ID A0A0A0A9Q1_CHAVO Unreviewed; 1249 AA.
AC A0A0A0A9Q1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Apoptotic protease-activating factor 1 {ECO:0000256|PIRNR:PIRNR037646};
DE Short=APAF-1 {ECO:0000256|PIRNR:PIRNR037646};
GN ORFNames=N301_14697 {ECO:0000313|EMBL:KGL91299.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL91299.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL91299.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL91299.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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|PIRNR:PIRNR037646}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL871235; KGL91299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0A9Q1; -.
DR STRING; 50402.A0A0A0A9Q1; -.
DR Proteomes; UP000053858; 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; cd08323; CARD_APAF1; 1.
DR CDD; cd00200; WD40; 2.
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; IPR037963; APAF1_CARD_dom.
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_supfam.
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; 10.
DR PIRSF; PIRSF037646; Apop_pept_activating-1; 1.
DR PRINTS; PR00364; DISEASERSIST.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 13.
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; 9.
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|PIRNR:PIRNR037646};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR037646};
KW Hydrolase {ECO:0000313|EMBL:KGL91299.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037646};
KW Protease {ECO:0000313|EMBL:KGL91299.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
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 1000..1032
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"
SQ SEQUENCE 1249 AA; 141586 MW; 32C5D517BB689211 CRC64;
MDAKSRNYLL RNRQALEKDI KTSYIMDRMI SDEVLTLQEE EKVKQQNTQK ERAAMLINII
LTKDNNSYRS FYNALLHEGY RDLAALLQDG IPAISSGNGK SSMDGMTSYV KTILCEGGVP
QRPVVFVTRP KLVDAIKQKL CCLGSDPGWV TVYGMAGCGK TVLTAEALRD HQLLEDYFPG
GVHWISVGKQ DKAGLLIKLQ NLCSRLEHDS TLSQRPPLNI EEAKDRLRLL MLRKYPRSLL
ILDDIWDSWV LKAFDNQCQV LITSRDRSVT DAVAGNKYEV HVESGLAHEK GLEILSLFVN
MKISELPEQA NCLVRECKGS PLVISLIGAL LRDFPSRWEY YLKQLQHKQF KRIRKSSSYD
YEALDEAMSI SVEQLNDNYK DYYKDLSILP KDVKVPTKVL CILWDMETEE VEDILQEFVN
KSLLFCDRNG KSFHYYLHDL QLDFLTEKNR NQLQELHKNI VNQYKKYYKL NTPVPSQEDC
MYWYNFLAYH MAGANMQKEL HDLMFSLDWI KAKTELVGPA HLIHEYVEYS SILDQKDSTV
RENFQEFLSL NGHLLGRQPF PDIVQLGLCQ PETSILNNKN ALGNPTHLKL TVLPCRNKKS
LKNLYRLVVR PHRDAVYHAC FSKDRQRIAS CGADKTLQVF KAESGERLLE ISAHDDEILC
CAFSADGEFV ATCSADKKVK IWNSRTGQCK CVYEEHAEQV NCCQFNNGTG QYLLATCSND
TFIKLWDLNK KYCRNTMIGH VNSVIHCRFS PNDEYVASCS ADGTVKLWEA RSANELKSIE
IKDFFRNADE QPDDVEVLVK CCSWSRNGDM LLVVAKNKLL LFDVKTCDLL TQVIVSHHST
IQYCDFCPGD ELVAVALSHC SVELWNIKSL SKVAYCRGHM SWVHCVTFSP DGSLFLTSSD
DQTIRIWETK KVCKSSDAVL KSELDVVFHS DEVMILAIYN QKHLQLINGN TDSVVMHTAA
QESPISCCCL SEDLKFAAFG QESGTIKVLQ LLDGKVLKSR EAYRTSVQHC RFTSDCQTLI
SSAHDSVIQV WNWQLSECVF LRGHKEAIKD FRLLENSKLL SWSFDGTVKV WNITTGNTEK
DFACHGGAVL SCAVSPDGSK FSSTSADKTA KIWSFESSSV LHELKGHEAC VRCCTFSPNN
KLLATGDDKG EIRIWDILTG ALLHFCSPVT VDEGEPTHGG WVTDLSFSPD SKMLVSSGGY
LKWWNVITGE SLQTFYTNGT NLKSIHVCPN FEVYVTVDNL GILYVLQKL
//