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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)

 CAN3_MOUSE              Reviewed;         821 AA.
Q64691; A2AVV3; Q9WUC5;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
30-AUG-2017, entry version 158.
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;
Name=Capn3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=8661728; DOI=10.1007/s003359900108;
Richard I., Beckmann J.S.;
"Molecular cloning of mouse canp3, the gene associated with limb-
girdle muscular dystrophy 2A in human.";
Mamm. Genome 7:377-379(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Dickson J.M.J., Love D., Evans C.W.E.;
"Alternatively exon-spliced calpain 3 isoform expressed in mouse
thymus.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[3]
SEQUENCE REVISION TO 638-640.
Dickson J.M.J., Love D., Evans C.W.E.;
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
-!- 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. Interacts with
TTN/titin. Interacts with CMYA5; this interaction, which results
in CMYA5 proteolysis, may protect CAPN3 from autolysis.
{ECO:0000250|UniProtKB:P20807}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=Q64691-1; Sequence=Displayed;
Name=Short;
IsoId=Q64691-2; Sequence=VSP_005230, VSP_005231;
-!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X92523; CAA63301.1; -; mRNA.
EMBL; AF127766; AAD28255.2; -; mRNA.
EMBL; AL935121; CAM24140.1; -; Genomic_DNA.
CCDS; CCDS16620.1; -. [Q64691-1]
CCDS; CCDS50679.1; -. [Q64691-2]
RefSeq; NP_001171270.1; NM_001177799.1. [Q64691-2]
RefSeq; NP_031627.2; NM_007601.3. [Q64691-1]
UniGene; Mm.458021; -.
UniGene; Mm.485295; -.
ProteinModelPortal; Q64691; -.
SMR; Q64691; -.
BioGrid; 198472; 2.
STRING; 10090.ENSMUSP00000028749; -.
MEROPS; C02.004; -.
iPTMnet; Q64691; -.
PhosphoSitePlus; Q64691; -.
PaxDb; Q64691; -.
PRIDE; Q64691; -.
Ensembl; ENSMUST00000028749; ENSMUSP00000028749; ENSMUSG00000079110. [Q64691-1]
Ensembl; ENSMUST00000110721; ENSMUSP00000106349; ENSMUSG00000079110. [Q64691-2]
GeneID; 12335; -.
KEGG; mmu:12335; -.
UCSC; uc008lvz.2; mouse. [Q64691-1]
UCSC; uc008lwa.2; mouse. [Q64691-2]
CTD; 825; -.
MGI; MGI:107437; Capn3.
eggNOG; KOG0045; Eukaryota.
eggNOG; ENOG410XP0B; LUCA.
GeneTree; ENSGT00760000118971; -.
HOGENOM; HOG000232035; -.
HOVERGEN; HBG012645; -.
InParanoid; Q64691; -.
KO; K08573; -.
OrthoDB; EOG091G049E; -.
TreeFam; TF314748; -.
BRENDA; 3.4.22.54; 3474.
PRO; PR:Q64691; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000079110; -.
CleanEx; MM_CAPN3; -.
ExpressionAtlas; Q64691; baseline and differential.
Genevisible; Q64691; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0030016; C:myofibril; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0030315; C:T-tubule; ISS:UniProtKB.
GO; GO:0030018; C:Z disc; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IDA:MGI.
GO; GO:0003824; F:catalytic activity; ISS:UniProtKB.
GO; GO:0055103; F:ligase regulator activity; ISS:UniProtKB.
GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
GO; GO:0032947; F:protein complex scaffold activity; IMP:UniProtKB.
GO; GO:0031402; F:sodium ion binding; IDA:UniProtKB.
GO; GO:0008307; F:structural constituent of muscle; IMP:UniProtKB.
GO; GO:0031432; F:titin binding; ISS:UniProtKB.
GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
GO; GO:0071472; P:cellular response to salt stress; IDA:UniProtKB.
GO; GO:0070315; P:G1 to G0 transition involved in cell differentiation; IDA:UniProtKB.
GO; GO:0061061; P:muscle structure development; IMP:UniProtKB.
GO; GO:0030239; P:myofibril assembly; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0033234; P:negative regulation of protein sumoylation; ISS:UniProtKB.
GO; GO:2001015; P:negative regulation of skeletal muscle cell differentiation; IMP:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0045862; P:positive regulation of proteolysis; IDA:UniProtKB.
GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IMP:UniProtKB.
GO; GO:0014718; P:positive regulation of satellite cell activation involved in skeletal muscle regeneration; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0012501; P:programmed cell death; IDA:UniProtKB.
GO; GO:0006461; P:protein complex assembly; IMP:UniProtKB.
GO; GO:0072657; P:protein localization to membrane; IMP:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0050790; P:regulation of catalytic activity; ISS:UniProtKB.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0045661; P:regulation of myoblast differentiation; IDA:UniProtKB.
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; IMP:MGI.
GO; GO:0097264; P:self proteolysis; ISS: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.
2: Evidence at transcript level;
Alternative splicing; Calcium; Complete proteome; Cytoplasm;
Hydrolase; Metal-binding; Protease; Reference proteome; Repeat;
Thiol protease.
CHAIN 1 821 Calpain-3.
/FTId=PRO_0000207708.
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:0000250|UniProtKB:P20807}.
CA_BIND 705 716 2. {ECO:0000250|UniProtKB:P20807,
ECO:0000255|PROSITE-ProRule:PRU00448}.
CA_BIND 735 741 3. {ECO:0000250|UniProtKB:P20807,
ECO:0000255|PROSITE-ProRule:PRU00448}.
CA_BIND 800 806 4. {ECO:0000250|UniProtKB:P20807}.
REGION 418 586 Domain III.
REGION 587 649 Linker.
REGION 650 820 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 268 315 Missing (in isoform Short).
{ECO:0000303|Ref.2}.
/FTId=VSP_005230.
VAR_SEQ 595 638 Missing (in isoform Short).
{ECO:0000303|Ref.2}.
/FTId=VSP_005231.
CONFLICT 66 66 R -> K (in Ref. 1; CAA63301 and 2;
AAD28255). {ECO:0000305}.
SEQUENCE 821 AA; 94242 MW; C7FC94E31E1084C9 CRC64;
MPTVISPTVA PRTGAEPRSP GPVPHPAQGK TTEAGGGHPS GIYSAIISRN FPIIGVKEKT
FEQLRRKCLE KKVLYLDPEF PPDETSLFYS QKFPIQFVWK RPPEICENPR FIIGGANRTD
ICQGDLGDCW FLAAIACLTL NERLLFRVIP HDQSFTENYA GIFHFQFWRY GDWVDVVIDD
CLPTYNNQLV FTKSNHRNEF WSALLEKAYA KLHGSYEALK GGNTTEAMED FTGGVTEFFE
IKDAPSDMYK IMRKAIERGS LMGCSIDDGT NMTYGTSPSG LNMGELIARM VRNMDNSLLR
DSDLDPRGSD DRPSRTIVPV QYETRMACGL VKGHAYSVTG LEEALFKGEK VKLVRLRNPW
GQVEWNGSWS DGWKDWSFVD KDEKARLQHQ VTEDGEFWMS YDDFVYHFTK LEICNLTADA
LESDKLQTWT VSVNEGRWVR GCSAGGCRNF PDTFWTNPQY RLKLLEEDDD PEDSEVICSF
LVALMQKNRR KDRKLGANLF TIGFAIYEVP KEMHGNKQHL QKDFFLYNAS KARSKTYINM
REVSQRFRLP PSEYVIVPST YEPHQEGEFI LRVFSEKRNL SEEAENTISV DRPVKKKKNK
PIIFVSDRAN SNKELGVDQE AEEGKDKAGP EKRGETPQPR PGHTDQESEE QQQFRNIFRQ
IAGDDMEICA DELKNVLNTV VNKHKDLKTQ GFTLESCRSM IALMDTDGSG RLNLQEFHHL
WKKIKAWQKI FKHYDTDHSG TINSYEMRNA VNDAGFHLNS QLYDIITMRY ADKHMNIDFD
SFICCFVRLE GMFRAFNAFD KDGDGIIKLN VLEWLQLTMY A


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