ID   SGCB_RABIT              Reviewed;         318 AA.
AC   Q28635;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Beta-sarcoglycan;
DE            Short=Beta-SG;
GN   Name=SGCB;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 161-174.
RC   TISSUE=Skeletal muscle;
RX   PubMed=7581449; DOI=10.1038/ng1195-266;
RA   Boennemann C.G., Modi R., Noguchi S., Mizuno Y., Yoshida M., Gussoni E.,
RA   McNally E.M., Duggan D.J., Angelini C., Hoffman E.P., Ozawa E.,
RA   Kunkel L.M.;
RT   "Beta-sarcoglycan (A3b) mutations cause autosomal recessive muscular
RT   dystrophy with loss of the sarcoglycan complex.";
RL   Nat. Genet. 11:266-273(1995).
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: 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; U31117; AAA87035.1; -; mRNA.
DR   RefSeq; NP_001075825.1; NM_001082356.1.
DR   AlphaFoldDB; Q28635; -.
DR   CORUM; Q28635; -.
DR   STRING; 9986.ENSOCUP00000004745; -.
DR   PRIDE; Q28635; -.
DR   Ensembl; ENSOCUT00000005471; ENSOCUP00000004745; ENSOCUG00000005474.
DR   GeneID; 100009208; -.
DR   KEGG; ocu:100009208; -.
DR   CTD; 6443; -.
DR   eggNOG; ENOG502QUW4; Eukaryota.
DR   GeneTree; ENSGT00390000008110; -.
DR   HOGENOM; CLU_066515_1_0_1; -.
DR   InParanoid; Q28635; -.
DR   OMA; TFAFWTI; -.
DR   OrthoDB; 1214843at2759; -.
DR   Proteomes; UP000001811; Chromosome 2.
DR   Bgee; ENSOCUG00000005474; Expressed in skeletal muscle tissue and 17 other tissues.
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   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..318
FT                   /note="Beta-sarcoglycan"
FT                   /id="PRO_0000326144"
FT   TOPO_DOM        1..65
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..318
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        288..314
FT                   /evidence="ECO:0000255"
FT   DISULFID        290..307
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   318 AA;  34726 MW;  081652274326B2D8 CRC64;
     MAAAAAAAAE QQSSNGPVKK SMREKAVERR NVNKEHNSNF KAGYIPIDED RLHKTGLRGR
     KGNLAICVIV LLFLLAVINL IITLVIWAVI RIGPNGCDSM EFHESGLLRF KQVSDMGVIH
     PLYKSTVGGR RNENLVITGN NQPIVFQQGT TKLSVEKNKT SITSDIGMQF FDPRTQNILF
     STDYETHEFH LPSGVKSLNV QKASTERITS NATSDLNIKV DGRAIVRGNE GVFIMGKTIE
     FHMGGNMELK AENSIILNGT VMVSTTRLPS SSSADQLGGG DWVRYKLCMC ADGTLFKVQV
     TGQNVGCQVS DNPCGNTH