ID B4DEU4_HUMAN Unreviewed; 266 AA.
AC B4DEU4;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 08-NOV-2023, entry version 59.
DE RecName: Full=Calpain-3 {ECO:0000256|RuleBase:RU367132};
DE EC=3.4.22.54 {ECO:0000256|RuleBase:RU367132};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG57205.1};
RN [1] {ECO:0000313|EMBL:BAG57205.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebellum {ECO:0000313|EMBL:BAG57205.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
CC {ECO:0000256|RuleBase:RU367132}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad endopeptidase activity.; EC=3.4.22.54;
CC Evidence={ECO:0000256|RuleBase:RU367132};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU367132}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367132}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623, ECO:0000256|RuleBase:RU367132}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00239}.
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DR EMBL; AK293792; BAG57205.1; -; mRNA.
DR AlphaFoldDB; B4DEU4; -.
DR MEROPS; C02.004; -.
DR PeptideAtlas; B4DEU4; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF329; CALPAIN-3; 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; SSF49758; Calpain large subunit, middle domain (domain III); 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
PE 2: Evidence at transcript level;
KW Calcium {ECO:0000256|RuleBase:RU367132};
KW Cytoplasm {ECO:0000256|RuleBase:RU367132};
KW Hydrolase {ECO:0000256|RuleBase:RU367132};
KW Metal-binding {ECO:0000256|RuleBase:RU367132};
KW Protease {ECO:0000256|RuleBase:RU367132};
KW Thiol protease {ECO:0000256|RuleBase:RU367132}.
FT DOMAIN 32..170
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT ACT_SITE 87
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1"
FT ACT_SITE 111
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1"
SQ SEQUENCE 266 AA; 30609 MW; 447E7C54F9162CCC CRC64;
MYKIMKKAIE RGSLMGCSID DGTNMTYGTS PSGLNMGELI ARMVRNMDNS LLQDSDLDPR
GSDERPTRTI IPVQYETRMA CGLVRGHAYS VTGLDEVPFK GEKVKLVRLR NPWGQVEWNG
SWSDRWKDWS FVDKDEKARL QHQVTEDGEF WMSYEDFIYH FTKLEICNLT ADALQSDKLQ
TWTVSVNEGR WVRGCSAGGC RNFPDTFWTN PQYRLKLLEE DDDPDDSEVI CSFLVALMQK
NRRKDRKLGA SLFTIGFAIY EVPKEV
//
