ID   SDC4_PIG                Reviewed;         202 AA.
AC   Q8HZJ6;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Syndecan-4;
DE            Short=SYND4;
DE   Flags: Precursor;
GN   Name=SDC4;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Aortic endothelium;
RA   Ruehland C., Kresse H.;
RT   "Differences between heparan sulphate proteoglycans of porcine brain
RT   capillary and aortic endothelial cells.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
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. Interacts (via its
CC       cytoplasmic domain) with GIPC (via its PDZ domain). Interacts (via its
CC       cytoplasmic domain) with NUDT16L1 (By similarity).
CC       {ECO:0000250|UniProtKB:O35988, ECO:0000250|UniProtKB:P31431}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000255}. Secreted
CC       {ECO:0000250|UniProtKB:P31431}. Note=Shedding of the ectodomain
CC       produces a soluble form. {ECO:0000250|UniProtKB:P31431}.
CC   -!- PTM: Shedding, cleavage of the extracellular domain to release a
CC       soluble form, is enhanced by a number of factors such as heparanase,
CC       growth factor receptor action for example by thrombin or EGF.
CC       Physiological events such as stress or wound healing can activate the
CC       shedding. PMA-mediated shedding is inhibited by TIMP3 (By similarity).
CC       {ECO:0000250|UniProtKB:P31431}.
CC   -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
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DR   EMBL; AF548542; AAN59952.1; -; mRNA.
DR   RefSeq; NP_999449.1; NM_214284.1.
DR   AlphaFoldDB; Q8HZJ6; -.
DR   SMR; Q8HZJ6; -.
DR   STRING; 9823.ENSSSCP00000007885; -.
DR   PaxDb; Q8HZJ6; -.
DR   PRIDE; Q8HZJ6; -.
DR   Ensembl; ENSSSCT00040023680; ENSSSCP00040010013; ENSSSCG00040017528.
DR   Ensembl; ENSSSCT00070024682; ENSSSCP00070020431; ENSSSCG00070012642.
DR   GeneID; 397528; -.
DR   KEGG; ssc:397528; -.
DR   CTD; 6385; -.
DR   eggNOG; ENOG502S1SZ; Eukaryota.
DR   HOGENOM; CLU_046599_3_0_1; -.
DR   InParanoid; Q8HZJ6; -.
DR   OMA; GSWVPTE; -.
DR   OrthoDB; 1507361at2759; -.
DR   Reactome; R-SSC-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR   Reactome; R-SSC-2022928; HS-GAG biosynthesis.
DR   Reactome; R-SSC-2024096; HS-GAG degradation.
DR   Reactome; R-SSC-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-SSC-3000170; Syndecan interactions.
DR   Reactome; R-SSC-975634; Retinoid metabolism and transport.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Chromosome 17.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
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:0016477; P:cell migration; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Glycoprotein; Heparan sulfate; Membrane; Proteoglycan; Reference proteome;
KW   Secreted; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..202
FT                   /note="Syndecan-4"
FT                   /id="PRO_0000290108"
FT   TOPO_DOM        23..152
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        174..202
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          41..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        43
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        65
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   202 AA;  22081 MW;  107CA9BEE5673C2C CRC64;
     MASPRLLALL LLLVGAFNAA AAESIRETEV INPQDLLEGR YFSGDLPDDE DVGGPGQEPD
     DFEWSGSGDL EGPEDKHMLP EVTHPLVPLD NHIPERTGPG GRVPTEPKEL EENEVIPKRM
     SPFDGDEDVS NKVSMSSTAQ GSNIFERTEV LSALIVGGIV GILFAVFLVL LLVYRMKKKD
     EGSYDLGKKP IYKKAPTNEF YA