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SGCG_CANLF
ID   SGCG_CANLF              Reviewed;         291 AA.
AC   Q8SQ72;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Gamma-sarcoglycan;
DE            Short=Gamma-SG;
GN   Name=SGCG;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11856878; DOI=10.1159/000048813;
RA   Conrad K., Deppe A., Neumann S., Breen M., Quignon P., Andre C., Brenig B.,
RA   Leeb T.;
RT   "Characterization and chromosome assignment of the canine gamma-sarcoglycan
RT   gene (SGCG) to CFA 25q21-->q23.";
RL   Cytogenet. Cell Genet. 94:186-189(2001).
CC   -!- FUNCTION: Component of the sarcoglycan complex, a subcomplex of the
CC       dystrophin-glycoprotein complex which forms a link between the F-actin
CC       cytoskeleton and the extracellular matrix. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the syntrophin SNTA1. Cross-link to form 2
CC       major subcomplexes: one consisting of SGCB, SGCD and SGCG and the other
CC       consisting of SGCB and SGCD. The association between SGCB and SGCG is
CC       particularly strong while SGCA is loosely associated with the other
CC       sarcoglycans. Interacts with FLNC (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
CC       {ECO:0000250}.
CC   -!- PTM: Disulfide bonds are present. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sarcoglycan beta/delta/gamma/zeta family.
CC       {ECO:0000305}.
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DR   EMBL; AJ306895; CAC88127.1; -; Genomic_DNA.
DR   EMBL; AJ306896; CAC88127.1; JOINED; Genomic_DNA.
DR   EMBL; AJ306897; CAC88127.1; JOINED; Genomic_DNA.
DR   EMBL; AJ306898; CAC88127.1; JOINED; Genomic_DNA.
DR   EMBL; AJ306899; CAC88127.1; JOINED; Genomic_DNA.
DR   EMBL; AJ306900; CAC88127.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_001014298.1; NM_001014276.2.
DR   RefSeq; XP_005635441.1; XM_005635384.2.
DR   AlphaFoldDB; Q8SQ72; -.
DR   STRING; 9615.ENSCAFP00000010630; -.
DR   PaxDb; Q8SQ72; -.
DR   PRIDE; Q8SQ72; -.
DR   Ensembl; ENSCAFT00030019974; ENSCAFP00030017408; ENSCAFG00030010748.
DR   Ensembl; ENSCAFT00040043720; ENSCAFP00040038148; ENSCAFG00040023502.
DR   GeneID; 486043; -.
DR   KEGG; cfa:486043; -.
DR   CTD; 6445; -.
DR   eggNOG; KOG3950; Eukaryota.
DR   HOGENOM; CLU_043450_0_0_1; -.
DR   InParanoid; Q8SQ72; -.
DR   OMA; SHNDNML; -.
DR   OrthoDB; 1407024at2759; -.
DR   TreeFam; TF313538; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016012; C:sarcoglycan complex; IBA:GO_Central.
DR   GO; GO:0042383; C:sarcolemma; IBA:GO_Central.
DR   GO; GO:0048738; P:cardiac muscle tissue development; IBA:GO_Central.
DR   GO; GO:0060047; P:heart contraction; IBA:GO_Central.
DR   InterPro; IPR006875; Sarcoglycan.
DR   InterPro; IPR039972; Sarcoglycan_gamma/delta/zeta.
DR   InterPro; IPR027660; SGCG.
DR   PANTHER; PTHR12939; PTHR12939; 1.
DR   PANTHER; PTHR12939:SF4; PTHR12939:SF4; 1.
DR   Pfam; PF04790; Sarcoglycan_1; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cytoplasm; Cytoskeleton; Disulfide bond; Glycoprotein;
KW   Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..291
FT                   /note="Gamma-sarcoglycan"
FT                   /id="PRO_0000289584"
FT   TRANSMEM        38..58
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..291
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        265..290
FT                   /evidence="ECO:0000255"
FT   DISULFID        267..283
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   291 AA;  32398 MW;  E549A5FEF5A22AA9 CRC64;
     MVREQYTTTT EGTHIQRPEN QCVYKIGIYG WRKRCLYLFV LLLLIILLVN FALTIWILKV
     MWFSPTGMGH LRVTKDGLRL EGESEFLFPL YAKEIHSRVD SSLLLQSTQN VTVNARNSEG
     EVTGRLKVGP KMVEVQSQQF QINSKDGKPL FTVDEKEVVV GTDKLRVTGP EGALFEHSVE
     TPLVRADPFQ DLRLESPTRS LSMDAPKGVH IKAHAGKIEA LSQMDIIFQS SDGMLVLDAE
     TVCLPKLVQG TQGPAGSSQR LYEICVCPDG KLYLSVAGVG TTCHEHSHIC L
 
 
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