SGCB_HUMAN
ID SGCB_HUMAN Reviewed; 318 AA.
AC Q16585; B7Z635; O00661;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Beta-sarcoglycan;
DE Short=Beta-SG;
DE AltName: Full=43 kDa dystrophin-associated glycoprotein;
DE Short=43DAG;
DE AltName: Full=A3b;
GN Name=SGCB;
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 1).
RC TISSUE=Muscle;
RX PubMed=7581449; DOI=10.1038/ng1195-266;
RA Boennemann C.G., Modi R., Noguchi S., Mizuno Y., Yoshida M., Gussoni E.,
RA McNally E.M., Duggan D.J., Angelini C., Hoffman E.P., Ozawa E.,
RA Kunkel L.M.;
RT "Beta-sarcoglycan (A3b) mutations cause autosomal recessive muscular
RT dystrophy with loss of the sarcoglycan complex.";
RL Nat. Genet. 11:266-273(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 42-54; 112-173;
RP 175-192 AND 228-253, AND DISEASE.
RC TISSUE=Skeletal muscle;
RX PubMed=7581448; DOI=10.1038/ng1195-257;
RA Lim L.E., Duclos F., Broux O., Bourg N., Sunada Y., Allamand V., Meyer J.,
RA Richard I., Moomaw C., Slaughter C., Tome F.M.S., Fardeau M., Jackson C.E.,
RA Beckmann J.S., Campbell K.P.;
RT "Beta-sarcoglycan: characterization and role in limb-girdle muscular
RT dystrophy linked to 4q12.";
RL Nat. Genet. 11:257-265(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANTS LGMDR4
RP PRO-91; LYS-100 AND ARG-108.
RX PubMed=8968749; DOI=10.1093/hmg/5.12.1953;
RA Bonnemann C.G., Passos-Bueno M.R., McNally E.M., Vainzof M.,
RA de Sa Moreira E., Marie S.K., Pavanello R.C., Noguchi S., Ozawa E.,
RA Zatz M., Kunkel L.M.;
RT "Genomic screening for beta-sarcoglycan gene mutations: missense mutations
RT may cause severe limb-girdle muscular dystrophy type 2E (LGMD 2E).";
RL Hum. Mol. Genet. 5:1953-1961(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bourg N.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158 AND ASN-211.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP VARIANT LGMDR4 LEU-91.
RX PubMed=9631401; DOI=10.1016/s0960-8966(98)00014-5;
RA Bonnemann C.G., Wong J., Ben-Hamida C., Ben-Hamida M., Hentati F.,
RA Kunkel L.M.;
RT "LGMD 2E in Tunisia is caused by a homozygous missense mutation in beta-
RT sarcoglycan exon 3.";
RL Neuromuscul. Disord. 8:193-197(1998).
RN [10]
RP VARIANTS LGMDR4 GLU-11; PHE-114; ASP-139 AND ALA-182.
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 [11]
RP VARIANT DMD-LIKE CYS-184.
RX PubMed=10660328;
RA dos Santos M.R., Jorge P., Ribeiro E.M., Pires M.M., Guimaraes A.;
RT "Novel mutation (Y184C) in exon 4 of the beta-sarcoglycan gene identified
RT in a Portuguese patient.";
RL Hum. Mutat. 12:214-215(1998).
RN [12]
RP VARIANTS LGMDR4 CYS-91; PHE-119 AND ARG-151.
RX PubMed=9565988; DOI=10.1016/s0960-8966(97)00135-1;
RA Duclos F., Broux O., Bourg N., Straub V., Feldman G.L., Sunada Y.,
RA Lim L.E., Piccolo F., Cutshall S., Gary F., Quetier F., Kaplan J.C.,
RA Jackson C.E., Beckmann J.S., Campbell K.P.;
RT "Beta-sarcoglycan: genomic analysis and identification of a novel missense
RT mutation in the LGMD2E Amish isolate.";
RL Neuromuscul. Disord. 8:30-38(1998).
RN [13]
RP VARIANT LGMDR4 38-SER--HIS-318 DEL.
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: Cross-link to form 2 major subcomplexes: one consisting of
CC SGCB, SGCD and SGCG and the other consisting of SGCB and SGCD. The
CC association between SGCB and SGCG is particularly strong while SGCA is
CC loosely associated with the other sarcoglycans (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q16585; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-5663627, EBI-10225815;
CC Q16585; O95236-2: APOL3; NbExp=3; IntAct=EBI-5663627, EBI-11976321;
CC Q16585; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-5663627, EBI-12244618;
CC Q16585; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-5663627, EBI-11989440;
CC Q16585; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-5663627, EBI-11522780;
CC Q16585; Q08426: EHHADH; NbExp=3; IntAct=EBI-5663627, EBI-2339219;
CC Q16585; P21145: MAL; NbExp=3; IntAct=EBI-5663627, EBI-3932027;
CC Q16585; Q99735: MGST2; NbExp=3; IntAct=EBI-5663627, EBI-11324706;
CC Q16585; Q92982: NINJ1; NbExp=3; IntAct=EBI-5663627, EBI-2802124;
CC Q16585; Q01453: PMP22; NbExp=3; IntAct=EBI-5663627, EBI-2845982;
CC Q16585; P53801: PTTG1IP; NbExp=3; IntAct=EBI-5663627, EBI-3906138;
CC Q16585; Q08AT0: SGCZ; NbExp=4; IntAct=EBI-5663627, EBI-12877338;
CC Q16585; Q9NWF4: SLC52A1; NbExp=3; IntAct=EBI-5663627, EBI-12904614;
CC Q16585; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-5663627, EBI-741850;
CC Q16585; P17152: TMEM11; NbExp=3; IntAct=EBI-5663627, EBI-723946;
CC Q16585; P01375: TNF; NbExp=3; IntAct=EBI-5663627, EBI-359977;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16585-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16585-2; Sequence=VSP_056894;
CC -!- TISSUE SPECIFICITY: Highest expression in heart and skeletal muscle.
CC Low expression in brain, kidney, placenta, pancreas and lung. High
CC expression in fetal brain. Also found in fetal lung, kidney and liver.
CC -!- PTM: Disulfide bonds are present. {ECO:0000250}.
CC -!- DISEASE: Muscular dystrophy, limb-girdle, autosomal recessive 4
CC (LGMDR4) [MIM:604286]: An autosomal recessive degenerative myopathy
CC characterized by pelvic and shoulder muscle wasting, onset usually in
CC childhood and variable progression rate. {ECO:0000269|PubMed:30345904,
CC ECO:0000269|PubMed:8968749, ECO:0000269|PubMed:9032047,
CC ECO:0000269|PubMed:9565988, ECO:0000269|PubMed:9631401}. 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=SGCB mutations
CC in LGMD2E;
CC URL="https://www.dmd.nl/sgcb_home.html";
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DR EMBL; U31116; AAA87034.1; -; mRNA.
DR EMBL; U29586; AAB41291.1; -; mRNA.
DR EMBL; U63801; AAB46956.1; -; Genomic_DNA.
DR EMBL; U63796; AAB46956.1; JOINED; Genomic_DNA.
DR EMBL; U63797; AAB46956.1; JOINED; Genomic_DNA.
DR EMBL; U63798; AAB46956.1; JOINED; Genomic_DNA.
DR EMBL; U63800; AAB46956.1; JOINED; Genomic_DNA.
DR EMBL; Y09781; CAA70920.1; -; Genomic_DNA.
DR EMBL; AK299765; BAH13121.1; -; mRNA.
DR EMBL; AC093858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020709; AAH20709.1; -; mRNA.
DR CCDS; CCDS3488.1; -. [Q16585-1]
DR PIR; I39151; I39151.
DR RefSeq; NP_000223.1; NM_000232.4. [Q16585-1]
DR AlphaFoldDB; Q16585; -.
DR BioGRID; 112341; 136.
DR CORUM; Q16585; -.
DR IntAct; Q16585; 32.
DR MINT; Q16585; -.
DR STRING; 9606.ENSP00000370839; -.
DR GlyGen; Q16585; 4 sites.
DR iPTMnet; Q16585; -.
DR PhosphoSitePlus; Q16585; -.
DR BioMuta; SGCB; -.
DR DMDM; 13431857; -.
DR EPD; Q16585; -.
DR jPOST; Q16585; -.
DR MassIVE; Q16585; -.
DR MaxQB; Q16585; -.
DR PaxDb; Q16585; -.
DR PeptideAtlas; Q16585; -.
DR PRIDE; Q16585; -.
DR ProteomicsDB; 60930; -. [Q16585-1]
DR ProteomicsDB; 6740; -.
DR Antibodypedia; 2557; 233 antibodies from 31 providers.
DR DNASU; 6443; -.
DR Ensembl; ENST00000381431.10; ENSP00000370839.6; ENSG00000163069.13. [Q16585-1]
DR GeneID; 6443; -.
DR KEGG; hsa:6443; -.
DR MANE-Select; ENST00000381431.10; ENSP00000370839.6; NM_000232.5; NP_000223.1.
DR CTD; 6443; -.
DR DisGeNET; 6443; -.
DR GeneCards; SGCB; -.
DR HGNC; HGNC:10806; SGCB.
DR HPA; ENSG00000163069; Tissue enhanced (skeletal).
DR MalaCards; SGCB; -.
DR MIM; 600900; gene.
DR MIM; 604286; phenotype.
DR neXtProt; NX_Q16585; -.
DR OpenTargets; ENSG00000163069; -.
DR Orphanet; 119; Beta-sarcoglycan-related limb-girdle muscular dystrophy R4.
DR PharmGKB; PA35717; -.
DR VEuPathDB; HostDB:ENSG00000163069; -.
DR eggNOG; ENOG502QUW4; Eukaryota.
DR GeneTree; ENSGT00390000008110; -.
DR HOGENOM; CLU_066515_1_0_1; -.
DR InParanoid; Q16585; -.
DR OMA; TFAFWTI; -.
DR PhylomeDB; Q16585; -.
DR TreeFam; TF313538; -.
DR PathwayCommons; Q16585; -.
DR SignaLink; Q16585; -.
DR SIGNOR; Q16585; -.
DR BioGRID-ORCS; 6443; 7 hits in 1067 CRISPR screens.
DR ChiTaRS; SGCB; human.
DR GeneWiki; SGCB; -.
DR GenomeRNAi; 6443; -.
DR Pharos; Q16585; Tbio.
DR PRO; PR:Q16585; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q16585; protein.
DR Bgee; ENSG00000163069; Expressed in tendon of biceps brachii and 205 other tissues.
DR ExpressionAtlas; Q16585; baseline and differential.
DR Genevisible; Q16585; HS.
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; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of 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:0055013; P:cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0097084; P:vascular associated smooth muscle cell development; IEA:Ensembl.
DR InterPro; IPR006875; Sarcoglycan.
DR InterPro; IPR027659; Sgcb.
DR PANTHER; PTHR21142; PTHR21142; 1.
DR Pfam; PF04790; Sarcoglycan_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Limb-girdle muscular dystrophy; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..318
FT /note="Beta-sarcoglycan"
FT /id="PRO_0000175242"
FT TOPO_DOM 1..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..318
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 288..314
FT /evidence="ECO:0000255"
FT DISULFID 290..307
FT /evidence="ECO:0000255"
FT VAR_SEQ 12..81
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056894"
FT VARIANT 11
FT /note="Q -> E (in LGMDR4; dbSNP:rs752492870)"
FT /evidence="ECO:0000269|PubMed:9032047"
FT /id="VAR_010421"
FT VARIANT 38..318
FT /note="Missing (in LGMDR4)"
FT /evidence="ECO:0000269|PubMed:30345904"
FT /id="VAR_081100"
FT VARIANT 91
FT /note="R -> C (in LGMDR4; dbSNP:rs555514820)"
FT /evidence="ECO:0000269|PubMed:9565988"
FT /id="VAR_010422"
FT VARIANT 91
FT /note="R -> L (in LGMDR4; dbSNP:rs104893869)"
FT /evidence="ECO:0000269|PubMed:9631401"
FT /id="VAR_010391"
FT VARIANT 91
FT /note="R -> P (in LGMDR4; dbSNP:rs104893869)"
FT /evidence="ECO:0000269|PubMed:8968749"
FT /id="VAR_010392"
FT VARIANT 100
FT /note="M -> K (in LGMDR4; dbSNP:rs104893871)"
FT /evidence="ECO:0000269|PubMed:8968749"
FT /id="VAR_010393"
FT VARIANT 108
FT /note="L -> R (in LGMDR4; dbSNP:rs104893870)"
FT /evidence="ECO:0000269|PubMed:8968749"
FT /id="VAR_010394"
FT VARIANT 114
FT /note="S -> F (in LGMDR4; dbSNP:rs150518260)"
FT /evidence="ECO:0000269|PubMed:9032047"
FT /id="VAR_010423"
FT VARIANT 119
FT /note="I -> F (in LGMDR4; dbSNP:rs762412447)"
FT /evidence="ECO:0000269|PubMed:9565988"
FT /id="VAR_010424"
FT VARIANT 139
FT /note="G -> D (in LGMDR4; dbSNP:rs1560567653)"
FT /evidence="ECO:0000269|PubMed:9032047"
FT /id="VAR_010425"
FT VARIANT 151
FT /note="T -> R (in LGMDR4; dbSNP:rs28936383)"
FT /evidence="ECO:0000269|PubMed:9565988"
FT /id="VAR_010395"
FT VARIANT 167
FT /note="G -> S (in LGMDR4; dbSNP:rs779516489)"
FT /id="VAR_010426"
FT VARIANT 182
FT /note="T -> A (in LGMDR4)"
FT /evidence="ECO:0000269|PubMed:9032047"
FT /id="VAR_010427"
FT VARIANT 184
FT /note="Y -> C (probable disease-associated variant found in
FT a patient with a myopathy resembling Becker muscular
FT dystrophy; dbSNP:rs1365923535)"
FT /evidence="ECO:0000269|PubMed:10660328"
FT /id="VAR_010428"
SQ SEQUENCE 318 AA; 34777 MW; DAC5E93D1AB6C80C CRC64;
MAAAAAAAAE QQSSNGPVKK SMREKAVERR SVNKEHNSNF KAGYIPIDED RLHKTGLRGR
KGNLAICVII LLFILAVINL IITLVIWAVI RIGPNGCDSM EFHESGLLRF KQVSDMGVIH
PLYKSTVGGR RNENLVITGN NQPIVFQQGT TKLSVENNKT SITSDIGMQF FDPRTQNILF
STDYETHEFH LPSGVKSLNV QKASTERITS NATSDLNIKV DGRAIVRGNE GVFIMGKTIE
FHMGGNMELK AENSIILNGS VMVSTTRLPS SSSGDQLGSG DWVRYKLCMC ADGTLFKVQV
TSQNMGCQIS DNPCGNTH
