SGCD_MOUSE
ID SGCD_MOUSE Reviewed; 289 AA.
AC P82347;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Delta-sarcoglycan;
DE Short=Delta-SG;
DE AltName: Full=35 kDa dystrophin-associated glycoprotein;
DE Short=35DAG;
GN Name=Sgcd;
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].
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 [2]
RP SUBCELLULAR LOCATION, SUBUNIT, DISULFIDE BONDS, AND INTERACTION WITH DAG1.
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Lung;
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: Interacts with FLNC (By similarity). 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. Interacts with DAG1. {ECO:0000250,
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; AB024923; BAA83494.1; -; mRNA.
DR CCDS; CCDS24584.1; -.
DR RefSeq; NP_036021.1; NM_011891.4.
DR RefSeq; XP_006533369.1; XM_006533306.3.
DR RefSeq; XP_006533370.1; XM_006533307.3.
DR AlphaFoldDB; P82347; -.
DR SMR; P82347; -.
DR BioGRID; 204865; 7.
DR CORUM; P82347; -.
DR IntAct; P82347; 2.
DR STRING; 10090.ENSMUSP00000076459; -.
DR GlyConnect; 2252; 1 N-Linked glycan (1 site).
DR GlyGen; P82347; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P82347; -.
DR PhosphoSitePlus; P82347; -.
DR SwissPalm; P82347; -.
DR PaxDb; P82347; -.
DR PeptideAtlas; P82347; -.
DR PRIDE; P82347; -.
DR ProteomicsDB; 257215; -.
DR Antibodypedia; 8150; 287 antibodies from 34 providers.
DR DNASU; 24052; -.
DR Ensembl; ENSMUST00000077221; ENSMUSP00000076459; ENSMUSG00000020354.
DR GeneID; 24052; -.
DR KEGG; mmu:24052; -.
DR UCSC; uc007ioz.1; mouse.
DR CTD; 6444; -.
DR MGI; MGI:1346525; Sgcd.
DR VEuPathDB; HostDB:ENSMUSG00000020354; -.
DR eggNOG; KOG3950; Eukaryota.
DR GeneTree; ENSGT00940000158509; -.
DR InParanoid; P82347; -.
DR OMA; XPKAVEA; -.
DR OrthoDB; 1407024at2759; -.
DR PhylomeDB; P82347; -.
DR TreeFam; TF313538; -.
DR BioGRID-ORCS; 24052; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Sgcd; mouse.
DR PRO; PR:P82347; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P82347; protein.
DR Bgee; ENSMUSG00000020354; Expressed in ascending aorta and 85 other tissues.
DR ExpressionAtlas; P82347; baseline and differential.
DR Genevisible; P82347; MM.
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:0016529; C:sarcoplasmic reticulum; IDA:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:MGI.
DR GO; GO:0086003; P:cardiac muscle cell contraction; IMP:MGI.
DR GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:MGI.
DR GO; GO:0048738; P:cardiac muscle tissue development; IBA:GO_Central.
DR GO; GO:0060977; P:coronary vasculature morphogenesis; IMP:MGI.
DR GO; GO:0060047; P:heart contraction; IBA:GO_Central.
DR GO; GO:0003015; P:heart process; IMP:MGI.
DR GO; GO:0061024; P:membrane organization; TAS:MGI.
DR GO; GO:0031503; P:protein-containing complex localization; IMP:MGI.
DR InterPro; IPR006875; Sarcoglycan.
DR InterPro; IPR039972; Sarcoglycan_gamma/delta/zeta.
DR InterPro; IPR027661; SGCD.
DR PANTHER; PTHR12939; PTHR12939; 1.
DR PANTHER; PTHR12939:SF6; PTHR12939:SF6; 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..289
FT /note="Delta-sarcoglycan"
FT /id="PRO_0000175247"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..56
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..289
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 263..288
FT /evidence="ECO:0000255"
FT DISULFID 265..281
FT /evidence="ECO:0000255"
SQ SEQUENCE 289 AA; 32133 MW; C44D7D9B511B3409 CRC64;
MPQEQYSHHR STMPSSEGPH IYKVGIYGWR KRCLYFFVLL LMILILVNLA MTIWILKVMN
FTIDGMGNLR ITEKGLKLEG DSEFLQPLYA KEIKSRPGNA LYFKSARNVT VNILNDQTKV
LTQLVTGPKA VEAYGKRFEV KTVSGKLLFS ADDSEVVVGA ERLRVLGAEG TVFPKSIETP
NVRADPFKEL RLESPTRSLV MEAPKGVEIN AEAGNMEAIC RSELRLESKD GEIKLDAAKI
KLPRLPRGSY TPTGTRQKVF EVCVCANGRL FLSQAGTGST CQINTSVCL
