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Calpain-2 catalytic subunit (EC 3.4.22.53) (80 kDa M-calpain subunit) (CALP80) (Calcium-activated neutral proteinase 2) (CANP 2) (Calpain M-type) (Calpain-2 large subunit) (Millimolar-calpain) (M-calpain)

 CAN2_MOUSE              Reviewed;         700 AA.
O08529; O35518; O54843;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
30-AUG-2017, entry version 174.
RecName: Full=Calpain-2 catalytic subunit;
EC=3.4.22.53;
AltName: Full=80 kDa M-calpain subunit;
Short=CALP80;
AltName: Full=Calcium-activated neutral proteinase 2;
Short=CANP 2;
AltName: Full=Calpain M-type;
AltName: Full=Calpain-2 large subunit;
AltName: Full=Millimolar-calpain;
Short=M-calpain;
Flags: Precursor;
Name=Capn2;
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].
STRAIN=BALB/cJ;
PubMed=9339374; DOI=10.1006/geno.1997.4870;
Dear T.N., Matena K., Vingron M., Boehm T.;
"A new subfamily of vertebrate calpains lacking a calmodulin-like
domain: implications for calpain regulation and evolution.";
Genomics 45:175-184(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
Ozaki Y.;
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=CNS;
PubMed=9669314;
DOI=10.1002/(SICI)1097-4547(19980615)52:6<653::AID-JNR4>3.3.CO;2-J;
Glass J.D., Nash N.R., Dry I., Culver D., Levey A.I., Wesselingh S.;
"Cloning of m-calpain 80 kD subunit from the axonal degeneration-
resistant WLD(S) mouse mutant.";
J. Neurosci. Res. 52:653-660(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION, AND INTERACTION WITH CPEB3.
PubMed=22711986; DOI=10.1128/MCB.00296-12;
Wang C.F., Huang Y.S.;
"Calpain 2 activated through N-methyl-D-aspartic acid receptor
signaling cleaves CPEB3 and abrogates CPEB3-repressed translation in
neurons.";
Mol. Cell. Biol. 32:3321-3332(2012).
-!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which
catalyzes limited proteolysis of substrates involved in
cytoskeletal remodeling and signal transduction. Proteolytically
cleaves MYOC at 'Arg-226' (By similarity). Proteolytically cleaves
CPEB3 following neuronal stimulation which abolishes CPEB3
translational repressor activity, leading to translation of CPEB3
target mRNAs (PubMed:22711986). {ECO:0000250|UniProtKB:P17655,
ECO:0000269|PubMed:22711986}.
-!- CATALYTIC ACTIVITY: Broad endopeptidase specificity.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 7 Ca(2+) ions. {ECO:0000250};
-!- ENZYME REGULATION: Activated by 200-1000 micromolar concentrations
of calcium and inhibited by calpastatin.
-!- SUBUNIT: Forms a heterodimer with a small (regulatory) subunit
(CAPNS1) (By similarity). Interacts with CPEB3; this leads to
cleavage of CPEB3 (PubMed:22711986).
{ECO:0000250|UniProtKB:Q07009, ECO:0000269|PubMed:22711986}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}. Note=Translocates to the plasma membrane upon
Ca(2+) binding. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y10139; CAA71227.1; -; mRNA.
EMBL; D38117; BAA22964.1; -; mRNA.
EMBL; AF015038; AAB94029.1; -; mRNA.
EMBL; BC054726; AAH54726.1; -; mRNA.
CCDS; CCDS35813.1; -.
RefSeq; NP_033924.2; NM_009794.3.
UniGene; Mm.19306; -.
UniGene; Mm.474138; -.
ProteinModelPortal; O08529; -.
SMR; O08529; -.
BioGrid; 198471; 3.
IntAct; O08529; 4.
MINT; MINT-1566045; -.
STRING; 10090.ENSMUSP00000068895; -.
MEROPS; C02.002; -.
iPTMnet; O08529; -.
PhosphoSitePlus; O08529; -.
SwissPalm; O08529; -.
EPD; O08529; -.
MaxQB; O08529; -.
PaxDb; O08529; -.
PeptideAtlas; O08529; -.
PRIDE; O08529; -.
Ensembl; ENSMUST00000068505; ENSMUSP00000068895; ENSMUSG00000026509.
GeneID; 12334; -.
KEGG; mmu:12334; -.
UCSC; uc007dye.2; mouse.
CTD; 824; -.
MGI; MGI:88264; Capn2.
eggNOG; KOG0045; Eukaryota.
eggNOG; ENOG410XP0B; LUCA.
GeneTree; ENSGT00760000118971; -.
HOGENOM; HOG000232035; -.
HOVERGEN; HBG012645; -.
InParanoid; O08529; -.
KO; K03853; -.
OMA; DTYKKWK; -.
OrthoDB; EOG091G049E; -.
PhylomeDB; O08529; -.
TreeFam; TF314748; -.
BRENDA; 3.4.22.53; 3474.
Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
Reactome; R-MMU-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
ChiTaRS; Capn2; mouse.
PRO; PR:O08529; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026509; -.
CleanEx; MM_CAPN2; -.
Genevisible; O08529; MM.
GO; GO:0000785; C:chromatin; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0005764; C:lysosome; IDA:MGI.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0097038; C:perinuclear endoplasmic reticulum; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
GO; GO:0031143; C:pseudopodium; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0008092; F:cytoskeletal protein binding; IEA:Ensembl.
GO; GO:0008233; F:peptidase activity; IDA:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0001824; P:blastocyst development; IMP:MGI.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
GO; GO:0007520; P:myoblast fusion; IMP:MGI.
GO; GO:0016540; P:protein autoprocessing; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; ISO:MGI.
GO; GO:0051493; P:regulation of cytoskeleton organization; IEA:InterPro.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
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; IPR029539; CAPN2.
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.
PANTHER; PTHR10183:SF340; PTHR10183:SF340; 1.
Pfam; PF01067; Calpain_III; 1.
Pfam; PF13833; EF-hand_8; 1.
Pfam; PF00648; Peptidase_C2; 1.
PRINTS; PR00704; CALPAIN.
SMART; SM00720; calpain_III; 1.
SMART; SM00230; CysPc; 1.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF49758; SSF49758; 1.
PROSITE; PS50203; CALPAIN_CAT; 1.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 2.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
1: Evidence at protein level;
Acetylation; Calcium; Cell membrane; Complete proteome; Cytoplasm;
Hydrolase; Membrane; Metal-binding; Protease; Reference proteome;
Repeat; Thiol protease.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P17655}.
PROPEP 2 19 Anchors to the small subunit.
{ECO:0000255}.
/FTId=PRO_0000026491.
CHAIN 20 700 Calpain-2 catalytic subunit.
/FTId=PRO_0000026492.
DOMAIN 45 344 Calpain catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00239}.
DOMAIN 572 605 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 602 637 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 585 596 1.
CA_BIND 615 626 2.
REGION 345 514 Domain III.
REGION 515 529 Linker.
REGION 530 700 Domain IV.
ACT_SITE 105 105 {ECO:0000250}.
ACT_SITE 262 262 {ECO:0000250}.
ACT_SITE 286 286 {ECO:0000250}.
METAL 89 89 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 91 91 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 96 96 Calcium 3. {ECO:0000250}.
METAL 175 175 Calcium 3. {ECO:0000250}.
METAL 229 229 Calcium 2. {ECO:0000250}.
METAL 230 230 Calcium 2. {ECO:0000250}.
METAL 292 292 Calcium 4. {ECO:0000250}.
METAL 299 299 Calcium 4. {ECO:0000250}.
METAL 319 319 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 323 323 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 542 542 Calcium 5; via carbonyl oxygen.
{ECO:0000250}.
METAL 545 545 Calcium 5. {ECO:0000250}.
METAL 547 547 Calcium 5; via carbonyl oxygen.
{ECO:0000250}.
METAL 552 552 Calcium 5. {ECO:0000250}.
METAL 585 585 Calcium 6. {ECO:0000250}.
METAL 587 587 Calcium 6. {ECO:0000250}.
METAL 589 589 Calcium 6; via carbonyl oxygen.
{ECO:0000250}.
METAL 591 591 Calcium 6; via carbonyl oxygen.
{ECO:0000250}.
METAL 596 596 Calcium 6. {ECO:0000250}.
METAL 615 615 Calcium 7. {ECO:0000250}.
METAL 617 617 Calcium 7. {ECO:0000250}.
METAL 619 619 Calcium 7; via carbonyl oxygen.
{ECO:0000250}.
METAL 621 621 Calcium 7; via carbonyl oxygen.
{ECO:0000250}.
METAL 626 626 Calcium 7. {ECO:0000250}.
METAL 658 658 Calcium 1. {ECO:0000250}.
METAL 661 661 Calcium 1. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P17655}.
CONFLICT 194 194 A -> T (in Ref. 1; CAA71227).
{ECO:0000305}.
CONFLICT 212 212 A -> G (in Ref. 2; BAA22964).
{ECO:0000305}.
CONFLICT 402 402 E -> G (in Ref. 1; CAA71227).
{ECO:0000305}.
SEQUENCE 700 AA; 79872 MW; 682146B290968316 CRC64;
MAGIAIKLAK DREAAEGLGS HERAIKYLNQ DYETLRNECL EAGALFQDPS FPALPSSLGY
KELGPYSSKT RGIEWKRPTE ICADPQFIIG GATRTDICQG ALGDCWLLAA IASLTLNEEI
LARVVPPDQS FQENYAGIFH FQFWQYGEWV EVVVDDRLPT KDGELLFVHS AEGSEFWSAL
LEKAYAKING CYEALSGGAT TEGFEDFTGG IAEWYELRKP PPNLFKIIQK ALEKGSLLGC
SIDITSAADS EAVTYQKLVK GHAYSVTGAE EVESSGSLQK LIRIRNPWGQ VEWTGKWNDN
CPSWNTVDPE VRANLTERQE DGEFWMSFSD FLRHYSRLEI CNLTPDTLTC DSYKKWKLTK
MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDEED GERGCTFLVG LIQKHRRRQR
KMGEDMHTIG FGIYEVPEEL TGQTNIHLGK NFFLTTRARE RSDTFINLRE VLNRFKLPPG
EYVLVPSTFE PHKDGDFCIR VFSEKKADYQ AVDDEIEANI EEIDANEEDI DDGFRRLFVQ
LAGEDAEISA FELQTILRRV LAKRQDIKSD GFSIETCKIM VDMLDEDGSG KLGLKEFYIL
WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKLPC QLHQVIVARF ADDELIIDFD
NFVRCLVRLE TLFKIFKQLD PENTGTIQLN LASWLSFSVL


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