SDC4_RAT
ID SDC4_RAT Reviewed; 202 AA.
AC P34901;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Syndecan-4;
DE Short=SYND4;
DE AltName: Full=Ryudocan core protein;
DE Flags: Precursor;
GN Name=Sdc4; Synonyms=Synd4;
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], AND PARTIAL PROTEIN SEQUENCE.
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].
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).
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 -!- INTERACTION:
CC P34901; P04937: Fn1; NbExp=2; IntAct=EBI-1173182, EBI-6127274;
CC P34901; P05696: Prkca; NbExp=3; IntAct=EBI-1173182, EBI-935801;
CC P34901; P34900: Sdc2; NbExp=4; IntAct=EBI-1173182, EBI-1173032;
CC P34901; P34901: Sdc4; NbExp=3; IntAct=EBI-1173182, EBI-1173182;
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 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:P31431}.
CC -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
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DR EMBL; M81786; AAA73167.1; -; mRNA.
DR EMBL; S61868; AAB26725.1; -; mRNA.
DR PIR; A42410; A42410.
DR RefSeq; NP_036781.1; NM_012649.2.
DR PDB; 5A2P; X-ray; 2.50 A; E/F/G/H=195-202.
DR PDB; 5G1D; X-ray; 2.81 A; C/D=195-202.
DR PDBsum; 5A2P; -.
DR PDBsum; 5G1D; -.
DR AlphaFoldDB; P34901; -.
DR BMRB; P34901; -.
DR SMR; P34901; -.
DR BioGRID; 246895; 2.
DR IntAct; P34901; 7.
DR MINT; P34901; -.
DR STRING; 10116.ENSRNOP00000019386; -.
DR GlyGen; P34901; 3 sites.
DR iPTMnet; P34901; -.
DR PhosphoSitePlus; P34901; -.
DR PaxDb; P34901; -.
DR PRIDE; P34901; -.
DR Ensembl; ENSRNOT00000019386; ENSRNOP00000019386; ENSRNOG00000014297.
DR GeneID; 24771; -.
DR KEGG; rno:24771; -.
DR UCSC; RGD:3650; rat.
DR CTD; 6385; -.
DR RGD; 3650; Sdc4.
DR eggNOG; ENOG502S1SZ; Eukaryota.
DR GeneTree; ENSGT00940000160663; -.
DR HOGENOM; CLU_046599_3_0_1; -.
DR InParanoid; P34901; -.
DR OMA; GSWVPTE; -.
DR OrthoDB; 1507361at2759; -.
DR PhylomeDB; P34901; -.
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-975634; Retinoid metabolism and transport.
DR PRO; PR:P34901; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000014297; Expressed in kidney and 20 other tissues.
DR Genevisible; P34901; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0043034; C:costamere; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0001968; F:fibronectin binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005080; F:protein kinase C binding; IDA:RGD.
DR GO; GO:0070053; F:thrombospondin receptor activity; 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:0060122; P:inner ear receptor cell stereocilium organization; ISO:RGD.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:RGD.
DR GO; GO:0001843; P:neural tube closure; ISO: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:0051894; P:positive regulation of focal adhesion assembly; IMP:RGD.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:RGD.
DR GO; GO:0010762; P:regulation of fibroblast migration; ISO:RGD.
DR GO; GO:0001657; P:ureteric bud development; IEP:RGD.
DR GO; GO:0042060; P:wound healing; ISO:RGD.
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 3D-structure; Direct protein sequencing; Glycoprotein; Heparan sulfate;
KW Membrane; Proteoglycan; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..202
FT /note="Syndecan-4"
FT /id="PRO_0000033513"
FT TOPO_DOM 24..149
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 42..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..69
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..126
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:0000305"
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"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:5A2P"
SQ SEQUENCE 202 AA; 21962 MW; 5D9C8B3BF4C0D58A CRC64;
MAPVCLFAPL LLLLLGGFPV APGESIRETE VIDPQDLLEG RYFSGALPDD EDAGGLEQDS
DFELSGSGDL DDTEEPRTFP EVISPLVPLD NHIPENAQPG IRVPSEPKEL EENEVIPKRV
PSDVGDDDVS NKVSMSSTSQ GSNIFERTEV LAALIVGGVV GILFAVFLIL LLVYRMKKKD
EGSYDLGKKP IYKKAPTNEF YA
