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   24-JAN-2024, entry version 182.
DE   RecName: Full=Syndecan-4 {ECO:0000305};
DE            Short=SYND4;
DE   AltName: Full=Ryudocan core protein;
DE   Flags: Precursor;
GN   Name=Sdc4 {ECO:0000312|MGI:MGI:1349164};
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   INTERACTION WITH DNM2.
RX   PubMed=15694365; DOI=10.1016/j.bbrc.2004.12.179;
RA   Yoo J., Jeong M.J., Cho H.J., Oh E.S., Han M.Y.;
RT   "Dynamin II interacts with syndecan-4, a regulator of focal adhesion and
RT   stress-fiber formation.";
RL   Biochem. Biophys. Res. Commun. 328:424-431(2005).
RN   [7]
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 which regulates exosome biogenesis
CC       in concert with SDCBP and PDCD6IP. {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. Interacts with
CC       DNM2; this interaction is markedly enhanced at focal ahesion site upon
CC       induction of focal adhesions and stress-fiber formation
CC       (PubMed:15694365). {ECO:0000250|UniProtKB:P31431,
CC       ECO:0000269|PubMed:10911369, ECO:0000269|PubMed:11805099,
CC       ECO:0000269|PubMed:15694365}.
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   -!- PTM: O-glycosylated; contains both chondroitin sulfate and heparan
CC       sulfate. Ser-44, Ser-62 and Ser-64 can all be modified by either
CC       chondroitin sulfate or heparan sulfate, and the protein exists in forms
CC       that contain only chondroitin sulfate, only heparan sulfate and both
CC       chondroitin sulfate and heparan sulfate.
CC       {ECO:0000250|UniProtKB:P34901}.
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; 6.
DR   IntAct; O35988; 3.
DR   MINT; O35988; -.
DR   STRING; 10090.ENSMUSP00000017153; -.
DR   ChEMBL; CHEMBL2062355; -.
DR   GlyCosmos; O35988; 3 sites, No reported glycans.
DR   GlyGen; O35988; 4 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; O35988; -.
DR   PhosphoSitePlus; O35988; -.
DR   EPD; O35988; -.
DR   jPOST; O35988; -.
DR   PaxDb; 10090-ENSMUSP00000017153; -.
DR   PeptideAtlas; O35988; -.
DR   ProteomicsDB; 255375; -.
DR   Pumba; O35988; -.
DR   Antibodypedia; 969; 543 antibodies from 40 providers.
DR   DNASU; 20971; -.
DR   Ensembl; ENSMUST00000017153.4; ENSMUSP00000017153.4; ENSMUSG00000017009.4.
DR   GeneID; 20971; -.
DR   KEGG; mmu:20971; -.
DR   UCSC; uc008nuq.1; mouse.
DR   AGR; MGI:1349164; -.
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; WVPTEPK; -.
DR   OrthoDB; 4258425at2759; -.
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 78 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 286 other cell types or tissues.
DR   ExpressionAtlas; O35988; baseline and differential.
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:0016020; C:membrane; IEA:UniProtKB-SubCell.
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: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; SYNDECAN; 1.
DR   PANTHER; PTHR10915:SF3; SYNDECAN-4; 1.
DR   Pfam; PF01034; Syndecan; 1.
DR   SMART; SM00294; 4.1m; 1.
DR   PROSITE; PS00964; SYNDECAN; 1.
DR   Genevisible; O35988; MM.
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...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P34901"
FT   CARBOHYD        62
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P34901"
FT   CARBOHYD        64
FT                   /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P34901"
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
//