ID A0A2Y9F8M2_PHYMC Unreviewed; 716 AA.
AC A0A2Y9F8M2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Calpain-1 catalytic subunit {ECO:0000256|ARBA:ARBA00020246};
DE EC=3.4.22.52 {ECO:0000256|ARBA:ARBA00012482};
DE AltName: Full=Calcium-activated neutral proteinase 1 {ECO:0000256|ARBA:ARBA00031279};
DE AltName: Full=Calpain mu-type {ECO:0000256|ARBA:ARBA00031878};
DE AltName: Full=Calpain-1 large subunit {ECO:0000256|ARBA:ARBA00032619};
DE AltName: Full=Micromolar-calpain {ECO:0000256|ARBA:ARBA00032278};
GN Name=CAPN1 {ECO:0000313|RefSeq:XP_007117479.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007117479.1};
RN [1] {ECO:0000313|RefSeq:XP_007117479.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007117479.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad endopeptidase specificity.; EC=3.4.22.52;
CC Evidence={ECO:0000256|ARBA:ARBA00001208};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_007117479.1; XM_007117417.3.
DR STRING; 9755.ENSPCTP00005011276; -.
DR Ensembl; ENSPCTT00005012461; ENSPCTP00005011276; ENSPCTG00005008016.
DR GeneID; 102984504; -.
DR KEGG; pcad:102984504; -.
DR CTD; 823; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000248484; Chromosome 16.
DR GO; GO:0005829; C:cytosol; 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; IEA:Ensembl.
DR GO; GO:0097264; P:self proteolysis; IEA:Ensembl.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR CDD; cd16198; EFh_PEF_CAPN1; 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; 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 PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF284; CALPAIN-1 CATALYTIC SUBUNIT; 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 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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT ACT_SITE 115
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1"
FT ACT_SITE 272
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1"
FT ACT_SITE 296
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1"
SQ SEQUENCE 716 AA; 81957 MW; 0DD058D67459880C CRC64;
MAEEVITPVY CTGVSAQVQK QRAKKLGLGR HENAIKYLGQ DYDQLRAHCL QSGALFRDEA
FPPVPQSLGF KDLGPNSSKT YGIKWKRPPE LFSNPQFIVD GATRTDICQG ALGDCWLLAA
IASLTLNDTL LHRVVPHGQS FQDGYVGIFH FQLWQFGEWV DVVVDDLLPT KDGKLVFVHS
AQGNEFWSAL LEKAYAKVSG SYEALSGGST SEGFEDFTGG VTEWYELRKA PSDLYSIILK
ALERGSLLGC SIDISSILDM EAVTFKKLVK GHAYSVTGAK QVNYQGQMVN LIRMRNPWGE
VEWTGAWSDG SLEWNRVDPY VREQLRVKME DGEFWMSFRD FMREFTRLEI CNLTPDALKS
QRFRNWNTTL YEGTWRRGST AGGCRNYPAT FWVNPQFKIR LEETDDPDND DYRAQESGCS
FLLALMQKHR RRERRLGRDM ETIGFAVYEV PPELTGQPAV HLKRDFFLAN ASRACSKQFI
NLREVSTRFR LPPGEYVVVP STFEPNKEGD FVLRFFSEKS AGTQELDDQI QANLPDEQVL
SAEEIDENFK SLFRQLAGKD MEISVKELQT ILNRIISKHK DLRTKGFSLQ SCRSMVNLMD
RDGNGKLGLV EFNILWNRIR NYLSIFRKFD LDKSGSMSAY EMRMAIESAG FKLNKKLYEL
IITRYSEPDL AVDFDNFVCC LVRLETMFRF FKTLDTDLDG VVTFDLFKWL QLTMFA
//