SDC4_MOUSE
ID SDC4_MOUSE Reviewed; 198 AA.
AC O35988;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Syndecan-4;
DE Short=SYND4;
DE AltName: Full=Ryudocan core protein;
DE Flags: Precursor;
GN Name=Sdc4;
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ, and C3H/An;
RX PubMed=9276666; DOI=10.1093/oxfordjournals.jbchem.a021724;
RA Tsuzuki S., Kojima T., Katsumi A., Yamazaki T., Sugiura I., Saito H.;
RT "Molecular cloning, genomic organization, promoter activity, and tissue-
RT specific expression of the mouse ryudocan gene.";
RL J. Biochem. 122:17-24(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [3]
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 [4]
RP INTERACTION WITH GIPC.
RX PubMed=10911369;
RX DOI=10.1002/1097-4652(200009)184:3<373::aid-jcp12>3.0.co;2-i;
RA Gao Y., Li M., Chen W., Simons M.;
RT "Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell
RT migration.";
RL J. Cell. Physiol. 184:373-379(2000).
RN [5]
RP INTERACTION WITH NUDT16L1.
RX PubMed=11805099; DOI=10.1074/jbc.m110291200;
RA Denhez F., Wilcox-Adelman S.A., Baciu P.C., Saoncella S., Lee S.,
RA French B., Neveu W., Goetinck P.F.;
RT "Syndesmos, a syndecan-4 cytoplasmic domain interactor, binds to the focal
RT adhesion adaptor proteins paxillin and Hic-5.";
RL J. Biol. Chem. 277:12270-12274(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, 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).
CC -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate.
CC Regulates exosome biogenesis in concert with SDCBP and PDCD6IP.
CC {ECO:0000250|UniProtKB:P31431}.
CC -!- SUBUNIT: Homodimer. Interacts with CDCP1 and SDCBP (By similarity).
CC Interacts (via its cytoplasmic domain) with GIPC (via its PDZ domain).
CC Interacts (via its cytoplasmic domain) with NUDT16L1.
CC {ECO:0000250|UniProtKB:P31431, ECO:0000269|PubMed:10911369,
CC ECO:0000269|PubMed:11805099}.
CC -!- INTERACTION:
CC O35988; Q15113: PCOLCE; Xeno; NbExp=2; IntAct=EBI-9986850, EBI-8869614;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:10684261}.
CC Note=Shedding of the ectodomain produces a soluble form.
CC {ECO:0000269|PubMed:10684261}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest levels in liver, kidney and
CC lung.
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 -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
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DR EMBL; D89571; BAA22135.1; -; mRNA.
DR EMBL; D89572; BAA22136.1; -; Genomic_DNA.
DR EMBL; BC005679; AAH05679.1; -; mRNA.
DR CCDS; CCDS17036.1; -.
DR PIR; JC5613; JC5613.
DR RefSeq; NP_035651.1; NM_011521.2.
DR AlphaFoldDB; O35988; -.
DR BMRB; O35988; -.
DR SMR; O35988; -.
DR BioGRID; 203604; 5.
DR IntAct; O35988; 3.
DR MINT; O35988; -.
DR STRING; 10090.ENSMUSP00000017153; -.
DR ChEMBL; CHEMBL2062355; -.
DR GlyGen; O35988; 3 sites.
DR iPTMnet; O35988; -.
DR PhosphoSitePlus; O35988; -.
DR EPD; O35988; -.
DR jPOST; O35988; -.
DR PaxDb; O35988; -.
DR PeptideAtlas; O35988; -.
DR PRIDE; O35988; -.
DR ProteomicsDB; 255375; -.
DR Antibodypedia; 969; 505 antibodies from 40 providers.
DR DNASU; 20971; -.
DR Ensembl; ENSMUST00000017153; ENSMUSP00000017153; ENSMUSG00000017009.
DR GeneID; 20971; -.
DR KEGG; mmu:20971; -.
DR UCSC; uc008nuq.1; mouse.
DR CTD; 6385; -.
DR MGI; MGI:1349164; Sdc4.
DR VEuPathDB; HostDB:ENSMUSG00000017009; -.
DR eggNOG; ENOG502S1SZ; Eukaryota.
DR GeneTree; ENSGT00940000160663; -.
DR HOGENOM; CLU_046599_3_0_1; -.
DR InParanoid; O35988; -.
DR OMA; GSWVPTE; -.
DR OrthoDB; 1507361at2759; -.
DR PhylomeDB; O35988; -.
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-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 20971; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Sdc4; mouse.
DR PRO; PR:O35988; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O35988; protein.
DR Bgee; ENSMUSG00000017009; Expressed in vestibular membrane of cochlear duct and 284 other tissues.
DR ExpressionAtlas; O35988; baseline and differential.
DR Genevisible; O35988; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0043034; C:costamere; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0070053; F:thrombospondin receptor activity; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IGI:MGI.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI.
DR GO; GO:0001843; P:neural tube closure; IGI:MGI.
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:0051894; P:positive regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0010762; P:regulation of fibroblast migration; IMP:UniProtKB.
DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IGI:MGI.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR001050; Syndecan.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR InterPro; IPR030479; Syndecan_CS.
DR PANTHER; PTHR10915; PTHR10915; 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; Proteoglycan; Reference proteome;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..198
FT /note="Syndecan-4"
FT /id="PRO_0000033512"
FT TOPO_DOM 24..145
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 42..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..66
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 44
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 62
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 198 AA; 21482 MW; 4246963EC6A25915 CRC64;
MAPACLLAPL LLLLLGGFPL VPGESIRETE VIDPQDLLEG RYFSGALPDD EDAGGSDDFE
LSGSGDLDDT EEPRPFPEVI EPLVPLDNHI PENAQPGIRV PSEPKELEEN EVIPKRAPSD
VGDDMSNKVS MSSTAQGSNI FERTEVLAAL IVGGVVGILF AVFLILLLVY RMKKKDEGSY
DLGKKPIYKK APTNEFYA
