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SDC4_CHICK
ID   SDC4_CHICK              Reviewed;         197 AA.
AC   P49416;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Syndecan-4;
DE   Flags: Precursor;
GN   Name=SDC4;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8276871; DOI=10.1016/s0021-9258(17)42405-7;
RA   Baciu P.C., Acaster C., Goetinck P.F.;
RT   "Molecular cloning and genomic organization of chicken syndecan-4.";
RL   J. Biol. Chem. 269:696-703(1994).
RN   [2]
RP   INTERACTION WITH SDOS.
RC   TISSUE=Embryo;
RX   PubMed=10633082; DOI=10.1242/jcs.113.2.315;
RA   Baciu P.C., Saoncella S., Lee S.H., Denhez F., Leuthardt D., Goetinck P.F.;
RT   "Syndesmos, a protein that interacts with the cytoplasmic domain of
RT   syndecan-4, mediates cell spreading and actin cytoskeletal organization.";
RL   J. Cell Sci. 113:315-324(2000).
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: Interacts with SDOS. {ECO:0000269|PubMed:10633082}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000305}.
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DR   EMBL; L23940; AAA16479.1; -; Unassigned_DNA.
DR   PIR; A53126; A53126.
DR   RefSeq; NP_001007870.1; NM_001007869.1.
DR   AlphaFoldDB; P49416; -.
DR   BMRB; P49416; -.
DR   SMR; P49416; -.
DR   STRING; 9031.ENSGALP00000006255; -.
DR   PaxDb; P49416; -.
DR   Ensembl; ENSGALT00000093118; ENSGALP00000070840; ENSGALG00000003932.
DR   GeneID; 419184; -.
DR   KEGG; gga:419184; -.
DR   CTD; 6385; -.
DR   VEuPathDB; HostDB:geneid_419184; -.
DR   eggNOG; ENOG502S1SZ; Eukaryota.
DR   GeneTree; ENSGT00940000160663; -.
DR   HOGENOM; CLU_046599_3_0_1; -.
DR   InParanoid; P49416; -.
DR   OMA; GSWVPTE; -.
DR   OrthoDB; 1507361at2759; -.
DR   PhylomeDB; P49416; -.
DR   TreeFam; TF320463; -.
DR   Reactome; R-GGA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR   Reactome; R-GGA-2022928; HS-GAG biosynthesis.
DR   Reactome; R-GGA-2024096; HS-GAG degradation.
DR   Reactome; R-GGA-3000170; Syndecan interactions.
DR   PRO; PR:P49416; -.
DR   Proteomes; UP000000539; Chromosome 20.
DR   Bgee; ENSGALG00000003932; Expressed in colon and 13 other tissues.
DR   ExpressionAtlas; P49416; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090630; P:activation of GTPase activity; ISS:AgBase.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:1902725; P:negative regulation of satellite cell differentiation; ISS:AgBase.
DR   GO; GO:1902723; P:negative regulation of skeletal muscle satellite cell proliferation; ISS:AgBase.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:AgBase.
DR   GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:AgBase.
DR   GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISS:AgBase.
DR   GO; GO:1902766; P:skeletal muscle satellite cell migration; ISS:AgBase.
DR   GO; GO:0044319; P:wound healing, spreading of cells; ISS:AgBase.
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   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..197
FT                   /note="Syndecan-4"
FT                   /id="PRO_0000033510"
FT   TOPO_DOM        20..147
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        169..197
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        38
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
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   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   197 AA;  21502 MW;  88F1C7E188A99848 CRC64;
     MPLPRAAFLL GLLLAAAAAE SVRETETMDA RWLDNVGSGD LPDDEDIGEF TPHLTSDEFD
     IDDTSGSGDY SDYDDAIYLT TVDTPAISDN YIPGDTERKM EGEKKNTMLD NEIIPDKASP
     VEANLSNKIS MASTANSSIF ERTEVLTALI AGGAVGLLFA VFLILLLVYR MKKKDEGSYD
     LGKKPIYKKA PTNEFYA
 
 
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