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 24-JAN-2024, entry version 204. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 ComplexPortal; CPX-2424; Dystrophin glycoprotein complex, skeletal muscle variant. DR ComplexPortal; CPX-2443; Dystrophin glycoprotein complex, neuromuscular junction variant. DR ComplexPortal; CPX-2454; Dystrophin glycoprotein complex, retinal outer plexiform layer variant. DR ComplexPortal; CPX-2455; Dystrophin glycoprotein complex, retinal inner limiting membrane variant. DR CORUM; Q16586; -. DR IntAct; Q16586; 15. DR MINT; Q16586; -. DR STRING; 9606.ENSP00000262018; -. DR GlyCosmos; Q16586; 2 sites, No reported glycans. DR GlyGen; Q16586; 2 sites. DR PhosphoSitePlus; Q16586; -. DR SwissPalm; Q16586; -. DR BioMuta; SGCA; -. DR MassIVE; Q16586; -. DR PaxDb; 9606-ENSP00000262018; -. DR PeptideAtlas; Q16586; -. DR ProteomicsDB; 60931; -. [Q16586-1] DR ProteomicsDB; 60932; -. [Q16586-2] DR Antibodypedia; 2323; 257 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 AGR; HGNC:10805; -. 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; 5391218at2759; -. DR PhylomeDB; Q16586; -. DR TreeFam; TF314655; -. DR PathwayCommons; Q16586; -. DR SignaLink; Q16586; -. DR SIGNOR; Q16586; -. DR BioGRID-ORCS; 6442; 23 hits in 1146 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 120 other cell types or tissues. DR ExpressionAtlas; Q16586; baseline and differential. 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: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; IPR006644; Cadg. DR InterPro; IPR015919; Cadherin-like_sf. DR InterPro; IPR008908; Sarcoglycan_alpha/epsilon. DR InterPro; IPR048347; Sarcoglycan_C. DR InterPro; IPR048346; Sarcoglycan_N. DR PANTHER; PTHR10132; ALPHA-/EPSILON-SARCOGLYCAN FAMILY MEMBER; 1. DR PANTHER; PTHR10132:SF16; ALPHA-SARCOGLYCAN; 1. DR Pfam; PF05510; Sarcoglycan_2; 1. DR Pfam; PF20989; Sarcoglycan_2_C; 1. DR SMART; SM00736; CADG; 1. DR SUPFAM; SSF49313; Cadherin-like; 1. DR Genevisible; Q16586; HS. 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 //