SGCG_HUMAN
ID SGCG_HUMAN Reviewed; 291 AA.
AC Q13326; Q32M32; Q5T9J6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Gamma-sarcoglycan;
DE Short=Gamma-SG;
DE AltName: Full=35 kDa dystrophin-associated glycoprotein;
DE Short=35DAG;
GN Name=SGCG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DISEASE, AND VARIANT SER-287.
RX PubMed=7481775; DOI=10.1126/science.270.5237.819;
RA Noguchi S., McNally E.M., Othmane K.B., Hagiwara Y., Mizuno Y., Yoshida M.,
RA Yamamoto H., Boennemann C.G., Gussoni E., Denton P.H., Kyriakides T.,
RA Middleton L., Hentati F., Hamida M.B., Nonaka I., Vance J.M., Kunkel L.M.,
RA Ozawa E.;
RT "Mutations in the dystrophin-associated protein gamma-sarcoglycan in
RT chromosome 13 muscular dystrophy.";
RL Science 270:819-822(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISEASE, AND VARIANTS HIS-116 AND
RP SER-287.
RX PubMed=8900232;
RA McNally E.M., Passos-Bueno M.R., Boennemann C.G., Vainzof M.,
RA de Sa Moreira E., Lidov H.G.W., Othmane K.B., Denton P.H., Vance J.M.,
RA Zatz M., Kunkel L.M.;
RT "Mild and severe muscular dystrophy caused by a single gamma-sarcoglycan
RT mutation.";
RL Am. J. Hum. Genet. 59:1040-1047(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-287.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH FLNC.
RX PubMed=10629222; DOI=10.1083/jcb.148.1.115;
RA Thompson T.G., Chan Y.-M., Hack A.A., Brosius M., Rajala M., Lidov H.G.W.,
RA McNally E.M., Watkins S., Kunkel L.M.;
RT "Filamin 2 (FLN2): a muscle-specific sarcoglycan interacting protein.";
RL J. Cell Biol. 148:115-126(2000).
RN [6]
RP VARIANT LGMDR5 TYR-283.
RX PubMed=8968757; DOI=10.1093/hmg/5.12.2019;
RA Piccolo F., Jeanpierre M., Leturcq F., Dode C., Azibi K., Toutain A.,
RA Merlini L., Jarre L., Navarro C., Krishnamoorthy R., Tome F.M.S.,
RA Urtizberea J.A., Beckmann J.S., Campbell K.P., Kaplan J.-C.;
RT "A founder mutation in the gamma-sarcoglycan gene of Gypsies possibly
RT predating their migration out of India.";
RL Hum. Mol. Genet. 5:2019-2022(1996).
RN [7]
RP VARIANT LGMDR5 ARG-69.
RX PubMed=10714584; DOI=10.1016/s0960-8966(99)00063-2;
RA Nowak K.J., Walsh P., Jacob R.L., Johnsen R.D., Peverall J., McNally E.M.,
RA Wilton S.D., Kakulas B.A., Laing N.G.;
RT "Severe gamma-sarcoglycanopathy caused by a novel missense mutation and a
RT large deletion.";
RL Neuromuscul. Disord. 10:100-107(2000).
RN [8]
RP VARIANT LGMDR5 SER-71.
RX PubMed=30345904; DOI=10.1152/physiolgenomics.00036.2018;
RA Saha M., Reddy H.M., Salih M., Estrella E., Jones M.D., Mitsuhashi S.,
RA Cho K.A., Suzuki-Hatano S., Rizzo S.A., Hamad M.H., Mukhtar M.M.,
RA Hamed A.A., Elseed M.A., Lek M., Valkanas E., MacArthur D.G., Kunkel L.M.,
RA Pacak C.A., Draper I., Kang P.B.;
RT "The impact of PYROXD1 deficiency on cellular respiration and correlations
RT with genetic analyses of limb-girdle muscular dystrophy in Saudi Arabia and
RT Sudan.";
RL Physiol. Genomics 50:929-939(2018).
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). Interacts with FLNC. {ECO:0000250,
CC ECO:0000269|PubMed:10629222}.
CC -!- INTERACTION:
CC Q13326; O00501: CLDN5; NbExp=3; IntAct=EBI-5357343, EBI-18400628;
CC Q13326; O75923: DYSF; NbExp=3; IntAct=EBI-5357343, EBI-2799016;
CC Q13326; Q9HBV2: SPACA1; NbExp=3; IntAct=EBI-5357343, EBI-17498703;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal and heart muscle.
CC -!- DISEASE: Muscular dystrophy, limb-girdle, autosomal recessive 5
CC (LGMDR5) [MIM:253700]: An autosomal recessive degenerative myopathy
CC characterized by rapidly progressive muscle wasting from early
CC childhood with loss of independent ambulation around age 12 years,
CC dystrophic pattern on muscle biopsy, absence of gamma-sarcoglycan and
CC normal dystrophin immunostaining. {ECO:0000269|PubMed:10714584,
CC ECO:0000269|PubMed:30345904, ECO:0000269|PubMed:8968757}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the sarcoglycan beta/delta/gamma/zeta family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Leiden Muscular Dystrophy pages; Note=SGCG mutations
CC in LGMD2C;
CC URL="https://www.dmd.nl/sgcg_home.html";
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DR EMBL; U34976; AAC50269.1; -; mRNA.
DR EMBL; U63395; AAD13475.1; -; Genomic_DNA.
DR EMBL; U63389; AAD13475.1; JOINED; Genomic_DNA.
DR EMBL; U63390; AAD13475.1; JOINED; Genomic_DNA.
DR EMBL; U63391; AAD13475.1; JOINED; Genomic_DNA.
DR EMBL; U63392; AAD13475.1; JOINED; Genomic_DNA.
DR EMBL; U63393; AAD13475.1; JOINED; Genomic_DNA.
DR EMBL; U63394; AAD13475.1; JOINED; Genomic_DNA.
DR EMBL; AL157766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC074777; AAH74777.1; -; mRNA.
DR EMBL; BC074778; AAH74778.1; -; mRNA.
DR EMBL; BC109321; AAI09322.1; -; mRNA.
DR CCDS; CCDS9299.1; -.
DR RefSeq; NP_000222.1; NM_000231.2.
DR RefSeq; XP_005266562.1; XM_005266505.2.
DR AlphaFoldDB; Q13326; -.
DR BioGRID; 112343; 18.
DR CORUM; Q13326; -.
DR IntAct; Q13326; 18.
DR MINT; Q13326; -.
DR STRING; 9606.ENSP00000218867; -.
DR GlyGen; Q13326; 1 site.
DR PhosphoSitePlus; Q13326; -.
DR BioMuta; SGCG; -.
DR DMDM; 313104319; -.
DR MassIVE; Q13326; -.
DR PaxDb; Q13326; -.
DR PeptideAtlas; Q13326; -.
DR PRIDE; Q13326; -.
DR ProteomicsDB; 59316; -.
DR Antibodypedia; 2309; 152 antibodies from 29 providers.
DR DNASU; 6445; -.
DR Ensembl; ENST00000218867.4; ENSP00000218867.3; ENSG00000102683.8.
DR GeneID; 6445; -.
DR KEGG; hsa:6445; -.
DR MANE-Select; ENST00000218867.4; ENSP00000218867.3; NM_000231.3; NP_000222.2.
DR UCSC; uc001uom.3; human.
DR CTD; 6445; -.
DR DisGeNET; 6445; -.
DR GeneCards; SGCG; -.
DR HGNC; HGNC:10809; SGCG.
DR HPA; ENSG00000102683; Group enriched (heart muscle, skeletal muscle, tongue).
DR MalaCards; SGCG; -.
DR MIM; 253700; phenotype.
DR MIM; 608896; gene.
DR neXtProt; NX_Q13326; -.
DR OpenTargets; ENSG00000102683; -.
DR Orphanet; 353; Gamma-sarcoglycan-related limb-girdle muscular dystrophy R5.
DR PharmGKB; PA35720; -.
DR VEuPathDB; HostDB:ENSG00000102683; -.
DR eggNOG; KOG3950; Eukaryota.
DR GeneTree; ENSGT00940000159187; -.
DR HOGENOM; CLU_043450_0_0_1; -.
DR InParanoid; Q13326; -.
DR OMA; SHNDNML; -.
DR OrthoDB; 1407024at2759; -.
DR PhylomeDB; Q13326; -.
DR TreeFam; TF313538; -.
DR PathwayCommons; Q13326; -.
DR SignaLink; Q13326; -.
DR SIGNOR; Q13326; -.
DR BioGRID-ORCS; 6445; 10 hits in 1070 CRISPR screens.
DR ChiTaRS; SGCG; human.
DR GeneWiki; SGCG; -.
DR GenomeRNAi; 6445; -.
DR Pharos; Q13326; Tbio.
DR PRO; PR:Q13326; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q13326; protein.
DR Bgee; ENSG00000102683; Expressed in skeletal muscle tissue of rectus abdominis and 120 other tissues.
DR Genevisible; Q13326; HS.
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:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0016012; C:sarcoglycan complex; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IBA:GO_Central.
DR GO; GO:0048738; P:cardiac muscle tissue development; IBA:GO_Central.
DR GO; GO:0060047; P:heart contraction; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR InterPro; IPR006875; Sarcoglycan.
DR InterPro; IPR039972; Sarcoglycan_gamma/delta/zeta.
DR InterPro; IPR027660; SGCG.
DR PANTHER; PTHR12939; PTHR12939; 1.
DR PANTHER; PTHR12939:SF4; PTHR12939:SF4; 1.
DR Pfam; PF04790; Sarcoglycan_1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Cytoskeleton; Disease variant; Disulfide bond;
KW Glycoprotein; Limb-girdle muscular dystrophy; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..291
FT /note="Gamma-sarcoglycan"
FT /id="PRO_0000175248"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 265..290
FT /evidence="ECO:0000255"
FT DISULFID 267..283
FT /evidence="ECO:0000255"
FT VARIANT 69
FT /note="G -> D (in LGMDR5)"
FT /id="VAR_010430"
FT VARIANT 69
FT /note="G -> R (in LGMDR5)"
FT /evidence="ECO:0000269|PubMed:10714584"
FT /id="VAR_012202"
FT VARIANT 71
FT /note="L -> S (in LGMDR5; dbSNP:rs143009120)"
FT /evidence="ECO:0000269|PubMed:30345904"
FT /id="VAR_081101"
FT VARIANT 116
FT /note="R -> H (in dbSNP:rs17314986)"
FT /evidence="ECO:0000269|PubMed:8900232"
FT /id="VAR_010397"
FT VARIANT 283
FT /note="C -> Y (in LGMDR5; dbSNP:rs104894422)"
FT /evidence="ECO:0000269|PubMed:8968757"
FT /id="VAR_010398"
FT VARIANT 287
FT /note="N -> S (in dbSNP:rs1800354)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:7481775, ECO:0000269|PubMed:8900232"
FT /id="VAR_010399"
SQ SEQUENCE 291 AA; 32379 MW; 6CF219706ABFB77B CRC64;
MVREQYTTAT EGICIERPEN QYVYKIGIYG WRKRCLYLFV LLLLIILVVN LALTIWILKV
MWFSPAGMGH LCVTKDGLRL EGESEFLFPL YAKEIHSRVD SSLLLQSTQN VTVNARNSEG
EVTGRLKVGP KMVEVQNQQF QINSNDGKPL FTVDEKEVVV GTDKLRVTGP EGALFEHSVE
TPLVRADPFQ DLRLESPTRS LSMDAPRGVH IQAHAGKIEA LSQMDILFHS SDGMLVLDAE
TVCLPKLVQG TWGPSGSSQS LYEICVCPDG KLYLSVAGVS TTCQEHNHIC L
