CASPD_BOVIN
ID CASPD_BOVIN Reviewed; 377 AA.
AC O75601;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Caspase-13;
DE Short=CASP-13;
DE EC=3.4.22.-;
DE AltName: Full=Evolutionary related interleukin-1-beta-converting enzyme;
DE Short=ERICE;
DE Contains:
DE RecName: Full=Caspase-13 subunit 1;
DE Contains:
DE RecName: Full=Caspase-13 subunit 2;
DE Flags: Precursor;
GN Name=CASP13;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND MUTAGENESIS OF CYS-258.
RC TISSUE=Fibroblast;
RX PubMed=9624166; DOI=10.1074/jbc.273.25.15702;
RA Humke E.W., Ni J., Dixit V.M.;
RT "ERICE, a novel FLICE-activatable caspase.";
RL J. Biol. Chem. 273:15702-15707(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RX PubMed=11478774; DOI=10.1006/bbrc.2001.5315;
RA Koenig U., Eckhart L., Tschachler E.;
RT "Evidence that caspase-13 is not a human but a bovine gene.";
RL Biochem. Biophys. Res. Commun. 285:1150-1154(2001).
CC -!- FUNCTION: Involved in the activation cascade of caspases responsible
CC for apoptosis execution. Might function by either activating some
CC proteins required for cell death or inactivating proteins necessary for
CC cell survival.
CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC heterodimers, each one formed by a small and a large subunit.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=O75601-1; Sequence=Displayed;
CC Name=B;
CC IsoId=O75601-2; Sequence=VSP_000823;
CC -!- TISSUE SPECIFICITY: Mainly expressed in peripheral blood lymphocytes,
CC spleen and placenta.
CC -!- PTM: The two subunits are derived from the precursor sequence by an
CC autocatalytic mechanism or by cleavage by Caspase-8.
CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to originate from human.
CC {ECO:0000305|PubMed:9624166}.
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DR EMBL; AF078533; AAC28380.1; -; mRNA.
DR EMBL; AF383946; AAK77964.1; -; mRNA.
DR EMBL; AF383947; AAK77965.1; -; mRNA.
DR RefSeq; NP_788811.1; NM_176638.5. [O75601-1]
DR AlphaFoldDB; O75601; -.
DR SMR; O75601; -.
DR MEROPS; C14.017; -.
DR PeptideAtlas; O75601; -.
DR PRIDE; O75601; -.
DR Ensembl; ENSBTAT00000027820; ENSBTAP00000027820; ENSBTAG00000020884. [O75601-1]
DR GeneID; 338039; -.
DR KEGG; bta:338039; -.
DR CTD; 837; -.
DR VEuPathDB; HostDB:ENSBTAG00000020884; -.
DR InParanoid; O75601; -.
DR OMA; KAHLNME; -.
DR TreeFam; TF102023; -.
DR Reactome; R-BTA-5620971; Pyroptosis.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000020884; Expressed in neutrophil and 103 other tissues.
DR ExpressionAtlas; O75601; baseline and differential.
DR GO; GO:0097169; C:AIM2 inflammasome complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0072557; C:IPAF inflammasome complex; IBA:GO_Central.
DR GO; GO:0072559; C:NLRP3 inflammasome complex; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
DR GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central.
DR CDD; cd00032; CASc; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR033139; Caspase_cys_AS.
DR InterPro; IPR016129; Caspase_his_AS.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR002398; Pept_C14.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR10454; PTHR10454; 1.
DR Pfam; PF00619; CARD; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00114; CARD; 1.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF52129; SSF52129; 1.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS01122; CASPASE_CYS; 1.
DR PROSITE; PS01121; CASPASE_HIS; 1.
DR PROSITE; PS50207; CASPASE_P10; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Hydrolase; Protease; Reference proteome;
KW Thiol protease; Zymogen.
FT PROPEP 1..?
FT /evidence="ECO:0000255"
FT /id="PRO_0000004649"
FT CHAIN ?..289
FT /note="Caspase-13 subunit 1"
FT /id="PRO_0000004650"
FT CHAIN 290..377
FT /note="Caspase-13 subunit 2"
FT /id="PRO_0000004651"
FT DOMAIN 1..86
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT ACT_SITE 210
FT /evidence="ECO:0000250"
FT ACT_SITE 258
FT /evidence="ECO:0000250"
FT VAR_SEQ 68..124
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11478774"
FT /id="VSP_000823"
FT MUTAGEN 258
FT /note="C->S: Inactivation."
FT /evidence="ECO:0000269|PubMed:9624166"
SQ SEQUENCE 377 AA; 43012 MW; 959A59424DAECBF4 CRC64;
MAEDKHNKNP LKMLESLGKE LISGLLDDFV EKNVLKLEEE EKKKIYDAKL QDKARVLVDS
IRQKNQEAGQ VFVQTFLNID KNSTSIKAPE ETVAGPDESV GSAATLKLCP HEEFLKLCKE
RAGEIYPIKE RKDRTRLALI ICNTEFDHMP PRNGAALDIL GMKQLLEGLG YTVEVEEKLT
ARDMESVLWK FAAREEHKSS DSTFLVFMSH GILDGICGTM HSEEEPDVLP YDTIFRTFNN
RNCLSLKDKP KVIIVQACRG ANRGELWVSD SPPALADSFS QSSENLEEDA VYKTHVEKDF
IAFCSSTPHN VSWRDIKKGS LFITRLITCF QKYAWCCHLE EVFRKVQQSF EKPNVKAQMP
TVERLSMTRY FYLFPGN
