ID A0A3Q3F6K4_KRYMA Unreviewed; 439 AA.
AC A0A3Q3F6K4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Caspase 2 {ECO:0000313|Ensembl:ENSKMAP00000009162.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000009162.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000009162.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase C14A family.
CC {ECO:0000256|ARBA:ARBA00010134, ECO:0000256|RuleBase:RU003971}.
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DR RefSeq; XP_017270907.1; XM_017415418.1.
DR AlphaFoldDB; A0A3Q3F6K4; -.
DR STRING; 37003.ENSKMAP00000009162; -.
DR Ensembl; ENSKMAT00000009297.1; ENSKMAP00000009162.1; ENSKMAG00000006878.1.
DR GeneID; 108235415; -.
DR CTD; 835; -.
DR GeneTree; ENSGT00940000156657; -.
DR OMA; VMVLMTH; -.
DR OrthoDB; 2873736at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00032; CASc; 1.
DR Gene3D; 3.40.50.1460; -; 1.
DR Gene3D; 3.30.70.1470; Caspase-like; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 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; IPR011600; Pept_C14_caspase.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR47901:SF7; CASPASE 2; 1.
DR PANTHER; PTHR47901; CASPASE RECRUITMENT DOMAIN-CONTAINING PROTEIN 18; 1.
DR Pfam; PF00619; CARD; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR PIRSF; PIRSF038001; Caspase_ICE; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00114; CARD; 1.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF52129; Caspase-like; 1.
DR SUPFAM; SSF47986; DEATH domain; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 6..96
FT /note="CARD"
FT /evidence="ECO:0000259|PROSITE:PS50209"
FT DOMAIN 169..297
FT /note="Caspase family p20"
FT /evidence="ECO:0000259|PROSITE:PS50208"
FT DOMAIN 340..433
FT /note="Caspase family p10"
FT /evidence="ECO:0000259|PROSITE:PS50207"
FT REGION 311..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 439 AA; 49822 MW; 83F57F1633935EFD CRC64;
MRECGMLERD KLALRRRSAD LCKDLVVDEM LIQLLHADNI LTESMAESIM AGQTSQKRNW
RLLLLLPKRG PRAFSSFCSA LRQTEQQHLC DLLAQSPEQD DKETHVDRVA RSPLPHPTQE
EISAKRARTH ESMEFSLDAD SPINTPVLPC TPDFYLSRCQ QSYRLKSSPR GYALVISNVT
FDSGAAPDLD PRKGGEVDDE VLRKVFTELD YLVSVHRDLT AQDMRTCIKT FCRRAEHRTV
DSCVVCLLSH GVEGAIYGTD GQLLQLDWVF EAFDNAHCPL LQNKPKMFFI QACRGDEMDC
GVEQIDGPAR TLSPSCEQRD AGREGEGDTD STQRGDPRRP RIKLPQRSDM ICGFASLKGT
AAMRNTKRGS WFIQELNTAL RLHARDTHLA DILVQVNRRI KEREGYAPGT AHHRCKEMSE
FTSSLCKDLY LFPKYQPQY
//
