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   16-JUN-2009, entry version 77.
DE   RecName: Full=Calpain-2 catalytic subunit;
DE            EC=3.4.22.53;
DE   AltName: Full=Calpain-2 large subunit;
DE   AltName: Full=Calcium-activated neutral proteinase 2;
DE            Short=CANP 2;
DE   AltName: Full=Calpain M-type;
DE   AltName: Full=M-calpain;
DE   AltName: Full=Millimolar-calpain;
DE   Flags: Precursor;
GN   Name=CAPN2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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
RT   from bovine muscle.";
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which
CC       catalyze limited proteolysis of substrates involved in
CC       cytoskeletal remodeling and signal transduction (By similarity).
CC   -!- CATALYTIC ACTIVITY: Broad endopeptidase specificity.
CC   -!- COFACTOR: Binds 3 calcium ions.
CC   -!- ENZYME REGULATION: Activated by 200-1000 micromolar concentrations
CC       of calcium and inhibited by calpastatin.
CC   -!- SUBUNIT: Forms a heterodimer with a small (regulatory) subunit
CC       (CAPNS1).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By
CC       similarity). Note=Translocates to the plasma membrane upon Ca(2+)
CC       binding (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family.
CC   -!- SIMILARITY: Contains 1 calpain catalytic domain.
CC   -!- SIMILARITY: Contains 3 EF-hand domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA18455.1; Type=Frameshift; Positions=470, 480;
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DR   EMBL; BC134526; AAI34527.1; -; mRNA.
DR   EMBL; U07850; AAA18455.1; ALT_FRAME; mRNA.
DR   IPI; IPI00695673; -.
DR   RefSeq; NP_001096556.1; -.
DR   UniGene; Bt.60825; -.
DR   HSSP; P17655; 1KFX.
DR   MEROPS; C02.002; -.
DR   Ensembl; ENSBTAG00000012778; Bos taurus.
DR   GeneID; 281662; -.
DR   KEGG; bta:281662; -.
DR   HOVERGEN; Q27971; -.
DR   OMA; Q27971; LTKMDGN.
DR   BRENDA; 3.4.22.53; 251.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptida...; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR011992; EF-Hand_type.
DR   InterPro; IPR018247; EF_HAND_1.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca_bd.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR001300; Peptidase_C2.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 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   SMART; SM00054; EFh; 2.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 3.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; FALSE_NEG.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Calcium; Cell membrane; Cytoplasm; Hydrolase; Membrane; Protease;
KW   Repeat; Thiol protease.
FT   INIT_MET      1      1       Removed (By similarity).
FT   PROPEP        2     19       Anchors to the small subunit (Potential).
FT                                /FTId=PRO_0000317423.
FT   CHAIN        20    700       Calpain-2 catalytic subunit.
FT                                /FTId=PRO_0000207702.
FT   DOMAIN       45    344       Calpain catalytic.
FT   DOMAIN      572    605       EF-hand 1.
FT   DOMAIN      602    637       EF-hand 2.
FT   DOMAIN      667    700       EF-hand 3.
FT   CA_BIND     585    596       1 (By similarity).
FT   CA_BIND     615    626       2 (By similarity).
FT   REGION      345    514       Domain III (By similarity).
FT   REGION      515    529       Linker (By similarity).
FT   REGION      530    700       Domain IV (By similarity).
FT   ACT_SITE    105    105       By similarity.
FT   ACT_SITE    262    262       By similarity.
FT   ACT_SITE    286    286       By similarity.
FT   CONFLICT    417    417       R -> Q (in Ref. 2; AAA18455).
FT   CONFLICT    460    462       ERS -> DV (in Ref. 2; AAA18455).
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
//