SGCB_MOUSE
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 03-AUG-2022, entry version 136.
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; 7.
DR CORUM; P82349; -.
DR STRING; 10090.ENSMUSP00000079937; -.
DR GlyConnect; 2154; 1 N-Linked glycan (1 site).
DR GlyGen; P82349; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P82349; -.
DR PhosphoSitePlus; P82349; -.
DR MaxQB; P82349; -.
DR PaxDb; P82349; -.
DR PeptideAtlas; P82349; -.
DR PRIDE; P82349; -.
DR ProteomicsDB; 261204; -.
DR Antibodypedia; 2557; 233 antibodies from 31 providers.
DR DNASU; 24051; -.
DR Ensembl; ENSMUST00000081170; ENSMUSP00000079937; ENSMUSG00000029156.
DR GeneID; 24051; -.
DR KEGG; mmu:24051; -.
DR UCSC; uc008xtb.1; mouse.
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; TFAFWTI; -.
DR OrthoDB; 1214843at2759; -.
DR PhylomeDB; P82349; -.
DR TreeFam; TF313538; -.
DR BioGRID-ORCS; 24051; 3 hits in 72 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 257 other tissues.
DR Genevisible; P82349; MM.
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:0005887; C:integral component of plasma membrane; TAS: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: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:0097084; P:vascular associated smooth muscle cell development; IMP:MGI.
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; 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
