ID   SGCA_MESAU              Reviewed;         387 AA.
AC   Q64255;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 97.
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   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Syrian; TISSUE=Heart muscle;
RX   PubMed=9391120; DOI=10.1073/pnas.94.25.13873;
RA   Sakamoto A., Ono K., Abe M., Jasmin G., Eki T., Murakami Y., Masaki T.,
RA   Toyo-oka T., Hanaoka F.;
RT   "Both hypertrophic and dilated cardiomyopathies are caused by mutation of
RT   the same gene, delta-sarcoglycan, in hamster: an animal model of disrupted
RT   dystrophin-associated glycoprotein complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:13873-13878(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=F1B; TISSUE=Skeletal muscle;
RX   PubMed=7758576; DOI=10.1016/0014-5793(95)00395-p;
RA   Roberds S.L., Campbell K.P.;
RT   "Adhalin mRNA and cDNA sequence are normal in the cardiomyopathic
RT   hamster.";
RL   FEBS Lett. 364:245-249(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.
CC   -!- SUBUNIT: Interacts with the syntrophin SNTA1. Cross-link to form 2
CC       major subcomplexes: one consisting of SGCB, SGCD and SGCG and the other
CC       consisting of SGCB and SGCD. The association between SGCB and SGCG is
CC       particularly strong while SGCA is loosely associated with the other
CC       sarcoglycans (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Single-
CC       pass type I membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in skeletal and heart muscle.
CC   -!- SIMILARITY: Belongs to the sarcoglycan alpha/epsilon family.
CC       {ECO:0000305}.
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DR   EMBL; D83651; BAA12025.1; -; mRNA.
DR   EMBL; U21677; AAA81645.1; -; mRNA.
DR   PIR; I48201; I48201.
DR   RefSeq; NP_001268592.1; NM_001281663.1.
DR   AlphaFoldDB; Q64255; -.
DR   SMR; Q64255; -.
DR   STRING; 10036.XP_005075909.1; -.
DR   GeneID; 101822397; -.
DR   CTD; 6442; -.
DR   eggNOG; KOG4482; Eukaryota.
DR   OrthoDB; 534519at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
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:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0016012; C:sarcoglycan complex; IEA:Ensembl.
DR   GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR028658; Alpha-SG.
DR   InterPro; IPR006644; Cadg.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
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   2: Evidence at transcript 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_0000031674"
FT   TOPO_DOM        24..290
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        312..387
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         377
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P82350"
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"
SQ   SEQUENCE   387 AA;  43326 MW;  D8599C0FAF646C3F CRC64;
     MAATLTWILL FVGLLAGLRD TKAQQTTLYP LVGRVFVHPL EHATFLRLPE HIAVPPTVRL
     TYQAHLQGHP DLPRWLRYTQ RSPYSPGFLY GTPTPEDRGR QVIEVTAYNR DSFDTTRQRL
     LLLIEDPEGP RLPYQAEFLV RSHDVEEVLP STPANRFLTA LGGLWELGEL QLLNITSALD
     RGGRVPLPIE GRKEGVYIKV GSATPFSTCL KMVASPDSYA RCAQGQPPLL SCYDSLAPHF
     RVDWCNVSLV DKSVPEPLDE VPTPGDGILE HDPFFCPPTE ATGRDFLADA LVTLLVPLLV
     ALLLTLLLAY IMCCRREGQL KRDMATSDIQ MVHHCTIHGN TEELRQMAAR REVPRPLSTL
     PMFNVRTGER LPPRVDSAQV PLILDQH