ID ANO5_HUMAN Reviewed; 913 AA.
AC Q75V66;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 156.
DE RecName: Full=Anoctamin-5;
DE AltName: Full=Gnathodiaphyseal dysplasia 1 protein;
DE AltName: Full=Transmembrane protein 16E;
GN Name=ANO5; Synonyms=GDD1, TMEM16E;
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP VARIANTS GDD GLY-356 AND ARG-356.
RC TISSUE=Skeletal muscle;
RX PubMed=15124103; DOI=10.1086/421527;
RA Tsutsumi S., Kamata N., Vokes T.J., Maruoka Y., Nakakuki K., Enomoto S.,
RA Omura K., Amagasa T., Nagayama M., Saito-Ohara F., Inazawa J., Moritani M.,
RA Yamaoka T., Inoue H., Itakura M.;
RT "The novel gene encoding a putative transmembrane protein is mutated in
RT gnathodiaphyseal dysplasia (GDD).";
RL Am. J. Hum. Genet. 74:1255-1261(2004).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=15067359;
RA Katoh M., Katoh M.;
RT "Identification and characterization of TMEM16E and TMEM16F genes in
RT silico.";
RL Int. J. Oncol. 24:1345-1349(2004).
RN [3]
RP ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20056604; DOI=10.1074/jbc.m109.065367;
RA Schreiber R., Uliyakina I., Kongsuphol P., Warth R., Mirza M.,
RA Martins J.R., Kunzelmann K.;
RT "Expression and function of epithelial anoctamins.";
RL J. Biol. Chem. 285:7838-7845(2010).
RN [4]
RP REVIEW.
RX PubMed=21642943; DOI=10.1038/aps.2011.48;
RA Duran C., Hartzell H.C.;
RT "Physiological roles and diseases of Tmem16/Anoctamin proteins: are they
RT all chloride channels?";
RL Acta Pharmacol. Sin. 32:685-692(2011).
RN [5]
RP REVIEW.
RX PubMed=21607626; DOI=10.1007/s00424-011-0975-9;
RA Kunzelmann K., Tian Y., Martins J.R., Faria D., Kongsuphol P.,
RA Ousingsawat J., Thevenod F., Roussa E., Rock J., Schreiber R.;
RT "Anoctamins.";
RL Pflugers Arch. 462:195-208(2011).
RN [6]
RP ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22075693; DOI=10.1152/ajpcell.00140.2011;
RA Duran C., Qu Z., Osunkoya A.O., Cui Y., Hartzell H.C.;
RT "ANOs 3-7 in the anoctamin/Tmem16 Cl- channel family are intracellular
RT proteins.";
RL Am. J. Physiol. 302:C482-C493(2012).
RN [7]
RP REVIEW.
RX PubMed=22302790; DOI=10.1113/expphysiol.2011.058214;
RA Winpenny J.P., Gray M.A.;
RT "The anoctamin (TMEM16) gene family: calcium-activated chloride channels
RT come of age.";
RL Exp. Physiol. 97:175-176(2012).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=22946059; DOI=10.1242/jcs.109553;
RA Tian Y., Schreiber R., Kunzelmann K.;
RT "Anoctamins are a family of Ca2+ activated Cl- channels.";
RL J. Cell Sci. 125:4991-4998(2012).
RN [9]
RP VARIANT LGMDR12 VAL-231, AND VARIANT MMD3 CYS-758.
RX PubMed=20096397; DOI=10.1016/j.ajhg.2009.12.013;
RA Bolduc V., Marlow G., Boycott K.M., Saleki K., Inoue H., Kroon J.,
RA Itakura M., Robitaille Y., Parent L., Baas F., Mizuta K., Kamata N.,
RA Richard I., Linssen W.H., Mahjneh I., de Visser M., Bashir R., Brais B.;
RT "Recessive mutations in the putative calcium-activated chloride channel
RT Anoctamin 5 cause proximal LGMD2L and distal MMD3 muscular dystrophies.";
RL Am. J. Hum. Genet. 86:213-221(2010).
RN [10]
RP VARIANT LGMDR12 TRP-58, AND VARIANT MMD3 CYS-655.
RX PubMed=22499103; DOI=10.1002/mus.23281;
RA Schessl J., Kress W., Schoser B.;
RT "Novel ANO5 mutations causing hyper-CK-emia, limb girdle muscular weakness
RT and Miyoshi type of muscular dystrophy.";
RL Muscle Nerve 45:740-742(2012).
RN [11]
RP VARIANT GDD ILE-513, AND FUNCTION.
RX PubMed=23047743; DOI=10.1038/ejhg.2012.224;
RA Marconi C., Brunamonti Binello P., Badiali G., Caci E., Cusano R.,
RA Garibaldi J., Pippucci T., Merlini A., Marchetti C., Rhoden K.J.,
RA Galietta L.J., Lalatta F., Balbi P., Seri M.;
RT "A novel missense mutation in ANO5/TMEM16E is causative for
RT gnathodiaphyseal dyplasia in a large Italian pedigree.";
RL Eur. J. Hum. Genet. 21:613-619(2013).
RN [12]
RP VARIANTS LGMDR12 SER-52; SER-54; TRP-58; ILE-87; GLU-93; CYS-143; LYS-202;
RP ALA-206; VAL-231; ASN-259; SER-265; LEU-266; SER-267; LEU-404;
RP 405-GLN--LEU-913 DEL; 421-GLN--LEU-913 DEL; GLY-506; 547-ARG--LEU-913 DEL;
RP GLN-547; ILE-555; SER-578; ILE-618; ASN-701 DEL; SER-714; CYS-758; PRO-781;
RP LEU-796; SER-804; VAL-830; LYS-833; ARG-839 AND LEU-900.
RX PubMed=25891276; DOI=10.1016/j.nmd.2015.03.011;
RA Savarese M., Di Fruscio G., Tasca G., Ruggiero L., Janssens S.,
RA De Bleecker J., Delpech M., Musumeci O., Toscano A., Angelini C.,
RA Sacconi S., Santoro L., Ricci E., Claes K., Politano L., Nigro V.;
RT "Next generation sequencing on patients with LGMD and nonspecific
RT myopathies: Findings associated with ANO5 mutations.";
RL Neuromuscul. Disord. 25:533-541(2015).
RN [13]
RP VARIANT LGMDR12 TRP-58.
RX PubMed=25864073; DOI=10.17712/nsj.2015.2.20140547;
RA Bohlega S., Monies D.M., Abulaban A.A., Murad H.N., Alhindi H.N.,
RA Meyer B.F.;
RT "Clinical and genetic features of anoctaminopathy in Saudi Arabia.";
RL Neurosciences 20:173-177(2015).
RN [14]
RP VARIANT GDD TYR-356.
RX PubMed=27216912; DOI=10.1038/srep26440;
RA Andreeva T.V., Tyazhelova T.V., Rykalina V.N., Gusev F.E., Goltsov A.Y.,
RA Zolotareva O.I., Aliseichik M.P., Borodina T.A., Grigorenko A.P.,
RA Reshetov D.A., Ginter E.K., Amelina S.S., Zinchenko R.A., Rogaev E.I.;
RT "Whole exome sequencing links dental tumor to an autosomal-dominant
RT mutation in ANO5 gene associated with gnathodiaphyseal dysplasia and muscle
RT dystrophies.";
RL Sci. Rep. 6:26440-26440(2016).
RN [15]
RP VARIANTS LGMDR12 TRP-58 AND VAL-231.
RX PubMed=32925086; DOI=10.3233/jnd-200515;
RA Vazquez J., Lefeuvre C., Escobar R.E., Luna Angulo A.B., Miranda Duarte A.,
RA Delia Hernandez A., Brisset M., Carlier R.Y., Leturcq F.,
RA Durand-Canard M.C., Nicolas G., Laforet P., Malfatti E.;
RT "Phenotypic Spectrum of Myopathies with Recessive Anoctamin-5 Mutations.";
RL J. Neuromuscul. Dis. 7:443-451(2020).
RN [16]
RP VARIANT LGMDR12 TRP-58, CHARACTERIZATION OF VARIANT LGMDR12 TRP-58, AND
RP FUNCTION.
RX PubMed=33496727; DOI=10.1083/jcb.202007059;
RA Foltz S.J., Cui Y.Y., Choo H.J., Hartzell H.C.;
RT "ANO5 ensures trafficking of annexins in wounded myofibers.";
RL J. Cell Biol. 220:0-0(2021).
CC -!- FUNCTION: Plays a role in plasma membrane repair in a process involving
CC annexins (PubMed:33496727). Does not exhibit calcium-activated chloride
CC channel (CaCC) activity. {ECO:0000269|PubMed:20056604,
CC ECO:0000269|PubMed:23047743, ECO:0000269|PubMed:33496727}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15124103}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:20056604,
CC ECO:0000269|PubMed:22946059}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Colocalized with CALR/calreticulin
CC (PubMed:15124103). Shows an intracellular localization according to
CC PubMed:22075693. {ECO:0000269|PubMed:15124103,
CC ECO:0000269|PubMed:22075693}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney, lung, and
CC skeletal muscle. Weakly expressed in bone marrow, fetal liver,
CC placenta, spleen, thymus, osteoblasts and periodontal ligament cells.
CC {ECO:0000269|PubMed:15067359, ECO:0000269|PubMed:15124103}.
CC -!- DISEASE: Gnathodiaphyseal dysplasia (GDD) [MIM:166260]: Rare skeletal
CC syndrome characterized by bone fragility, sclerosis of tubular bones,
CC and cemento-osseous lesions of the jawbone. Patients experience
CC frequent bone fractures caused by trivial accidents in childhood;
CC however the fractures heal normally without bone deformity. The jaw
CC lesions replace the tooth-bearing segments of the maxilla and mandible
CC with fibrous connective tissues, including various amounts of cementum-
CC like calcified mass, sometimes causing facial deformities. Patients
CC also have a propensity for jaw infection and often suffer from purulent
CC osteomyelitis-like symptoms, such as swelling of and pus discharge from
CC the gums, mobility of the teeth, insufficient healing after tooth
CC extraction and exposure of the lesions into the oral cavity.
CC {ECO:0000269|PubMed:15124103, ECO:0000269|PubMed:23047743,
CC ECO:0000269|PubMed:27216912}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Muscular dystrophy, limb-girdle, autosomal recessive 12
CC (LGMDR12) [MIM:611307]: An autosomal recessive degenerative myopathy
CC characterized by proximal weakness, weakness of the hip and shoulder
CC girdles and prominent asymmetrical quadriceps femoris and biceps
CC brachii atrophy. {ECO:0000269|PubMed:20096397,
CC ECO:0000269|PubMed:22499103, ECO:0000269|PubMed:25864073,
CC ECO:0000269|PubMed:25891276, ECO:0000269|PubMed:32925086,
CC ECO:0000269|PubMed:33496727}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Miyoshi muscular dystrophy 3 (MMD3) [MIM:613319]: A late-onset
CC muscular dystrophy characterized by distal muscle weakness of the lower
CC limbs, calf muscle discomfort and weakness, quadriceps atrophy. Muscle
CC weakness and atrophy may be asymmetric. {ECO:0000269|PubMed:20096397,
CC ECO:0000269|PubMed:22499103}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: The term 'anoctamin' was coined because these channels
CC are anion selective and have eight (OCT) transmembrane segments. There
CC is some dissatisfaction in the field with the Ano nomenclature because
CC it is not certain that all the members of this family are anion
CC channels or have the 8-transmembrane topology.
CC -!- SIMILARITY: Belongs to the anoctamin family. {ECO:0000305}.
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DR EMBL; AB125267; BAD17859.1; -; mRNA.
DR CCDS; CCDS31444.1; -.
DR RefSeq; NP_001136121.1; NM_001142649.1.
DR RefSeq; NP_998764.1; NM_213599.2.
DR AlphaFoldDB; Q75V66; -.
DR SMR; Q75V66; -.
DR BioGRID; 128482; 14.
DR IntAct; Q75V66; 3.
DR STRING; 9606.ENSP00000315371; -.
DR TCDB; 1.A.17.1.21; the calcium-dependent chloride channel (ca-clc) family.
DR GlyCosmos; Q75V66; 6 sites, No reported glycans.
DR GlyGen; Q75V66; 6 sites.
DR iPTMnet; Q75V66; -.
DR PhosphoSitePlus; Q75V66; -.
DR BioMuta; ANO5; -.
DR DMDM; 74749827; -.
DR MassIVE; Q75V66; -.
DR PaxDb; 9606-ENSP00000315371; -.
DR PeptideAtlas; Q75V66; -.
DR ProteomicsDB; 68653; -.
DR ABCD; Q75V66; 1 sequenced antibody.
DR Antibodypedia; 53749; 89 antibodies from 18 providers.
DR DNASU; 203859; -.
DR Ensembl; ENST00000324559.9; ENSP00000315371.9; ENSG00000171714.13.
DR GeneID; 203859; -.
DR KEGG; hsa:203859; -.
DR MANE-Select; ENST00000324559.9; ENSP00000315371.9; NM_213599.3; NP_998764.1.
DR UCSC; uc001mqi.3; human.
DR AGR; HGNC:27337; -.
DR CTD; 203859; -.
DR DisGeNET; 203859; -.
DR GeneCards; ANO5; -.
DR GeneReviews; ANO5; -.
DR HGNC; HGNC:27337; ANO5.
DR HPA; ENSG00000171714; Group enriched (heart muscle, parathyroid gland, skeletal muscle, tongue).
DR MalaCards; ANO5; -.
DR MIM; 166260; phenotype.
DR MIM; 608662; gene.
DR MIM; 611307; phenotype.
DR MIM; 613319; phenotype.
DR neXtProt; NX_Q75V66; -.
DR OpenTargets; ENSG00000171714; -.
DR Orphanet; 206549; Anoctamin-5-related limb-girdle muscular dystrophy R12.
DR Orphanet; 399096; Distal anoctaminopathy.
DR Orphanet; 53697; Gnathodiaphyseal dysplasia.
DR PharmGKB; PA164715641; -.
DR VEuPathDB; HostDB:ENSG00000171714; -.
DR eggNOG; KOG2514; Eukaryota.
DR GeneTree; ENSGT00940000155692; -.
DR HOGENOM; CLU_006685_1_4_1; -.
DR InParanoid; Q75V66; -.
DR OMA; LRNVQYW; -.
DR OrthoDB; 534027at2759; -.
DR PhylomeDB; Q75V66; -.
DR TreeFam; TF314265; -.
DR PathwayCommons; Q75V66; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR Reactome; R-HSA-9733458; Induction of Cell-Cell Fusion.
DR SignaLink; Q75V66; -.
DR BioGRID-ORCS; 203859; 8 hits in 1151 CRISPR screens.
DR ChiTaRS; ANO5; human.
DR GenomeRNAi; 203859; -.
DR Pharos; Q75V66; Tbio.
DR PRO; PR:Q75V66; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q75V66; Protein.
DR Bgee; ENSG00000171714; Expressed in cardiac muscle of right atrium and 167 other cell types or tissues.
DR Genevisible; Q75V66; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IEA:Ensembl.
DR GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
DR GO; GO:0034220; P:monoatomic ion transmembrane transport; TAS:Reactome.
DR InterPro; IPR032394; Anoct_dimer.
DR InterPro; IPR007632; Anoctamin.
DR InterPro; IPR049452; Anoctamin_TM.
DR PANTHER; PTHR12308; ANOCTAMIN; 1.
DR PANTHER; PTHR12308:SF23; ANOCTAMIN-5; 1.
DR Pfam; PF16178; Anoct_dimer; 1.
DR Pfam; PF04547; Anoctamin; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disease variant; Endoplasmic reticulum; Glycoprotein;
KW Limb-girdle muscular dystrophy; Membrane; Osteogenesis imperfecta;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..913
FT /note="Anoctamin-5"
FT /id="PRO_0000191755"
FT TOPO_DOM 1..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..380
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 484..511
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 533..557
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 579..679
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 680..700
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 701..732
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 733..753
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 754..834
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 835..855
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 856..913
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 768
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 52
FT /note="N -> S (in LGMDR12; uncertain significance;
FT dbSNP:rs143777403)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080271"
FT VARIANT 54
FT /note="F -> S (in LGMDR12; uncertain significance;
FT dbSNP:rs886043577)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080272"
FT VARIANT 58
FT /note="R -> W (in LGMDR12; pathogenic; results in defective
FT sarcolemma repair in cultured muscle cells;
FT dbSNP:rs201725369)"
FT /evidence="ECO:0000269|PubMed:22499103,
FT ECO:0000269|PubMed:25864073, ECO:0000269|PubMed:25891276,
FT ECO:0000269|PubMed:32925086, ECO:0000269|PubMed:33496727"
FT /id="VAR_068247"
FT VARIANT 87
FT /note="V -> I (in LGMDR12; uncertain significance;
FT dbSNP:rs34994927)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080273"
FT VARIANT 93
FT /note="D -> E (in LGMDR12; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080274"
FT VARIANT 143
FT /note="Y -> C (in LGMDR12; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080275"
FT VARIANT 202
FT /note="E -> K (in LGMDR12; uncertain significance;
FT dbSNP:rs115750596)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080276"
FT VARIANT 206
FT /note="T -> A (in LGMDR12; uncertain significance;
FT dbSNP:rs78266558)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080277"
FT VARIANT 231
FT /note="G -> V (in LGMDR12; dbSNP:rs137854523)"
FT /evidence="ECO:0000269|PubMed:20096397,
FT ECO:0000269|PubMed:25891276, ECO:0000269|PubMed:32925086"
FT /id="VAR_063582"
FT VARIANT 259
FT /note="K -> N (in LGMDR12; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080278"
FT VARIANT 265
FT /note="N -> S (in LGMDR12; uncertain significance;
FT dbSNP:rs377553546)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080279"
FT VARIANT 266
FT /note="P -> L (in LGMDR12; uncertain significance;
FT dbSNP:rs745908606)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080280"
FT VARIANT 267
FT /note="T -> S (in LGMDR12; uncertain significance;
FT dbSNP:rs138144479)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080281"
FT VARIANT 322
FT /note="L -> F (in dbSNP:rs7481951)"
FT /id="VAR_052339"
FT VARIANT 356
FT /note="C -> G (in GDD; dbSNP:rs119103234)"
FT /evidence="ECO:0000269|PubMed:15124103"
FT /id="VAR_023524"
FT VARIANT 356
FT /note="C -> R (in GDD; dbSNP:rs119103234)"
FT /evidence="ECO:0000269|PubMed:15124103"
FT /id="VAR_023525"
FT VARIANT 356
FT /note="C -> Y (in GDD)"
FT /evidence="ECO:0000269|PubMed:27216912"
FT /id="VAR_076476"
FT VARIANT 404
FT /note="R -> L (in LGMDR12; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080282"
FT VARIANT 405..913
FT /note="Missing (in LGMDR12)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080301"
FT VARIANT 421..913
FT /note="Missing (in LGMDR12)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080283"
FT VARIANT 506
FT /note="S -> G (in LGMDR12; uncertain significance;
FT dbSNP:rs141799673)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080284"
FT VARIANT 513
FT /note="T -> I (in GDD; uncertain significance;
FT dbSNP:rs281865467)"
FT /evidence="ECO:0000269|PubMed:23047743"
FT /id="VAR_076477"
FT VARIANT 547..913
FT /note="Missing (in LGMDR12; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080285"
FT VARIANT 547
FT /note="R -> Q (in LGMDR12; uncertain significance;
FT dbSNP:rs139618850)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080286"
FT VARIANT 555
FT /note="S -> I (in LGMDR12; uncertain significance;
FT dbSNP:rs375014127)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080287"
FT VARIANT 578
FT /note="F -> S (in LGMDR12; uncertain significance;
FT dbSNP:rs137854526)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080288"
FT VARIANT 618
FT /note="M -> I (in LGMDR12; uncertain significance;
FT dbSNP:rs1422717390)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080289"
FT VARIANT 655
FT /note="W -> C (in MMD3; uncertain significance;
FT dbSNP:rs760137559)"
FT /evidence="ECO:0000269|PubMed:22499103"
FT /id="VAR_068248"
FT VARIANT 701
FT /note="Missing (in LGMDR12; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080290"
FT VARIANT 714
FT /note="T -> S (in LGMDR12; uncertain significance;
FT dbSNP:rs200631556)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080291"
FT VARIANT 758
FT /note="R -> C (in MMD3 and LGMDR12; uncertain significance;
FT dbSNP:rs137854529)"
FT /evidence="ECO:0000269|PubMed:20096397,
FT ECO:0000269|PubMed:25891276"
FT /id="VAR_063583"
FT VARIANT 781
FT /note="L -> P (in LGMDR12; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080292"
FT VARIANT 796
FT /note="S -> L (in LGMDR12; uncertain significance;
FT dbSNP:rs61910685)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080293"
FT VARIANT 804
FT /note="C -> S (in LGMDR12; uncertain significance;
FT dbSNP:rs1233836740)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080294"
FT VARIANT 830
FT /note="A -> V (in LGMDR12; uncertain significance;
FT dbSNP:rs766853141)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080295"
FT VARIANT 833
FT /note="M -> K (in LGMDR12; uncertain significance;
FT dbSNP:rs142073798)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080296"
FT VARIANT 839
FT /note="M -> R (in LGMDR12; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080297"
FT VARIANT 882
FT /note="N -> K (in dbSNP:rs34969327)"
FT /id="VAR_052340"
FT VARIANT 900
FT /note="M -> L (in LGMDR12; uncertain significance;
FT dbSNP:rs148293985)"
FT /evidence="ECO:0000269|PubMed:25891276"
FT /id="VAR_080298"
SQ SEQUENCE 913 AA; 107188 MW; 98BC40318678C073 CRC64;
MGDPDLLEVL AEEGEKVNKH IDYSFQMSEQ SLSSRETSFL INEETMPAKR FNLFLRRRLM
FQKNQQSKDS IFFRDGIRQI DFVLSYVDDV KKDAELKAER RKEFETNLRK TGLELEIEDK
RDSEDGRTYF VKIHAPWEVL VTYAEVLGIK MPIKESDIPR PKHTPISYVL GPVRLPLSVK
YPHPEYFTAQ FSRHRQELFL IEDQATFFPS SSRNRIVYYI LSRCPFGIED GKKRFGIERL
LNSNTYSSAY PLHDGQYWKP SEPPNPTNER YTLHQNWARF SYFYKEQPLD LIKNYYGEKI
GIYFVFLGFY TEMLFFAAVV GLACFIYGLL SMEHNTSSTE ICDPEIGGQM IMCPLCDQVC
DYWRLNSTCL ASKFSHLFDN ESTVFFAIFM GIWVTLFLEF WKQRQARLEY EWDLVDFEEE
QQQLQLRPEF EAMCKHRKLN AVTKEMEPYM PLYTRIPWYF LSGATVTLWM SLVVTSMVAV
IVYRLSVFAT FASFMESDAS LKQVKSFLTP QITTSLTGSC LNFIVILILN FFYEKISAWI
TKMEIPRTYQ EYESSLTLKM FLFQFVNFYS SCFYVAFFKG KFVGYPGKYT YLFNEWRSEE
CDPGGCLIEL TTQLTIIMTG KQIFGNIKEA IYPLALNWWR RRKARTNSEK LYSRWEQDHD
LESFGPLGLF YEYLETVTQF GFVTLFVASF PLAPLLALIN NIVEIRVDAW KLTTQYRRTV
ASKAHSIGVW QDILYGMAVL SVATNAFIVA FTSDIIPRLV YYYAYSTNAT QPMTGYVNNS
LSVFLIADFP NHTAPSEKRD FITCRYRDYR YPPDDENKYF HNMQFWHVLA AKMTFIIVME
HVVFLVKFLL AWMIPDVPKD VVERIKREKL MTIKILHDFE LNKLKENLGI NSNEFAKHVM
IEENKAQLAK STL
//
