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Database: UniProt
Entry: A0A2Y9F8M2_PHYMC
LinkDB: A0A2Y9F8M2_PHYMC
Original site: A0A2Y9F8M2_PHYMC 
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}.
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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
//
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