ID   SGCA_RABIT              Reviewed;         387 AA.
AC   Q28686;
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   AltName: Full=Dystroglycan-2;
DE   Flags: Precursor;
GN   Name=SGCA; Synonyms=ADL, DAG2;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=8226900; DOI=10.1016/s0021-9258(20)80440-2;
RA   Roberds S.L., Anderson R.D., Ibraghimov-Beskrovnaya O., Campbell K.P.;
RT   "Primary structure and muscle-specific expression of the 50-kDa dystrophin-
RT   associated glycoprotein (adhalin).";
RL   J. Biol. Chem. 268:23739-23742(1993).
RN   [2]
RP   INTERACTION WITH SNTA1.
RX   PubMed=7890602; DOI=10.1074/jbc.270.10.4975;
RA   Yang B., Jung D., Rafael J.A., Chamberlain J.S., Campbell K.P.;
RT   "Identification of alpha-syntrophin binding to syntrophin triplet,
RT   dystrophin, and utrophin.";
RL   J. Biol. Chem. 270:4975-4978(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: 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 (By similarity).
CC       Interacts with the syntrophin SNTA1. {ECO:0000250,
CC       ECO:0000269|PubMed:7890602}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Single-
CC       pass type I membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sarcoglycan alpha/epsilon family.
CC       {ECO:0000305}.
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DR   EMBL; U01117; AAB60264.1; -; mRNA.
DR   PIR; A49498; A49498.
DR   RefSeq; NP_001075801.1; NM_001082332.2.
DR   AlphaFoldDB; Q28686; -.
DR   CORUM; Q28686; -.
DR   GeneID; 100009178; -.
DR   KEGG; ocu:100009178; -.
DR   CTD; 6442; -.
DR   InParanoid; Q28686; -.
DR   OrthoDB; 534519at2759; -.
DR   Proteomes; UP000001811; Unplaced.
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:0016012; C:sarcoglycan complex; IEA:InterPro.
DR   GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..387
FT                   /note="Alpha-sarcoglycan"
FT                   /id="PRO_0000031676"
FT   TOPO_DOM        25..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"
FT   VARIANT         358..359
FT                   /note="FP -> ST"
SQ   SEQUENCE   387 AA;  42498 MW;  F7167513B8309773 CRC64;
     MAAAALLWLP LLVGCLAGPG GTEAQQTTLY PLVGRVFVHT LEPASFLHLP EHAAPATIPV
     TYHAHLQGHP DLPRWLRYTQ RSPHHPGFLY GAATPEDRGR QVIEVTAYNR DSFDTAGQSL
     VLLIRDPEGS PLPYQTEFLV RSHDVEEVLP PTPASHFLTA LAGLWEPGEL KLLNITSALD
     RGGRVPLPIG GQKEGVYIKV GSASPFSTCL KMVASPDSHA RCARGQPPLL SCYDTLAPHF
     RVDWCNVSLV DTSVPEPVDE VPTPGDGILE HDPFFCPPTE ATARDFLADA LVTLLVPLLV
     ALLLALLLAY IMCCRREGRL KRDLATSDIQ MVHHCTIHEN TEELRQMAAS REVPRPLFPL
     PMFNVRTGER MPPRVDSAQV PLILDQH