ID   SGCB_MOUSE              Reviewed;         320 AA.
AC   P82349; Q3TEU9;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 144.
DE   RecName: Full=Beta-sarcoglycan;
DE            Short=Beta-SG;
DE   AltName: Full=43 kDa dystrophin-associated glycoprotein;
DE            Short=43DAG;
GN   Name=Sgcb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10678176; DOI=10.1016/s1097-2765(00)80410-4;
RA   Durbeej M., Campbell K.P.;
RT   "Disruption of the beta-sarcoglycan gene reveals pathogenetic complexity of
RT   limb-girdle muscular dystrophy type 2E.";
RL   Mol. Cell 5:141-151(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=10448073; DOI=10.1006/bbrc.1999.1163;
RA   Noguchi S., Wakabayashi E., Imamura M., Yoshida M., Ozawa E.;
RT   "Developmental expression of sarcoglycan gene products in cultured
RT   myocytes.";
RL   Biochem. Biophys. Res. Commun. 262:88-93(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   SUBCELLULAR LOCATION, SUBUNIT, AND DISULFIDE BONDS.
RX   PubMed=9864373; DOI=10.1083/jcb.143.7.2033;
RA   Chan Y.-M., Boennemann C.G., Lidov H.G.W., Kunkel L.M.;
RT   "Molecular organization of sarcoglycan complex in mouse myotubes in
RT   culture.";
RL   J. Cell Biol. 143:2033-2044(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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.
CC       {ECO:0000269|PubMed:9864373}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC       {ECO:0000269|PubMed:9864373}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:9864373}. Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:9864373}.
CC   -!- TISSUE SPECIFICITY: Most strongly expressed in skeletal and heart
CC       muscle. Also detected in proliferating myoblasts.
CC   -!- PTM: Disulfide bonds are present.
CC   -!- SIMILARITY: Belongs to the sarcoglycan beta/delta/gamma/zeta family.
CC       {ECO:0000305}.
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DR   EMBL; AF169288; AAF28458.1; -; Genomic_DNA.
DR   EMBL; AB024921; BAA83492.1; -; mRNA.
DR   EMBL; AK014381; BAB29310.1; -; mRNA.
DR   EMBL; AK132306; BAE21093.1; -; mRNA.
DR   EMBL; AK169403; BAE41149.1; -; mRNA.
DR   EMBL; BC052349; AAH52349.1; -; mRNA.
DR   CCDS; CCDS19344.1; -.
DR   RefSeq; NP_036020.1; NM_011890.4.
DR   AlphaFoldDB; P82349; -.
DR   BioGRID; 204864; 8.
DR   CORUM; P82349; -.
DR   STRING; 10090.ENSMUSP00000079937; -.
DR   GlyConnect; 2154; 1 N-Linked glycan (1 site).
DR   GlyCosmos; P82349; 3 sites, 1 glycan.
DR   GlyGen; P82349; 3 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; P82349; -.
DR   PhosphoSitePlus; P82349; -.
DR   MaxQB; P82349; -.
DR   PaxDb; 10090-ENSMUSP00000079937; -.
DR   PeptideAtlas; P82349; -.
DR   ProteomicsDB; 261204; -.
DR   Pumba; P82349; -.
DR   Antibodypedia; 2557; 258 antibodies from 31 providers.
DR   DNASU; 24051; -.
DR   Ensembl; ENSMUST00000081170.9; ENSMUSP00000079937.8; ENSMUSG00000029156.12.
DR   GeneID; 24051; -.
DR   KEGG; mmu:24051; -.
DR   UCSC; uc008xtb.1; mouse.
DR   AGR; MGI:1346523; -.
DR   CTD; 6443; -.
DR   MGI; MGI:1346523; Sgcb.
DR   VEuPathDB; HostDB:ENSMUSG00000029156; -.
DR   eggNOG; ENOG502QUW4; Eukaryota.
DR   GeneTree; ENSGT00390000008110; -.
DR   HOGENOM; CLU_066515_1_0_1; -.
DR   InParanoid; P82349; -.
DR   OMA; KGVQGME; -.
DR   OrthoDB; 3107632at2759; -.
DR   PhylomeDB; P82349; -.
DR   TreeFam; TF313538; -.
DR   BioGRID-ORCS; 24051; 3 hits in 77 CRISPR screens.
DR   ChiTaRS; Sgcb; mouse.
DR   PRO; PR:P82349; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; P82349; Protein.
DR   Bgee; ENSMUSG00000029156; Expressed in triceps brachii and 259 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0016011; C:dystroglycan complex; IDA:MGI.
DR   GO; GO:0016010; C:dystrophin-associated glycoprotein complex; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0016012; C:sarcoglycan complex; IDA:MGI.
DR   GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR   GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI.
DR   GO; GO:0010467; P:gene expression; IMP:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0044381; P:glucose import in response to insulin stimulus; IMP:MGI.
DR   GO; GO:0061024; P:membrane organization; TAS:MGI.
DR   GO; GO:0055001; P:muscle cell development; IMP:MGI.
DR   GO; GO:0007517; P:muscle organ development; IEA:InterPro.
DR   GO; GO:0009749; P:response to glucose; IMP:MGI.
DR   GO; GO:0097084; P:vascular associated smooth muscle cell development; IMP:MGI.
DR   InterPro; IPR006875; Sarcoglycan.
DR   InterPro; IPR027659; Sgcb.
DR   PANTHER; PTHR21142:SF2; BETA-SARCOGLYCAN; 1.
DR   PANTHER; PTHR21142; SARCOGLYCANS; 1.
DR   Pfam; PF04790; Sarcoglycan_1; 1.
DR   Genevisible; P82349; MM.
PE   1: Evidence at protein 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_0000175244"
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"
SQ   SEQUENCE   320 AA;  34873 MW;  AFA5E28496003618 CRC64;
     MAAAAAAAAA TEQQGSNGPV KKSMREKAVE RRNVNKEHNS NFKAGYIPID EDRLHKTGLR
     GRKGNLAICV IVLLFILAVI NLLITLVIWA VIRIGPNGCD SMEFHESGLL RFKQVSDMGV
     IHPLYKSTVG GRRNENLVIT GNNQPIVFQQ GTTKLSVEKN KTSITSDIGM QFFDPRTHNI
     LFSTDYETHE FHLPSGVKSL NVQKASTERI TSNATSDLNI KVDGRAIVRG NEGVFIMGKT
     IEFHMGGDVE LKAENSIILN GTVMVSPTRL PSSSSGDQSG SGDWVRYKLC MCADGTLFKV
     QVTGHNMGCQ VSDNPCGNTH
//