SGCG_MESAU
ID SGCG_MESAU Reviewed; 291 AA.
AC O08597; O09095; O09153; Q64265;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Gamma-sarcoglycan;
DE Short=Gamma-SG;
DE AltName: Full=35 kDa dystrophin-associated glycoprotein;
DE Short=35DAG;
GN Name=SGCG;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Syrian; TISSUE=Heart muscle;
RX PubMed=9391120; DOI=10.1073/pnas.94.25.13873;
RA Sakamoto A., Ono K., Abe M., Jasmin G., Eki T., Murakami Y., Masaki T.,
RA Toyo-oka T., Hanaoka F.;
RT "Both hypertrophic and dilated cardiomyopathies are caused by mutation of
RT the same gene, delta-sarcoglycan, in hamster: an animal model of disrupted
RT dystrophin-associated glycoprotein complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13873-13878(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ACN(A), and BIO14.6;
RX PubMed=9057973; DOI=10.1248/bpb.20.134;
RA Hanada H., Yoshida T., Pan Y., Iwata Y., Nishimura M., Shigekawa M.;
RT "mRNA expression and cDNA sequences of beta- and gamma-sarcoglycans are
RT normal in cardiomyopathic hamster heart.";
RL Biol. Pharm. Bull. 20:134-137(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8628353; DOI=10.1056/nejm199606133342417;
RA McNally E.M., Bonnemann C.G., Bhattacharya S., Kunkel L.M.;
RT "Deficiency of adhalin in a patient with muscular dystrophy and
RT cardiomyopathy.";
RL N. Engl. J. Med. 334:1610-1611(1996).
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.
CC -!- SUBUNIT: Cross-link to form 2 major subcomplexes: one consisting of
CC SGCB, SGCD and SGCG and the other consisting of SGCB and SGCD. The
CC association between SGCB and SGCG is particularly strong while SGCA is
CC loosely associated with the other sarcoglycans. Interacts with the
CC syntrophin SNTA1 and 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 -!- SIMILARITY: Belongs to the sarcoglycan beta/delta/gamma/zeta family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D83653; BAA12027.1; -; mRNA.
DR EMBL; U63895; AAB52395.1; -; Genomic_DNA.
DR EMBL; U49792; AAC52621.1; -; mRNA.
DR PIR; JC5541; JC5541.
DR RefSeq; NP_001268320.1; NM_001281391.1.
DR AlphaFoldDB; O08597; -.
DR STRING; 10036.XP_005075344.1; -.
DR PRIDE; O08597; -.
DR GeneID; 101825067; -.
DR CTD; 6445; -.
DR eggNOG; KOG3950; Eukaryota.
DR OrthoDB; 1407024at2759; -.
DR Proteomes; UP000189706; 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; IEA:InterPro.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
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_0000175249"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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; 32342 MW; 6E8BD2CDD7328714 CRC64;
MAREQYTTVT EGTHIERPES QLVHRIGIYG WRKRCLYLFV LLLLIILVVN LALTIWILKV
MWFSPIGMGH LHVTQDGLRL EGESEFLFPL YVKEIRSRVD SSLLLQSTQN VTVNARNSEG
EVTGRVKVGA QMVEVQSQHF QIRSEDGKPL FTAEERGVMV DTGRLRVTGP EGAIFEHSVE
TPLVRADPFE DLRLESPTRS LSMDAPRGVH IKAHTGKMEA LSQMDIILQS SDGVLVLDAE
TVGLPELEQG TPGPSGSSKG FYEICVCPDG KLYLSAADEA TTCEEHSHIC L
