CAN3_HUMAN
ID CAN3_HUMAN Reviewed; 821 AA.
AC P20807; A6H8K6; Q7L4R0; Q9BQC8; Q9BTU4; Q9Y5S6; Q9Y5S7;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=Calpain-3 {ECO:0000305};
DE EC=3.4.22.54;
DE AltName: Full=Calcium-activated neutral proteinase 3;
DE Short=CANP 3;
DE AltName: Full=Calpain L3;
DE AltName: Full=Calpain p94;
DE AltName: Full=Muscle-specific calcium-activated neutral protease 3;
DE AltName: Full=New calpain 1;
DE Short=nCL-1;
GN Name=CAPN3 {ECO:0000312|HGNC:HGNC:1480}; Synonyms=CANP3, CANPL3, NCL1;
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 I), AND VARIANTS LGMDR1.
RX PubMed=7720071; DOI=10.1016/0092-8674(95)90368-2;
RA Richard I., Broux O., Allamand V., Fougerousse F., Chiannilkulchai N.,
RA Bourg N., Brenguier L., Devaud C., Pasturaud P., Roudaut C., Hillaire D.,
RA Passos-Bueno M.-R., Zatz M., Tischfield J.A., Fardeau M., Jackson C.E.,
RA Cohen D., Beckmann J.S.;
RT "Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular
RT dystrophy type 2A.";
RL Cell 81:27-40(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM I).
RA Mashima H., Horikawa Y., Cox N.J., Bell G.I.;
RT "hCAPN3-hZFP106 genomic sequence.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS II AND III).
RA Dickson J.M.J., Love D., Evans C.W.E.;
RT "Alternatively exon-spliced isoforms of calpain 3 expressed in human
RT leukocytes.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IV).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-21; GLY-160 AND
RP THR-236.
RG NIEHS SNPs program;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS IV AND V).
RC TISSUE=Skin, and Uterus;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 44-821 (ISOFORM I).
RX PubMed=2555341; DOI=10.1016/s0021-9258(19)47225-6;
RA Sorimachi H., Imajoh-Ohmi S., Emori Y., Kawasaki H., Ohno S., Minami Y.,
RA Suzuki K.;
RT "Molecular cloning of a novel mammalian calcium-dependent protease distinct
RT from both m- and mu-types. Specific expression of the mRNA in skeletal
RT muscle.";
RL J. Biol. Chem. 264:20106-20111(1989).
RN [9]
RP INTERACTION WITH TTN.
RX PubMed=14583192; DOI=10.1016/j.jmb.2003.09.012;
RA Miller M.K., Bang M.-L., Witt C.C., Labeit D., Trombitas C., Watanabe K.,
RA Granzier H., McElhinny A.S., Gregorio C.C., Labeit S.;
RT "The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a family
RT of titin filament-based stress response molecules.";
RL J. Mol. Biol. 333:951-964(2003).
RN [10]
RP REVIEW ON VARIANTS.
RX PubMed=10330340; DOI=10.1086/302426;
RA Richard I., Roudaut C., Saenz A., Pogue R., Grimbergen J.E.M.A.,
RA Anderson L.V.B., Beley C., Cobo A.-M., de Diego C., Eymard B., Gallano P.,
RA Ginjaar H.B., Lasa A., Pollitt C., Topaloglu H., Urtizberea J.A.,
RA de Visser M., van der Kooi A., Bushby K., Bakker E., Lopez de Munain A.,
RA Fardeau M., Beckmann J.S.;
RT "Calpainopathy -- a survey of mutations and polymorphisms.";
RL Am. J. Hum. Genet. 64:1524-1540(1999).
RN [11]
RP INTERACTION WITH CMYA5, AND MUTAGENESIS OF CYS-129.
RX PubMed=20634290; DOI=10.1074/jbc.m110.108720;
RA Sarparanta J., Blandin G., Charton K., Vihola A., Marchand S., Milic A.,
RA Hackman P., Ehler E., Richard I., Udd B.;
RT "Interactions with M-band titin and calpain 3 link myospryn (CMYA5) to
RT tibial and limb-girdle muscular dystrophies.";
RL J. Biol. Chem. 285:30304-30315(2010).
RN [12]
RP FUNCTION, INTERACTION WITH UTP25, AND SUBCELLULAR LOCATION.
RX PubMed=23357851; DOI=10.1038/cr.2013.16;
RA Tao T., Shi H., Guan Y., Huang D., Chen Y., Lane D.P., Chen J., Peng J.;
RT "Def defines a conserved nucleolar pathway that leads p53 to proteasome-
RT independent degradation.";
RL Cell Res. 23:620-634(2013).
RN [13]
RP FUNCTION, AND INTERACTION WITH SIMC1.
RX PubMed=23707407; DOI=10.1016/j.jmb.2013.05.009;
RA Ono Y., Iemura S., Novak S.M., Doi N., Kitamura F., Natsume T.,
RA Gregorio C.C., Sorimachi H.;
RT "PLEIAD/SIMC1/C5orf25, a novel autolysis regulator for a skeletal-muscle-
RT specific calpain, CAPN3, scaffolds a CAPN3 substrate, CTBP1.";
RL J. Mol. Biol. 425:2955-2972(2013).
RN [14]
RP FUNCTION, INTERACTION WITH CAPN3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-129.
RX PubMed=27657329; DOI=10.1371/journal.pbio.1002555;
RA Guan Y., Huang D., Chen F., Gao C., Tao T., Shi H., Zhao S., Liao Z.,
RA Lo L.J., Wang Y., Chen J., Peng J.;
RT "Phosphorylation of Def Regulates Nucleolar p53 Turnover and Cell Cycle
RT Progression through Def Recruitment of Calpain3.";
RL PLoS Biol. 14:e1002555-e1002555(2016).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 642-821 IN COMPLEX WITH CALCIUM,
RP AND SUBUNIT.
RX PubMed=24846670; DOI=10.1111/febs.12849;
RA Partha S.K., Ravulapalli R., Allingham J.S., Campbell R.L., Davies P.L.;
RT "Crystal structure of calpain-3 penta-EF-hand (PEF) domain - a
RT homodimerized PEF family member with calcium bound at the fifth EF-hand.";
RL FEBS J. 281:3138-3149(2014).
RN [16]
RP VARIANTS LGMDR1 GLN-572 AND GLY-744.
RX PubMed=8624690; DOI=10.1093/brain/119.1.295;
RA Fardeau M., Hillaire D., Mignard C., Feingold N., Feingold J., Mignard D.,
RA de Ubeda B., Collin H., Tome F.M.S., Richard I., Beckmann J.S.;
RT "Juvenile limb-girdle muscular dystrophy. Clinical, histopathological and
RT genetic data from a small community living in the Reunion island.";
RL Brain 119:295-308(1996).
RN [17]
RP VARIANTS LGMDR1 PHE-86; 215-SER--GLY-221 DEL; PRO-215; LEU-319; GLN-334;
RP TRP-440; TRP-490; ARG-496; TRP-567; TRP-572; LEU-606; VAL-702 AND GLN-748.
RX PubMed=9150160;
RA Richard I., Brenguier L., Dincer P., Roudaut C., Bady B., Burgunder J.-M.,
RA Chemaly R., Garcia C.A., Halaby G., Jackson C.E., Kurnit D.M., Lefranc G.,
RA Legum C., Loiselet J., Merlini L., Nivelon-Chevallier A.,
RA Ollagnon-Roman E., Restagno G., Topaloglu H., Beckmann J.S.;
RT "Multiple independent molecular etiology for limb-girdle muscular dystrophy
RT type 2A patients from various geographical origins.";
RL Am. J. Hum. Genet. 60:1128-1138(1997).
RN [18]
RP VARIANTS LGMDR1 ASN-336; GLN-490; VAL-702 AND GLN-748.
RX PubMed=9266733; DOI=10.1002/ana.410420214;
RA Dincer P., Leturcq F., Richard I., Piccolo F., Yalnizoglu D., de Toma C.,
RA Akcoeren Z., Broux O., Deburgrave N., Brenguier L., Roudaut C.,
RA Urtizberea J.A., Jung D., Tan E., Jeanpierre M., Campbell K.P.,
RA Kaplan J.-C., Beckmann J.S., Topaloglu H.;
RT "A biochemical, genetic, and clinical survey of autosomal recessive limb
RT girdle muscular dystrophies in Turkey.";
RL Ann. Neurol. 42:222-229(1997).
RN [19]
RP VARIANTS LGMDR1 ARG-222; GLU-486; TRP-489 AND GLN-748.
RX PubMed=9762961; DOI=10.1093/brain/121.9.1735;
RA Urtasun M., Saenz A., Roudaut C., Poza J.J., Urtizberea J.A., Cobo A.-M.,
RA Richard I., Garcia Bragado F., Leturcq F., Kaplan J.-C., Marti Masso J.F.,
RA Beckmann J.S., Lopez de Munain A.;
RT "Limb-girdle muscular dystrophy in Guipuzcoa (Basque Country, Spain).";
RL Brain 121:1735-1747(1998).
RN [20]
RP VARIANT LGMDR1 200-PHE--LEU-204 DEL.
RX PubMed=9452114; DOI=10.1002/humu.1380110193;
RA Haeffner K., Speer A., Huebner C., Voit T., Oexle K.;
RT "A small in-frame deletion within the protease domain of muscle-specific
RT calpain, p94 causes early-onset limb-girdle muscular dystrophy 2A.";
RL Hum. Mutat. Suppl. 1:S298-S300(1998).
RN [21]
RP VARIANT LGMDR1 GLY-744.
RX PubMed=9655129;
RX DOI=10.1002/(sici)1097-4598(199808)21:8<1078::aid-mus15>3.0.co;2-q;
RA Penisson-Besnier I., Richard I., Dubas F., Beckmann J.S., Fardeau M.;
RT "Pseudometabolic expression and phenotypic variability of calpain
RT deficiency in two siblings.";
RL Muscle Nerve 21:1078-1080(1998).
RN [22]
RP VARIANT LGMDR1 CYS-360.
RX PubMed=9771675;
RX DOI=10.1002/(sici)1097-4598(199811)21:11<1493::aid-mus19>3.0.co;2-1;
RA Kawai H., Akaike M., Kunishige M., Inui T., Adachi K., Kimura C.,
RA Kawajiri M., Nishida Y., Endo I., Kashiwagi S., Nishino H., Fujiwara T.,
RA Okuno S., Roudaut C., Richard I., Beckmann J.S., Miyoshi K., Matsumoto T.;
RT "Clinical, pathological, and genetic features of limb-girdle muscular
RT dystrophy type 2A with new calpain 3 gene mutations in seven patients from
RT three Japanese families.";
RL Muscle Nerve 21:1493-1501(1998).
RN [23]
RP VARIANTS LGMDR1 266-ILE-ASP-267 DEL; TRP-572; VAL-702 AND GLN-748.
RX PubMed=27234031; DOI=10.1111/cge.12810;
RA Fattahi Z., Kalhor Z., Fadaee M., Vazehan R., Parsimehr E., Abolhassani A.,
RA Beheshtian M., Zamani G., Nafissi S., Nilipour Y., Akbari M.R., Kahrizi K.,
RA Kariminejad A., Najmabadi H.;
RT "Improved diagnostic yield of neuromuscular disorders applying clinical
RT exome sequencing in patients arising from a consanguineous population.";
RL Clin. Genet. 91:386-402(2017).
RN [24]
RP VARIANTS LGMDR1 266-ILE-ASP-267 DEL AND GLN-748.
RX PubMed=27020652; DOI=10.1016/j.nmd.2016.02.003;
RA Fadaee M., Kariminejad A., Fattahi Z., Nafissi S., Godarzi H.R.,
RA Beheshtian M., Vazehan R., Akbari M.R., Kahrizi K., Najmabadi H.;
RT "Report of limb girdle muscular dystrophy type 2a in 6 Iranian patients,
RT one with a novel deletion in CAPN3 gene.";
RL Neuromuscul. Disord. 26:277-282(2016).
RN [25]
RP VARIANT LGMDD4 215-SER--GLY-221 DEL, AND INVOLVEMENT IN LGMDD4.
RX PubMed=27259757; DOI=10.1093/brain/aww133;
RA Vissing J., Barresi R., Witting N., Van Ghelue M., Gammelgaard L.,
RA Bindoff L.A., Straub V., Lochmueller H., Hudson J., Wahl C.M.,
RA Arnardottir S., Dahlbom K., Jonsrud C., Duno M.;
RT "A heterozygous 21-bp deletion in CAPN3 causes dominantly inherited limb
RT girdle muscular dystrophy.";
RL Brain 139:2154-2163(2016).
RN [26]
RP VARIANT LGMDD4 215-SER--GLY-221 DEL, AND INVOLVEMENT IN LGMDD4.
RX PubMed=28881388; DOI=10.1002/mus.25970;
RA Martinez-Thompson J.M., Niu Z., Tracy J.A., Moore S.A., Swenson A.,
RA Wieben E.D., Milone M.;
RT "Autosomal dominant calpainopathy due to heterozygous CAPN3
RT C.643_663del21.";
RL Muscle Nerve 57:679-683(2018).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
CC Proteolytically cleaves CTBP1 at 'His-409'. Mediates, with UTP25, the
CC proteasome-independent degradation of p53/TP53 (PubMed:23357851,
CC PubMed:27657329). {ECO:0000269|PubMed:23357851,
CC ECO:0000269|PubMed:23707407, ECO:0000269|PubMed:27657329}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad endopeptidase activity.; EC=3.4.22.54;
CC -!- ACTIVITY REGULATION: Activated by micromolar concentrations of calcium
CC and inhibited by calpastatin.
CC -!- SUBUNIT: Homodimer; via EF-hand domain 4 (PubMed:24846670). Interacts
CC with TTN/titin (PubMed:14583192). Interacts with CMYA5; this
CC interaction, which results in CMYA5 proteolysis, may protect CAPN3 from
CC autolysis (PubMed:20634290). Interacts with SIMC1 (PubMed:23707407).
CC Interacts with UTP25; the interaction is required for CAPN3
CC translocation to the nucleolus (PubMed:23357851, PubMed:27657329).
CC {ECO:0000269|PubMed:14583192, ECO:0000269|PubMed:20634290,
CC ECO:0000269|PubMed:23357851, ECO:0000269|PubMed:23707407,
CC ECO:0000269|PubMed:24846670, ECO:0000269|PubMed:27657329}.
CC -!- INTERACTION:
CC P20807; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-5655000, EBI-741158;
CC P20807; Q9UJX0: OSGIN1; NbExp=4; IntAct=EBI-5655000, EBI-9057006;
CC P20807; Q8WZ42: TTN; NbExp=4; IntAct=EBI-5655000, EBI-681210;
CC P20807-2; Q12800: TFCP2; NbExp=3; IntAct=EBI-16433991, EBI-717422;
CC P20807-4; Q13895: BYSL; NbExp=3; IntAct=EBI-11532021, EBI-358049;
CC P20807-4; P20807-4: CAPN3; NbExp=3; IntAct=EBI-11532021, EBI-11532021;
CC P20807-4; P55212: CASP6; NbExp=3; IntAct=EBI-11532021, EBI-718729;
CC P20807-4; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-11532021, EBI-10171570;
CC P20807-4; P28329-3: CHAT; NbExp=3; IntAct=EBI-11532021, EBI-25837549;
CC P20807-4; Q08426: EHHADH; NbExp=3; IntAct=EBI-11532021, EBI-2339219;
CC P20807-4; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-11532021, EBI-742102;
CC P20807-4; P22607: FGFR3; NbExp=3; IntAct=EBI-11532021, EBI-348399;
CC P20807-4; P06396: GSN; NbExp=3; IntAct=EBI-11532021, EBI-351506;
CC P20807-4; Q969Y2: GTPBP3; NbExp=3; IntAct=EBI-11532021, EBI-740290;
CC P20807-4; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-11532021, EBI-2556193;
CC P20807-4; P13473-2: LAMP2; NbExp=3; IntAct=EBI-11532021, EBI-21591415;
CC P20807-4; Q9BXW4: MAP1LC3C; NbExp=3; IntAct=EBI-11532021, EBI-2603996;
CC P20807-4; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-11532021, EBI-741158;
CC P20807-4; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-11532021, EBI-5280197;
CC P20807-4; P62826: RAN; NbExp=3; IntAct=EBI-11532021, EBI-286642;
CC P20807-4; Q7L099: RUFY3; NbExp=3; IntAct=EBI-11532021, EBI-722392;
CC P20807-4; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-11532021, EBI-2623095;
CC P20807-4; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-11532021, EBI-741480;
CC P20807-4; Q14119: VEZF1; NbExp=3; IntAct=EBI-11532021, EBI-11980193;
CC P20807-4; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-11532021, EBI-11741890;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus
CC {ECO:0000269|PubMed:23357851, ECO:0000269|PubMed:27657329}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=I;
CC IsoId=P20807-1; Sequence=Displayed;
CC Name=II;
CC IsoId=P20807-2; Sequence=VSP_005227, VSP_005228;
CC Name=III;
CC IsoId=P20807-3; Sequence=VSP_005229;
CC Name=IV;
CC IsoId=P20807-4; Sequence=VSP_007813;
CC Name=V;
CC IsoId=P20807-5; Sequence=VSP_044255;
CC -!- TISSUE SPECIFICITY: Isoform I is skeletal muscle specific.
CC -!- DISEASE: Muscular dystrophy, limb-girdle, autosomal recessive 1
CC (LGMDR1) [MIM:253600]: An autosomal recessive degenerative myopathy
CC characterized by progressive symmetrical atrophy and weakness of the
CC proximal limb muscles and elevated serum creatine kinase. The symptoms
CC usually begin during the first two decades of life, and the disease
CC gradually worsens, often resulting in loss of walking ability 10 or 20
CC years after onset. {ECO:0000269|PubMed:27020652,
CC ECO:0000269|PubMed:27234031, ECO:0000269|PubMed:7720071,
CC ECO:0000269|PubMed:8624690, ECO:0000269|PubMed:9150160,
CC ECO:0000269|PubMed:9266733, ECO:0000269|PubMed:9452114,
CC ECO:0000269|PubMed:9655129, ECO:0000269|PubMed:9762961,
CC ECO:0000269|PubMed:9771675}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Muscular dystrophy, limb-girdle, autosomal dominant 4 (LGMDD4)
CC [MIM:618129]: A form of autosomal dominant limb-girdle muscular
CC dystrophy, a myopathy characterized by proximal and/or distal muscle
CC weakness and atrophy. The age at onset is variable and can range from
CC the first to the sixth decade, although later onset is less common.
CC LGMDD4 is characterized by onset of proximal muscle weakness in young
CC adulthood, gait difficulties, increased serum creatine kinase, myalgia,
CC and back pain. Some patients may have upper limb involvement. Disease
CC severity and expressivity are highly variable.
CC {ECO:0000269|PubMed:27259757, ECO:0000269|PubMed:28881388}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Leiden Muscular Dystrophy pages; Note=Calpain-3
CC mutations in LGMD2A;
CC URL="https://www.dmd.nl/capn3_home.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/capn3/";
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; X85030; CAA59403.1; -; mRNA.
DR EMBL; AF209502; AAL40183.1; -; Genomic_DNA.
DR EMBL; AF127764; AAD28253.1; -; mRNA.
DR EMBL; AF127765; AAD28254.3; -; mRNA.
DR EMBL; BT007322; AAP35986.1; -; mRNA.
DR EMBL; AY902237; AAW69391.1; -; Genomic_DNA.
DR EMBL; AC012651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003169; AAH03169.1; -; mRNA.
DR EMBL; BC003521; AAH03521.1; -; mRNA.
DR EMBL; BC004883; AAH04883.1; -; mRNA.
DR EMBL; BC007810; AAH07810.3; -; mRNA.
DR EMBL; BC067126; AAH67126.1; -; mRNA.
DR EMBL; BC100782; AAI00783.1; -; mRNA.
DR EMBL; BC107791; AAI07792.1; -; mRNA.
DR EMBL; BC128605; AAI28606.1; -; mRNA.
DR EMBL; BC146649; AAI46650.1; -; mRNA.
DR EMBL; BC146672; AAI46673.1; -; mRNA.
DR CCDS; CCDS10085.1; -. [P20807-2]
DR CCDS; CCDS10086.1; -. [P20807-5]
DR CCDS; CCDS32207.1; -. [P20807-3]
DR CCDS; CCDS45245.1; -. [P20807-1]
DR CCDS; CCDS45246.1; -. [P20807-4]
DR PIR; A56218; CIHUH3.
DR RefSeq; NP_000061.1; NM_000070.2. [P20807-1]
DR RefSeq; NP_077320.1; NM_024344.1. [P20807-3]
DR RefSeq; NP_775110.1; NM_173087.1. [P20807-2]
DR RefSeq; NP_775111.1; NM_173088.1. [P20807-4]
DR RefSeq; NP_775112.1; NM_173089.1. [P20807-5]
DR RefSeq; NP_775113.1; NM_173090.1. [P20807-5]
DR PDB; 4OKH; X-ray; 2.45 A; A/B/C=642-821.
DR PDB; 6BDT; X-ray; 2.30 A; A/B/C/D=46-419.
DR PDB; 6BGP; X-ray; 2.75 A; A/B/C/D=46-419.
DR PDB; 6BJD; X-ray; 2.80 A; A/B/C/D=46-419.
DR PDB; 6BKJ; X-ray; 3.20 A; A/B/C/D=46-419.
DR PDBsum; 4OKH; -.
DR PDBsum; 6BDT; -.
DR PDBsum; 6BGP; -.
DR PDBsum; 6BJD; -.
DR PDBsum; 6BKJ; -.
DR AlphaFoldDB; P20807; -.
DR SMR; P20807; -.
DR BioGRID; 107275; 37.
DR IntAct; P20807; 44.
DR MINT; P20807; -.
DR STRING; 9606.ENSP00000380349; -.
DR DrugBank; DB06124; L-aminocarnityl-succinyl-leucyl-argininal-diethylacetal.
DR MEROPS; C02.004; -.
DR GlyGen; P20807; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; P20807; -.
DR PhosphoSitePlus; P20807; -.
DR BioMuta; CAPN3; -.
DR jPOST; P20807; -.
DR MassIVE; P20807; -.
DR PaxDb; P20807; -.
DR PeptideAtlas; P20807; -.
DR PRIDE; P20807; -.
DR ProteomicsDB; 53791; -. [P20807-1]
DR ProteomicsDB; 53792; -. [P20807-2]
DR ProteomicsDB; 53793; -. [P20807-3]
DR ProteomicsDB; 53794; -. [P20807-4]
DR ProteomicsDB; 78657; -.
DR Antibodypedia; 10719; 198 antibodies from 29 providers.
DR DNASU; 825; -.
DR Ensembl; ENST00000337571.9; ENSP00000336840.4; ENSG00000092529.25. [P20807-5]
DR Ensembl; ENST00000349748.8; ENSP00000183936.4; ENSG00000092529.25. [P20807-2]
DR Ensembl; ENST00000356316.7; ENSP00000348667.4; ENSG00000092529.25. [P20807-5]
DR Ensembl; ENST00000357568.8; ENSP00000350181.3; ENSG00000092529.25. [P20807-3]
DR Ensembl; ENST00000397163.8; ENSP00000380349.3; ENSG00000092529.25. [P20807-1]
DR Ensembl; ENST00000397200.8; ENSP00000380384.4; ENSG00000092529.25. [P20807-4]
DR Ensembl; ENST00000397204.9; ENSP00000380387.4; ENSG00000092529.25. [P20807-5]
DR Ensembl; ENST00000569136.6; ENSP00000455254.1; ENSG00000092529.25. [P20807-5]
DR Ensembl; ENST00000673692.1; ENSP00000501138.1; ENSG00000092529.25. [P20807-5]
DR Ensembl; ENST00000673771.1; ENSP00000501023.1; ENSG00000092529.25. [P20807-5]
DR Ensembl; ENST00000673851.1; ENSP00000501142.1; ENSG00000092529.25. [P20807-5]
DR Ensembl; ENST00000673886.1; ENSP00000501155.1; ENSG00000092529.25. [P20807-5]
DR Ensembl; ENST00000673890.1; ENSP00000501293.1; ENSG00000092529.25. [P20807-5]
DR Ensembl; ENST00000673928.1; ENSP00000501099.1; ENSG00000092529.25. [P20807-5]
DR Ensembl; ENST00000673936.1; ENSP00000501189.1; ENSG00000092529.25. [P20807-5]
DR Ensembl; ENST00000674018.1; ENSP00000501271.1; ENSG00000092529.25. [P20807-5]
DR Ensembl; ENST00000674093.1; ENSP00000501303.1; ENSG00000092529.25. [P20807-5]
DR Ensembl; ENST00000674119.1; ENSP00000501217.1; ENSG00000092529.25. [P20807-5]
DR Ensembl; ENST00000674139.1; ENSP00000501054.1; ENSG00000092529.25. [P20807-5]
DR Ensembl; ENST00000674146.1; ENSP00000501175.1; ENSG00000092529.25. [P20807-5]
DR Ensembl; ENST00000674149.1; ENSP00000501112.1; ENSG00000092529.25. [P20807-5]
DR GeneID; 825; -.
DR KEGG; hsa:825; -.
DR MANE-Select; ENST00000397163.8; ENSP00000380349.3; NM_000070.3; NP_000061.1.
DR UCSC; uc001zpn.2; human. [P20807-1]
DR CTD; 825; -.
DR DisGeNET; 825; -.
DR GeneCards; CAPN3; -.
DR GeneReviews; CAPN3; -.
DR HGNC; HGNC:1480; CAPN3.
DR HPA; ENSG00000092529; Tissue enhanced (brain, skeletal muscle, tongue).
DR MalaCards; CAPN3; -.
DR MIM; 114240; gene.
DR MIM; 253600; phenotype.
DR MIM; 618129; phenotype.
DR neXtProt; NX_P20807; -.
DR OpenTargets; ENSG00000092529; -.
DR Orphanet; 267; Calpain-3-related limb-girdle muscular dystrophy R1.
DR PharmGKB; PA26061; -.
DR VEuPathDB; HostDB:ENSG00000092529; -.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000156092; -.
DR HOGENOM; CLU_010982_0_1_1; -.
DR InParanoid; P20807; -.
DR OMA; EMNLIEW; -.
DR OrthoDB; 704215at2759; -.
DR PhylomeDB; P20807; -.
DR TreeFam; TF314748; -.
DR BRENDA; 3.4.22.54; 2681.
DR BRENDA; 3.4.22.56; 2681.
DR PathwayCommons; P20807; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR SignaLink; P20807; -.
DR SIGNOR; P20807; -.
DR BioGRID-ORCS; 825; 16 hits in 1073 CRISPR screens.
DR ChiTaRS; CAPN3; human.
DR GeneWiki; CAPN3; -.
DR GenomeRNAi; 825; -.
DR Pharos; P20807; Tbio.
DR PRO; PR:P20807; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P20807; protein.
DR Bgee; ENSG00000092529; Expressed in hindlimb stylopod muscle and 91 other tissues.
DR ExpressionAtlas; P20807; baseline and differential.
DR Genevisible; P20807; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030016; C:myofibril; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0030315; C:T-tubule; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0003824; F:catalytic activity; IDA:UniProtKB.
DR GO; GO:0008234; F:cysteine-type peptidase activity; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0055103; F:ligase regulator activity; IDA:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; ISS:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0031402; F:sodium ion binding; ISS:UniProtKB.
DR GO; GO:0008307; F:structural constituent of muscle; ISS:UniProtKB.
DR GO; GO:0031432; F:titin binding; IPI:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
DR GO; GO:1990092; P:calcium-dependent self proteolysis; IDA:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0071472; P:cellular response to salt stress; ISS:UniProtKB.
DR GO; GO:0070315; P:G1 to G0 transition involved in cell differentiation; IEA:Ensembl.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; TAS:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; TAS:UniProtKB.
DR GO; GO:0061061; P:muscle structure development; ISS:UniProtKB.
DR GO; GO:0030239; P:myofibril assembly; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISS:UniProtKB.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR GO; GO:0014718; P:positive regulation of satellite cell activation involved in skeletal muscle regeneration; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IDA:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
DR GO; GO:0072657; P:protein localization to membrane; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0050790; P:regulation of catalytic activity; IDA:UniProtKB.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0045661; P:regulation of myoblast differentiation; IEA:Ensembl.
DR GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
DR GO; GO:0014850; P:response to muscle activity; ISS:UniProtKB.
DR GO; GO:0045214; P:sarcomere organization; ISS:UniProtKB.
DR GO; GO:0097264; P:self proteolysis; IDA:UniProtKB.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR DisProt; DP02838; -.
DR InterPro; IPR033883; C2_III.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR022682; Calpain_domain_III.
DR InterPro; IPR022683; Calpain_III.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR029531; CAPN3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183:SF329; PTHR10183:SF329; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49758; SSF49758; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cytoplasm; Disease variant;
KW Hydrolase; Limb-girdle muscular dystrophy; Metal-binding; Nucleus;
KW Protease; Reference proteome; Repeat; Thiol protease.
FT CHAIN 1..821
FT /note="Calpain-3"
FT /id="PRO_0000207706"
FT DOMAIN 74..417
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 649..683
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 692..725
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 722..757
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 787..821
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 7..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..586
FT /note="Domain III"
FT REGION 587..649
FT /note="Linker"
FT REGION 609..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..821
FT /note="Domain IV"
FT COMPBIAS 613..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT ACT_SITE 358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT BINDING 662
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24846670,
FT ECO:0007744|PDB:4OKH"
FT BINDING 665
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24846670,
FT ECO:0007744|PDB:4OKH"
FT BINDING 667
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24846670,
FT ECO:0007744|PDB:4OKH"
FT BINDING 672
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24846670,
FT ECO:0007744|PDB:4OKH"
FT BINDING 705
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24846670, ECO:0007744|PDB:4OKH"
FT BINDING 707
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24846670, ECO:0007744|PDB:4OKH"
FT BINDING 709
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24846670, ECO:0007744|PDB:4OKH"
FT BINDING 711
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24846670, ECO:0007744|PDB:4OKH"
FT BINDING 716
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24846670, ECO:0007744|PDB:4OKH"
FT BINDING 735
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24846670, ECO:0007744|PDB:4OKH"
FT BINDING 737
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24846670, ECO:0007744|PDB:4OKH"
FT BINDING 739
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24846670, ECO:0007744|PDB:4OKH"
FT BINDING 741
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:24846670, ECO:0007744|PDB:4OKH"
FT BINDING 746
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 800
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:24846670,
FT ECO:0007744|PDB:4OKH"
FT BINDING 802
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:24846670,
FT ECO:0007744|PDB:4OKH"
FT BINDING 804
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:24846670,
FT ECO:0007744|PDB:4OKH"
FT BINDING 806
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:24846670,
FT ECO:0007744|PDB:4OKH"
FT VAR_SEQ 1..665
FT /note="Missing (in isoform V)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044255"
FT VAR_SEQ 1..512
FT /note="Missing (in isoform IV)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_007813"
FT VAR_SEQ 268..315
FT /note="Missing (in isoform II)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_005227"
FT VAR_SEQ 595..638
FT /note="Missing (in isoform II)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_005228"
FT VAR_SEQ 595..600
FT /note="Missing (in isoform III)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_005229"
FT VARIANT 4
FT /note="V -> I (in LGMDR1; dbSNP:rs140660066)"
FT /id="VAR_009548"
FT VARIANT 21
FT /note="G -> E (in dbSNP:rs28364364)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_022272"
FT VARIANT 26
FT /note="P -> L (in LGMDR1; dbSNP:rs762020512)"
FT /id="VAR_009549"
FT VARIANT 77
FT /note="D -> N (in LGMDR1)"
FT /id="VAR_009550"
FT VARIANT 86
FT /note="S -> F (in LGMDR1; severe; dbSNP:rs121434546)"
FT /evidence="ECO:0000269|PubMed:9150160"
FT /id="VAR_009551"
FT VARIANT 93..100
FT /note="Missing (in LGMDR1)"
FT /id="VAR_009552"
FT VARIANT 107
FT /note="E -> K (in dbSNP:rs1801505)"
FT /id="VAR_009553"
FT VARIANT 118
FT /note="R -> G (in LGMDR1; dbSNP:rs1566973583)"
FT /id="VAR_009554"
FT VARIANT 137
FT /note="C -> R (in LGMDR1)"
FT /id="VAR_009555"
FT VARIANT 160
FT /note="A -> G (in dbSNP:rs17592)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_015389"
FT VARIANT 162
FT /note="I -> L (in LGMDR1)"
FT /id="VAR_009556"
FT VARIANT 182
FT /note="L -> Q (in LGMDR1)"
FT /id="VAR_001363"
FT VARIANT 183
FT /note="P -> L (in LGMDR1)"
FT /id="VAR_009557"
FT VARIANT 184
FT /note="T -> M (in dbSNP:rs35889956)"
FT /id="VAR_009558"
FT VARIANT 189
FT /note="L -> P (in LGMDR1; dbSNP:rs758795961)"
FT /id="VAR_009559"
FT VARIANT 200..204
FT /note="Missing (in LGMDR1)"
FT /evidence="ECO:0000269|PubMed:9452114"
FT /id="VAR_001364"
FT VARIANT 214
FT /note="G -> S (in LGMDR1; dbSNP:rs369784333)"
FT /id="VAR_009560"
FT VARIANT 215..221
FT /note="Missing (in LGMDR1 and LGMDD4)"
FT /evidence="ECO:0000269|PubMed:27259757,
FT ECO:0000269|PubMed:28881388, ECO:0000269|PubMed:9150160"
FT /id="VAR_009562"
FT VARIANT 215
FT /note="S -> P (in LGMDR1)"
FT /evidence="ECO:0000269|PubMed:9150160"
FT /id="VAR_009561"
FT VARIANT 217
FT /note="E -> K (in LGMDR1; dbSNP:rs773001194)"
FT /id="VAR_009563"
FT VARIANT 222
FT /note="G -> R (in LGMDR1; dbSNP:rs1345121557)"
FT /evidence="ECO:0000269|PubMed:9762961"
FT /id="VAR_009564"
FT VARIANT 226
FT /note="E -> K (in LGMDR1)"
FT /id="VAR_009565"
FT VARIANT 232
FT /note="T -> I (in LGMDR1)"
FT /id="VAR_009566"
FT VARIANT 234
FT /note="G -> E (in LGMDR1; dbSNP:rs1555420634)"
FT /id="VAR_001365"
FT VARIANT 236
FT /note="A -> T (in dbSNP:rs1801449)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_009567"
FT VARIANT 254
FT /note="Missing (in LGMDR1)"
FT /id="VAR_009568"
FT VARIANT 266..267
FT /note="Missing (in LGMDR1)"
FT /evidence="ECO:0000269|PubMed:27020652,
FT ECO:0000269|PubMed:27234031"
FT /id="VAR_076561"
FT VARIANT 319
FT /note="P -> L (in LGMDR1; dbSNP:rs121434547)"
FT /evidence="ECO:0000269|PubMed:9150160"
FT /id="VAR_009569"
FT VARIANT 334
FT /note="H -> Q (in LGMDR1)"
FT /evidence="ECO:0000269|PubMed:9150160"
FT /id="VAR_009570"
FT VARIANT 336
FT /note="Y -> N (in LGMDR1)"
FT /evidence="ECO:0000269|PubMed:9266733"
FT /id="VAR_009571"
FT VARIANT 354
FT /note="V -> G (in LGMDR1; dbSNP:rs1555421271)"
FT /id="VAR_001366"
FT VARIANT 360
FT /note="W -> C (in LGMDR1; dbSNP:rs267606703)"
FT /evidence="ECO:0000269|PubMed:9771675"
FT /id="VAR_009572"
FT VARIANT 437
FT /note="R -> C (in LGMDR1; dbSNP:rs777483913)"
FT /id="VAR_009573"
FT VARIANT 440
FT /note="R -> W (in LGMDR1; dbSNP:rs777323132)"
FT /evidence="ECO:0000269|PubMed:9150160"
FT /id="VAR_009574"
FT VARIANT 441
FT /note="G -> D (in LGMDR1)"
FT /id="VAR_009575"
FT VARIANT 445
FT /note="G -> R (in LGMDR1; dbSNP:rs773827877)"
FT /id="VAR_009576"
FT VARIANT 448
FT /note="R -> C (in LGMDR1; dbSNP:rs776043976)"
FT /id="VAR_009577"
FT VARIANT 448
FT /note="R -> G (in LGMDR1; dbSNP:rs776043976)"
FT /id="VAR_009578"
FT VARIANT 448
FT /note="R -> H (in LGMDR1; dbSNP:rs863224956)"
FT /id="VAR_009579"
FT VARIANT 479
FT /note="S -> G (in LGMDR1; dbSNP:rs201736037)"
FT /id="VAR_009580"
FT VARIANT 486
FT /note="Q -> E (in LGMDR1)"
FT /evidence="ECO:0000269|PubMed:9762961"
FT /id="VAR_009581"
FT VARIANT 489
FT /note="R -> Q (in LGMDR1; dbSNP:rs147764579)"
FT /id="VAR_009582"
FT VARIANT 489
FT /note="R -> W (in LGMDR1; dbSNP:rs863224957)"
FT /evidence="ECO:0000269|PubMed:9762961"
FT /id="VAR_009583"
FT VARIANT 490
FT /note="R -> Q (in LGMDR1; dbSNP:rs121434548)"
FT /evidence="ECO:0000269|PubMed:9266733"
FT /id="VAR_009584"
FT VARIANT 490
FT /note="R -> W (in LGMDR1; dbSNP:rs141656719)"
FT /evidence="ECO:0000269|PubMed:9150160"
FT /id="VAR_001367"
FT VARIANT 493
FT /note="R -> W (in LGMDR1; dbSNP:rs557164942)"
FT /id="VAR_009585"
FT VARIANT 496
FT /note="G -> R (in LGMDR1; dbSNP:rs761637940)"
FT /evidence="ECO:0000269|PubMed:9150160"
FT /id="VAR_009586"
FT VARIANT 502
FT /note="I -> T (in LGMDR1; dbSNP:rs148044781)"
FT /id="VAR_009587"
FT VARIANT 541
FT /note="R -> Q (in LGMDR1; dbSNP:rs398123143)"
FT /id="VAR_009588"
FT VARIANT 567
FT /note="G -> W (in LGMDR1; dbSNP:rs727503839)"
FT /evidence="ECO:0000269|PubMed:9150160"
FT /id="VAR_009589"
FT VARIANT 572
FT /note="R -> Q (in LGMDR1; dbSNP:rs121434544)"
FT /evidence="ECO:0000269|PubMed:8624690"
FT /id="VAR_001368"
FT VARIANT 572
FT /note="R -> W (in LGMDR1; dbSNP:rs863224959)"
FT /evidence="ECO:0000269|PubMed:27234031,
FT ECO:0000269|PubMed:9150160"
FT /id="VAR_009590"
FT VARIANT 606
FT /note="S -> L (in LGMDR1; dbSNP:rs199806879)"
FT /evidence="ECO:0000269|PubMed:9150160"
FT /id="VAR_009591"
FT VARIANT 622
FT /note="E -> A (in dbSNP:rs11557723)"
FT /id="VAR_047691"
FT VARIANT 638
FT /note="Q -> P (in LGMDR1)"
FT /id="VAR_009592"
FT VARIANT 698
FT /note="R -> P (in LGMDR1)"
FT /id="VAR_009593"
FT VARIANT 702
FT /note="A -> V (in LGMDR1; dbSNP:rs886042557)"
FT /evidence="ECO:0000269|PubMed:27234031,
FT ECO:0000269|PubMed:9150160, ECO:0000269|PubMed:9266733"
FT /id="VAR_009594"
FT VARIANT 705
FT /note="D -> G (in LGMDR1)"
FT /id="VAR_009595"
FT VARIANT 705
FT /note="D -> H (in LGMDR1)"
FT /id="VAR_009596"
FT VARIANT 731
FT /note="F -> S (in LGMDR1)"
FT /id="VAR_009597"
FT VARIANT 744
FT /note="S -> G (in LGMDR1; dbSNP:rs750083132)"
FT /evidence="ECO:0000269|PubMed:8624690,
FT ECO:0000269|PubMed:9655129"
FT /id="VAR_001369"
FT VARIANT 748
FT /note="R -> Q (in LGMDR1; dbSNP:rs587780290)"
FT /evidence="ECO:0000269|PubMed:27020652,
FT ECO:0000269|PubMed:27234031, ECO:0000269|PubMed:9150160,
FT ECO:0000269|PubMed:9266733, ECO:0000269|PubMed:9762961"
FT /id="VAR_009598"
FT VARIANT 769
FT /note="R -> Q (in LGMDR1; dbSNP:rs80338802)"
FT /id="VAR_001370"
FT VARIANT 774
FT /note="H -> D (in LGMDR1; unknown pathological
FT significance)"
FT /id="VAR_009599"
FT VARIANT 798
FT /note="A -> E (in LGMDR1; unknown pathological
FT significance; dbSNP:rs149095128)"
FT /id="VAR_009600"
FT MUTAGEN 129
FT /note="C->S: Loss of activity. No effect on CMYA5-binding.
FT Does not degradate p53/TP53."
FT /evidence="ECO:0000269|PubMed:20634290,
FT ECO:0000269|PubMed:27657329"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:6BDT"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6BDT"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:6BDT"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6BJD"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:6BDT"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:6BDT"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:6BJD"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:6BJD"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6BDT"
FT HELIX 129..138
FT /evidence="ECO:0007829|PDB:6BDT"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:6BDT"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:6BDT"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:6BDT"
FT STRAND 170..179
FT /evidence="ECO:0007829|PDB:6BDT"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:6BDT"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:6BDT"
FT HELIX 201..212
FT /evidence="ECO:0007829|PDB:6BDT"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:6BDT"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:6BDT"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:6BDT"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:6BDT"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:6BDT"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:6BDT"
FT STRAND 336..346
FT /evidence="ECO:0007829|PDB:6BDT"
FT STRAND 349..357
FT /evidence="ECO:0007829|PDB:6BDT"
FT HELIX 374..378
FT /evidence="ECO:0007829|PDB:6BDT"
FT HELIX 381..386
FT /evidence="ECO:0007829|PDB:6BDT"
FT STRAND 394..400
FT /evidence="ECO:0007829|PDB:6BDT"
FT HELIX 401..407
FT /evidence="ECO:0007829|PDB:6BDT"
FT STRAND 410..415
FT /evidence="ECO:0007829|PDB:6BDT"
FT HELIX 654..662
FT /evidence="ECO:0007829|PDB:4OKH"
FT TURN 663..666
FT /evidence="ECO:0007829|PDB:4OKH"
FT HELIX 670..680
FT /evidence="ECO:0007829|PDB:4OKH"
FT HELIX 694..704
FT /evidence="ECO:0007829|PDB:4OKH"
FT STRAND 708..712
FT /evidence="ECO:0007829|PDB:4OKH"
FT HELIX 714..734
FT /evidence="ECO:0007829|PDB:4OKH"
FT STRAND 740..743
FT /evidence="ECO:0007829|PDB:4OKH"
FT HELIX 744..753
FT /evidence="ECO:0007829|PDB:4OKH"
FT HELIX 760..770
FT /evidence="ECO:0007829|PDB:4OKH"
FT STRAND 775..778
FT /evidence="ECO:0007829|PDB:4OKH"
FT HELIX 779..797
FT /evidence="ECO:0007829|PDB:4OKH"
FT STRAND 804..809
FT /evidence="ECO:0007829|PDB:4OKH"
FT HELIX 811..821
FT /evidence="ECO:0007829|PDB:4OKH"
SQ SEQUENCE 821 AA; 94254 MW; BC608E8B67AA2741 CRC64;
MPTVISASVA PRTAAEPRSP GPVPHPAQSK ATEAGGGNPS GIYSAIISRN FPIIGVKEKT
FEQLHKKCLE KKVLYVDPEF PPDETSLFYS QKFPIQFVWK RPPEICENPR FIIDGANRTD
ICQGELGDCW FLAAIACLTL NQHLLFRVIP HDQSFIENYA GIFHFQFWRY GEWVDVVIDD
CLPTYNNQLV FTKSNHRNEF WSALLEKAYA KLHGSYEALK GGNTTEAMED FTGGVAEFFE
IRDAPSDMYK IMKKAIERGS LMGCSIDDGT NMTYGTSPSG LNMGELIARM VRNMDNSLLQ
DSDLDPRGSD ERPTRTIIPV QYETRMACGL VRGHAYSVTG LDEVPFKGEK VKLVRLRNPW
GQVEWNGSWS DRWKDWSFVD KDEKARLQHQ VTEDGEFWMS YEDFIYHFTK LEICNLTADA
LQSDKLQTWT VSVNEGRWVR GCSAGGCRNF PDTFWTNPQY RLKLLEEDDD PDDSEVICSF
LVALMQKNRR KDRKLGASLF TIGFAIYEVP KEMHGNKQHL QKDFFLYNAS KARSKTYINM
REVSQRFRLP PSEYVIVPST YEPHQEGEFI LRVFSEKRNL SEEVENTISV DRPVKKKKTK
PIIFVSDRAN SNKELGVDQE SEEGKGKTSP DKQKQSPQPQ PGSSDQESEE QQQFRNIFKQ
IAGDDMEICA DELKKVLNTV VNKHKDLKTH GFTLESCRSM IALMDTDGSG KLNLQEFHHL
WNKIKAWQKI FKHYDTDQSG TINSYEMRNA VNDAGFHLNN QLYDIITMRY ADKHMNIDFD
SFICCFVRLE GMFRAFHAFD KDGDGIIKLN VLEWLQLTMY A
