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P20807 (CAN3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 171. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calpain-3

EC=3.4.22.54
Alternative name(s):
Calcium-activated neutral proteinase 3
Short name=CANP 3
Calpain L3
Calpain p94
Muscle-specific calcium-activated neutral protease 3
New calpain 1
Short name=nCL-1
Gene names
Name:CAPN3
Synonyms:CANP3, CANPL3, NCL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length821 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 structure

Interacts with TTN/titin. Interacts with CMYA5; this interaction, which results in CMYA5 proteolysis, may protect CAPN3 from autolysis. Ref.9 Ref.11

Subcellular location

Cytoplasm.

Tissue specificity

Isoform I is skeletal muscle specific.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Sequence similarities

Belongs to the peptidase C2 family.

Contains 1 calpain catalytic domain.

Contains 4 EF-hand domains.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Limb-girdle muscular dystrophy
   DomainRepeat
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Thiol protease
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1 to G0 transition involved in cell differentiation

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Traceable author statement PubMed 19386580. Source: UniProtKB

autolysis

Inferred from electronic annotation. Source: Ensembl

cellular response to calcium ion

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to salt stress

Inferred from sequence or structural similarity. Source: UniProtKB

muscle cell cellular homeostasis

Traceable author statement PubMed 19386580. Source: UniProtKB

muscle organ development

Traceable author statement PubMed 9642272. Source: UniProtKB

muscle structure development

Inferred from sequence or structural similarity. Source: UniProtKB

myofibril assembly

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 18073330. Source: UniProtKB

negative regulation of protein sumoylation

Inferred from direct assay PubMed 20694146. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype PubMed 18073330. Source: UniProtKB

positive regulation of proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of release of sequestered calcium ion into cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of satellite cell activation involved in skeletal muscle regeneration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 18073330. Source: UniProtKB

protein complex assembly

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to membrane

Inferred from sequence or structural similarity. Source: UniProtKB

proteolysis

Inferred from direct assay PubMed 18310072PubMed 19386580PubMed 20694146PubMed 9642272. Source: UniProtKB

regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 18073330. Source: UniProtKB

regulation of catalytic activity

Inferred from direct assay PubMed 20694146. Source: UniProtKB

regulation of myoblast differentiation

Inferred from electronic annotation. Source: Ensembl

response to calcium ion

Inferred from sequence or structural similarity. Source: UniProtKB

response to muscle activity

Inferred from sequence or structural similarity. Source: UniProtKB

sarcomere organization

Inferred from sequence or structural similarity. Source: UniProtKB

self proteolysis

Inferred from direct assay PubMed 9642272. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: GOC

   Cellular_componentT-tubule

Inferred from sequence or structural similarity. Source: UniProtKB

Z disc

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 19386580PubMed 19556129. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular

Traceable author statement PubMed 9642272. Source: UniProtKB

myofibril

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 19386580. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

calcium-dependent cysteine-type endopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

catalytic activity

Inferred from direct assay PubMed 9642272. Source: UniProtKB

cysteine-type peptidase activity

Traceable author statement Ref.8. Source: ProtInc

ligase regulator activity

Inferred from direct assay PubMed 20694146. Source: UniProtKB

peptidase activity

Inferred from direct assay PubMed 9642272. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 20860623PubMed 23414517. Source: IntAct

protein complex scaffold

Inferred from sequence or structural similarity. Source: UniProtKB

signal transducer activity

Traceable author statement Ref.1. Source: ProtInc

sodium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

structural constituent of muscle

Inferred from sequence or structural similarity. Source: UniProtKB

titin binding

Inferred from physical interaction PubMed 18310072PubMed 9642272. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TTNQ8WZ424EBI-5655000,EBI-681210

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform I (identifier: P20807-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform II (identifier: P20807-2)

The sequence of this isoform differs from the canonical sequence as follows:
     268-315: Missing.
     595-638: Missing.
Isoform III (identifier: P20807-3)

The sequence of this isoform differs from the canonical sequence as follows:
     595-600: Missing.
Isoform IV (identifier: P20807-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-512: Missing.
Isoform V (identifier: P20807-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-665: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 821821Calpain-3
PRO_0000207706

Regions

Domain74 – 417344Calpain catalytic
Domain649 – 68335EF-hand 1
Domain692 – 72534EF-hand 2
Domain722 – 75736EF-hand 3
Domain787 – 82135EF-hand 4
Calcium binding705 – 716121 Probable
Calcium binding735 – 746122 Probable
Region418 – 586169Domain III
Region587 – 64963Linker
Region650 – 821172Domain IV

Sites

Active site1291 By similarity
Active site3341 By similarity
Active site3581 By similarity

Natural variations

Alternative sequence1 – 665665Missing in isoform V.
VSP_044255
Alternative sequence1 – 512512Missing in isoform IV.
VSP_007813
Alternative sequence268 – 31548Missing in isoform II.
VSP_005227
Alternative sequence595 – 63844Missing in isoform II.
VSP_005228
Alternative sequence595 – 6006Missing in isoform III.
VSP_005229
Natural variant41V → I in LGMD2A.
VAR_009548
Natural variant211G → E. Ref.5
Corresponds to variant rs28364364 [ dbSNP | Ensembl ].
VAR_022272
Natural variant261P → L in LGMD2A.
VAR_009549
Natural variant771D → N in LGMD2A.
VAR_009550
Natural variant861S → F in LGMD2A; severe.
VAR_009551
Natural variant93 – 1008Missing in LGMD2A.
VAR_009552
Natural variant1071E → K.
Corresponds to variant rs1801505 [ dbSNP | Ensembl ].
VAR_009553
Natural variant1181R → G in LGMD2A.
VAR_009554
Natural variant1371C → R in LGMD2A.
VAR_009555
Natural variant1601A → G. Ref.5
Corresponds to variant rs17592 [ dbSNP | Ensembl ].
VAR_015389
Natural variant1621I → L in LGMD2A.
VAR_009556
Natural variant1821L → Q in LGMD2A.
VAR_001363
Natural variant1831P → L in LGMD2A.
VAR_009557
Natural variant1841T → M in LGMD2A.
Corresponds to variant rs35889956 [ dbSNP | Ensembl ].
VAR_009558
Natural variant1891L → P in LGMD2A.
VAR_009559
Natural variant200 – 2045Missing in LGMD2A.
VAR_001364
Natural variant2141G → S in LGMD2A.
VAR_009560
Natural variant215 – 2217Missing in LGMD2A.
VAR_009562
Natural variant2151S → P in LGMD2A.
VAR_009561
Natural variant2171E → K in LGMD2A.
VAR_009563
Natural variant2221G → R in LGMD2A. Ref.15
VAR_009564
Natural variant2261E → K in LGMD2A.
VAR_009565
Natural variant2321T → I in LGMD2A.
VAR_009566
Natural variant2341G → E in LGMD2A.
VAR_001365
Natural variant2361A → T. Ref.5
Corresponds to variant rs1801449 [ dbSNP | Ensembl ].
VAR_009567
Natural variant2541Missing in LGMD2A.
VAR_009568
Natural variant3191P → L in LGMD2A.
VAR_009569
Natural variant3341H → Q in LGMD2A.
VAR_009570
Natural variant3361Y → N in LGMD2A. Ref.14
VAR_009571
Natural variant3541V → G in LGMD2A.
VAR_001366
Natural variant3601W → C in LGMD2A. Ref.18
VAR_009572
Natural variant4371R → C in LGMD2A.
VAR_009573
Natural variant4401R → W in LGMD2A.
VAR_009574
Natural variant4411G → D in LGMD2A.
VAR_009575
Natural variant4451G → R in LGMD2A.
VAR_009576
Natural variant4481R → C in LGMD2A.
VAR_009577
Natural variant4481R → G in LGMD2A.
VAR_009578
Natural variant4481R → H in LGMD2A.
VAR_009579
Natural variant4791S → G in LGMD2A.
VAR_009580
Natural variant4861Q → E in LGMD2A. Ref.15
VAR_009581
Natural variant4891R → Q in LGMD2A.
VAR_009582
Natural variant4891R → W in LGMD2A. Ref.15
VAR_009583
Natural variant4901R → Q in LGMD2A. Ref.14
VAR_009584
Natural variant4901R → W in LGMD2A.
Corresponds to variant rs141656719 [ dbSNP | Ensembl ].
VAR_001367
Natural variant4931R → W in LGMD2A.
VAR_009585
Natural variant4961G → R in LGMD2A.
VAR_009586
Natural variant5021I → T in LGMD2A.
VAR_009587
Natural variant5411R → Q in LGMD2A.
VAR_009588
Natural variant5671G → W in LGMD2A.
VAR_009589
Natural variant5721R → Q in LGMD2A. Ref.12
VAR_001368
Natural variant5721R → W in LGMD2A.
VAR_009590
Natural variant6061S → L in LGMD2A.
Corresponds to variant rs199806879 [ dbSNP | Ensembl ].
VAR_009591
Natural variant6221E → A.
Corresponds to variant rs11557723 [ dbSNP | Ensembl ].
VAR_047691
Natural variant6381Q → P in LGMD2A.
VAR_009592
Natural variant6981R → P in LGMD2A.
VAR_009593
Natural variant7021A → V in LGMD2A. Ref.14
VAR_009594
Natural variant7051D → G in LGMD2A.
VAR_009595
Natural variant7051D → H in LGMD2A.
VAR_009596
Natural variant7311F → S in LGMD2A.
VAR_009597
Natural variant7441S → G in LGMD2A. Ref.12 Ref.17
VAR_001369
Natural variant7481R → Q in LGMD2A. Ref.14 Ref.15
VAR_009598
Natural variant7691R → Q in LGMD2A.
VAR_001370
Natural variant7741H → D in LGMD2A; unknown pathological significance.
VAR_009599
Natural variant7981A → E in LGMD2A; unknown pathological significance.
VAR_009600

Experimental info

Mutagenesis1291C → S: Loss of activity. No effect on CMYA5-binding. Ref.11

Sequences

Sequence LengthMass (Da)Tools
Isoform I [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: BC608E8B67AA2741

FASTA82194,254
        10         20         30         40         50         60 
MPTVISASVA PRTAAEPRSP GPVPHPAQSK ATEAGGGNPS GIYSAIISRN FPIIGVKEKT 

        70         80         90        100        110        120 
FEQLHKKCLE KKVLYVDPEF PPDETSLFYS QKFPIQFVWK RPPEICENPR FIIDGANRTD 

       130        140        150        160        170        180 
ICQGELGDCW FLAAIACLTL NQHLLFRVIP HDQSFIENYA GIFHFQFWRY GEWVDVVIDD 

       190        200        210        220        230        240 
CLPTYNNQLV FTKSNHRNEF WSALLEKAYA KLHGSYEALK GGNTTEAMED FTGGVAEFFE 

       250        260        270        280        290        300 
IRDAPSDMYK IMKKAIERGS LMGCSIDDGT NMTYGTSPSG LNMGELIARM VRNMDNSLLQ 

       310        320        330        340        350        360 
DSDLDPRGSD ERPTRTIIPV QYETRMACGL VRGHAYSVTG LDEVPFKGEK VKLVRLRNPW 

       370        380        390        400        410        420 
GQVEWNGSWS DRWKDWSFVD KDEKARLQHQ VTEDGEFWMS YEDFIYHFTK LEICNLTADA 

       430        440        450        460        470        480 
LQSDKLQTWT VSVNEGRWVR GCSAGGCRNF PDTFWTNPQY RLKLLEEDDD PDDSEVICSF 

       490        500        510        520        530        540 
LVALMQKNRR KDRKLGASLF TIGFAIYEVP KEMHGNKQHL QKDFFLYNAS KARSKTYINM 

       550        560        570        580        590        600 
REVSQRFRLP PSEYVIVPST YEPHQEGEFI LRVFSEKRNL SEEVENTISV DRPVKKKKTK 

       610        620        630        640        650        660 
PIIFVSDRAN SNKELGVDQE SEEGKGKTSP DKQKQSPQPQ PGSSDQESEE QQQFRNIFKQ 

       670        680        690        700        710        720 
IAGDDMEICA DELKKVLNTV VNKHKDLKTH GFTLESCRSM IALMDTDGSG KLNLQEFHHL 

       730        740        750        760        770        780 
WNKIKAWQKI FKHYDTDQSG TINSYEMRNA VNDAGFHLNN QLYDIITMRY ADKHMNIDFD 

       790        800        810        820 
SFICCFVRLE GMFRAFHAFD KDGDGIIKLN VLEWLQLTMY A 

« Hide

Isoform II [UniParc].

Checksum: DE8265BA362725FD
Show »

FASTA72984,089
Isoform III [UniParc].

Checksum: E51E96C05024617C
Show »

FASTA81593,512
Isoform IV [UniParc].

Checksum: 8F6F0380D4DE8262
Show »

FASTA30935,930
Isoform V [UniParc].

Checksum: 240D1D4F331C4AA0
Show »

FASTA15618,246

References

« Hide 'large scale' references
[1]"Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A."
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.
Cell 81:27-40(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I), VARIANTS LGMD2A.
[2]"hCAPN3-hZFP106 genomic sequence."
Mashima H., Horikawa Y., Cox N.J., Bell G.I.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM I).
[3]"Alternatively exon-spliced isoforms of calpain 3 expressed in human leukocytes."
Dickson J.M.J., Love D., Evans C.W.E.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS II AND III).
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IV).
[5]NIEHS SNPs program
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-21; GLY-160 AND THR-236.
[6]"Analysis of the DNA sequence and duplication history of human chromosome 15."
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. expand/collapse author list , 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.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS IV AND V).
Tissue: Skin and Uterus.
[8]"Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle."
Sorimachi H., Imajoh-Ohmi S., Emori Y., Kawasaki H., Ohno S., Minami Y., Suzuki K.
J. Biol. Chem. 264:20106-20111(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 44-821 (ISOFORM I).
[9]"The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a family of titin filament-based stress response molecules."
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.
J. Mol. Biol. 333:951-964(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TTN.
[10]"Calpainopathy -- a survey of mutations and polymorphisms."
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. expand/collapse author list , Bushby K., Bakker E., Lopez de Munain A., Fardeau M., Beckmann J.S.
Am. J. Hum. Genet. 64:1524-1540(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[11]"Interactions with M-band titin and calpain 3 link myospryn (CMYA5) to tibial and limb-girdle muscular dystrophies."
Sarparanta J., Blandin G., Charton K., Vihola A., Marchand S., Milic A., Hackman P., Ehler E., Richard I., Udd B.
J. Biol. Chem. 285:30304-30315(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CMYA5, MUTAGENESIS OF CYS-129.
[12]"Juvenile limb-girdle muscular dystrophy. Clinical, histopathological and genetic data from a small community living in the Reunion island."
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.
Brain 119:295-308(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LGMD2A GLN-572 AND GLY-744.
[13]"Multiple independent molecular etiology for limb-girdle muscular dystrophy type 2A patients from various geographical origins."
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.
Am. J. Hum. Genet. 60:1128-1138(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LGMD2A.
[14]"A biochemical, genetic, and clinical survey of autosomal recessive limb girdle muscular dystrophies in Turkey."
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.
Ann. Neurol. 42:222-229(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LGMD2A ASN-336; GLN-490; VAL-702 AND GLN-748.
[15]"Limb-girdle muscular dystrophy in Guipuzcoa (Basque Country, Spain)."
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.
Brain 121:1735-1747(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LGMD2A ARG-222; GLU-486; TRP-489 AND GLN-748.
[16]"A small in-frame deletion within the protease domain of muscle-specific calpain, p94 causes early-onset limb-girdle muscular dystrophy 2A."
Haeffner K., Speer A., Huebner C., Voit T., Oexle K.
Hum. Mutat. Suppl. 1:S298-S300(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LGMD2A 200-PHE--LEU-204 DEL.
[17]"Pseudometabolic expression and phenotypic variability of calpain deficiency in two siblings."
Penisson-Besnier I., Richard I., Dubas F., Beckmann J.S., Fardeau M.
Muscle Nerve 21:1078-1080(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LGMD2A GLY-744.
[18]"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."
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.
Muscle Nerve 21:1493-1501(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LGMD2A CYS-360.
+Additional computationally mapped references.

Web resources

Leiden Muscular Dystrophy pages

Calpain-3 mutations in LGMD2A

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X85030 mRNA. Translation: CAA59403.1.
AF209502 Genomic DNA. Translation: AAL40183.1.
AF127764 mRNA. Translation: AAD28253.1.
AF127765 mRNA. Translation: AAD28254.3.
BT007322 mRNA. Translation: AAP35986.1.
AY902237 Genomic DNA. Translation: AAW69391.1.
AC012651 Genomic DNA. No translation available.
BC003169 mRNA. Translation: AAH03169.1.
BC003521 mRNA. Translation: AAH03521.1.
BC004883 mRNA. Translation: AAH04883.1.
BC007810 mRNA. Translation: AAH07810.3.
BC067126 mRNA. Translation: AAH67126.1.
BC100782 mRNA. Translation: AAI00783.1.
BC107791 mRNA. Translation: AAI07792.1.
BC128605 mRNA. Translation: AAI28606.1.
BC146649 mRNA. Translation: AAI46650.1.
BC146672 mRNA. Translation: AAI46673.1.
CCDSCCDS10085.1. [P20807-2]
CCDS10086.1. [P20807-5]
CCDS32207.1. [P20807-3]
CCDS45245.1. [P20807-1]
CCDS45246.1. [P20807-4]
PIRCIHUH3. A56218.
RefSeqNP_000061.1. NM_000070.2. [P20807-1]
NP_077320.1. NM_024344.1. [P20807-3]
NP_775110.1. NM_173087.1. [P20807-2]
NP_775111.1. NM_173088.1. [P20807-4]
NP_775112.1. NM_173089.1. [P20807-5]
NP_775113.1. NM_173090.1. [P20807-5]
UniGeneHs.143261.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y9Vmodel-A/B649-821[»]
ProteinModelPortalP20807.
SMRP20807. Positions 59-821.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107275. 3 interactions.
IntActP20807. 15 interactions.
MINTMINT-7990282.
STRING9606.ENSP00000380349.

Protein family/group databases

MEROPSC02.004.

PTM databases

PhosphoSiteP20807.

Proteomic databases

PaxDbP20807.
PRIDEP20807.

Protocols and materials databases

DNASU825.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337571; ENSP00000336840; ENSG00000092529. [P20807-5]
ENST00000349748; ENSP00000183936; ENSG00000092529. [P20807-2]
ENST00000357568; ENSP00000350181; ENSG00000092529. [P20807-3]
ENST00000397163; ENSP00000380349; ENSG00000092529. [P20807-1]
ENST00000397200; ENSP00000380384; ENSG00000092529. [P20807-4]
ENST00000397204; ENSP00000380387; ENSG00000092529. [P20807-5]
ENST00000569136; ENSP00000455254; ENSG00000092529. [P20807-5]
GeneID825.
KEGGhsa:825.
UCSCuc001zpk.1. human. [P20807-3]
uc001zpn.1. human. [P20807-1]
uc001zpp.1. human. [P20807-2]
uc001zpq.1. human. [P20807-4]
uc001zpr.1. human. [P20807-5]

Organism-specific databases

CTD825.
GeneCardsGC15P042640.
GeneReviewsCAPN3.
HGNCHGNC:1480. CAPN3.
HPACAB033438.
HPA040052.
MIM114240. gene.
253600. phenotype.
neXtProtNX_P20807.
Orphanet267. Autosomal recessive limb girdle muscular dystrophy type 2A.
PharmGKBPA26061.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327523.
HOGENOMHOG000232035.
HOVERGENHBG012645.
InParanoidP20807.
KOK08573.
OMAGFRLNNQ.
OrthoDBEOG7RV9FM.
PhylomeDBP20807.
TreeFamTF314748.

Enzyme and pathway databases

BRENDA3.4.22.54. 2681.

Gene expression databases

BgeeP20807.
CleanExHS_CAPN3.
GenevestigatorP20807.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000169. Pept_cys_AS.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view]
PfamPF01067. Calpain_III. 1 hit.
PF13405. EF-hand_6. 1 hit.
PF00648. Peptidase_C2. 2 hits.
[Graphical view]
PRINTSPR00704. CALPAIN.
SMARTSM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
SM00054. EFh. 3 hits.
[Graphical view]
SUPFAMSSF49758. SSF49758. 1 hit.
PROSITEPS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCAPN3. human.
GeneWikiCAPN3.
GenomeRNAi825.
NextBio3378.
PROP20807.
SOURCESearch...

Entry information

Entry nameCAN3_HUMAN
AccessionPrimary (citable) accession number: P20807
Secondary accession number(s): A6H8K6 expand/collapse secondary AC list , Q7L4R0, Q9BQC8, Q9BTU4, Q9Y5S6, Q9Y5S7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 171 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM