Sequence of CAN2_RAT
EC Number:3.4.22.53
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
broad endopeptidase specificity
General information:
Sequence
0 MAGIAMKLAK DREAAEGLGS HERAIKYLNQ DYETLRNECL EAGALFQDPS FPALPSSLGF
60 KELGPYSSKT RGIEWKRPTE ICADPQFIIG GATRTDICQG ALGDCWLLAA IASLTLNEEI
120 LARVVPLDQS FQENYAGIFH FQFWQYGEWV EVVVDDRLPT KDGELLFVHS AEGSEFWSAL
180 LEKAYAKING CYEALSGGAT TEGFEDFTGG IAEWYELRKP PPNLFKIIQK ALEKGSLLGC
240 SIDITSAADS EAVTYQKLVK GHAYSVTGAE EVESSGSLQK LIRIRNPWGQ VEWTGKWNDN
300 CPSWNTVDPE VRANLTERQE DGEFWMSFSD FLRHYSRLEI CNLTPDTLTC DSYKKWKLTK
360 MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDDED GERGCTFLVG LIQKHRRRQR
420 KMGEDMHTIG FGIYEVPEEL TGQTNIHLSK NFFLTTRARE RSDTFINLRE VLNRFKLPPG
480 EYVLVPSTFE PHKNGDFCIR VFSEKKADYQ TVDDEIEANI EEIEANEEDI GDGFRRLFAQ
540 LAGEDAEISA FELQTILRRV LAKREDIKSD GFSIETCKIM VDMLDEDGSG KLGLKEFYIL
600 WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKLPC QLHQVIVARF ADDELIIDFD
660 NFVRCLVRLE ILFKIFKQLD PENTGTIQLD LISWLSFSVL
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
698408
Deluca C.I.,Davies P.L.,Samis J.A.,Elce J.S.
Molecular cloning and bacterial expression of cDNA for rat calpain II 80 kDa subunit.
Biochim. Biophys. Acta
1216
81-93
1993
698409
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
698410
Moldoveanu T.,Hosfield C.M.,Jia Z.,Elce J.S.,Davies P.L.
Ca(2+)-induced structural changes in rat m-calpain revealed by partial proteolysis.
Biochim. Biophys. Acta
1545
245-254
2001
698411
Hosfield C.M.,Moldoveanu T.,Davies P.L.,Elce J.S.,Jia Z.
Calpain mutants with increased Ca2+ sensitivity and implications for the role of the C(2)-like domain.
J. Biol. Chem.
276
7404-7407
2001
698412
Arthur J.S.,Gauthier S.,Elce J.S.
Active site residues in m-calpain: identification by site-directed mutagenesis.
FEBS Lett.
368
397-400
1995
698413
Hosfield C.M.,Elce J.S.,Davies P.L.,Jia Z.
Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation.
EMBO J.
18
6880-6889
1999
698414
Moldoveanu T.,Gehring K.,Green D.R.
Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains.
Nature
456
404-408
2008
698415
Hanna R.A.,Campbell R.L.,Davies P.L.
Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin.
Nature
456
409-412
2008
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