SGCD_MESAU
ID SGCD_MESAU Reviewed; 289 AA.
AC P97281; O09073; O09090;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Delta-sarcoglycan;
DE Short=Delta-SG;
DE AltName: Full=35 kDa dystrophin-associated glycoprotein;
DE Short=35DAG;
GN Name=SGCD;
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], AND DISEASE.
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 [MRNA], AND DISEASE.
RC STRAIN=F1B;
RX PubMed=9097966; DOI=10.1093/hmg/6.4.601;
RA Nigro V., Okazaki Y., Belsito A., Piluso G., Matsuda Y., Politano L.,
RA Nigro G., Ventura C., Abbondanza C., Molinari A.M., Acampora D.,
RA Nishimura M., Hayashizaki Y., Puca G.A.;
RT "Identification of the Syrian hamster cardiomyopathy gene.";
RL Hum. Mol. Genet. 6:601-607(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RA Duclos F., Lee J.C., Coral R., Campbell K.P.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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: Interacts with FLNC and DAG1. Cross-link to form 2 major
CC 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 (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 -!- TISSUE SPECIFICITY: Most strongly expressed in skeletal and heart
CC muscle. Also detected in stomach and uterus muscle.
CC -!- PTM: Disulfide bonds are present. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in SGCD are the cause of cardiomyopathy, an
CC autosomal recessive disease which is characterized by progressive
CC myocardial necrosis and heart failure leading to premature death. A
CC large portion of the 5'-end of the gene, including the first exon, is
CC deleted and an alternative promoter and first exon are used.
CC {ECO:0000269|PubMed:9097966, ECO:0000269|PubMed:9391120}.
CC -!- SIMILARITY: Belongs to the sarcoglycan beta/delta/gamma/zeta family.
CC {ECO:0000305}.
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DR EMBL; Y08838; CAA70066.1; -; mRNA.
DR EMBL; AB001508; BAA19402.1; -; mRNA.
DR EMBL; U93575; AAB51725.1; -; mRNA.
DR RefSeq; NP_001268547.1; NM_001281618.1.
DR AlphaFoldDB; P97281; -.
DR SMR; P97281; -.
DR GeneID; 101837953; -.
DR CTD; 6444; -.
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; IPR027661; SGCD.
DR PANTHER; PTHR12939; PTHR12939; 1.
DR PANTHER; PTHR12939:SF6; PTHR12939:SF6; 1.
DR Pfam; PF04790; Sarcoglycan_1; 1.
PE 2: Evidence at transcript level;
KW Cardiomyopathy; Cell membrane; Cytoplasm; Cytoskeleton; Disulfide bond;
KW Glycoprotein; Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..289
FT /note="Delta-sarcoglycan"
FT /id="PRO_0000175246"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..289
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 263..288
FT /evidence="ECO:0000255"
FT DISULFID 265..281
FT /evidence="ECO:0000255"
SQ SEQUENCE 289 AA; 32162 MW; A16A2038DC1BD4B8 CRC64;
MPQEQYSHHR STMPSSEGPH IYKVGIYGWR KRCLYFFVLL LMILILVNLA MTIWILKVMN
FTIDGMGNLR ITEKGLKLEG DSEFLQPLYA KEIQSRPGNA LYFKSARNVT VNILNDQTKV
LTRLVTGPKA VEAYGKKFEV KTVSGKLLFS ADDNEVVVGA ERLRVLGAEG TVFPKSIETP
NVRADPFKEL RLESPTRSLV MEAPKGVEIN AEAGNMEATC RSELRLESKD GEIKLDAAKI
KLPRLPRGSY TPTGTRQKVF EVCICANGRL FLSQAGTGST CQINTSVCL
