SGCD_HUMAN
ID SGCD_HUMAN Reviewed; 289 AA.
AC Q92629; A8K9S9; Q53XA5; Q99644;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Delta-sarcoglycan;
DE Short=Delta-SG;
DE AltName: Full=35 kDa dystrophin-associated glycoprotein;
DE Short=35DAG;
GN Name=SGCD;
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] (ISOFORM 2), AND VARIANT GLN-96.
RC TISSUE=Skeletal muscle;
RX PubMed=8842738; DOI=10.1093/hmg/5.8.1179;
RA Nigro V., Piluso G., Belsito A., Politano L., Puca A.A., Papparella S.,
RA Rossi E., Viglietto G., Esposito M.G., Abbondanza C., Medici N.,
RA Molinari A.M., Nigro G., Puca G.A.;
RT "Identification of a novel sarcoglycan gene at 5q33 encoding a sarcolemmal
RT 35kDa glycoprotein.";
RL Hum. Mol. Genet. 5:1179-1186(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
RX PubMed=8943294; DOI=10.1074/jbc.271.50.32321;
RA Jung D., Duclos F., Apostol B., Straub V., Lee J.C., Allamand V.,
RA Venzke D.P., Sunada Y., Moomaw C.R., Leveille C.J., Slaughter C.A.,
RA Crawford T.O., McPherson J.D., Campbell K.P.;
RT "Characterization of delta-sarcoglycan, a novel component of the oligomeric
RT sarcoglycan complex involved in limb-girdle muscular dystrophy.";
RL J. Biol. Chem. 271:32321-32329(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP VARIANT LGMDR6 LYS-261.
RX PubMed=9832045; DOI=10.1136/jmg.35.11.951;
RA Moreira E.S., Vainzof M., Marie S.K., Nigro V., Zatz M., Passos-Bueno M.R.;
RT "A first missense mutation in the delta sarcoglycan gene associated with a
RT severe phenotype and frequency of limb-girdle muscular dystrophy type 2F
RT (LGMD2F) in Brazilian sarcoglycanopathies.";
RL J. Med. Genet. 35:951-953(1998).
RN [8]
RP VARIANT CMD1L ALA-150.
RX PubMed=10974018; DOI=10.1172/jci9224;
RA Tsubata S., Bowles K.R., Vatta M., Zintz C., Titus J., Muhonen L.,
RA Bowles N.E., Towbin J.A.;
RT "Mutations in the human delta-sarcoglycan gene in familial and sporadic
RT dilated cardiomyopathy.";
RL J. Clin. Invest. 106:655-662(2000).
RN [9]
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).
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 and DAG1. Cross-link to form 2 major
CC 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; Single-pass type II
CC membrane protein. Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q92629-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92629-2; Sequence=VSP_039245;
CC Name=3;
CC IsoId=Q92629-3; Sequence=VSP_039245, VSP_039246, VSP_039247;
CC -!- TISSUE SPECIFICITY: Most strongly expressed in skeletal and cardiac
CC muscle. Also detected in smooth muscle. Weak expression in brain and
CC lung.
CC -!- PTM: Glycosylated.
CC -!- PTM: Disulfide bonds are present. {ECO:0000250}.
CC -!- DISEASE: Muscular dystrophy, limb-girdle, autosomal recessive 6
CC (LGMDR6) [MIM:601287]: An autosomal recessive degenerative myopathy
CC initially affecting the proximal limb girdle musculature. Muscle from
CC patients shows a complete loss of delta-sarcoglycan as well as of the
CC others components of the sarcoglycan complex.
CC {ECO:0000269|PubMed:9832045}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Cardiomyopathy, dilated 1L (CMD1L) [MIM:606685]: A disorder
CC characterized by ventricular dilation and impaired systolic function,
CC resulting in congestive heart failure and arrhythmia. Patients are at
CC risk of premature death. {ECO:0000269|PubMed:10974018}. 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=SGCD mutations
CC in LGMD2F/CMD1L;
CC URL="https://www.dmd.nl/sgcd_home.html";
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DR EMBL; X95191; CAA64490.1; -; mRNA.
DR EMBL; U58331; AAC50921.1; -; mRNA.
DR EMBL; AK292794; BAF85483.1; -; mRNA.
DR EMBL; BX537948; CAD97916.1; -; mRNA.
DR EMBL; BC020740; AAH20740.1; -; mRNA.
DR CCDS; CCDS47325.1; -. [Q92629-2]
DR CCDS; CCDS47326.1; -. [Q92629-3]
DR CCDS; CCDS47327.1; -. [Q92629-1]
DR RefSeq; NP_000328.2; NM_000337.5. [Q92629-2]
DR RefSeq; NP_001121681.1; NM_001128209.1. [Q92629-1]
DR RefSeq; NP_758447.1; NM_172244.2. [Q92629-3]
DR RefSeq; XP_005266023.1; XM_005265966.4. [Q92629-2]
DR RefSeq; XP_011532923.1; XM_011534621.2. [Q92629-1]
DR RefSeq; XP_016865212.1; XM_017009723.1. [Q92629-2]
DR RefSeq; XP_016865213.1; XM_017009724.1. [Q92629-2]
DR AlphaFoldDB; Q92629; -.
DR BioGRID; 112342; 65.
DR CORUM; Q92629; -.
DR IntAct; Q92629; 13.
DR MINT; Q92629; -.
DR STRING; 9606.ENSP00000338343; -.
DR GlyGen; Q92629; 3 sites.
DR iPTMnet; Q92629; -.
DR PhosphoSitePlus; Q92629; -.
DR BioMuta; SGCD; -.
DR DMDM; 212276471; -.
DR jPOST; Q92629; -.
DR MassIVE; Q92629; -.
DR MaxQB; Q92629; -.
DR PaxDb; Q92629; -.
DR PeptideAtlas; Q92629; -.
DR PRIDE; Q92629; -.
DR ProteomicsDB; 75384; -. [Q92629-1]
DR ProteomicsDB; 75385; -. [Q92629-2]
DR ProteomicsDB; 75386; -. [Q92629-3]
DR Antibodypedia; 8150; 287 antibodies from 34 providers.
DR DNASU; 6444; -.
DR Ensembl; ENST00000337851.9; ENSP00000338343.4; ENSG00000170624.14. [Q92629-2]
DR Ensembl; ENST00000435422.7; ENSP00000403003.2; ENSG00000170624.14. [Q92629-1]
DR Ensembl; ENST00000517913.5; ENSP00000429378.1; ENSG00000170624.14. [Q92629-3]
DR GeneID; 6444; -.
DR KEGG; hsa:6444; -.
DR MANE-Select; ENST00000337851.9; ENSP00000338343.4; NM_000337.6; NP_000328.2. [Q92629-2]
DR UCSC; uc003lwc.5; human. [Q92629-1]
DR CTD; 6444; -.
DR DisGeNET; 6444; -.
DR GeneCards; SGCD; -.
DR GeneReviews; SGCD; -.
DR HGNC; HGNC:10807; SGCD.
DR HPA; ENSG00000170624; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR MalaCards; SGCD; -.
DR MIM; 601287; phenotype.
DR MIM; 601411; gene.
DR MIM; 606685; phenotype.
DR neXtProt; NX_Q92629; -.
DR OpenTargets; ENSG00000170624; -.
DR Orphanet; 219; Delta-sarcoglycan-related limb-girdle muscular dystrophy R6.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR PharmGKB; PA35718; -.
DR VEuPathDB; HostDB:ENSG00000170624; -.
DR eggNOG; KOG3950; Eukaryota.
DR GeneTree; ENSGT00940000158509; -.
DR HOGENOM; CLU_043450_0_0_1; -.
DR InParanoid; Q92629; -.
DR OMA; XPKAVEA; -.
DR OrthoDB; 1407024at2759; -.
DR PhylomeDB; Q92629; -.
DR TreeFam; TF313538; -.
DR PathwayCommons; Q92629; -.
DR SignaLink; Q92629; -.
DR SIGNOR; Q92629; -.
DR BioGRID-ORCS; 6444; 17 hits in 1070 CRISPR screens.
DR ChiTaRS; SGCD; human.
DR GeneWiki; Delta-sarcoglycan; -.
DR GeneWiki; SGCD; -.
DR GenomeRNAi; 6444; -.
DR Pharos; Q92629; Tbio.
DR PRO; PR:Q92629; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q92629; protein.
DR Bgee; ENSG00000170624; Expressed in left ventricle myocardium and 179 other tissues.
DR ExpressionAtlas; Q92629; baseline and differential.
DR Genevisible; Q92629; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:UniProtKB.
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:0016529; C:sarcoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0055074; P:calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0086003; P:cardiac muscle cell contraction; IEA:Ensembl.
DR GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0048738; P:cardiac muscle tissue development; IBA:GO_Central.
DR GO; GO:0060977; P:coronary vasculature morphogenesis; IEA:Ensembl.
DR GO; GO:0060047; P:heart contraction; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0031503; P:protein-containing complex localization; IEA:Ensembl.
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 Alternative splicing; Cardiomyopathy; Cell membrane; Cytoplasm;
KW Cytoskeleton; Disease variant; Disulfide bond; Glycoprotein;
KW Limb-girdle muscular dystrophy; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..289
FT /note="Delta-sarcoglycan"
FT /id="PRO_0000175245"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..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"
FT VAR_SEQ 1
FT /note="M -> MM (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8842738,
FT ECO:0000303|PubMed:8943294"
FT /id="VSP_039245"
FT VAR_SEQ 233..255
FT /note="IKLDAAKIRLPRLPHGSYTPTGT -> VRDEKDRSSKSYSFNRPTLPITG
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8943294"
FT /id="VSP_039246"
FT VAR_SEQ 256..289
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8943294"
FT /id="VSP_039247"
FT VARIANT 96
FT /note="R -> Q (in dbSNP:rs45559835)"
FT /evidence="ECO:0000269|PubMed:8842738"
FT /id="VAR_010429"
FT VARIANT 150
FT /note="S -> A (in CMD1L; dbSNP:rs121909298)"
FT /evidence="ECO:0000269|PubMed:10974018"
FT /id="VAR_013181"
FT VARIANT 261
FT /note="E -> K (in LGMDR6; dbSNP:rs121909297)"
FT /evidence="ECO:0000269|PubMed:9832045"
FT /id="VAR_010396"
SQ SEQUENCE 289 AA; 32071 MW; EB775E2427D260B7 CRC64;
MPQEQYTHHR STMPGSVGPQ VYKVGIYGWR KRCLYFFVLL LMILILVNLA MTIWILKVMN
FTIDGMGNLR ITEKGLKLEG DSEFLQPLYA KEIQSRPGNA LYFKSARNVT VNILNDQTKV
LTQLITGPKA VEAYGKKFEV KTVSGKLLFS ADNNEVVVGA ERLRVLGAEG TVFPKSIETP
NVRADPFKEL RLESPTRSLV MEAPKGVEIN AEAGNMEATC RTELRLESKD GEIKLDAAKI
RLPRLPHGSY TPTGTRQKVF EICVCANGRL FLSQAGAGST CQINTSVCL
