CASP2_CHICK
ID CASP2_CHICK Reviewed; 424 AA.
AC Q98943;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Caspase-2;
DE Short=CASP-2;
DE EC=3.4.22.55;
DE AltName: Full=ICH-1L/1S;
DE AltName: Full=Protease ICH-1;
DE Contains:
DE RecName: Full=Caspase-2 subunit p18;
DE Contains:
DE RecName: Full=Caspase-2 subunit p13;
DE Contains:
DE RecName: Full=Caspase-2 subunit p12;
DE Flags: Precursor;
GN Name=CASP2; Synonyms=ICH1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ICH-1L AND ICH-1S).
RC STRAIN=White leghorn; TISSUE=Ovarian granulosa cell;
RX PubMed=9224894; DOI=10.1016/s0378-1119(97)00068-1;
RA Johnson A.L., Bridgham J.T., Bergeron L., Yuan J.;
RT "Characterization of the avian Ich-1 cDNA and expression of Ich-1L mRNA in
RT the hen ovary.";
RL Gene 192:227-233(1997).
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. {ECO:0000250|UniProtKB:P42575}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Strict requirement for an Asp residue at P1, with 316-Asp
CC being essential for proteolytic activity and has a preferred cleavage
CC sequence of Val-Asp-Val-Ala-Asp-|-.; EC=3.4.22.55;
CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC heterodimers, each one formed by a p18 subunit and a p12 subunit.
CC {ECO:0000250|UniProtKB:P42575}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=ICH-1L;
CC IsoId=Q98943-1; Sequence=Displayed;
CC Name=ICH-1S;
CC IsoId=Q98943-2; Sequence=VSP_000803, VSP_000804;
CC -!- MISCELLANEOUS: [Isoform ICH-1L]: Only form found in the ovary.
CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC29881.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U64963; AAC29881.1; ALT_INIT; mRNA.
DR RefSeq; NP_001161173.1; NM_001167701.1.
DR AlphaFoldDB; Q98943; -.
DR SMR; Q98943; -.
DR STRING; 9031.ENSGALP00000029853; -.
DR MEROPS; C14.006; -.
DR PaxDb; Q98943; -.
DR GeneID; 395857; -.
DR KEGG; gga:395857; -.
DR CTD; 835; -.
DR VEuPathDB; HostDB:geneid_395857; -.
DR eggNOG; KOG3573; Eukaryota.
DR InParanoid; Q98943; -.
DR PhylomeDB; Q98943; -.
DR BRENDA; 3.4.22.55; 1306.
DR PRO; PR:Q98943; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1905369; C:endopeptidase complex; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IEA:Ensembl.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
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; IPR035702; Caspase_2.
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 PANTHER; PTHR10454:SF151; PTHR10454:SF151; 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 2: Evidence at transcript level;
KW Alternative splicing; Apoptosis; Hydrolase; Protease; Reference proteome;
KW Thiol protease; Zymogen.
FT PROPEP 1..140
FT /evidence="ECO:0000250"
FT /id="PRO_0000004553"
FT CHAIN 141..308
FT /note="Caspase-2 subunit p18"
FT /evidence="ECO:0000250"
FT /id="PRO_0000004554"
FT CHAIN 309..424
FT /note="Caspase-2 subunit p13"
FT /evidence="ECO:0000250"
FT /id="PRO_0000004555"
FT CHAIN 315..424
FT /note="Caspase-2 subunit p12"
FT /evidence="ECO:0000250"
FT /id="PRO_0000004556"
FT DOMAIN 7..96
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT REGION 296..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 248
FT /evidence="ECO:0000250"
FT ACT_SITE 291
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..6
FT /note="Missing (in isoform ICH-1S)"
FT /evidence="ECO:0000303|PubMed:9224894"
FT /id="VSP_000803"
FT VAR_SEQ 294..424
FT /note="DETDRGVDQRDGKERSDSPGCEESDANKEENLKLRLPTRSDMICGYACLKGT
FT AAMRNTKRGSWYIEALTTVFAEDSRDTHVADMLVKVNRQIKQREGYAPGTEFHRCKEMS
FT EYCSTLCRDLYLFPGYVPGK -> GVSGIHIHLPLPCCCHCICCSMRQTGEWIREMAKN
FT GQIPQAVRRVMQTRKKISSCVCLHAPI (in isoform ICH-1S)"
FT /evidence="ECO:0000303|PubMed:9224894"
FT /id="VSP_000804"
SQ SEQUENCE 424 AA; 47960 MW; 792810508B8B2F60 CRC64;
MLGACGMQRY HQEALKKNRV MLARELVLKE LMEHMIEKDI ITIEMVEMIQ AKSGSFSQNV
EFLNLLPKRG PNAFSAFCEA LQETKQQHLA EMILKTESSL RHGIATLEQR YGSNLPLPLS
ESCNSKRPRL IVEHSLDSGD GPPIPPVKHC TPEFYRDHQH LAYKLISEPR GLALILSNIH
FSSEKDLEYR SGGDVDCASL ELLFKHLGYQ VTVFHDQSAE EMESALERFS KLPDHQDVDS
CIVALLSHGV EGGVYGTDGK LLQLQEAFRL FDNANCPNLQ NKPKMFFIQA CRGDETDRGV
DQRDGKERSD SPGCEESDAN KEENLKLRLP TRSDMICGYA CLKGTAAMRN TKRGSWYIEA
LTTVFAEDSR DTHVADMLVK VNRQIKQREG YAPGTEFHRC KEMSEYCSTL CRDLYLFPGY
VPGK
