ID A0A3B3D666_ORYME Unreviewed; 1249 AA.
AC A0A3B3D666;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 18-JUN-2025, entry version 29.
DE RecName: Full=Apoptotic protease-activating factor 1 {ECO:0000256|ARBA:ARBA00073202, ECO:0000256|PIRNR:PIRNR037646};
DE Short=APAF-1 {ECO:0000256|PIRNR:PIRNR037646};
GN ORFNames=FQA47_015125 {ECO:0000313|EMBL:KAF6731236.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000024964.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000024964.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (DEC-2024) to UniProtKB.
RN [2] {ECO:0000313|EMBL:KAF6731236.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bigg-433 {ECO:0000313|EMBL:KAF6731236.1};
RX PubMed=32938378;
RA Liang P., Saqib H.S.A., Ni X., Shen Y.;
RT "Long-read sequencing and de novo genome assembly of marine medaka (Oryzias
RT melastigma).";
RL BMC Genomics 21:0-0(0).
CC -!- FUNCTION: Oligomeric Apaf-1 mediates the cytochrome c-dependent
CC autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the
CC activation of caspase-3 and apoptosis. This activation requires ATP.
CC {ECO:0000256|PIRNR:PIRNR037646}.
CC -!- SUBUNIT: Monomer. Oligomerizes upon binding of cytochrome c and dATP.
CC {ECO:0000256|PIRNR:PIRNR037646}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR037646}.
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DR EMBL; WKFB01000217; KAF6731236.1; -; Genomic_DNA.
DR STRING; 30732.ENSOMEP00000024964; -.
DR PaxDb; 30732-ENSOMEP00000024964; -.
DR Ensembl; ENSOMET00000008332.1; ENSOMEP00000024964.1; ENSOMEG00000000126.1.
DR GeneTree; ENSGT00940000157710; -.
DR OMA; GAYLKWW; -.
DR OrthoDB; 1357022at2759; -.
DR Proteomes; UP000261560; Unplaced.
DR Proteomes; UP000646548; Unassembled WGS sequence.
DR GO; GO:0043293; C:apoptosome; IEA:InterPro.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR CDD; cd00200; WD40; 2.
DR FunFam; 1.10.533.10:FF:000081; Apoptotic protease-activating factor 1; 1.
DR FunFam; 1.10.8.430:FF:000001; Apoptotic protease-activating factor 1; 1.
DR FunFam; 1.25.40.370:FF:000001; Apoptotic protease-activating factor 1; 1.
DR FunFam; 2.130.10.10:FF:000135; Apoptotic protease-activating factor 1; 1.
DR FunFam; 3.40.50.300:FF:000502; Apoptotic protease-activating factor 1; 1.
DR Gene3D; 1.25.40.370; -; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 1.10.8.430; Helical domain of apoptotic protease-activating factors; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR017251; Apaf-1.
DR InterPro; IPR041452; APAF1_C.
DR InterPro; IPR048975; APAF1_WHD.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR22845; APOPTOTIC PROTEASE-ACTIVATING FACTOR 1; 1.
DR PANTHER; PTHR22845:SF5; APOPTOTIC PROTEASE-ACTIVATING FACTOR 1; 1.
DR Pfam; PF21296; APAF-1-like_WHD; 1.
DR Pfam; PF17908; APAF1_C; 1.
DR Pfam; PF00619; CARD; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF00400; WD40; 8.
DR PIRSF; PIRSF037646; Apop_pept_activating-1; 1.
DR PRINTS; PR00364; DISEASERSIST.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 12.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 2.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 6.
PE 4: Predicted;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703, ECO:0000256|PIRNR:PIRNR037646};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR037646};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR037646};
KW Hydrolase {ECO:0000313|EMBL:KAF6731236.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037646}; Protease {ECO:0000313|EMBL:KAF6731236.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000646548};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 3..92
FT /note="CARD"
FT /evidence="ECO:0000259|PROSITE:PS50209"
FT REPEAT 651..687
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 735..776
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 871..912
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 995..1036
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1036..1080
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1081..1112
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1123..1164
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ SEQUENCE 1249 AA; 140823 MW; 3BE8A6AEC5D50F27 CRC64;
MALDERAHAC LLRSRHKLEE VMKPDVLLDH MISDEAVTVE EEDTITNQKT KKEQAAALVE
LLLKKGNSCF KSFYNALLKE EYEELACLLT SHLPPTQINS NPQYHVQTVL SEGGVPPRPE
AFVHRPTEED EIREKLYKLQ KQPGWVTVFG MAGSGKSVLA SEAVRHKALI EECFPEGIHW
LSIGRLDKPD LLTKIQTLCF RLEQNLDSQP FHRPPSTLDE AKERLRFLVI RKYARSLLIL
DDVWDSTVLK AFDINCRILL TTRNRSLADV VNGNKHEVEV NSGVDEDKAL EILSQLSKVE
RYKLPVEALS IVKKCKGSPL AVSMIGSLLR ENPDRWGYYL GQLEKKQFRR IRKSSSYNYE
ALDQAMAAGI EDLPDDYREL YNHLAVLHKD IKVTAKLMSV FWDLDQVEAE DILSDFVNRA
MLFVDQPNVF YLHDLQLDFL LEQNKNQLQS LHTKVVRLYQ HRYKDGPPTS RDEESLYWIR
YLAYHMANAN LSQELHSLLL SLDWISVKGQ IMGPAHLIND YLEYGSILDK ENSEMCSEFQ
EFLSLSGHYL EQRPFPDIVQ LALSQPHTSE VYRQARLLAQ ERAKDGKLYF DVTNETSVES
LSRLVIHPYQ GSLFASLSND GTKIASCGAT KNVKVFKATS GEKLTEIQLC DEVVCCAFSP
DDSLLAVCSS AKTIQVWSVD KGIVLRTFQE EHQGQINHCV FTNTTHRLLL ATCSSGELLN
AMLWNLNKPT SQNTMFGHFE TVNHCCFSPD DAYVATSSND GTVQLFEVPS GNNWKSIDVK
GAFKDVDDDD EVAVRCSSWT ADGKRIVCAA RNAALMFDVE TADLLLEIRP SFFSTVLHCD
VCPTSNLLAL ALSNYAVELW DIEENTKKAD CSGHLSWVER VQFSRDGSQL LSSSDDETIR
LWETKKLHMS SAVFLKRNSD VLFNDNNIIV SAPDHCNRLQ VREGRTGDVL LQSEKKPSRI
RCTCLCRDPP VVGLGQEDGT VQVLEVPSGK PLATLLGHTK TVLHCQFTHN GQTLITSSED
STIRVWKWPS GECQVLQGHK EQVRCFALLS SSSNDSRLLS WSFDGTVKVW NTESGQKLQD
VDAHQGAILS CHVSPDGRLF ATSSADKTAK LWHCEAWQWA FTLTGHRECV RSCRFSWDSE
CLATGDDNGE IRLWNVNDGS LLRVCSREVK DSTDSFHGGW VTDLHFSPDS SLLVSAGGYI
KWWDVKAGVA LQTFYPKGNA LRKIHVSSDF STFVTVDSIG ILYALQRVP
//
