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Calpain-3 (EC 3.4.22.54) (Calcium-activated neutral proteinase 3) (CANP 3) (Calpain L3) (Calpain p94) (Muscle-specific calcium-activated neutral protease 3) (New calpain 1) (nCL-1)

 CAN3_HUMAN              Reviewed;         821 AA.
P20807; A6H8K6; Q7L4R0; Q9BQC8; Q9BTU4; Q9Y5S6; Q9Y5S7;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
30-AUG-2017, entry version 200.
RecName: Full=Calpain-3;
EC=3.4.22.54;
AltName: Full=Calcium-activated neutral proteinase 3;
Short=CANP 3;
AltName: Full=Calpain L3;
AltName: Full=Calpain p94;
AltName: Full=Muscle-specific calcium-activated neutral protease 3;
AltName: Full=New calpain 1;
Short=nCL-1;
Name=CAPN3; Synonyms=CANP3, CANPL3, NCL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I), AND VARIANTS LGMD2A.
PubMed=7720071; DOI=10.1016/0092-8674(95)90368-2;
Richard I., Broux O., Allamand V., Fougerousse F., Chiannilkulchai N.,
Bourg N., Brenguier L., Devaud C., Pasturaud P., Roudaut C.,
Hillaire D., Passos-Bueno M.-R., Zatz M., Tischfield J.A., Fardeau M.,
Jackson C.E., Cohen D., Beckmann J.S.;
"Mutations in the proteolytic enzyme calpain 3 cause limb-girdle
muscular dystrophy type 2A.";
Cell 81:27-40(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM I).
Mashima H., Horikawa Y., Cox N.J., Bell G.I.;
"hCAPN3-hZFP106 genomic sequence.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS II AND III).
Dickson J.M.J., Love D., Evans C.W.E.;
"Alternatively exon-spliced isoforms of calpain 3 expressed in human
leukocytes.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IV).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-21; GLY-160 AND
THR-236.
NIEHS SNPs program;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS IV AND V).
TISSUE=Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 44-821 (ISOFORM I).
PubMed=2555341;
Sorimachi H., Imajoh-Ohmi S., Emori Y., Kawasaki H., Ohno S.,
Minami Y., Suzuki K.;
"Molecular cloning of a novel mammalian calcium-dependent protease
distinct from both m- and mu-types. Specific expression of the mRNA in
skeletal muscle.";
J. Biol. Chem. 264:20106-20111(1989).
[9]
INTERACTION WITH TTN.
PubMed=14583192; DOI=10.1016/j.jmb.2003.09.012;
Miller M.K., Bang M.-L., Witt C.C., Labeit D., Trombitas C.,
Watanabe K., Granzier H., McElhinny A.S., Gregorio C.C., Labeit S.;
"The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a
family of titin filament-based stress response molecules.";
J. Mol. Biol. 333:951-964(2003).
[10]
REVIEW ON VARIANTS.
PubMed=10330340; DOI=10.1086/302426;
Richard I., Roudaut C., Saenz A., Pogue R., Grimbergen J.E.M.A.,
Anderson L.V.B., Beley C., Cobo A.-M., de Diego C., Eymard B.,
Gallano P., Ginjaar H.B., Lasa A., Pollitt C., Topaloglu H.,
Urtizberea J.A., de Visser M., van der Kooi A., Bushby K., Bakker E.,
Lopez de Munain A., Fardeau M., Beckmann J.S.;
"Calpainopathy -- a survey of mutations and polymorphisms.";
Am. J. Hum. Genet. 64:1524-1540(1999).
[11]
INTERACTION WITH CMYA5, AND MUTAGENESIS OF CYS-129.
PubMed=20634290; DOI=10.1074/jbc.M110.108720;
Sarparanta J., Blandin G., Charton K., Vihola A., Marchand S.,
Milic A., Hackman P., Ehler E., Richard I., Udd B.;
"Interactions with M-band titin and calpain 3 link myospryn (CMYA5) to
tibial and limb-girdle muscular dystrophies.";
J. Biol. Chem. 285:30304-30315(2010).
[12]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 642-821 IN COMPLEX WITH
CALCIUM, AND SUBUNIT.
PubMed=24846670; DOI=10.1111/febs.12849;
Partha S.K., Ravulapalli R., Allingham J.S., Campbell R.L.,
Davies P.L.;
"Crystal structure of calpain-3 penta-EF-hand (PEF) domain - a
homodimerized PEF family member with calcium bound at the fifth EF-
hand.";
FEBS J. 281:3138-3149(2014).
[13]
VARIANTS LGMD2A GLN-572 AND GLY-744.
PubMed=8624690; DOI=10.1093/brain/119.1.295;
Fardeau M., Hillaire D., Mignard C., Feingold N., Feingold J.,
Mignard D., de Ubeda B., Collin H., Tome F.M.S., Richard I.,
Beckmann J.S.;
"Juvenile limb-girdle muscular dystrophy. Clinical, histopathological
and genetic data from a small community living in the Reunion
island.";
Brain 119:295-308(1996).
[14]
VARIANTS LGMD2A.
PubMed=9150160;
Richard I., Brenguier L., Dincer P., Roudaut C., Bady B.,
Burgunder J.-M., Chemaly R., Garcia C.A., Halaby G., Jackson C.E.,
Kurnit D.M., Lefranc G., Legum C., Loiselet J., Merlini L.,
Nivelon-Chevallier A., Ollagnon-Roman E., Restagno G., Topaloglu H.,
Beckmann J.S.;
"Multiple independent molecular etiology for limb-girdle muscular
dystrophy type 2A patients from various geographical origins.";
Am. J. Hum. Genet. 60:1128-1138(1997).
[15]
VARIANTS LGMD2A ASN-336; GLN-490; VAL-702 AND GLN-748.
PubMed=9266733; DOI=10.1002/ana.410420214;
Dincer P., Leturcq F., Richard I., Piccolo F., Yalnizoglu D.,
de Toma C., Akcoeren Z., Broux O., Deburgrave N., Brenguier L.,
Roudaut C., Urtizberea J.A., Jung D., Tan E., Jeanpierre M.,
Campbell K.P., Kaplan J.-C., Beckmann J.S., Topaloglu H.;
"A biochemical, genetic, and clinical survey of autosomal recessive
limb girdle muscular dystrophies in Turkey.";
Ann. Neurol. 42:222-229(1997).
[16]
VARIANTS LGMD2A ARG-222; GLU-486; TRP-489 AND GLN-748.
PubMed=9762961; DOI=10.1093/brain/121.9.1735;
Urtasun M., Saenz A., Roudaut C., Poza J.J., Urtizberea J.A.,
Cobo A.-M., Richard I., Garcia Bragado F., Leturcq F., Kaplan J.-C.,
Marti Masso J.F., Beckmann J.S., Lopez de Munain A.;
"Limb-girdle muscular dystrophy in Guipuzcoa (Basque Country,
Spain).";
Brain 121:1735-1747(1998).
[17]
VARIANT LGMD2A 200-PHE--LEU-204 DEL.
PubMed=9452114;
Haeffner K., Speer A., Huebner C., Voit T., Oexle K.;
"A small in-frame deletion within the protease domain of muscle-
specific calpain, p94 causes early-onset limb-girdle muscular
dystrophy 2A.";
Hum. Mutat. Suppl. 1:S298-S300(1998).
[18]
VARIANT LGMD2A GLY-744.
PubMed=9655129;
DOI=10.1002/(SICI)1097-4598(199808)21:8<1078::AID-MUS15>3.0.CO;2-Q;
Penisson-Besnier I., Richard I., Dubas F., Beckmann J.S., Fardeau M.;
"Pseudometabolic expression and phenotypic variability of calpain
deficiency in two siblings.";
Muscle Nerve 21:1078-1080(1998).
[19]
VARIANT LGMD2A CYS-360.
PubMed=9771675;
DOI=10.1002/(SICI)1097-4598(199811)21:11<1493::AID-MUS19>3.0.CO;2-1;
Kawai H., Akaike M., Kunishige M., Inui T., Adachi K., Kimura C.,
Kawajiri M., Nishida Y., Endo I., Kashiwagi S., Nishino H.,
Fujiwara T., Okuno S., Roudaut C., Richard I., Beckmann J.S.,
Miyoshi K., Matsumoto T.;
"Clinical, pathological, and genetic features of limb-girdle muscular
dystrophy type 2A with new calpain 3 gene mutations in seven patients
from three Japanese families.";
Muscle Nerve 21:1493-1501(1998).
[20]
VARIANTS LGMD2A 266-ILE-ASP-267 DEL; TRP-572; VAL-702 AND GLN-748.
PubMed=27234031; DOI=10.1111/cge.12810;
Fattahi Z., Kalhor Z., Fadaee M., Vazehan R., Parsimehr E.,
Abolhassani A., Beheshtian M., Zamani G., Nafissi S., Nilipour Y.,
Akbari M.R., Kahrizi K., Kariminejad A., Najmabadi H.;
"Improved diagnostic yield of neuromuscular disorders applying
clinical exome sequencing in patients arising from a consanguineous
population.";
Clin. Genet. 91:386-402(2017).
[21]
VARIANTS LGMD2A 266-ILE-ASP-267 DEL AND GLN-748.
PubMed=27020652; DOI=10.1016/j.nmd.2016.02.003;
Fadaee M., Kariminejad A., Fattahi Z., Nafissi S., Godarzi H.R.,
Beheshtian M., Vazehan R., Akbari M.R., Kahrizi K., Najmabadi H.;
"Report of limb girdle muscular dystrophy type 2a in 6 Iranian
patients, one with a novel deletion in CAPN3 gene.";
Neuromuscul. Disord. 26:277-282(2016).
-!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
-!- CATALYTIC ACTIVITY: Broad endopeptidase activity.
-!- ENZYME REGULATION: Activated by micromolar concentrations of
calcium and inhibited by calpastatin.
-!- SUBUNIT: Homodimer; via EF-hand domain 4 (PubMed:24846670).
Interacts with TTN/titin (PubMed:14583192). Interacts with CMYA5;
this interaction, which results in CMYA5 proteolysis, may protect
CAPN3 from autolysis (PubMed:20634290).
{ECO:0000269|PubMed:14583192, ECO:0000269|PubMed:20634290,
ECO:0000269|PubMed:24846670}.
-!- INTERACTION:
Q9UJX0:OSGIN1; NbExp=3; IntAct=EBI-5655000, EBI-9057006;
Q8WZ42:TTN; NbExp=4; IntAct=EBI-5655000, EBI-681210;
Q96HA8:WDYHV1; NbExp=3; IntAct=EBI-5655000, EBI-741158;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=I;
IsoId=P20807-1; Sequence=Displayed;
Name=II;
IsoId=P20807-2; Sequence=VSP_005227, VSP_005228;
Name=III;
IsoId=P20807-3; Sequence=VSP_005229;
Name=IV;
IsoId=P20807-4; Sequence=VSP_007813;
Name=V;
IsoId=P20807-5; Sequence=VSP_044255;
-!- TISSUE SPECIFICITY: Isoform I is skeletal muscle specific.
-!- DISEASE: Limb-girdle muscular dystrophy 2A (LGMD2A) [MIM:253600]:
An autosomal recessive degenerative myopathy characterized by
progressive symmetrical atrophy and weakness of the proximal limb
muscles and elevated serum creatine kinase. The symptoms usually
begin during the first two decades of life, and the disease
gradually worsens, often resulting in loss of walking ability 10
or 20 years after onset. {ECO:0000269|PubMed:27020652,
ECO:0000269|PubMed:27234031, ECO:0000269|PubMed:7720071,
ECO:0000269|PubMed:8624690, ECO:0000269|PubMed:9150160,
ECO:0000269|PubMed:9266733, ECO:0000269|PubMed:9452114,
ECO:0000269|PubMed:9655129, ECO:0000269|PubMed:9762961,
ECO:0000269|PubMed:9771675}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Leiden Muscular Dystrophy pages; Note=Calpain-3
mutations in LGMD2A;
URL="http://www.dmd.nl/capn3_home.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/capn3/";
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EMBL; X85030; CAA59403.1; -; mRNA.
EMBL; AF209502; AAL40183.1; -; Genomic_DNA.
EMBL; AF127764; AAD28253.1; -; mRNA.
EMBL; AF127765; AAD28254.3; -; mRNA.
EMBL; BT007322; AAP35986.1; -; mRNA.
EMBL; AY902237; AAW69391.1; -; Genomic_DNA.
EMBL; AC012651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003169; AAH03169.1; -; mRNA.
EMBL; BC003521; AAH03521.1; -; mRNA.
EMBL; BC004883; AAH04883.1; -; mRNA.
EMBL; BC007810; AAH07810.3; -; mRNA.
EMBL; BC067126; AAH67126.1; -; mRNA.
EMBL; BC100782; AAI00783.1; -; mRNA.
EMBL; BC107791; AAI07792.1; -; mRNA.
EMBL; BC128605; AAI28606.1; -; mRNA.
EMBL; BC146649; AAI46650.1; -; mRNA.
EMBL; BC146672; AAI46673.1; -; mRNA.
CCDS; CCDS10085.1; -. [P20807-2]
CCDS; CCDS10086.1; -. [P20807-5]
CCDS; CCDS32207.1; -. [P20807-3]
CCDS; CCDS45245.1; -. [P20807-1]
CCDS; CCDS45246.1; -. [P20807-4]
PIR; A56218; CIHUH3.
RefSeq; NP_000061.1; NM_000070.2. [P20807-1]
RefSeq; NP_077320.1; NM_024344.1. [P20807-3]
RefSeq; NP_775110.1; NM_173087.1. [P20807-2]
RefSeq; NP_775111.1; NM_173088.1. [P20807-4]
RefSeq; NP_775112.1; NM_173089.1. [P20807-5]
RefSeq; NP_775113.1; NM_173090.1. [P20807-5]
UniGene; Hs.143261; -.
PDB; 1Y9V; Model; -; A/B=649-821.
PDB; 4OKH; X-ray; 2.45 A; A/B/C=642-821.
PDBsum; 1Y9V; -.
PDBsum; 4OKH; -.
ProteinModelPortal; P20807; -.
SMR; P20807; -.
BioGrid; 107275; 6.
IntAct; P20807; 21.
MINT; MINT-7990282; -.
STRING; 9606.ENSP00000380349; -.
MEROPS; C02.004; -.
iPTMnet; P20807; -.
PhosphoSitePlus; P20807; -.
BioMuta; CAPN3; -.
PaxDb; P20807; -.
PeptideAtlas; P20807; -.
PRIDE; P20807; -.
DNASU; 825; -.
Ensembl; ENST00000337571; ENSP00000336840; ENSG00000092529. [P20807-5]
Ensembl; ENST00000349748; ENSP00000183936; ENSG00000092529. [P20807-2]
Ensembl; ENST00000356316; ENSP00000348667; ENSG00000092529. [P20807-5]
Ensembl; ENST00000357568; ENSP00000350181; ENSG00000092529. [P20807-3]
Ensembl; ENST00000397163; ENSP00000380349; ENSG00000092529. [P20807-1]
Ensembl; ENST00000397200; ENSP00000380384; ENSG00000092529. [P20807-4]
Ensembl; ENST00000397204; ENSP00000380387; ENSG00000092529. [P20807-5]
Ensembl; ENST00000569136; ENSP00000455254; ENSG00000092529. [P20807-5]
GeneID; 825; -.
KEGG; hsa:825; -.
UCSC; uc001zpn.2; human. [P20807-1]
CTD; 825; -.
DisGeNET; 825; -.
GeneCards; CAPN3; -.
GeneReviews; CAPN3; -.
HGNC; HGNC:1480; CAPN3.
HPA; HPA040052; -.
MalaCards; CAPN3; -.
MIM; 114240; gene.
MIM; 253600; phenotype.
neXtProt; NX_P20807; -.
OpenTargets; ENSG00000092529; -.
Orphanet; 267; Autosomal recessive limb-girdle muscular dystrophy type 2A.
PharmGKB; PA26061; -.
eggNOG; KOG0045; Eukaryota.
eggNOG; ENOG410XP0B; LUCA.
GeneTree; ENSGT00760000118971; -.
HOGENOM; HOG000232035; -.
HOVERGEN; HBG012645; -.
InParanoid; P20807; -.
KO; K08573; -.
OMA; TDIAKWR; -.
OrthoDB; EOG091G049E; -.
PhylomeDB; P20807; -.
TreeFam; TF314748; -.
BRENDA; 3.4.22.54; 2681.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
SIGNOR; P20807; -.
ChiTaRS; CAPN3; human.
GeneWiki; CAPN3; -.
GenomeRNAi; 825; -.
PRO; PR:P20807; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000092529; -.
CleanEx; HS_CAPN3; -.
ExpressionAtlas; P20807; baseline and differential.
Genevisible; P20807; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; TAS:UniProtKB.
GO; GO:0030016; C:myofibril; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0030315; C:T-tubule; ISS:UniProtKB.
GO; GO:0030018; C:Z disc; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; ISS:UniProtKB.
GO; GO:0003824; F:catalytic activity; IDA:UniProtKB.
GO; GO:0008234; F:cysteine-type peptidase activity; TAS:ProtInc.
GO; GO:0055103; F:ligase regulator activity; IDA:UniProtKB.
GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO; GO:0032947; F:protein complex scaffold activity; ISS:UniProtKB.
GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
GO; GO:0031402; F:sodium ion binding; ISS:UniProtKB.
GO; GO:0008307; F:structural constituent of muscle; ISS:UniProtKB.
GO; GO:0031432; F:titin binding; IPI:UniProtKB.
GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
GO; GO:0071472; P:cellular response to salt stress; ISS:UniProtKB.
GO; GO:0070315; P:G1 to G0 transition involved in cell differentiation; IEA:Ensembl.
GO; GO:0046716; P:muscle cell cellular homeostasis; TAS:UniProtKB.
GO; GO:0007517; P:muscle organ development; TAS:UniProtKB.
GO; GO:0061061; P:muscle structure development; ISS:UniProtKB.
GO; GO:0030239; P:myofibril assembly; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0033234; P:negative regulation of protein sumoylation; IDA:UniProtKB.
GO; GO:2001015; P:negative regulation of skeletal muscle cell differentiation; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0045862; P:positive regulation of proteolysis; ISS:UniProtKB.
GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
GO; GO:0014718; P:positive regulation of satellite cell activation involved in skeletal muscle regeneration; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0006461; P:protein complex assembly; ISS:UniProtKB.
GO; GO:0072657; P:protein localization to membrane; ISS:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0050790; P:regulation of catalytic activity; IDA:UniProtKB.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0045661; P:regulation of myoblast differentiation; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
GO; GO:0014850; P:response to muscle activity; ISS:UniProtKB.
GO; GO:0045214; P:sarcomere organization; ISS:UniProtKB.
GO; GO:0097264; P:self proteolysis; IDA:UniProtKB.
CDD; cd00214; Calpain_III; 1.
CDD; cd00044; CysPc; 1.
InterPro; IPR033883; C2_III.
InterPro; IPR022684; Calpain_cysteine_protease.
InterPro; IPR022682; Calpain_domain_III.
InterPro; IPR022683; Calpain_III.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR001300; Peptidase_C2_calpain_cat.
Pfam; PF01067; Calpain_III; 1.
Pfam; PF13202; EF-hand_5; 1.
Pfam; PF13833; EF-hand_8; 1.
Pfam; PF00648; Peptidase_C2; 1.
PRINTS; PR00704; CALPAIN.
SMART; SM00720; calpain_III; 1.
SMART; SM00230; CysPc; 1.
SMART; SM00054; EFh; 3.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF49758; SSF49758; 1.
PROSITE; PS50203; CALPAIN_CAT; 1.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 4.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Complete proteome;
Cytoplasm; Disease mutation; Hydrolase;
Limb-girdle muscular dystrophy; Metal-binding; Polymorphism; Protease;
Reference proteome; Repeat; Thiol protease.
CHAIN 1 821 Calpain-3.
/FTId=PRO_0000207706.
DOMAIN 74 417 Calpain catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00239}.
DOMAIN 649 683 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 692 725 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 722 757 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 787 821 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 662 672 1. {ECO:0000244|PDB:4OKH,
ECO:0000269|PubMed:24846670}.
CA_BIND 705 716 2. {ECO:0000244|PDB:4OKH,
ECO:0000255|PROSITE-ProRule:PRU00448,
ECO:0000269|PubMed:24846670}.
CA_BIND 735 741 3. {ECO:0000244|PDB:4OKH,
ECO:0000255|PROSITE-ProRule:PRU00448,
ECO:0000269|PubMed:24846670}.
CA_BIND 800 806 4. {ECO:0000244|PDB:4OKH,
ECO:0000269|PubMed:24846670}.
REGION 418 586 Domain III.
REGION 587 649 Linker.
REGION 650 821 Domain IV.
ACT_SITE 129 129 {ECO:0000255|PROSITE-ProRule:PRU00239}.
ACT_SITE 334 334 {ECO:0000255|PROSITE-ProRule:PRU00239}.
ACT_SITE 358 358 {ECO:0000255|PROSITE-ProRule:PRU00239}.
VAR_SEQ 1 665 Missing (in isoform V).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044255.
VAR_SEQ 1 512 Missing (in isoform IV).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_007813.
VAR_SEQ 268 315 Missing (in isoform II).
{ECO:0000303|Ref.3}.
/FTId=VSP_005227.
VAR_SEQ 595 638 Missing (in isoform II).
{ECO:0000303|Ref.3}.
/FTId=VSP_005228.
VAR_SEQ 595 600 Missing (in isoform III).
{ECO:0000303|Ref.3}.
/FTId=VSP_005229.
VARIANT 4 4 V -> I (in LGMD2A; dbSNP:rs140660066).
/FTId=VAR_009548.
VARIANT 21 21 G -> E (in dbSNP:rs28364364).
{ECO:0000269|Ref.5}.
/FTId=VAR_022272.
VARIANT 26 26 P -> L (in LGMD2A; dbSNP:rs762020512).
/FTId=VAR_009549.
VARIANT 77 77 D -> N (in LGMD2A).
/FTId=VAR_009550.
VARIANT 86 86 S -> F (in LGMD2A; severe;
dbSNP:rs121434546).
/FTId=VAR_009551.
VARIANT 93 100 Missing (in LGMD2A).
/FTId=VAR_009552.
VARIANT 107 107 E -> K (in dbSNP:rs1801505).
/FTId=VAR_009553.
VARIANT 118 118 R -> G (in LGMD2A).
/FTId=VAR_009554.
VARIANT 137 137 C -> R (in LGMD2A).
/FTId=VAR_009555.
VARIANT 160 160 A -> G (in dbSNP:rs17592).
{ECO:0000269|Ref.5}.
/FTId=VAR_015389.
VARIANT 162 162 I -> L (in LGMD2A).
/FTId=VAR_009556.
VARIANT 182 182 L -> Q (in LGMD2A).
/FTId=VAR_001363.
VARIANT 183 183 P -> L (in LGMD2A).
/FTId=VAR_009557.
VARIANT 184 184 T -> M (in LGMD2A; dbSNP:rs35889956).
/FTId=VAR_009558.
VARIANT 189 189 L -> P (in LGMD2A; dbSNP:rs758795961).
/FTId=VAR_009559.
VARIANT 200 204 Missing (in LGMD2A).
{ECO:0000269|PubMed:9452114}.
/FTId=VAR_001364.
VARIANT 214 214 G -> S (in LGMD2A; dbSNP:rs369784333).
/FTId=VAR_009560.
VARIANT 215 221 Missing (in LGMD2A).
/FTId=VAR_009562.
VARIANT 215 215 S -> P (in LGMD2A).
/FTId=VAR_009561.
VARIANT 217 217 E -> K (in LGMD2A; dbSNP:rs773001194).
/FTId=VAR_009563.
VARIANT 222 222 G -> R (in LGMD2A).
{ECO:0000269|PubMed:9762961}.
/FTId=VAR_009564.
VARIANT 226 226 E -> K (in LGMD2A).
/FTId=VAR_009565.
VARIANT 232 232 T -> I (in LGMD2A).
/FTId=VAR_009566.
VARIANT 234 234 G -> E (in LGMD2A).
/FTId=VAR_001365.
VARIANT 236 236 A -> T (in dbSNP:rs1801449).
{ECO:0000269|Ref.5}.
/FTId=VAR_009567.
VARIANT 254 254 Missing (in LGMD2A).
/FTId=VAR_009568.
VARIANT 266 267 Missing (in LGMD2A).
{ECO:0000269|PubMed:27020652,
ECO:0000269|PubMed:27234031}.
/FTId=VAR_076561.
VARIANT 319 319 P -> L (in LGMD2A; dbSNP:rs121434547).
/FTId=VAR_009569.
VARIANT 334 334 H -> Q (in LGMD2A).
/FTId=VAR_009570.
VARIANT 336 336 Y -> N (in LGMD2A).
{ECO:0000269|PubMed:9266733}.
/FTId=VAR_009571.
VARIANT 354 354 V -> G (in LGMD2A).
/FTId=VAR_001366.
VARIANT 360 360 W -> C (in LGMD2A; dbSNP:rs267606703).
{ECO:0000269|PubMed:9771675}.
/FTId=VAR_009572.
VARIANT 437 437 R -> C (in LGMD2A; dbSNP:rs777483913).
/FTId=VAR_009573.
VARIANT 440 440 R -> W (in LGMD2A; dbSNP:rs777323132).
/FTId=VAR_009574.
VARIANT 441 441 G -> D (in LGMD2A).
/FTId=VAR_009575.
VARIANT 445 445 G -> R (in LGMD2A; dbSNP:rs773827877).
/FTId=VAR_009576.
VARIANT 448 448 R -> C (in LGMD2A; dbSNP:rs776043976).
/FTId=VAR_009577.
VARIANT 448 448 R -> G (in LGMD2A; dbSNP:rs776043976).
/FTId=VAR_009578.
VARIANT 448 448 R -> H (in LGMD2A; dbSNP:rs863224956).
/FTId=VAR_009579.
VARIANT 479 479 S -> G (in LGMD2A; dbSNP:rs201736037).
/FTId=VAR_009580.
VARIANT 486 486 Q -> E (in LGMD2A).
{ECO:0000269|PubMed:9762961}.
/FTId=VAR_009581.
VARIANT 489 489 R -> Q (in LGMD2A; dbSNP:rs147764579).
/FTId=VAR_009582.
VARIANT 489 489 R -> W (in LGMD2A; dbSNP:rs863224957).
{ECO:0000269|PubMed:9762961}.
/FTId=VAR_009583.
VARIANT 490 490 R -> Q (in LGMD2A; dbSNP:rs121434548).
{ECO:0000269|PubMed:9266733}.
/FTId=VAR_009584.
VARIANT 490 490 R -> W (in LGMD2A; dbSNP:rs141656719).
/FTId=VAR_001367.
VARIANT 493 493 R -> W (in LGMD2A; dbSNP:rs557164942).
/FTId=VAR_009585.
VARIANT 496 496 G -> R (in LGMD2A; dbSNP:rs761637940).
/FTId=VAR_009586.
VARIANT 502 502 I -> T (in LGMD2A; dbSNP:rs148044781).
/FTId=VAR_009587.
VARIANT 541 541 R -> Q (in LGMD2A; dbSNP:rs398123143).
/FTId=VAR_009588.
VARIANT 567 567 G -> W (in LGMD2A; dbSNP:rs727503839).
/FTId=VAR_009589.
VARIANT 572 572 R -> Q (in LGMD2A; dbSNP:rs121434544).
{ECO:0000269|PubMed:8624690}.
/FTId=VAR_001368.
VARIANT 572 572 R -> W (in LGMD2A; dbSNP:rs863224959).
{ECO:0000269|PubMed:27234031}.
/FTId=VAR_009590.
VARIANT 606 606 S -> L (in LGMD2A; dbSNP:rs199806879).
/FTId=VAR_009591.
VARIANT 622 622 E -> A (in dbSNP:rs11557723).
/FTId=VAR_047691.
VARIANT 638 638 Q -> P (in LGMD2A).
/FTId=VAR_009592.
VARIANT 698 698 R -> P (in LGMD2A).
/FTId=VAR_009593.
VARIANT 702 702 A -> V (in LGMD2A).
{ECO:0000269|PubMed:27234031,
ECO:0000269|PubMed:9266733}.
/FTId=VAR_009594.
VARIANT 705 705 D -> G (in LGMD2A).
/FTId=VAR_009595.
VARIANT 705 705 D -> H (in LGMD2A).
/FTId=VAR_009596.
VARIANT 731 731 F -> S (in LGMD2A).
/FTId=VAR_009597.
VARIANT 744 744 S -> G (in LGMD2A; dbSNP:rs750083132).
{ECO:0000269|PubMed:8624690,
ECO:0000269|PubMed:9655129}.
/FTId=VAR_001369.
VARIANT 748 748 R -> Q (in LGMD2A; dbSNP:rs587780290).
{ECO:0000269|PubMed:27020652,
ECO:0000269|PubMed:27234031,
ECO:0000269|PubMed:9266733,
ECO:0000269|PubMed:9762961}.
/FTId=VAR_009598.
VARIANT 769 769 R -> Q (in LGMD2A; dbSNP:rs80338802).
/FTId=VAR_001370.
VARIANT 774 774 H -> D (in LGMD2A; unknown pathological
significance).
/FTId=VAR_009599.
VARIANT 798 798 A -> E (in LGMD2A; unknown pathological
significance; dbSNP:rs149095128).
/FTId=VAR_009600.
MUTAGEN 129 129 C->S: Loss of activity. No effect on
CMYA5-binding.
{ECO:0000269|PubMed:20634290}.
HELIX 654 662 {ECO:0000244|PDB:4OKH}.
TURN 663 666 {ECO:0000244|PDB:4OKH}.
HELIX 670 680 {ECO:0000244|PDB:4OKH}.
HELIX 694 704 {ECO:0000244|PDB:4OKH}.
STRAND 708 712 {ECO:0000244|PDB:4OKH}.
HELIX 714 734 {ECO:0000244|PDB:4OKH}.
STRAND 740 743 {ECO:0000244|PDB:4OKH}.
HELIX 744 753 {ECO:0000244|PDB:4OKH}.
HELIX 760 770 {ECO:0000244|PDB:4OKH}.
STRAND 775 778 {ECO:0000244|PDB:4OKH}.
HELIX 779 797 {ECO:0000244|PDB:4OKH}.
STRAND 804 809 {ECO:0000244|PDB:4OKH}.
HELIX 811 821 {ECO:0000244|PDB:4OKH}.
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


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