SGCA_HUMAN
ID SGCA_HUMAN Reviewed; 387 AA.
AC Q16586; A6NEB8; A8K3K7; Q13710; Q13712;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 197.
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 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], AND VARIANTS LGMDR3 HIS-98 AND ALA-175.
RC TISSUE=Skeletal muscle;
RX PubMed=8069911; DOI=10.1016/0092-8674(94)90527-4;
RA Roberds S.L., Leturcq F., Allamand V., Piccolo F., Jeanpierre M.,
RA Anderson R.D., Lim L.E., Lee J.C., Tome F.M.S., Romero N.B., Fardeau M.,
RA Beckmann J.S., Kaplan J.-C., Campbell K.P.;
RT "Missense mutations in the adhalin gene linked to autosomal recessive
RT muscular dystrophy.";
RL Cell 78:625-633(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Heart ventricle;
RX PubMed=7937874; DOI=10.1073/pnas.91.21.9690;
RA McNally E., Yoshida M., Mizuno Y., Ozawa E., Kunkel L.M.;
RT "Human adhalin is alternatively spliced and the gene is on chromosome
RT 17q21.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9690-9694(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Spleen;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-214, AND VARIANT LGMDR3 CYS-77.
RX PubMed=8528203; DOI=10.1093/hmg/4.7.1163;
RA Bueno M.R.P., Moreira E.S., Vainzof M., Chamberlain J., Marie S.K.,
RA Pereira L., Akiyama J., Roberds S.L., Campbell K.P., Zatz M.;
RT "A common missense mutation in the adhalin gene in three unrelated
RT Brazilian families with a relatively mild form of autosomal recessive limb-
RT girdle muscular dystrophy.";
RL Hum. Mol. Genet. 4:1163-1167(1995).
RN [8]
RP VARIANTS LGMDR3 CYS-77; PRO-GLY-ALA-GLN-PRO-136 INS AND GLY-137.
RX PubMed=7657792; DOI=10.1172/jci118152;
RA Kawai H., Akaike M., Endo T., Adachi K., Inui T., Mitsui T., Kashiwagi S.,
RA Fujiwara T., Okuno S., Shin S., Miyoshi K., Campbell K.P., Yamada H.,
RA Shimizu T., Matsumura K., Saito S.;
RT "Adhalin gene mutations in patients with autosomal recessive childhood
RT onset muscular dystrophy with adhalin deficiency.";
RL J. Clin. Invest. 96:1202-1207(1995).
RN [9]
RP VARIANTS LGMDR3 HIS-34; HIS-62; GLU-68; CYS-77 AND HIS-98.
RX PubMed=7663524; DOI=10.1038/ng0695-243;
RA Piccolo F., Roberds S.L., Jeanpierre M., Leturcq F., Azibi K., Beldjord C.,
RA Carrie A., Recan D., Chaouch M., Reghis A., El Kerch F., Sefiani A.,
RA Voit T., Merlini L., Collin H., Eymard B., Beckmann J.S., Romero N.B.,
RA Tome F.M.S., Fardeau M., Campbell K.P., Kaplan J.-C.;
RT "Primary adhalinopathy: a common cause of autosomal recessive muscular
RT dystrophy of variable severity.";
RL Nat. Genet. 10:243-245(1995).
RN [10]
RP ERRATUM OF PUBMED:7663524.
RA Piccolo F., Roberds S.L., Jeanpierre M., Leturcq F., Azibi K., Beldjord C.,
RA Carrie A., Recan D., Chaouch M., Reghis A., El Kerch F., Sefiani A.,
RA Voit T., Merlini L., Collin H., Eymard B., Beckmann J.S., Romero N.B.,
RA Tome F.M.S., Fardeau M., Campbell K.P., Kaplan J.-C.;
RL Nat. Genet. 11:104-104(1995).
RN [11]
RP VARIANTS LGMDR3 LEU-30; CYS-34; CYS-77; ARG-91; THR-124; LYS-137; PRO-173
RP AND CYS-284.
RX PubMed=9192266; DOI=10.1136/jmg.34.6.470;
RA Carrie A., Piccolo F., Leturcq F., de Toma C., Azibi K., Beldjord C.,
RA Vallat J.-M., Merlini L., Voit T., Sewry C., Urtizberea J.A., Romero N.B.,
RA Tome F.M.S., Fardeau M., Sunada Y., Campbell K.P., Kaplan J.-C.,
RA Jeanpierre M.;
RT "Mutational diversity and hot spots in the alpha-sarcoglycan gene in
RT autosomal recessive muscular dystrophy (LGMD2D).";
RL J. Med. Genet. 34:470-475(1997).
RN [12]
RP VARIANTS LGMDR3 CYS-77; VAL-93; GLY-97; THR-124; PHE-158; PRO-173; ILE-196
RP AND HIS-205.
RX PubMed=9032047; DOI=10.1056/nejm199702273360904;
RA Duggan D.J., Gorospe J.R., Fanin M., Hoffman E.P., Angelini C.;
RT "Mutations in the sarcoglycan genes in patients with myopathy.";
RL N. Engl. J. Med. 336:618-624(1997).
RN [13]
RP VARIANT LGMDR3 CYS-284.
RX PubMed=9585331;
RX DOI=10.1002/(sici)1097-4598(199806)21:6<769::aid-mus9>3.0.co;2-5;
RA Angelini C., Fanin M., Menegazzo E., Freda M.P., Duggan D.J., Hoffman E.P.;
RT "Homozygous alpha-sarcoglycan mutation in two siblings: one asymptomatic
RT and one steroid-responsive mild limb-girdle muscular dystrophy patient.";
RL Muscle Nerve 21:769-775(1998).
RN [14]
RP VARIANTS LGMDR3 TRP-74; PHE-76 AND CYS-81.
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). {ECO:0000250}.
CC -!- INTERACTION:
CC Q16586; P54725: RAD23A; NbExp=3; IntAct=EBI-5663553, EBI-746453;
CC Q16586; P50454: SERPINH1; NbExp=3; IntAct=EBI-5663553, EBI-350723;
CC Q16586; O43765: SGTA; NbExp=13; IntAct=EBI-5663553, EBI-347996;
CC Q16586; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-5663553, EBI-744081;
CC Q16586; P37173: TGFBR2; NbExp=3; IntAct=EBI-5663553, EBI-296151;
CC Q16586-2; O43765: SGTA; NbExp=4; IntAct=EBI-16434133, EBI-347996;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Single-
CC pass type I membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=SGCA-1;
CC IsoId=Q16586-1; Sequence=Displayed;
CC Name=SGCA-2;
CC IsoId=Q16586-2; Sequence=VSP_006017;
CC -!- TISSUE SPECIFICITY: Most strongly expressed in skeletal muscle. Also
CC expressed in cardiac muscle and, at much lower levels, in lung. In the
CC fetus, most abundant in cardiac muscle and, at lower levels, in lung.
CC Also detected in liver and kidney. Not expressed in brain.
CC -!- DISEASE: Muscular dystrophy, limb-girdle, autosomal recessive 3
CC (LGMDR3) [MIM:608099]: An autosomal recessive degenerative myopathy
CC characterized by progressive muscle wasting from early childhood with
CC loss of independent ambulation by teenage years. Muscle biopsy shows
CC necrosis, decreased immunostaining for alpha sarcoglycan, and adhalin
CC deficiency. {ECO:0000269|PubMed:30345904, ECO:0000269|PubMed:7657792,
CC ECO:0000269|PubMed:7663524, ECO:0000269|PubMed:8069911,
CC ECO:0000269|PubMed:8528203, ECO:0000269|PubMed:9032047,
CC ECO:0000269|PubMed:9192266, ECO:0000269|PubMed:9585331}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the sarcoglycan alpha/epsilon family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Leiden Muscular Dystrophy pages; Note=SGCA mutations
CC in LGMD2D;
CC URL="https://www.dmd.nl/sgca_home.html";
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DR EMBL; U08895; AAA81637.1; -; mRNA.
DR EMBL; L34355; AAA35510.1; -; mRNA.
DR EMBL; L35853; AAA50461.1; -; mRNA.
DR EMBL; AK290622; BAF83311.1; -; mRNA.
DR EMBL; AC015909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94635.1; -; Genomic_DNA.
DR EMBL; BC025702; AAH25702.1; -; mRNA.
DR EMBL; L46810; AAC37583.1; -; mRNA.
DR CCDS; CCDS32679.1; -. [Q16586-1]
DR CCDS; CCDS45729.1; -. [Q16586-2]
DR PIR; A54746; A54746.
DR RefSeq; NP_000014.1; NM_000023.3. [Q16586-1]
DR RefSeq; NP_001129169.1; NM_001135697.2. [Q16586-2]
DR AlphaFoldDB; Q16586; -.
DR SMR; Q16586; -.
DR BioGRID; 112340; 131.
DR CORUM; Q16586; -.
DR IntAct; Q16586; 15.
DR MINT; Q16586; -.
DR STRING; 9606.ENSP00000262018; -.
DR GlyGen; Q16586; 2 sites.
DR PhosphoSitePlus; Q16586; -.
DR BioMuta; SGCA; -.
DR MassIVE; Q16586; -.
DR PaxDb; Q16586; -.
DR PeptideAtlas; Q16586; -.
DR PRIDE; Q16586; -.
DR ProteomicsDB; 60931; -. [Q16586-1]
DR ProteomicsDB; 60932; -. [Q16586-2]
DR Antibodypedia; 2323; 221 antibodies from 32 providers.
DR DNASU; 6442; -.
DR Ensembl; ENST00000262018.8; ENSP00000262018.3; ENSG00000108823.17. [Q16586-1]
DR Ensembl; ENST00000344627.10; ENSP00000345522.6; ENSG00000108823.17. [Q16586-2]
DR GeneID; 6442; -.
DR KEGG; hsa:6442; -.
DR MANE-Select; ENST00000262018.8; ENSP00000262018.3; NM_000023.4; NP_000014.1.
DR UCSC; uc002iqi.4; human. [Q16586-1]
DR CTD; 6442; -.
DR DisGeNET; 6442; -.
DR GeneCards; SGCA; -.
DR HGNC; HGNC:10805; SGCA.
DR HPA; ENSG00000108823; Group enriched (heart muscle, skeletal muscle, tongue).
DR MalaCards; SGCA; -.
DR MIM; 600119; gene.
DR MIM; 608099; phenotype.
DR neXtProt; NX_Q16586; -.
DR OpenTargets; ENSG00000108823; -.
DR Orphanet; 62; Alpha-sarcoglycan-related limb-girdle muscular dystrophy R3.
DR PharmGKB; PA35716; -.
DR VEuPathDB; HostDB:ENSG00000108823; -.
DR eggNOG; KOG4482; Eukaryota.
DR GeneTree; ENSGT00390000005672; -.
DR HOGENOM; CLU_053258_0_0_1; -.
DR InParanoid; Q16586; -.
DR OMA; VGSEQYF; -.
DR OrthoDB; 534519at2759; -.
DR PhylomeDB; Q16586; -.
DR TreeFam; TF314655; -.
DR PathwayCommons; Q16586; -.
DR SignaLink; Q16586; -.
DR SIGNOR; Q16586; -.
DR BioGRID-ORCS; 6442; 22 hits in 1068 CRISPR screens.
DR ChiTaRS; SGCA; human.
DR GeneWiki; SGCA; -.
DR GenomeRNAi; 6442; -.
DR Pharos; Q16586; Tbio.
DR PRO; PR:Q16586; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q16586; protein.
DR Bgee; ENSG00000108823; Expressed in hindlimb stylopod muscle and 118 other tissues.
DR ExpressionAtlas; Q16586; baseline and differential.
DR Genevisible; Q16586; HS.
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:0016010; C:dystrophin-associated glycoprotein complex; TAS:ProtInc.
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; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; IEA:Ensembl.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IEA:Ensembl.
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 Alternative splicing; Cell membrane; Cytoplasm; Cytoskeleton;
KW Disease variant; Glycoprotein; Limb-girdle muscular dystrophy; 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_0000031673"
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"
FT VAR_SEQ 196..319
FT /note="Missing (in isoform SGCA-2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006017"
FT VARIANT 30
FT /note="P -> L (in LGMDR3; dbSNP:rs886043256)"
FT /evidence="ECO:0000269|PubMed:9192266"
FT /id="VAR_010402"
FT VARIANT 31
FT /note="L -> P (in LGMDR3; dbSNP:rs903823830)"
FT /id="VAR_010403"
FT VARIANT 34
FT /note="R -> C (in LGMDR3; dbSNP:rs758647756)"
FT /evidence="ECO:0000269|PubMed:9192266"
FT /id="VAR_010404"
FT VARIANT 34
FT /note="R -> H (in LGMDR3; dbSNP:rs371675217)"
FT /evidence="ECO:0000269|PubMed:7663524"
FT /id="VAR_010405"
FT VARIANT 62
FT /note="Y -> H (in LGMDR3)"
FT /evidence="ECO:0000269|PubMed:7663524"
FT /id="VAR_010406"
FT VARIANT 68
FT /note="G -> E (in LGMDR3)"
FT /evidence="ECO:0000269|PubMed:7663524"
FT /id="VAR_010407"
FT VARIANT 74
FT /note="R -> W (in LGMDR3; dbSNP:rs757888349)"
FT /evidence="ECO:0000269|PubMed:30345904"
FT /id="VAR_010408"
FT VARIANT 76
FT /note="L -> F (in LGMDR3; dbSNP:rs1555568335)"
FT /evidence="ECO:0000269|PubMed:30345904"
FT /id="VAR_081098"
FT VARIANT 77
FT /note="R -> C (in LGMDR3; dbSNP:rs28933693)"
FT /evidence="ECO:0000269|PubMed:7657792,
FT ECO:0000269|PubMed:7663524, ECO:0000269|PubMed:8528203,
FT ECO:0000269|PubMed:9032047, ECO:0000269|PubMed:9192266"
FT /id="VAR_010387"
FT VARIANT 81
FT /note="R -> C (in LGMDR3; dbSNP:rs398123098)"
FT /evidence="ECO:0000269|PubMed:30345904"
FT /id="VAR_081099"
FT VARIANT 89
FT /note="L -> P (in LGMDR3; dbSNP:rs1435014211)"
FT /id="VAR_010409"
FT VARIANT 91
FT /note="G -> R (in LGMDR3)"
FT /evidence="ECO:0000269|PubMed:9192266"
FT /id="VAR_010410"
FT VARIANT 93
FT /note="A -> V (in LGMDR3)"
FT /evidence="ECO:0000269|PubMed:9032047"
FT /id="VAR_010411"
FT VARIANT 97
FT /note="D -> G (in LGMDR3; dbSNP:rs1555568396)"
FT /evidence="ECO:0000269|PubMed:9032047"
FT /id="VAR_010412"
FT VARIANT 98
FT /note="R -> C (in LGMDR3; dbSNP:rs138945081)"
FT /id="VAR_010413"
FT VARIANT 98
FT /note="R -> H (in LGMDR3; dbSNP:rs137852621)"
FT /evidence="ECO:0000269|PubMed:7663524,
FT ECO:0000269|PubMed:8069911"
FT /id="VAR_010388"
FT VARIANT 103
FT /note="I -> T (in LGMDR3; dbSNP:rs1161291343)"
FT /id="VAR_010414"
FT VARIANT 124
FT /note="I -> T (in LGMDR3; dbSNP:rs768814872)"
FT /evidence="ECO:0000269|PubMed:9032047,
FT ECO:0000269|PubMed:9192266"
FT /id="VAR_010415"
FT VARIANT 136
FT /note="A -> APGAQP (in LGMDR3; associated with G-137)"
FT /id="VAR_037965"
FT VARIANT 137
FT /note="E -> G (in LGMDR3; associated with P-G-A-Q-P-136
FT ins; dbSNP:rs397514451)"
FT /evidence="ECO:0000269|PubMed:7657792"
FT /id="VAR_037966"
FT VARIANT 137
FT /note="E -> K (in LGMDR3; dbSNP:rs372210292)"
FT /evidence="ECO:0000269|PubMed:9192266"
FT /id="VAR_010416"
FT VARIANT 158
FT /note="L -> F (in LGMDR3)"
FT /evidence="ECO:0000269|PubMed:9032047"
FT /id="VAR_010417"
FT VARIANT 173
FT /note="L -> P (in LGMDR3; dbSNP:rs143962150)"
FT /evidence="ECO:0000269|PubMed:9032047,
FT ECO:0000269|PubMed:9192266"
FT /id="VAR_010431"
FT VARIANT 175
FT /note="V -> A (in LGMDR3; dbSNP:rs137852622)"
FT /evidence="ECO:0000269|PubMed:8069911"
FT /id="VAR_010389"
FT VARIANT 196
FT /note="V -> I (in LGMDR3; dbSNP:rs752695991)"
FT /evidence="ECO:0000269|PubMed:9032047"
FT /id="VAR_010418"
FT VARIANT 205
FT /note="P -> H (in LGMDR3; dbSNP:rs757481230)"
FT /evidence="ECO:0000269|PubMed:9032047"
FT /id="VAR_010419"
FT VARIANT 228
FT /note="P -> Q (in LGMDR3)"
FT /id="VAR_010432"
FT VARIANT 242
FT /note="V -> A (in LGMDR3; dbSNP:rs1384158714)"
FT /id="VAR_010420"
FT VARIANT 247
FT /note="V -> M (in LGMDR3; dbSNP:rs143570936)"
FT /id="VAR_010433"
FT VARIANT 284
FT /note="R -> C (in LGMDR3; dbSNP:rs137852623)"
FT /evidence="ECO:0000269|PubMed:9192266,
FT ECO:0000269|PubMed:9585331"
FT /id="VAR_010390"
SQ SEQUENCE 387 AA; 42875 MW; 9CD0270A00BE03E6 CRC64;
MAETLFWTPL LVVLLAGLGD TEAQQTTLHP LVGRVFVHTL DHETFLSLPE HVAVPPAVHI
TYHAHLQGHP DLPRWLRYTQ RSPHHPGFLY GSATPEDRGL QVIEVTAYNR DSFDTTRQRL
VLEIGDPEGP LLPYQAEFLV RSHDAEEVLP STPASRFLSA LGGLWEPGEL QLLNVTSALD
RGGRVPLPIE GRKEGVYIKV GSASPFSTCL KMVASPDSHA RCAQGQPPLL SCYDTLAPHF
RVDWCNVTLV DKSVPEPADE VPTPGDGILE HDPFFCPPTE APDRDFLVDA LVTLLVPLLV
ALLLTLLLAY VMCCRREGRL KRDLATSDIQ MVHHCTIHGN TEELRQMAAS REVPRPLSTL
PMFNVHTGER LPPRVDSAQV PLILDQH
