ID A0A7L4EV98_HIRRU Unreviewed; 1249 AA.
AC A0A7L4EV98;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 13.
DE RecName: Full=Apoptotic protease-activating factor 1 {ECO:0000256|ARBA:ARBA00073202, ECO:0000256|PIRNR:PIRNR037646};
DE Short=APAF-1 {ECO:0000256|PIRNR:PIRNR037646};
DE Flags: Fragment;
GN Name=Apaf1 {ECO:0000313|EMBL:NXW78097.1};
GN ORFNames=HIRRUS_R14567 {ECO:0000313|EMBL:NXW78097.1};
OS Hirundo rustica (Barn swallow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sylvioidea; Hirundinidae; Hirundo.
OX NCBI_TaxID=43150 {ECO:0000313|EMBL:NXW78097.1, ECO:0000313|Proteomes:UP000585317};
RN [1] {ECO:0000313|EMBL:NXW78097.1, ECO:0000313|Proteomes:UP000585317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-001-67 {ECO:0000313|EMBL:NXW78097.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXW78097.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NXW78097.1}.
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DR EMBL; VZZX01009958; NXW78097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L4EV98; -.
DR Proteomes; UP000585317; 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:0097190; P:apoptotic signaling pathway; IEA:InterPro.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR CDD; cd00200; WD40; 2.
DR FunFam; 1.10.10.10:FF:000204; Apoptotic protease-activating factor 1; 1.
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; 2.130.10.10:FF:000196; 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; IPR011047; Quinoprotein_ADH-like_sf.
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; 9.
DR PIRSF; PIRSF037646; Apop_pept_activating-1; 1.
DR PRINTS; PR00364; DISEASERSIST.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 14.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 8.
DR PROSITE; PS50294; WD_REPEATS_REGION; 7.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037646};
KW Reference proteome {ECO:0000313|Proteomes:UP000585317};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 1..90
FT /note="CARD"
FT /evidence="ECO:0000259|PROSITE:PS50209"
FT REPEAT 609..650
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 651..692
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 693..736
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 737..778
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 876..908
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1041..1081
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1082..1123
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1124..1165
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXW78097.1"
FT NON_TER 1249
FT /evidence="ECO:0000313|EMBL:NXW78097.1"
SQ SEQUENCE 1249 AA; 142193 MW; 711AEA420DCE3955 CRC64;
MDVKSRNYLL MNRQALENDI KTSYIMDRMI SDEVLTLQEE ERVKQQSTRK ERAAMLINII
LTKDNNSYRS FYNALLHEGY RDLAALLQDG IPAVSSGNRK SSMDGMTSYV KTILCEGGVP
QRPVVFVTRP KLVDAIKKKL YCLGSDPGWV TVYGMAGCGK TVLTAEALRD PQLLEDYFPG
GVHWISVGKQ DKAGLLIKLQ NLCSRLEQDS ALSQRPPLNI EEAKDRLRLL MLRKYPRSLL
VLDDIWDSWV LKAFDNQCQV LITSRDRSVT DAVAGNKYEV HVESGLAHEK GLEILSLFVN
MKISELPEQA NSLVRECKGS PLVISLIGAL LRDFPSRWEY YLRQLQNKQF KRIRKSSSYD
YEALDEAMSI SVEQLDDNYK DYYKDLSILP KDVKVPTKVL CILWDMETEE VEDILQEFVN
KSLLFCDRNG KSFHYYLHDL QLDFLTEKNH NQLQELHKNI VNQYMKYYKL NTPVLSQEDC
MYWYNFLAYH MAGAKMQQEL CDLMFSLDWI KAKTELVGPA HLIHEYVEYS SILDQKDSTV
RENFQEFLSL NGHLLGRQPF PDIIQLGLCQ PETSEVYRQA KLHAQRETGT FYLEWINKKS
LKNLYRLVVR PHRDAVYHAC FSKDRQRIAS CGADKTLQVF KTESGERILE INAHDDEILC
CAFSADGEFV ATCSSDKKVK VWNSRTGQCR CVYEEHTEQV NCCQFNNKSG QYLLATCSND
TFIKIWDLNE KYCRNTMIGH ENPVNHCRFS PNDEYVASCS TDGTVKLWEA RSGNELKSIE
IKDFFKNADE QPDDVEVLVK CCSWSRNGNM ILVVAKNKLL LFDINTCGLL TQIIVSHHST
IQYCDFCPGD ELVAVALSHC SVELWNIRSL SKVAYCRGHM SWVHCVTFSP DGSLFLTSSD
DQTIRIWETK KVCKSSDAVL KSDLDVVFHN GEVMILAIYN HKNLQLINGN TDNVIMQTAA
QESPISCCCL SEDLKFAAFG QESGTIKVLQ LSDGKVLKSW EAYRTSVQHC RFTPDCQTLI
ISAHNSVVQV WNWQLSECVF LRGHKEAIKD FRILENSKIL SWSFDGTVKV WNITTGKPEK
DFACHGGAVL SCAVSPDGSK FSSASADKTA KIWSFESSSV LHELKDHEAC VRCCTFSPNN
KLLATGDDKG EIRIWDILTG ALLHFCSPVT VDEGEPTHGG WVTDLSFSPD SKMLVSSGGY
LKWWNVTTGE CLQTFYTNGT NLKSIHVSPN FKVYVTVDNL GILYVLQKF
//
