ID A0A452C8L0_BALAS Unreviewed; 959 AA.
AC A0A452C8L0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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_028019422.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_028019422.1};
RN [1] {ECO:0000313|RefSeq:XP_028019422.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028019422.1};
RG RefSeq;
RL Submitted (JAN-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 Speedy/Ringo family.
CC {ECO:0000256|ARBA:ARBA00010932}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR RefSeq; XP_028019422.1; XM_028163621.1.
DR AlphaFoldDB; A0A452C8L0; -.
DR STRING; 310752.A0A452C8L0; -.
DR InParanoid; A0A452C8L0; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000261681; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR001300; Peptidase_C2_calpain_cat.
DR InterPro; IPR020984; Speedy.
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 Pfam; PF11357; Spy1; 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.
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, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU00239}.
FT DOMAIN 358..598
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT DOMAIN 860..895
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT ACT_SITE 359
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 516
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 540
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 959 AA; 109944 MW; 3589B741835EA12F CRC64;
MSDAQDPATI PAVGTQVNLR GWSRRGEGGE SFHFRRHQEL QAFLNLLEHS FLQDFLSKDP
CFQISDKYLL AMVLVYFQRA NLQLSEYTHS NLFLALYLAN DMEEDLEDPK SVIFLWALGQ
DWHHRVSDFL RQRDKLWARM GFRAVVRRQS CEEVMAKEPT HWAWTRERHP HHGRAQRSYP
KAQIPLPRGP GLSPPHCPLC GLPPCRSHRC RHPCPLPVIS KCPSQNPERH RPPSQACVSV
AGASWSGNFL IVLPTQRQLE PGTYTLHRWL RRSSLRCTAP GCLHKCKSSG PRSWAWAAMK
TPSSTWARIM LSCGLTACRV GPSSVMRLSP QCPRAWASRT WALTPPKPMA SSGSVPRDCW
LLAAIASLTL NDTLLHRVVP HGQSFQDGYV GIFHFQLWQF GEWVDVVVDD LLPTKDGKLV
FVHSAQGNEF WSALLEKAYA KVNGSYEALS GGSTSEGFED FTGGVTEWYE LRKAPSDLYS
IILKALERGS LLGCSIDISS ILDMEAVTFK KLVKGHAYSV TGAKQVNYQG QMVNLIRMRN
PWGEVEWTGA WSDGSSEWNN VDPYVREQLR VKMEDGEFWM SFRDFMREFT RLEICNLTPD
ALKSQRFCNW NTTLYEGTWR RGSTAGGCRN YPATFWVNPQ FKIQLEETDD PDDDYSGRES
GCSFLLALMQ KHRRRERRFG RDMETIGFAV YEVPPELMGQ PAVHLKRDFF LANASRARSE
QFINLREVST RFRLPPGEYV VVPSTFEPNK EGDFVLRFFS EKSAGTQELD DQIQANLPDE
QVLSEEEIDE NFKSLFRQLA GEDMEISVKE LRTILNRIIS KHKDLRTKGF SLESCRSMVN
LMDRDGNGKL GLVEFNILWN RIRNYLSIFR KFDLDKSGSM SAYEMRMAIE SAGFKLSKKL
YELIITRYSE PDLAVDFDNF VCCLVRLETM FRFFKTLDTD LDGVVTFDLF KWLQLTMFA
//
