CANX_CHICK
ID CANX_CHICK Reviewed; 705 AA.
AC P00789;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Calpain-1 catalytic subunit;
DE EC=3.4.22.52;
DE AltName: Full=Calcium-activated neutral proteinase;
DE Short=CANP;
DE AltName: Full=Calpain-1 large subunit;
DE AltName: Full=Mu/M-type;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6095110; DOI=10.1038/312566a0;
RA Ohno S., Emori Y., Imajoh S., Kawasaki H., Kisaragi M., Suzuki K.;
RT "Evolutionary origin of a calcium-dependent protease by fusion of genes for
RT a thiol protease and a calcium-binding protein?";
RL Nature 312:566-570(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3000828; DOI=10.1016/0014-5793(86)80094-1;
RA Emori Y., Ohno S., Tobita M., Suzuki K.;
RT "Gene structure of calcium-dependent protease retains the ancestral
RT organization of the calcium-binding protein gene.";
RL FEBS Lett. 194:249-252(1986).
RN [3]
RP CALCIUM-BINDING DATA.
RX PubMed=3038855; DOI=10.1093/oxfordjournals.jbchem.a121956;
RA Minami Y., Emori Y., Kawasaki H., Suzuki K.;
RT "E-F hand structure-domain of calcium-activated neutral protease (CANP) can
RT bind Ca2+ ions.";
RL J. Biochem. 101:889-895(1987).
RN [4]
RP CHARACTERIZATION.
RX PubMed=7742367; DOI=10.1016/0167-4781(95)00027-e;
RA Sorimachi H., Tsukahara T., Okada-Ban M., Sugita H., Ishiura S., Suzuki K.;
RT "Identification of a third ubiquitous calpain species -- chicken muscle
RT expresses four distinct calpains.";
RL Biochim. Biophys. Acta 1261:381-393(1995).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyze
CC limited proteolysis of substrates involved in cytoskeletal remodeling
CC and signal transduction.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad endopeptidase specificity.; EC=3.4.22.52;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 3 Ca(2+) ions.;
CC -!- ACTIVITY REGULATION: Activated by micromolar concentrations of calcium
CC and inhibited by calpastatin.
CC -!- SUBUNIT: Heterodimer of large (catalytic) and a small (regulatory)
CC subunit.
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: Ubiquitously expressed.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
CC -!- CAUTION: This protein was previously thought to be M-calpain but has
CC since been found to be an intermediate form between the M and Mu types.
CC {ECO:0000305}.
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DR EMBL; X01415; CAA25658.1; -; mRNA.
DR PIR; A00979; CICHH.
DR RefSeq; NP_990634.1; NM_205303.1.
DR RefSeq; XP_015139111.1; XM_015283625.1.
DR AlphaFoldDB; P00789; -.
DR SMR; P00789; -.
DR STRING; 9031.ENSGALP00000016538; -.
DR BindingDB; P00789; -.
DR ChEMBL; CHEMBL3147; -.
DR MEROPS; C02.003; -.
DR PaxDb; P00789; -.
DR Ensembl; ENSGALT00000075282; ENSGALP00000052109; ENSGALG00000010186.
DR GeneID; 396240; -.
DR KEGG; gga:396240; -.
DR CTD; 11131; -.
DR VEuPathDB; HostDB:geneid_396240; -.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000158672; -.
DR HOGENOM; CLU_010982_0_1_1; -.
DR InParanoid; P00789; -.
DR OMA; NFFKYKS; -.
DR OrthoDB; 704215at2759; -.
DR PhylomeDB; P00789; -.
DR TreeFam; TF314748; -.
DR BRENDA; 3.4.22.52; 1306.
DR PRO; PR:P00789; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000010186; Expressed in lung and 12 other tissues.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 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; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
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 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; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Cytoplasm; Hydrolase; Membrane; Metal-binding;
KW Protease; Reference proteome; Repeat; Thiol protease.
FT CHAIN 1..705
FT /note="Calpain-1 catalytic subunit"
FT /id="PRO_0000207701"
FT DOMAIN 48..347
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 530..565
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 606..641
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 671..705
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 348..517
FT /note="Domain III"
FT REGION 518..533
FT /note="Linker"
FT REGION 534..704
FT /note="Domain IV"
FT ACT_SITE 108
FT /evidence="ECO:0000250"
FT ACT_SITE 265
FT /evidence="ECO:0000250"
FT ACT_SITE 289
FT /evidence="ECO:0000250"
FT BINDING 549
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:3038855, ECO:0000305"
FT BINDING 551
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:3038855, ECO:0000305"
FT BINDING 556
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:3038855, ECO:0000305"
FT BINDING 589
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:3038855, ECO:0000305"
FT BINDING 591
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:3038855, ECO:0000305"
FT BINDING 593
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:3038855, ECO:0000305"
FT BINDING 595
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:3038855, ECO:0000305"
FT BINDING 600
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:3038855, ECO:0000305"
FT BINDING 619
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:3038855"
FT BINDING 621
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:3038855"
FT BINDING 623
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:3038855"
FT BINDING 625
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:3038855"
FT BINDING 630
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:3038855"
SQ SEQUENCE 705 AA; 80352 MW; ABCDDC56298E48AA CRC64;
MMPFGGIAAR LQRDRLRAEG VGEHNNAVKY LNQDYEALKQ ECIESGTLFR DPQFPAGPTA
LGFKELGPYS SKTRGVEWKR PSELVDDPQF IVGGATRTDI CQGALGDCWL LAAIGSLTLN
EELLHRVVPH GQSFQEDYAG IFHFQIWQFG EWVDVVVDDL LPTKDGELLF VHSAECTEFW
SALLEKAYAK LNGCYESLSG GSTTEGFEDF TGGVAEMYDL KRAPRNMGHI IRKALERGSL
LGCSIDITSA FDMEAVTFKK LVKGHAYSVT AFKDVNYRGQ QEQLIRIRNP WGQVEWTGAW
SDGSSEWDNI DPSDREELQL KMEDGEFWMS FRDFMREFSR LEICNLTPDA LTKDELSRWH
TQVFEGTWRR GSTAGGCRNN PATFWINPQF KIKLLEEDDD PGDDEVACSF LVALMQKHRR
RERRVGGDMH TIGFAVYEVP EEAQGSQNVH LKKDFFLRNQ SRARSETFIN LREVSNQIRL
PPGEYIVVPS TFEPHKEADF ILRVFTEKQS DTAELDEEIS ADLADEEEIT EDDIEDGFKN
MFQQLAGEDM EISVFELKTI LNRVIARHKD LKTDGFSLDS CRNMVNLMDK DGSARLGLVE
FQILWNKIRS WLTIFRQYDL DKSGTMSSYE MRMALESAGF KLNNKLHQVV VARYADAETG
VDFDNFVCCL VKLETMFRFF HSMDRDGTGT AVMNLAEWLL LTMCG
