CAN2_BOVIN
ID CAN2_BOVIN Reviewed; 700 AA.
AC Q27971; A4IFD3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Calpain-2 catalytic subunit;
DE EC=3.4.22.53;
DE AltName: Full=Calcium-activated neutral proteinase 2;
DE Short=CANP 2;
DE AltName: Full=Calpain M-type;
DE AltName: Full=Calpain-2 large subunit;
DE AltName: Full=Millimolar-calpain;
DE Short=M-calpain;
DE Flags: Precursor;
GN Name=CAPN2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 377-585.
RC TISSUE=Skeletal muscle;
RA Sun W., Bidwell C.A., Ji S., Hancock D.L.;
RT "Cloning the partial cDNA's for the calpain family of protease genes from
RT bovine muscle.";
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which
CC catalyzes limited proteolysis of substrates involved in cytoskeletal
CC remodeling and signal transduction. Proteolytically cleaves MYOC at
CC 'Arg-226'. Proteolytically cleaves CPEB3 following neuronal stimulation
CC which abolishes CPEB3 translational repressor activity, leading to
CC translation of CPEB3 target mRNAs. {ECO:0000250|UniProtKB:O08529,
CC ECO:0000250|UniProtKB:P17655}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad endopeptidase specificity.; EC=3.4.22.53;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 7 Ca(2+) ions. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by 200-1000 micromolar concentrations of
CC calcium and inhibited by calpastatin.
CC -!- SUBUNIT: Forms a heterodimer with a small (regulatory) subunit
CC (CAPNS1). Interacts with CPEB3; this leads to cleavage of CPEB3.
CC {ECO:0000250|UniProtKB:O08529, ECO:0000250|UniProtKB:Q07009}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Translocates to the plasma membrane upon Ca(2+)
CC binding. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA18455.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC134526; AAI34527.1; -; mRNA.
DR EMBL; U07850; AAA18455.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001096556.1; NM_001103086.1.
DR AlphaFoldDB; Q27971; -.
DR SMR; Q27971; -.
DR CORUM; Q27971; -.
DR IntAct; Q27971; 3.
DR MINT; Q27971; -.
DR STRING; 9913.ENSBTAP00000044733; -.
DR BindingDB; Q27971; -.
DR ChEMBL; CHEMBL3612; -.
DR MEROPS; C02.002; -.
DR PaxDb; Q27971; -.
DR PeptideAtlas; Q27971; -.
DR PRIDE; Q27971; -.
DR Ensembl; ENSBTAT00000047532; ENSBTAP00000044733; ENSBTAG00000012778.
DR GeneID; 281662; -.
DR KEGG; bta:281662; -.
DR CTD; 824; -.
DR VEuPathDB; HostDB:ENSBTAG00000012778; -.
DR VGNC; VGNC:55037; CAPN2.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000154784; -.
DR HOGENOM; CLU_010982_0_1_1; -.
DR InParanoid; Q27971; -.
DR OMA; AFELCNI; -.
DR OrthoDB; 704215at2759; -.
DR TreeFam; TF314748; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000012778; Expressed in myometrium and 105 other tissues.
DR ExpressionAtlas; Q27971; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IEA:InterPro.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR CDD; cd16199; EFh_PEF_CAPN2; 1.
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; IPR029539; CAPN2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR042736; EFh_PEF_CAPN2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183:SF268; PTHR10183:SF268; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
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; 3.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Calcium; Cell membrane; Cytoplasm; Hydrolase; Membrane;
KW Metal-binding; Protease; Reference proteome; Repeat; Thiol protease.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P17655"
FT PROPEP 2..19
FT /note="Anchors to the small subunit"
FT /evidence="ECO:0000255"
FT /id="PRO_0000317423"
FT CHAIN 20..700
FT /note="Calpain-2 catalytic subunit"
FT /id="PRO_0000207702"
FT DOMAIN 45..344
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 572..597
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 602..637
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 652..672
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 345..514
FT /note="Domain III"
FT /evidence="ECO:0000250"
FT REGION 515..529
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 530..700
FT /note="Domain IV"
FT /evidence="ECO:0000250"
FT ACT_SITE 105
FT /evidence="ECO:0000250"
FT ACT_SITE 262
FT /evidence="ECO:0000250"
FT ACT_SITE 286
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 542
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 545
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 552
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 585
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 587
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 589
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 591
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 596
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 615
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 617
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 619
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 621
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 626
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 658
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 661
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P17655"
FT CONFLICT 417
FT /note="R -> Q (in Ref. 2; AAA18455)"
FT /evidence="ECO:0000305"
FT CONFLICT 460..462
FT /note="ERS -> DV (in Ref. 2; AAA18455)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 700 AA; 79935 MW; 00FD932E9C6AB268 CRC64;
MAGIAAKLAK DREAAEGLGS HERAVKYLNQ DYAALRDECL EAGALFQDPS FPALPSSLGF
KELGPYSSKT RGIEWKRPTE ICDNPQFITG GATRTDICQG ALGDCWLLAA IASLTLNEEI
LARVVPLDQS FQENYAGIFH FQFWQYGEWV EVVVDDRLPT KDGELLFVHS AEGSEFWSAL
LEKAYAKING CYEALSGGAT TEGFEDFTGG IAEWYELRKA PPNLFRIIQK ALQKGSLLGC
SIDITSAADS EAITFQKLVK GHAYSVTGAE EVESRGSLQK LIRIRNPWGE VEWTGQWNDN
CPNWNTVDPE VRETLTRQHE DGEFWMSFND FLRHYSRLEI CNLTPDTLTS DSYKKWKLTK
MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDQED GESGCTFLVG LIQKHRRRQR
KMGEDMHTIG FGIYEVPEEL TGQTNIHLSK KFFLTTRARE RSDTFINLRE VLNRFKLPPG
EYIVVPSTFE PNKDGDFCIR VFSEKKADYQ VVDDEIEANI DEIDISEDDI DDGFRRLFAQ
LAGEDAEISA FELQTILRRV LAKRQDIKSD GFSIETCKIM VDMLDSDGSG KLGLKEFYIL
WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKMPC QLHQVIVARF ADDDLIIDFD
NFVRCLIRLE TLFRIFKQLD PENTGMIQLD LISWLSFSVL
