ID   SGCB_MESAU              Reviewed;         320 AA.
AC   Q60538; O08596; O09094; O09152; Q60532;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Beta-sarcoglycan;
DE            Short=Beta-SG;
DE   AltName: Full=43 kDa dystrophin-associated glycoprotein;
DE            Short=43DAG;
GN   Name=SGCB;
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 [MRNA].
RC   STRAIN=ACN(A), and BIO14.6; TISSUE=Heart ventricle;
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 (By similarity).
CC       {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; D83652; BAA12026.1; -; mRNA.
DR   EMBL; U63894; AAB52394.1; -; mRNA.
DR   EMBL; U49791; AAC52620.1; -; mRNA.
DR   PIR; JC5540; JC5540.
DR   RefSeq; NP_001268603.1; NM_001281674.1.
DR   AlphaFoldDB; Q60538; -.
DR   STRING; 10036.XP_005139378.1; -.
DR   GeneID; 101831878; -.
DR   CTD; 6443; -.
DR   eggNOG; ENOG502QUW4; Eukaryota.
DR   OrthoDB; 1214843at2759; -.
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   GO; GO:0007517; P:muscle organ development; IEA:InterPro.
DR   InterPro; IPR006875; Sarcoglycan.
DR   InterPro; IPR027659; Sgcb.
DR   PANTHER; PTHR21142; PTHR21142; 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..320
FT                   /note="Beta-sarcoglycan"
FT                   /id="PRO_0000175243"
FT   TOPO_DOM        1..67
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        89..320
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        290..316
FT                   /evidence="ECO:0000255"
FT   DISULFID        292..309
FT                   /evidence="ECO:0000255"
FT   CONFLICT        279
FT                   /note="S -> L (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   320 AA;  34847 MW;  72E8DF9745076955 CRC64;
     MAAAAAAAAA TEQQSSNGPV KKSMREKAVE RRNVNKEHNS NFKAGYIPID EDRLHKTGLR
     GRKGNLAICV IVLLFILAVI NLLITLVIWA VIRIGPNGCD SMEFHESGLL RFKQVSDMGV
     IHPLYKSTVG GRRNENLVIT GNNQPIVFQQ GTTKLSVEKN KTSITSDIGM QFFDPRTQNI
     LFSTDYETHE FHLPSGVKSL NVQKASTERI TSNATSDLNI KVDGRAIVRG NEGVFIMGKT
     IEFHMGGNVE LKAENSIILN GTVMVSPTRL PSSSSGDQSG GGDWVRYKLC MCADGTLFKV
     QVTGHNMGCQ VADNPCGNTH