; -. [P18828-2]
DR Antibodypedia; 1489; 1530 antibodies from 51 providers.
DR DNASU; 20969; -.
DR Ensembl; ENSMUST00000020911; ENSMUSP00000020911; ENSMUSG00000020592. [P18828-1]
DR Ensembl; ENSMUST00000171158; ENSMUSP00000131491; ENSMUSG00000020592. [P18828-1]
DR GeneID; 20969; -.
DR KEGG; mmu:20969; -.
DR UCSC; uc007nac.1; mouse. [P18828-1]
DR UCSC; uc007nad.1; mouse. [P18828-2]
DR CTD; 6382; -.
DR MGI; MGI:1349162; Sdc1.
DR VEuPathDB; HostDB:ENSMUSG00000020592; -.
DR eggNOG; ENOG502RZWT; Eukaryota.
DR GeneTree; ENSGT00940000161171; -.
DR HOGENOM; CLU_887201_0_0_1; -.
DR InParanoid; P18828; -.
DR OMA; QPAMPQI; -.
DR PhylomeDB; P18828; -.
DR TreeFam; TF320463; -.
DR Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-MMU-2022928; HS-GAG biosynthesis.
DR Reactome; R-MMU-2024096; HS-GAG degradation.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-3000170; Syndecan interactions.
DR Reactome; R-MMU-449836; Other interleukin signaling.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 20969; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Sdc1; mouse.
DR PRO; PR:P18828; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P18828; protein.
DR Bgee; ENSMUSG00000020592; Expressed in cumulus cell and 227 other tissues.
DR ExpressionAtlas; P18828; baseline and differential.
DR Genevisible; P18828; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; ISO:MGI.
DR GO; GO:0048627; P:myoblast development; IDA:UniProtKB.
DR GO; GO:0042476; P:odontogenesis; IEA:Ensembl.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; ISO:MGI.
DR GO; GO:1903553; P:positive regulation of extracellular exosome assembly; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0060009; P:Sertoli cell development; IEA:Ensembl.
DR GO; GO:0055002; P:striated muscle cell development; IEA:Ensembl.
DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
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 Alternative splicing; Glycoprotein; Heparan sulfate; Membrane;
KW Phosphoprotein; Proteoglycan; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..311
FT /note="Syndecan-1"
FT /id="PRO_0000033501"
FT TOPO_DOM 23..255
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 29..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 243..244
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:16156648"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18827"
FT CARBOHYD 37
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000305|PubMed:8163535"
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:0000305"
FT CARBOHYD 47
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000305"
FT CARBOHYD 207
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:8163535"
FT CARBOHYD 217
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:8163535"
FT VAR_SEQ 50..93
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10373479"
FT /id="VSP_007542"
FT CONFLICT 21
FT /note="L -> V (in Ref. 5; AAA40159)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 32905 MW; 283FEC396FF40FCE CRC64;
MRRAALWLWL CALALRLQPA LPQIVAVNVP PEDQDGSGDD SDNFSGSGTG ALPDTLSRQT
PSTWKDVWLL TATPTAPEPT SSNTETAFTS VLPAGEKPEE GEPVLHVEAE PGFTARDKEK
EVTTRPRETV QLPITQRAST VRVTTAQAAV TSHPHGGMQP GLHETSAPTA PGQPDHQPPR
VEGGGTSVIK EVVEDGTANQ LPAGEGSGEQ DFTFETSGEN TAVAAVEPGL RNQPPVDEGA
TGASQSLLDR KEVLGGVIAG GLVGLIFAVC LVAFMLYRMK KKDEGSYSLE EPKQANGGAY
QKPTKQEEFY A
