SGCA_MOUSE
ID SGCA_MOUSE Reviewed; 387 AA.
AC P82350; O35311; O88490;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Alpha-sarcoglycan;
DE Short=Alpha-SG;
DE AltName: Full=50 kDa dystrophin-associated glycoprotein;
DE Short=50DAG;
DE AltName: Full=Adhalin;
DE Flags: Precursor;
GN Name=Sgca;
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 [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=FVB/N; TISSUE=Myoblast;
RX PubMed=9196068; DOI=10.1006/bbrc.1997.6757;
RA Liu L., Vachon P.H., Kuang W., Xu H., Wewer U.M., Kylsten P., Engvall E.;
RT "Mouse adhalin: primary structure and expression during late stages of
RT muscle differentiation in vitro.";
RL Biochem. Biophys. Res. Commun. 235:227-235(1997).
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.
RC STRAIN=129/Sv;
RA Duclos F., Straub V., Moore S., Hrstka R., Crosbie R.H., Durbeej M.,
RA Lebakken C.S., Holt K.H., Lim L.E., Ettinger A., Sanes J.R., Davidson B.L.,
RA Williamson R., Campbell K.P.;
RT "Alpha-sarcoglycan-deficient mice as an animal model for autosomal
RT recessive limb-girdle muscular dystrophy.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [5]
RP INTERACTION WITH SNTA1.
RX PubMed=7547961; DOI=10.1021/bi00038a014;
RA Madhavan R., Jarrett H.W.;
RT "Interactions between dystrophin glycoprotein complex proteins.";
RL Biochemistry 34:12204-12209(1995).
RN [6]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION BY
RP 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. Interacts with the
CC syntrophin SNTA1. {ECO:0000269|PubMed:7547961,
CC ECO:0000269|PubMed:9864373}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:9864373}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:9864373}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9864373}.
CC -!- TISSUE SPECIFICITY: Striated muscle, both skeletal and cardiac.
CC {ECO:0000269|PubMed:9196068}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, expression begins at day 14 and
CC coincides with the onset of primary myogenesis.
CC {ECO:0000269|PubMed:9196068}.
CC -!- SIMILARITY: Belongs to the sarcoglycan alpha/epsilon family.
CC {ECO:0000305}.
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DR EMBL; AF019564; AAB70754.1; -; mRNA.
DR EMBL; AB024920; BAA83491.1; -; mRNA.
DR EMBL; AF064081; AAC33447.1; -; Genomic_DNA.
DR EMBL; AK075915; BAC36051.1; -; mRNA.
DR CCDS; CCDS25266.1; -.
DR PIR; JC5556; JC5556.
DR RefSeq; NP_033187.1; NM_009161.4.
DR RefSeq; XP_011247138.1; XM_011248836.2.
DR AlphaFoldDB; P82350; -.
DR BioGRID; 203195; 9.
DR CORUM; P82350; -.
DR IntAct; P82350; 2.
DR STRING; 10090.ENSMUSP00000099451; -.
DR GlyGen; P82350; 2 sites.
DR iPTMnet; P82350; -.
DR PhosphoSitePlus; P82350; -.
DR PaxDb; P82350; -.
DR PeptideAtlas; P82350; -.
DR PRIDE; P82350; -.
DR ProteomicsDB; 261203; -.
DR Antibodypedia; 2323; 221 antibodies from 32 providers.
DR DNASU; 20391; -.
DR Ensembl; ENSMUST00000100551; ENSMUSP00000098118; ENSMUSG00000001508.
DR Ensembl; ENSMUST00000103162; ENSMUSP00000099451; ENSMUSG00000001508.
DR Ensembl; ENSMUST00000166320; ENSMUSP00000130617; ENSMUSG00000001508.
DR GeneID; 20391; -.
DR KEGG; mmu:20391; -.
DR UCSC; uc007kzo.3; mouse.
DR CTD; 6442; -.
DR MGI; MGI:894698; Sgca.
DR VEuPathDB; HostDB:ENSMUSG00000001508; -.
DR eggNOG; KOG4482; Eukaryota.
DR GeneTree; ENSGT00390000005672; -.
DR HOGENOM; CLU_053258_0_1_1; -.
DR InParanoid; P82350; -.
DR OMA; VGSEQYF; -.
DR OrthoDB; 534519at2759; -.
DR PhylomeDB; P82350; -.
DR TreeFam; TF314655; -.
DR BioGRID-ORCS; 20391; 3 hits in 72 CRISPR screens.
DR PRO; PR:P82350; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P82350; protein.
DR Bgee; ENSMUSG00000001508; Expressed in hindlimb stylopod muscle and 92 other tissues.
DR ExpressionAtlas; P82350; baseline and differential.
DR Genevisible; P82350; MM.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
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:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0045121; C:membrane raft; IDA: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:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0061024; P:membrane organization; TAS:MGI.
DR GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; IEA:Ensembl.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IEA:Ensembl.
DR InterPro; IPR028658; Alpha-SG.
DR InterPro; IPR006644; Cadg.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR008908; Sarcoglycan_alpha/epsilon.
DR PANTHER; PTHR10132; PTHR10132; 1.
DR PANTHER; PTHR10132:SF16; PTHR10132:SF16; 1.
DR Pfam; PF05510; Sarcoglycan_2; 1.
DR SMART; SM00736; CADG; 1.
DR SUPFAM; SSF49313; SSF49313; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Cytoskeleton; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..387
FT /note="Alpha-sarcoglycan"
FT /id="PRO_0000031675"
FT TOPO_DOM 24..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 19
FT /note="R -> K (in Ref. 1; AAB70754)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="L -> V (in Ref. 1; AAB70754)"
FT /evidence="ECO:0000305"
FT CONFLICT 149..150
FT /note="LP -> VS (in Ref. 1; AAB70754)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 43287 MW; 7C3D98A853D04591 CRC64;
MAAAVTWIPL LAGLLAGLRD TKAQQTTLHL LVGRVFVHPL EHATFLRLPE HVAVPPTVRL
TYHAHLQGHP DLPRWLHYTQ RSPYNPGFLY GSPTPEDRGY QVIEVTAYNR DSFDTTRQRL
LLLIGDPEGP RLPYQAEFLV RSHDVEEVLP TTPANRFLTA LGGLWEPGEL QLLNITSALD
RGGRVPLPIE GRKEGVYIKV GSATPFSTCL KMVASPDSYA RCAQGQPPLL SCYDTLAPHF
RVDWCNVSLV DKSVPEPLDE VPTPGDGILE HDPFFCPPTE ATDRDFLTDA LVTLLVPLLV
ALLLTLLLAY IMCFRREGRL KRDMATSDIQ MFHHCSIHGN TEELRQMAAS REVPRPLSTL
PMFNVRTGER LPPRVDSAQM PLILDQH
