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   27-MAR-2024, entry version 157.
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   GlyCosmos; P82350; 2 sites, No reported glycans.
DR   GlyGen; P82350; 3 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P82350; -.
DR   PhosphoSitePlus; P82350; -.
DR   PaxDb; 10090-ENSMUSP00000099451; -.
DR   PeptideAtlas; P82350; -.
DR   ProteomicsDB; 261203; -.
DR   Antibodypedia; 2323; 257 antibodies from 32 providers.
DR   DNASU; 20391; -.
DR   Ensembl; ENSMUST00000100551.11; ENSMUSP00000098118.5; ENSMUSG00000001508.16.
DR   Ensembl; ENSMUST00000103162.8; ENSMUSP00000099451.2; ENSMUSG00000001508.16.
DR   Ensembl; ENSMUST00000166320.8; ENSMUSP00000130617.2; ENSMUSG00000001508.16.
DR   GeneID; 20391; -.
DR   KEGG; mmu:20391; -.
DR   UCSC; uc007kzo.3; mouse.
DR   AGR; MGI:894698; -.
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; 5391218at2759; -.
DR   PhylomeDB; P82350; -.
DR   TreeFam; TF314655; -.
DR   BioGRID-ORCS; 20391; 3 hits in 77 CRISPR screens.
DR   PRO; PR:P82350; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P82350; Protein.
DR   Bgee; ENSMUSG00000001508; Expressed in hindlimb stylopod muscle and 94 other cell types or tissues.
DR   ExpressionAtlas; P82350; baseline and differential.
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: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; IPR006644; Cadg.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR008908; Sarcoglycan_alpha/epsilon.
DR   InterPro; IPR048347; Sarcoglycan_C.
DR   InterPro; IPR048346; Sarcoglycan_N.
DR   PANTHER; PTHR10132; ALPHA-/EPSILON-SARCOGLYCAN FAMILY MEMBER; 1.
DR   PANTHER; PTHR10132:SF16; ALPHA-SARCOGLYCAN; 1.
DR   Pfam; PF05510; Sarcoglycan_2; 1.
DR   Pfam; PF20989; Sarcoglycan_2_C; 1.
DR   SMART; SM00736; CADG; 1.
DR   SUPFAM; SSF49313; Cadherin-like; 1.
DR   Genevisible; P82350; MM.
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
//