ID G3NNN5_GASAC Unreviewed; 713 AA.
AC G3NNN5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Calpain-3 {ECO:0000256|RuleBase:RU367132};
DE EC=3.4.22.54 {ECO:0000256|RuleBase:RU367132};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000006949.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000006949.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000006949.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; G3NNN5; -.
DR STRING; 69293.ENSGACP00000006949; -.
DR Ensembl; ENSGACT00000006967.1; ENSGACP00000006949.1; ENSGACG00000005212.1.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000156092; -.
DR InParanoid; G3NNN5; -.
DR OMA; RASCVAN; -.
DR TreeFam; TF314748; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000005212; Expressed in intestinal epithelial cell and 2 other cell types or tissues.
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 CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.10.238.10; EF-hand; 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; 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 PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF329; CALPAIN-3; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF13833; EF-hand_8; 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; Calpain large subunit, middle domain (domain III); 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU367132};
KW Cytoplasm {ECO:0000256|RuleBase:RU367132};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Metal-binding {ECO:0000256|RuleBase:RU367132};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU00239}.
FT DOMAIN 50..353
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT DOMAIN 614..649
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 679..713
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT ACT_SITE 110
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 267
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 713 AA; 82212 MW; C822F502859F4D19 CRC64;
MPYTPSGFFC DRLIRERERR DGEGSLNKPL RFNGQDFNAL RQECLQRKSP FEDDSFPATV
ESLGFKELGH KSNKVKNIVW KRPKEICENP QFIVGGASRT DICQGDLGDC WLLAAIACLT
LNEKLLYRVV PQEQSFSEGY GGIFHFQFWR YGDWVDVVID DRIPTFNNQL VFTKSAERNE
FWSALLEKAY AKLHGSYEAL KGGNTTEAME DFTGGVTEFY ELKEAPKELY KIMKKALLRG
SLMGCSIDSL VPARFETRTA TGLVKGHAYS VTAVDECKPS QQKDSKVRLV RLRNPWGQVE
WNGPWSDNSK EWANLSAAEK EKLQHQSAED GEFWMSFEDF KKNYTKIEIC NLTPDALEDD
KIHKWTVSVN EGRWVKGCSA GGCRNYPDTF WTNPQYRLRL LEEDDDPEDN EVGCTFVVAL
MQKNRRKERK MGANLFTIGF AIYEVPKEMH GNKQHMQKDF FVFSSSKARC KSYINLREVT
QRFRLSPGEY VIVPSTYEPH QEGEFILRVF SEKKNTSEEI ENRIEADHPV PAPASVGEES
EEDQQFRTIF QEIAGDDMEI TANELKNVLN RVITKHKELN TKGFSLESCR SMIALMDMDG
TGRLNLQEFR HLWNKIKQWQ GIFKHYNADQ SGSINSYEMR NAVNDAGFRL NNQLYDIITM
RYANEGMNID FDSFISCLVR LEAMFRAFQA FDQDGDGTIR LSVLEWLQLT MYA
//
