Full text data of CAPN2
CAPN2
(CANPL2)
[Confidence: low (only semi-automatic identification from reviews)]
Calpain-2 catalytic subunit; 3.4.22.53 (Calcium-activated neutral proteinase 2; CANP 2; Calpain M-type; Calpain large polypeptide L2; Calpain-2 large subunit; Millimolar-calpain; M-calpain; Flags: Precursor)
Calpain-2 catalytic subunit; 3.4.22.53 (Calcium-activated neutral proteinase 2; CANP 2; Calpain M-type; Calpain large polypeptide L2; Calpain-2 large subunit; Millimolar-calpain; M-calpain; Flags: Precursor)
UniProt
P17655
ID CAN2_HUMAN Reviewed; 700 AA.
AC P17655; A6NDG7; B7ZA96; E7ES58; Q16738; Q6PJT3; Q8WU26; Q9HBB1;
read moreDT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 6.
DT 22-JAN-2014, entry version 174.
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 large polypeptide L2;
DE AltName: Full=Calpain-2 large subunit;
DE AltName: Full=Millimolar-calpain;
DE Short=M-calpain;
DE Flags: Precursor;
GN Name=CAPN2; Synonyms=CANPL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLU-22.
RX PubMed=2852952; DOI=10.1021/bi00421a022;
RA Imajoh S., Aoki K., Ohno S., Emori Y., Kawasaki H., Sugihara H.,
RA Suzuki K.;
RT "Molecular cloning of the cDNA for the large subunit of the high-Ca2+-
RT requiring form of human Ca2+-activated neutral protease.";
RL Biochemistry 27:8122-8128(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLU-22.
RC TISSUE=Astrocytoma;
RX PubMed=10944468; DOI=10.1006/bbrc.2000.3282;
RA Ye Z., Connor J.R.;
RT "cDNA cloning by amplification of circularized first strand cDNAs
RT reveals non-IRE-regulated iron-responsive mRNAs.";
RL Biochem. Biophys. Res. Commun. 275:223-227(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-22; GLY-68;
RP ARG-476; GLN-521; GLN-568 AND GLN-677.
RG NIEHS SNPs program;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP GLU-22.
RC TISSUE=Pancreas, Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79, AND VARIANTS GLU-22 AND
RP GLY-68.
RC TISSUE=Lymph node;
RX PubMed=2539381;
RA Hata A., Ohno S., Akita Y., Suzuki K.;
RT "Tandemly reiterated negative enhancer-like elements regulate
RT transcription of a human gene for the large subunit of calcium-
RT dependent protease.";
RL J. Biol. Chem. 264:6404-6411(1989).
RN [8]
RP PROTEIN SEQUENCE OF 2-12.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=10639123; DOI=10.1073/pnas.97.2.588;
RA Strobl S., Fernandez-Catalan C., Braun M., Huber R., Masumoto H.,
RA Nakagawa K., Irie A., Sorimachi H., Bourenkow G., Bartunik H.,
RA Suzuki K., Bode W.;
RT "The crystal structure of calcium-free human m-calpain suggests an
RT electrostatic switch mechanism for activation by calcium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:588-592(2000).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-22, AND MASS SPECTROMETRY.
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which
CC catalyze limited proteolysis of substrates involved in
CC cytoskeletal remodeling and signal transduction.
CC -!- CATALYTIC ACTIVITY: Broad endopeptidase specificity.
CC -!- COFACTOR: Binds 7 calcium ions (By similarity).
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 -!- INTERACTION:
CC P04632:CAPNS1; NbExp=3; IntAct=EBI-1028956, EBI-711828;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocates
CC to the plasma membrane upon Ca(2+) binding.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P17655-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P17655-2; Sequence=VSP_043027, VSP_043028;
CC Note=No experimental confirmation available;
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=AAH07686.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=AAH11828.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/capn2/";
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DR EMBL; M23254; AAA35645.1; -; mRNA.
DR EMBL; AF261089; AAF99682.1; -; mRNA.
DR EMBL; AK316211; BAH14582.1; -; mRNA.
DR EMBL; AY835586; AAV80421.1; -; Genomic_DNA.
DR EMBL; AC096542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007686; AAH07686.1; ALT_SEQ; mRNA.
DR EMBL; BC011828; AAH11828.1; ALT_SEQ; mRNA.
DR EMBL; BC021303; AAH21303.1; -; mRNA.
DR EMBL; J04700; AAA52760.1; -; Genomic_DNA.
DR PIR; S10590; CIHUH2.
DR RefSeq; NP_001139540.1; NM_001146068.1.
DR RefSeq; NP_001739.2; NM_001748.4.
DR UniGene; Hs.350899; -.
DR PDB; 1KFU; X-ray; 2.50 A; L=2-700.
DR PDB; 1KFX; X-ray; 3.15 A; L=2-700.
DR PDB; 2NQA; X-ray; 2.20 A; A/B=26-346.
DR PDBsum; 1KFU; -.
DR PDBsum; 1KFX; -.
DR PDBsum; 2NQA; -.
DR ProteinModelPortal; P17655; -.
DR SMR; P17655; 2-700.
DR IntAct; P17655; 5.
DR MINT; MINT-120195; -.
DR STRING; 9606.ENSP00000295006; -.
DR BindingDB; P17655; -.
DR ChEMBL; CHEMBL2382; -.
DR MEROPS; C02.002; -.
DR PhosphoSite; P17655; -.
DR DMDM; 60416356; -.
DR PaxDb; P17655; -.
DR PeptideAtlas; P17655; -.
DR PRIDE; P17655; -.
DR DNASU; 824; -.
DR Ensembl; ENST00000295006; ENSP00000295006; ENSG00000162909.
DR Ensembl; ENST00000433674; ENSP00000413158; ENSG00000162909.
DR GeneID; 824; -.
DR KEGG; hsa:824; -.
DR UCSC; uc001hob.4; human.
DR CTD; 824; -.
DR GeneCards; GC01P223890; -.
DR HGNC; HGNC:1479; CAPN2.
DR HPA; HPA024470; -.
DR MIM; 114230; gene.
DR neXtProt; NX_P17655; -.
DR PharmGKB; PA26060; -.
DR eggNOG; NOG327523; -.
DR HOVERGEN; HBG012645; -.
DR InParanoid; P17655; -.
DR KO; K03853; -.
DR OMA; DTYKKWK; -.
DR OrthoDB; EOG7RV9FM; -.
DR BRENDA; 3.4.22.53; 2681.
DR EvolutionaryTrace; P17655; -.
DR GeneWiki; CAPN2; -.
DR GenomeRNAi; 824; -.
DR NextBio; 3374; -.
DR PRO; PR:P17655; -.
DR ArrayExpress; P17655; -.
DR Bgee; P17655; -.
DR CleanEx; HS_CAPN2; -.
DR Genevestigator; P17655; -.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0001824; P:blastocyst development; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
DR GO; GO:0016540; P:protein autoprocessing; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR022682; Calpain_domain_III.
DR InterPro; IPR022683; Calpain_III.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
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; 3.
DR SUPFAM; SSF49758; SSF49758; 1.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Calcium;
KW Cell membrane; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Membrane; Metal-binding;
KW Polymorphism; Protease; Reference proteome; Repeat; Thiol protease.
FT INIT_MET 1 1 Removed.
FT PROPEP 2 19 Anchors to the small subunit (Potential).
FT /FTId=PRO_0000026487.
FT CHAIN 20 700 Calpain-2 catalytic subunit.
FT /FTId=PRO_0000026488.
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.
FT CA_BIND 615 626 2.
FT REGION 345 514 Domain III.
FT REGION 515 529 Linker.
FT REGION 530 700 Domain IV.
FT ACT_SITE 105 105 By similarity.
FT ACT_SITE 262 262 By similarity.
FT ACT_SITE 286 286 By similarity.
FT METAL 89 89 Calcium 3; via carbonyl oxygen (By
FT similarity).
FT METAL 91 91 Calcium 3; via carbonyl oxygen (By
FT similarity).
FT METAL 96 96 Calcium 3 (By similarity).
FT METAL 175 175 Calcium 3 (By similarity).
FT METAL 229 229 Calcium 2 (By similarity).
FT METAL 230 230 Calcium 2 (By similarity).
FT METAL 292 292 Calcium 4 (By similarity).
FT METAL 299 299 Calcium 4 (By similarity).
FT METAL 323 323 Calcium 4; via carbonyl oxygen (By
FT similarity).
FT METAL 542 542 Calcium 5; via carbonyl oxygen (By
FT similarity).
FT METAL 545 545 Calcium 5 (By similarity).
FT METAL 547 547 Calcium 5; via carbonyl oxygen (By
FT similarity).
FT METAL 552 552 Calcium 5 (By similarity).
FT METAL 585 585 Calcium 6 (By similarity).
FT METAL 587 587 Calcium 6 (By similarity).
FT METAL 589 589 Calcium 6; via carbonyl oxygen (By
FT similarity).
FT METAL 591 591 Calcium 6; via carbonyl oxygen (By
FT similarity).
FT METAL 596 596 Calcium 6 (By similarity).
FT METAL 615 615 Calcium 7 (By similarity).
FT METAL 617 617 Calcium 7 (By similarity).
FT METAL 619 619 Calcium 7; via carbonyl oxygen (By
FT similarity).
FT METAL 621 621 Calcium 7; via carbonyl oxygen (By
FT similarity).
FT METAL 626 626 Calcium 7 (By similarity).
FT METAL 658 658 Calcium 1 (By similarity).
FT METAL 661 661 Calcium 1 (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 78 Missing (in isoform 2).
FT /FTId=VSP_043027.
FT VAR_SEQ 79 79 T -> M (in isoform 2).
FT /FTId=VSP_043028.
FT VARIANT 22 22 D -> E (in dbSNP:rs25655).
FT /FTId=VAR_014435.
FT VARIANT 68 68 S -> G (in dbSNP:rs2230083).
FT /FTId=VAR_021404.
FT VARIANT 476 476 K -> R (in dbSNP:rs9804140).
FT /FTId=VAR_021405.
FT VARIANT 521 521 E -> Q (in dbSNP:rs28370127).
FT /FTId=VAR_021406.
FT VARIANT 568 568 K -> Q (in dbSNP:rs17599).
FT /FTId=VAR_014436.
FT VARIANT 677 677 K -> Q (in dbSNP:rs2230082).
FT /FTId=VAR_021407.
FT CONFLICT 73 74 IE -> MR (in Ref. 1; AAA35645).
FT CONFLICT 256 256 Q -> K (in Ref. 2; AAF99682).
FT CONFLICT 300 300 N -> S (in Ref. 2; AAF99682).
FT CONFLICT 534 534 F -> V (in Ref. 1; AAA35645 and 2;
FT AAF99682).
FT HELIX 4 16
FT TURN 17 19
FT HELIX 27 29
FT HELIX 32 42
FT STRAND 49 51
FT HELIX 55 58
FT STRAND 60 68
FT STRAND 74 76
FT HELIX 78 81
FT STRAND 82 84
FT HELIX 94 96
FT STRAND 97 99
FT HELIX 105 115
FT HELIX 118 124
FT STRAND 131 134
FT STRAND 136 144
FT STRAND 146 155
FT STRAND 158 161
FT STRAND 164 167
FT STRAND 169 175
FT HELIX 177 189
FT STRAND 190 192
FT HELIX 193 195
FT STRAND 196 199
FT TURN 204 206
FT HELIX 207 209
FT STRAND 212 216
FT HELIX 224 233
FT STRAND 237 241
FT HELIX 247 249
FT STRAND 259 261
FT STRAND 264 274
FT STRAND 277 285
FT STRAND 294 297
FT STRAND 299 301
FT HELIX 302 306
FT HELIX 309 315
FT STRAND 321 327
FT HELIX 328 334
FT STRAND 336 341
FT HELIX 344 346
FT STRAND 347 349
FT STRAND 363 365
FT TURN 367 370
FT TURN 378 380
FT HELIX 381 383
FT STRAND 388 390
FT STRAND 400 402
FT STRAND 406 413
FT STRAND 420 425
FT STRAND 429 435
FT TURN 442 444
FT HELIX 450 455
FT STRAND 459 461
FT STRAND 466 471
FT STRAND 474 476
FT STRAND 479 492
FT STRAND 495 505
FT STRAND 507 509
FT STRAND 527 530
FT HELIX 533 541
FT STRAND 542 546
FT HELIX 550 560
FT TURN 561 564
FT HELIX 574 582
FT STRAND 586 588
FT STRAND 590 592
FT HELIX 595 612
FT STRAND 622 624
FT HELIX 627 630
FT TURN 631 635
FT HELIX 640 650
FT STRAND 655 657
FT HELIX 659 679
FT STRAND 687 690
FT HELIX 691 698
SQ SEQUENCE 700 AA; 79995 MW; 8CF8294351A024E3 CRC64;
MAGIAAKLAK DREAAEGLGS HDRAIKYLNQ DYEALRNECL EAGTLFQDPS FPAIPSALGF
KELGPYSSKT RGIEWKRPTE ICADPQFIIG GATRTDICQG ALGDCWLLAA IASLTLNEEI
LARVVPLNQS FQENYAGIFH FQFWQYGEWV EVVVDDRLPT KDGELLFVHS AEGSEFWSAL
LEKAYAKING CYEALSGGAT TEGFEDFTGG IAEWYELKKP PPNLFKIIQK ALQKGSLLGC
SIDITSAADS EAITFQKLVK GHAYSVTGAE EVESNGSLQK LIRIRNPWGE VEWTGRWNDN
CPSWNTIDPE ERERLTRRHE DGEFWMSFSD FLRHYSRLEI CNLTPDTLTS DTYKKWKLTK
MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDEED GESGCTFLVG LIQKHRRRQR
KMGEDMHTIG FGIYEVPEEL SGQTNIHLSK NFFLTNRARE RSDTFINLRE VLNRFKLPPG
EYILVPSTFE PNKDGDFCIR VFSEKKADYQ AVDDEIEANL EEFDISEDDI DDGFRRLFAQ
LAGEDAEISA FELQTILRRV LAKRQDIKSD GFSIETCKIM VDMLDSDGSG KLGLKEFYIL
WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKMPC QLHQVIVARF ADDQLIIDFD
NFVRCLVRLE TLFKIFKQLD PENTGTIELD LISWLCFSVL
//
ID CAN2_HUMAN Reviewed; 700 AA.
AC P17655; A6NDG7; B7ZA96; E7ES58; Q16738; Q6PJT3; Q8WU26; Q9HBB1;
read moreDT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 6.
DT 22-JAN-2014, entry version 174.
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 large polypeptide L2;
DE AltName: Full=Calpain-2 large subunit;
DE AltName: Full=Millimolar-calpain;
DE Short=M-calpain;
DE Flags: Precursor;
GN Name=CAPN2; Synonyms=CANPL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLU-22.
RX PubMed=2852952; DOI=10.1021/bi00421a022;
RA Imajoh S., Aoki K., Ohno S., Emori Y., Kawasaki H., Sugihara H.,
RA Suzuki K.;
RT "Molecular cloning of the cDNA for the large subunit of the high-Ca2+-
RT requiring form of human Ca2+-activated neutral protease.";
RL Biochemistry 27:8122-8128(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLU-22.
RC TISSUE=Astrocytoma;
RX PubMed=10944468; DOI=10.1006/bbrc.2000.3282;
RA Ye Z., Connor J.R.;
RT "cDNA cloning by amplification of circularized first strand cDNAs
RT reveals non-IRE-regulated iron-responsive mRNAs.";
RL Biochem. Biophys. Res. Commun. 275:223-227(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-22; GLY-68;
RP ARG-476; GLN-521; GLN-568 AND GLN-677.
RG NIEHS SNPs program;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP GLU-22.
RC TISSUE=Pancreas, Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79, AND VARIANTS GLU-22 AND
RP GLY-68.
RC TISSUE=Lymph node;
RX PubMed=2539381;
RA Hata A., Ohno S., Akita Y., Suzuki K.;
RT "Tandemly reiterated negative enhancer-like elements regulate
RT transcription of a human gene for the large subunit of calcium-
RT dependent protease.";
RL J. Biol. Chem. 264:6404-6411(1989).
RN [8]
RP PROTEIN SEQUENCE OF 2-12.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=10639123; DOI=10.1073/pnas.97.2.588;
RA Strobl S., Fernandez-Catalan C., Braun M., Huber R., Masumoto H.,
RA Nakagawa K., Irie A., Sorimachi H., Bourenkow G., Bartunik H.,
RA Suzuki K., Bode W.;
RT "The crystal structure of calcium-free human m-calpain suggests an
RT electrostatic switch mechanism for activation by calcium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:588-592(2000).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-22, AND MASS SPECTROMETRY.
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which
CC catalyze limited proteolysis of substrates involved in
CC cytoskeletal remodeling and signal transduction.
CC -!- CATALYTIC ACTIVITY: Broad endopeptidase specificity.
CC -!- COFACTOR: Binds 7 calcium ions (By similarity).
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 -!- INTERACTION:
CC P04632:CAPNS1; NbExp=3; IntAct=EBI-1028956, EBI-711828;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocates
CC to the plasma membrane upon Ca(2+) binding.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P17655-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P17655-2; Sequence=VSP_043027, VSP_043028;
CC Note=No experimental confirmation available;
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=AAH07686.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=AAH11828.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/capn2/";
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DR EMBL; M23254; AAA35645.1; -; mRNA.
DR EMBL; AF261089; AAF99682.1; -; mRNA.
DR EMBL; AK316211; BAH14582.1; -; mRNA.
DR EMBL; AY835586; AAV80421.1; -; Genomic_DNA.
DR EMBL; AC096542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007686; AAH07686.1; ALT_SEQ; mRNA.
DR EMBL; BC011828; AAH11828.1; ALT_SEQ; mRNA.
DR EMBL; BC021303; AAH21303.1; -; mRNA.
DR EMBL; J04700; AAA52760.1; -; Genomic_DNA.
DR PIR; S10590; CIHUH2.
DR RefSeq; NP_001139540.1; NM_001146068.1.
DR RefSeq; NP_001739.2; NM_001748.4.
DR UniGene; Hs.350899; -.
DR PDB; 1KFU; X-ray; 2.50 A; L=2-700.
DR PDB; 1KFX; X-ray; 3.15 A; L=2-700.
DR PDB; 2NQA; X-ray; 2.20 A; A/B=26-346.
DR PDBsum; 1KFU; -.
DR PDBsum; 1KFX; -.
DR PDBsum; 2NQA; -.
DR ProteinModelPortal; P17655; -.
DR SMR; P17655; 2-700.
DR IntAct; P17655; 5.
DR MINT; MINT-120195; -.
DR STRING; 9606.ENSP00000295006; -.
DR BindingDB; P17655; -.
DR ChEMBL; CHEMBL2382; -.
DR MEROPS; C02.002; -.
DR PhosphoSite; P17655; -.
DR DMDM; 60416356; -.
DR PaxDb; P17655; -.
DR PeptideAtlas; P17655; -.
DR PRIDE; P17655; -.
DR DNASU; 824; -.
DR Ensembl; ENST00000295006; ENSP00000295006; ENSG00000162909.
DR Ensembl; ENST00000433674; ENSP00000413158; ENSG00000162909.
DR GeneID; 824; -.
DR KEGG; hsa:824; -.
DR UCSC; uc001hob.4; human.
DR CTD; 824; -.
DR GeneCards; GC01P223890; -.
DR HGNC; HGNC:1479; CAPN2.
DR HPA; HPA024470; -.
DR MIM; 114230; gene.
DR neXtProt; NX_P17655; -.
DR PharmGKB; PA26060; -.
DR eggNOG; NOG327523; -.
DR HOVERGEN; HBG012645; -.
DR InParanoid; P17655; -.
DR KO; K03853; -.
DR OMA; DTYKKWK; -.
DR OrthoDB; EOG7RV9FM; -.
DR BRENDA; 3.4.22.53; 2681.
DR EvolutionaryTrace; P17655; -.
DR GeneWiki; CAPN2; -.
DR GenomeRNAi; 824; -.
DR NextBio; 3374; -.
DR PRO; PR:P17655; -.
DR ArrayExpress; P17655; -.
DR Bgee; P17655; -.
DR CleanEx; HS_CAPN2; -.
DR Genevestigator; P17655; -.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0001824; P:blastocyst development; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
DR GO; GO:0016540; P:protein autoprocessing; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR022682; Calpain_domain_III.
DR InterPro; IPR022683; Calpain_III.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
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; 3.
DR SUPFAM; SSF49758; SSF49758; 1.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Calcium;
KW Cell membrane; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Membrane; Metal-binding;
KW Polymorphism; Protease; Reference proteome; Repeat; Thiol protease.
FT INIT_MET 1 1 Removed.
FT PROPEP 2 19 Anchors to the small subunit (Potential).
FT /FTId=PRO_0000026487.
FT CHAIN 20 700 Calpain-2 catalytic subunit.
FT /FTId=PRO_0000026488.
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.
FT CA_BIND 615 626 2.
FT REGION 345 514 Domain III.
FT REGION 515 529 Linker.
FT REGION 530 700 Domain IV.
FT ACT_SITE 105 105 By similarity.
FT ACT_SITE 262 262 By similarity.
FT ACT_SITE 286 286 By similarity.
FT METAL 89 89 Calcium 3; via carbonyl oxygen (By
FT similarity).
FT METAL 91 91 Calcium 3; via carbonyl oxygen (By
FT similarity).
FT METAL 96 96 Calcium 3 (By similarity).
FT METAL 175 175 Calcium 3 (By similarity).
FT METAL 229 229 Calcium 2 (By similarity).
FT METAL 230 230 Calcium 2 (By similarity).
FT METAL 292 292 Calcium 4 (By similarity).
FT METAL 299 299 Calcium 4 (By similarity).
FT METAL 323 323 Calcium 4; via carbonyl oxygen (By
FT similarity).
FT METAL 542 542 Calcium 5; via carbonyl oxygen (By
FT similarity).
FT METAL 545 545 Calcium 5 (By similarity).
FT METAL 547 547 Calcium 5; via carbonyl oxygen (By
FT similarity).
FT METAL 552 552 Calcium 5 (By similarity).
FT METAL 585 585 Calcium 6 (By similarity).
FT METAL 587 587 Calcium 6 (By similarity).
FT METAL 589 589 Calcium 6; via carbonyl oxygen (By
FT similarity).
FT METAL 591 591 Calcium 6; via carbonyl oxygen (By
FT similarity).
FT METAL 596 596 Calcium 6 (By similarity).
FT METAL 615 615 Calcium 7 (By similarity).
FT METAL 617 617 Calcium 7 (By similarity).
FT METAL 619 619 Calcium 7; via carbonyl oxygen (By
FT similarity).
FT METAL 621 621 Calcium 7; via carbonyl oxygen (By
FT similarity).
FT METAL 626 626 Calcium 7 (By similarity).
FT METAL 658 658 Calcium 1 (By similarity).
FT METAL 661 661 Calcium 1 (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 78 Missing (in isoform 2).
FT /FTId=VSP_043027.
FT VAR_SEQ 79 79 T -> M (in isoform 2).
FT /FTId=VSP_043028.
FT VARIANT 22 22 D -> E (in dbSNP:rs25655).
FT /FTId=VAR_014435.
FT VARIANT 68 68 S -> G (in dbSNP:rs2230083).
FT /FTId=VAR_021404.
FT VARIANT 476 476 K -> R (in dbSNP:rs9804140).
FT /FTId=VAR_021405.
FT VARIANT 521 521 E -> Q (in dbSNP:rs28370127).
FT /FTId=VAR_021406.
FT VARIANT 568 568 K -> Q (in dbSNP:rs17599).
FT /FTId=VAR_014436.
FT VARIANT 677 677 K -> Q (in dbSNP:rs2230082).
FT /FTId=VAR_021407.
FT CONFLICT 73 74 IE -> MR (in Ref. 1; AAA35645).
FT CONFLICT 256 256 Q -> K (in Ref. 2; AAF99682).
FT CONFLICT 300 300 N -> S (in Ref. 2; AAF99682).
FT CONFLICT 534 534 F -> V (in Ref. 1; AAA35645 and 2;
FT AAF99682).
FT HELIX 4 16
FT TURN 17 19
FT HELIX 27 29
FT HELIX 32 42
FT STRAND 49 51
FT HELIX 55 58
FT STRAND 60 68
FT STRAND 74 76
FT HELIX 78 81
FT STRAND 82 84
FT HELIX 94 96
FT STRAND 97 99
FT HELIX 105 115
FT HELIX 118 124
FT STRAND 131 134
FT STRAND 136 144
FT STRAND 146 155
FT STRAND 158 161
FT STRAND 164 167
FT STRAND 169 175
FT HELIX 177 189
FT STRAND 190 192
FT HELIX 193 195
FT STRAND 196 199
FT TURN 204 206
FT HELIX 207 209
FT STRAND 212 216
FT HELIX 224 233
FT STRAND 237 241
FT HELIX 247 249
FT STRAND 259 261
FT STRAND 264 274
FT STRAND 277 285
FT STRAND 294 297
FT STRAND 299 301
FT HELIX 302 306
FT HELIX 309 315
FT STRAND 321 327
FT HELIX 328 334
FT STRAND 336 341
FT HELIX 344 346
FT STRAND 347 349
FT STRAND 363 365
FT TURN 367 370
FT TURN 378 380
FT HELIX 381 383
FT STRAND 388 390
FT STRAND 400 402
FT STRAND 406 413
FT STRAND 420 425
FT STRAND 429 435
FT TURN 442 444
FT HELIX 450 455
FT STRAND 459 461
FT STRAND 466 471
FT STRAND 474 476
FT STRAND 479 492
FT STRAND 495 505
FT STRAND 507 509
FT STRAND 527 530
FT HELIX 533 541
FT STRAND 542 546
FT HELIX 550 560
FT TURN 561 564
FT HELIX 574 582
FT STRAND 586 588
FT STRAND 590 592
FT HELIX 595 612
FT STRAND 622 624
FT HELIX 627 630
FT TURN 631 635
FT HELIX 640 650
FT STRAND 655 657
FT HELIX 659 679
FT STRAND 687 690
FT HELIX 691 698
SQ SEQUENCE 700 AA; 79995 MW; 8CF8294351A024E3 CRC64;
MAGIAAKLAK DREAAEGLGS HDRAIKYLNQ DYEALRNECL EAGTLFQDPS FPAIPSALGF
KELGPYSSKT RGIEWKRPTE ICADPQFIIG GATRTDICQG ALGDCWLLAA IASLTLNEEI
LARVVPLNQS FQENYAGIFH FQFWQYGEWV EVVVDDRLPT KDGELLFVHS AEGSEFWSAL
LEKAYAKING CYEALSGGAT TEGFEDFTGG IAEWYELKKP PPNLFKIIQK ALQKGSLLGC
SIDITSAADS EAITFQKLVK GHAYSVTGAE EVESNGSLQK LIRIRNPWGE VEWTGRWNDN
CPSWNTIDPE ERERLTRRHE DGEFWMSFSD FLRHYSRLEI CNLTPDTLTS DTYKKWKLTK
MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDEED GESGCTFLVG LIQKHRRRQR
KMGEDMHTIG FGIYEVPEEL SGQTNIHLSK NFFLTNRARE RSDTFINLRE VLNRFKLPPG
EYILVPSTFE PNKDGDFCIR VFSEKKADYQ AVDDEIEANL EEFDISEDDI DDGFRRLFAQ
LAGEDAEISA FELQTILRRV LAKRQDIKSD GFSIETCKIM VDMLDSDGSG KLGLKEFYIL
WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKMPC QLHQVIVARF ADDQLIIDFD
NFVRCLVRLE TLFKIFKQLD PENTGTIELD LISWLCFSVL
//
MIM
114230
*RECORD*
*FIELD* NO
114230
*FIELD* TI
*114230 CALPAIN 2; CAPN2
;;CALPAIN, LARGE POLYPEPTIDE L2;;
CALPAIN II, LARGE SUBUNIT; CANPL2;;
read moreCALCIUM-ACTIVATED NEUTRAL PROTEASE 2, CATALYTIC SUBUNIT; CANP2
*FIELD* TX
DESCRIPTION
The calpains, or calcium-activated neutral proteases (EC 3.4.22.17), are
nonlysosomal intracellular cysteine proteases. The mammalian calpains
include 2 ubiquitous isoforms, calpain I (mu-calpain) and calpain II
(m-calpain), 2 stomach-specific proteins, and CAPN3 (114240), which is
muscle-specific. Calpain I and calpain II are heterodimers with distinct
large subunits, encoded by the CAPN1 (114220) and CAPN2 genes,
respectively, associated with a common small subunit (CAPNS1; 114170).
CLONING
By screening a human skeletal muscle cDNA library using the large
subunits of rabbit and chicken CANP as probes, Imajoh et al. (1988)
cloned CAPN2. The deduced protein contains 700 amino acids. N-terminal
sequencing of CAPN2 purified from human liver indicated that the
N-terminal methionine is removed, resulting in a mature 699-amino acid
subunit with a calculated molecular mass of 79.9 kD. Comparison of the
CAPN2 sequence with CAPN1 and the chicken CANP large subunit showed
conservation of the 4-domain structure and of the active-site cysteine
(cys140) in the protease domain (domain II) and the 4 putative
Ca(2+)-binding sites in domain IV. Domain III, presumably a regulatory
domain, is also highly conserved between the 3 proteins, but domain I is
not.
GENE FUNCTION
By quantitative RT-PCR, Ueyama et al. (1998) found that expression of
calpain-1 and calpain-2 mRNA was significantly increased in muscle
biopsy samples derived from 5 men with progressive muscular dystrophy
(e.g., DMD; 310200) and 2 men and 3 women with amyotrophic lateral
sclerosis (ALS; 105400) compared with controls.
Morford et al. (2002) found that calpain-2, but not calpain-1,
associated with membrane lipid rafts on human peripheral blood T cells
and Jurkat T cells. Membrane raft-associated calpain activity in human T
cells was enhanced with exogenous calcium. Calpain cleaved the
cytoskeletal-associated protein talin (TLN1; 186745) during the first 30
minutes after cell stimulation. Morford et al. (2002) hypothesized that
lipid raft-associated calpain-2 could function early in T-cell receptor
signaling to facilitate immune synapse formation through cytoskeletal
remodeling mechanisms.
Using confocal microscopy and isopycnic density centrifugation, Hood et
al. (2003) found that calpain-1, calpain-2, the small regulatory calpain
subunit, and calpastatin (CAST; 114090) associated with the endoplasmic
reticulum and Golgi apparatus of human fibroblasts and glioblastoma
cells. The association between these proteins and the endoplasmic
reticulum and Golgi apparatus increased in the glioblastoma cell line
following laminin (see LAMA1; 150320) stimulation. Calpain-2 also
colocalized with inositol 4,5-bisphosphate and with membrane lipid
rafts.
Adamec et al. (2002) investigated calpain-2 activation in a broad range
of neurodegenerative diseases using immunofluorescence imaging.
Activated calpain-2 was detected in all neurodegenerative diseases
examined, including Alzheimer disease (AD; 104300), Down syndrome
(190685), and Pick disease (172700), with the possible exception of
frontotemporal dementia with inclusions (see 600274). Activated
calpain-2 was detected in different cell types and colocalized with
different pathologic structures. In neurons and glial cells, calpain-2
primarily colocalized with hyperphosphorylated tau protein (MAPT;
157140). In brains with AD neurofibrillary changes, colocalization of
calpain-2 with phosphorylated tau was most extensive at transentorhinal
stages of neurofibrillary degeneration rather than at later limbic
stages. Aggregates of different proteins, such as huntingtin (HTT;
613004) and alpha-synuclein (SNCA; 163890), were negative for activated
calpain-2, indicating that the presence of pathologic inclusions was not
by itself the stimulus responsible for calpain-2 activation.
Using cell biologic, pharmacologic, and genetic methods,
Chandramohanadas et al. (2009) found that the apicomplexan parasites
Plasmodium falciparum and Toxoplasma gondii, the causative agents of
malaria and toxoplasmosis, respectively, used host cell calpains to
facilitate parasite egress. Immunodepletion and inhibition experiments
showed that calpain-1 was required for escape of P. falciparum from
human erythrocytes. Similarly, elimination of both calpain-1 and
calpain-2 via small interfering RNA against the common regulatory
subunit CAPNS1 in human osteosarcoma cells or deletion of Capns1 in
mouse embryonic fibroblasts blocked egress of T. gondii.
Chandramohanadas et al. (2009) concluded that P. falciparum and T.
gondii both exploit host cell calpains to facilitate escape from
intracellular parasitophorous vacuoles and/or the host plasma membrane,
a process required for parasite proliferation.
BIOCHEMICAL FEATURES
- Crystal Structure
Moldoveanu et al. (2008) reported the 3.0-angstrom crystal structure of
calcium-bound m-calpain (calpain II) in complex with the first
calpastatin (114090) repeat, both from rat, revealing the mechanism of
exclusive specificity. The structure highlighted the complexity of
calpain activation by calcium, illustrating key residues in a peripheral
domain that serve to stabilize the protease core on calcium binding.
Fully activated calpain binds 10 Ca(2+) atoms, resulting in several
conformational changes allowing recognition by calpastatin. Calpain
inhibition is mediated by the intimate contact with 3 critical regions
of calpastatin. Two regions target the penta-EF-hand domains of calpain,
and the third occupies the substrate-binding cleft, projecting a loop
around the active site thiol to evade proteolysis.
Hanna et al. (2008) reported the 2.4-angstrom resolution crystal
structure of the calcium-bound calpain II heterodimer bound by 1 of the
4 inhibitory domains of calpastatin. They observed that calpastatin
inhibits calpain by occupying both sides of the active site cleft.
Although the inhibitor passes through the active site cleft, it escapes
cleavage in a novel manner by looping out and around the active site
cysteine. The inhibitory domain of calpastatin recognizes multiple lower
affinity sites present only in the calcium-bound form of the enzyme,
resulting in an interaction that is tight, specific, and
calcium-dependent. Hanna et al. (2008) concluded that this crystal
structure, and that of the related complex described by Moldoveanu et
al. (2008), also revealed the conformational changes that calpain
undergoes on binding calcium, which include opening of the active site
cleft and movement of the domains relative to each other to produce a
more compact enzyme.
MAPPING
By a combination of spot blot hybridization with sorted chromosomes and
Southern hybridization with human-mouse cell hybrid DNAs, Ohno et al.
(1989, 1990) mapped the CANPL2 gene to chromosome 1.
*FIELD* RF
1. Adamec, E.; Mohan, P.; Vonsattel, J. P.; Nixon, R. A.: Calpain
activation in neurodegenerative diseases: confocal immunofluorescence
study with antibodies specifically recognizing the active form of
calpain 2. Acta Neuropath. 104: 92-104, 2002.
2. Chandramohanadas, R.; Davis, P. H.; Beiting, D. P.; Harbut, M.
B.; Darling, C.; Velmourougane, G.; Lee, M. Y.; Greer, P. A.; Roos,
D. S.; Greenbaum, D. C.: Apicomplexan parasites co-opt host calpains
to facilitate their escape from infected cells. Science 324: 794-797,
2009.
3. 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.
4. Hood, J. L.; Logan, B. B.; Sinai, A. P.; Brooks, W. H.; Roszman,
T. L.: Association of the calpain/calpastatin network with subcellular
organelles. Biochem. Biophys. Res. Commun. 310: 1200-1212, 2003.
5. Imajoh, S.; Aoki, K.; Ohno, S.; Emori, Y.; Kawasaki, H.; Sugihara,
H.; Suzuki, K.: Molecular cloning of the cDNA for the large subunit
of the high Ca(2+)-requiring form of human Ca(2+)-activated neutral
protease. Biochemistry 27: 8122-8128, 1988.
6. 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.
7. Morford, L. A.; Forrest, K.; Logan, B.; Overstreet, L. K.; Goebel,
J.; Brooks, W. H.; Roszman, T. L.: Calpain II colocalizes with detergent-insoluble
rafts on human and Jurkat T-cells. Biochem. Biophys. Res. Commun. 295:
540-546, 2002.
8. Ohno, S.; Minoshima, S.; Kudoh, J.; Fukuyama, R.; Ohmi-Imajoh,
S.; Suzuki, K.; Shimizu, Y.; Shimizu, N.: Four genes for the calpain
family locate on four distinct human chromosomes. Cytogenet. Cell
Genet. 51: 1054-1055, 1989.
9. Ohno, S.; Minoshima, S.; Kudoh, J.; Fukuyama, R.; Shimizu, Y.;
Ohmi-Imajoh, S.; Shimizu, N.; Suzuki, K.: Four genes for the calpain
family locate on four distinct human chromosomes. Cytogenet. Cell
Genet. 53: 225-229, 1990.
10. Ueyama, H.; Kumamoto, T.; Fujimoto, S.; Murakami, T.; Tsuda, T.
: Expression of three calpain isoform genes in human skeletal muscles. J.
Neurol. Sci. 155: 163-169, 1998.
*FIELD* CN
Paul J. Converse - updated: 7/7/2009
Ada Hamosh - updated: 3/11/2009
Patricia A. Hartz - updated: 11/22/2005
*FIELD* CD
Victor A. McKusick: 6/5/1989
*FIELD* ED
carol: 09/15/2009
mgross: 7/7/2009
alopez: 3/16/2009
terry: 3/11/2009
mgross: 12/2/2005
terry: 11/22/2005
psherman: 4/10/2000
carol: 8/18/1998
carol: 4/7/1992
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
root: 9/23/1989
root: 6/5/1989
*RECORD*
*FIELD* NO
114230
*FIELD* TI
*114230 CALPAIN 2; CAPN2
;;CALPAIN, LARGE POLYPEPTIDE L2;;
CALPAIN II, LARGE SUBUNIT; CANPL2;;
read moreCALCIUM-ACTIVATED NEUTRAL PROTEASE 2, CATALYTIC SUBUNIT; CANP2
*FIELD* TX
DESCRIPTION
The calpains, or calcium-activated neutral proteases (EC 3.4.22.17), are
nonlysosomal intracellular cysteine proteases. The mammalian calpains
include 2 ubiquitous isoforms, calpain I (mu-calpain) and calpain II
(m-calpain), 2 stomach-specific proteins, and CAPN3 (114240), which is
muscle-specific. Calpain I and calpain II are heterodimers with distinct
large subunits, encoded by the CAPN1 (114220) and CAPN2 genes,
respectively, associated with a common small subunit (CAPNS1; 114170).
CLONING
By screening a human skeletal muscle cDNA library using the large
subunits of rabbit and chicken CANP as probes, Imajoh et al. (1988)
cloned CAPN2. The deduced protein contains 700 amino acids. N-terminal
sequencing of CAPN2 purified from human liver indicated that the
N-terminal methionine is removed, resulting in a mature 699-amino acid
subunit with a calculated molecular mass of 79.9 kD. Comparison of the
CAPN2 sequence with CAPN1 and the chicken CANP large subunit showed
conservation of the 4-domain structure and of the active-site cysteine
(cys140) in the protease domain (domain II) and the 4 putative
Ca(2+)-binding sites in domain IV. Domain III, presumably a regulatory
domain, is also highly conserved between the 3 proteins, but domain I is
not.
GENE FUNCTION
By quantitative RT-PCR, Ueyama et al. (1998) found that expression of
calpain-1 and calpain-2 mRNA was significantly increased in muscle
biopsy samples derived from 5 men with progressive muscular dystrophy
(e.g., DMD; 310200) and 2 men and 3 women with amyotrophic lateral
sclerosis (ALS; 105400) compared with controls.
Morford et al. (2002) found that calpain-2, but not calpain-1,
associated with membrane lipid rafts on human peripheral blood T cells
and Jurkat T cells. Membrane raft-associated calpain activity in human T
cells was enhanced with exogenous calcium. Calpain cleaved the
cytoskeletal-associated protein talin (TLN1; 186745) during the first 30
minutes after cell stimulation. Morford et al. (2002) hypothesized that
lipid raft-associated calpain-2 could function early in T-cell receptor
signaling to facilitate immune synapse formation through cytoskeletal
remodeling mechanisms.
Using confocal microscopy and isopycnic density centrifugation, Hood et
al. (2003) found that calpain-1, calpain-2, the small regulatory calpain
subunit, and calpastatin (CAST; 114090) associated with the endoplasmic
reticulum and Golgi apparatus of human fibroblasts and glioblastoma
cells. The association between these proteins and the endoplasmic
reticulum and Golgi apparatus increased in the glioblastoma cell line
following laminin (see LAMA1; 150320) stimulation. Calpain-2 also
colocalized with inositol 4,5-bisphosphate and with membrane lipid
rafts.
Adamec et al. (2002) investigated calpain-2 activation in a broad range
of neurodegenerative diseases using immunofluorescence imaging.
Activated calpain-2 was detected in all neurodegenerative diseases
examined, including Alzheimer disease (AD; 104300), Down syndrome
(190685), and Pick disease (172700), with the possible exception of
frontotemporal dementia with inclusions (see 600274). Activated
calpain-2 was detected in different cell types and colocalized with
different pathologic structures. In neurons and glial cells, calpain-2
primarily colocalized with hyperphosphorylated tau protein (MAPT;
157140). In brains with AD neurofibrillary changes, colocalization of
calpain-2 with phosphorylated tau was most extensive at transentorhinal
stages of neurofibrillary degeneration rather than at later limbic
stages. Aggregates of different proteins, such as huntingtin (HTT;
613004) and alpha-synuclein (SNCA; 163890), were negative for activated
calpain-2, indicating that the presence of pathologic inclusions was not
by itself the stimulus responsible for calpain-2 activation.
Using cell biologic, pharmacologic, and genetic methods,
Chandramohanadas et al. (2009) found that the apicomplexan parasites
Plasmodium falciparum and Toxoplasma gondii, the causative agents of
malaria and toxoplasmosis, respectively, used host cell calpains to
facilitate parasite egress. Immunodepletion and inhibition experiments
showed that calpain-1 was required for escape of P. falciparum from
human erythrocytes. Similarly, elimination of both calpain-1 and
calpain-2 via small interfering RNA against the common regulatory
subunit CAPNS1 in human osteosarcoma cells or deletion of Capns1 in
mouse embryonic fibroblasts blocked egress of T. gondii.
Chandramohanadas et al. (2009) concluded that P. falciparum and T.
gondii both exploit host cell calpains to facilitate escape from
intracellular parasitophorous vacuoles and/or the host plasma membrane,
a process required for parasite proliferation.
BIOCHEMICAL FEATURES
- Crystal Structure
Moldoveanu et al. (2008) reported the 3.0-angstrom crystal structure of
calcium-bound m-calpain (calpain II) in complex with the first
calpastatin (114090) repeat, both from rat, revealing the mechanism of
exclusive specificity. The structure highlighted the complexity of
calpain activation by calcium, illustrating key residues in a peripheral
domain that serve to stabilize the protease core on calcium binding.
Fully activated calpain binds 10 Ca(2+) atoms, resulting in several
conformational changes allowing recognition by calpastatin. Calpain
inhibition is mediated by the intimate contact with 3 critical regions
of calpastatin. Two regions target the penta-EF-hand domains of calpain,
and the third occupies the substrate-binding cleft, projecting a loop
around the active site thiol to evade proteolysis.
Hanna et al. (2008) reported the 2.4-angstrom resolution crystal
structure of the calcium-bound calpain II heterodimer bound by 1 of the
4 inhibitory domains of calpastatin. They observed that calpastatin
inhibits calpain by occupying both sides of the active site cleft.
Although the inhibitor passes through the active site cleft, it escapes
cleavage in a novel manner by looping out and around the active site
cysteine. The inhibitory domain of calpastatin recognizes multiple lower
affinity sites present only in the calcium-bound form of the enzyme,
resulting in an interaction that is tight, specific, and
calcium-dependent. Hanna et al. (2008) concluded that this crystal
structure, and that of the related complex described by Moldoveanu et
al. (2008), also revealed the conformational changes that calpain
undergoes on binding calcium, which include opening of the active site
cleft and movement of the domains relative to each other to produce a
more compact enzyme.
MAPPING
By a combination of spot blot hybridization with sorted chromosomes and
Southern hybridization with human-mouse cell hybrid DNAs, Ohno et al.
(1989, 1990) mapped the CANPL2 gene to chromosome 1.
*FIELD* RF
1. Adamec, E.; Mohan, P.; Vonsattel, J. P.; Nixon, R. A.: Calpain
activation in neurodegenerative diseases: confocal immunofluorescence
study with antibodies specifically recognizing the active form of
calpain 2. Acta Neuropath. 104: 92-104, 2002.
2. Chandramohanadas, R.; Davis, P. H.; Beiting, D. P.; Harbut, M.
B.; Darling, C.; Velmourougane, G.; Lee, M. Y.; Greer, P. A.; Roos,
D. S.; Greenbaum, D. C.: Apicomplexan parasites co-opt host calpains
to facilitate their escape from infected cells. Science 324: 794-797,
2009.
3. 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.
4. Hood, J. L.; Logan, B. B.; Sinai, A. P.; Brooks, W. H.; Roszman,
T. L.: Association of the calpain/calpastatin network with subcellular
organelles. Biochem. Biophys. Res. Commun. 310: 1200-1212, 2003.
5. Imajoh, S.; Aoki, K.; Ohno, S.; Emori, Y.; Kawasaki, H.; Sugihara,
H.; Suzuki, K.: Molecular cloning of the cDNA for the large subunit
of the high Ca(2+)-requiring form of human Ca(2+)-activated neutral
protease. Biochemistry 27: 8122-8128, 1988.
6. 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.
7. Morford, L. A.; Forrest, K.; Logan, B.; Overstreet, L. K.; Goebel,
J.; Brooks, W. H.; Roszman, T. L.: Calpain II colocalizes with detergent-insoluble
rafts on human and Jurkat T-cells. Biochem. Biophys. Res. Commun. 295:
540-546, 2002.
8. Ohno, S.; Minoshima, S.; Kudoh, J.; Fukuyama, R.; Ohmi-Imajoh,
S.; Suzuki, K.; Shimizu, Y.; Shimizu, N.: Four genes for the calpain
family locate on four distinct human chromosomes. Cytogenet. Cell
Genet. 51: 1054-1055, 1989.
9. Ohno, S.; Minoshima, S.; Kudoh, J.; Fukuyama, R.; Shimizu, Y.;
Ohmi-Imajoh, S.; Shimizu, N.; Suzuki, K.: Four genes for the calpain
family locate on four distinct human chromosomes. Cytogenet. Cell
Genet. 53: 225-229, 1990.
10. Ueyama, H.; Kumamoto, T.; Fujimoto, S.; Murakami, T.; Tsuda, T.
: Expression of three calpain isoform genes in human skeletal muscles. J.
Neurol. Sci. 155: 163-169, 1998.
*FIELD* CN
Paul J. Converse - updated: 7/7/2009
Ada Hamosh - updated: 3/11/2009
Patricia A. Hartz - updated: 11/22/2005
*FIELD* CD
Victor A. McKusick: 6/5/1989
*FIELD* ED
carol: 09/15/2009
mgross: 7/7/2009
alopez: 3/16/2009
terry: 3/11/2009
mgross: 12/2/2005
terry: 11/22/2005
psherman: 4/10/2000
carol: 8/18/1998
carol: 4/7/1992
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
root: 9/23/1989
root: 6/5/1989