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Apoptotic protease-activating factor 1 (APAF-1)

 F1Q410_CANLF            Unreviewed;      1258 AA.
F1Q410;
03-MAY-2011, integrated into UniProtKB/TrEMBL.
31-OCT-2012, sequence version 2.
12-SEP-2018, entry version 62.
RecName: Full=Apoptotic protease-activating factor 1 {ECO:0000256|PIRNR:PIRNR037646};
Short=APAF-1 {ECO:0000256|PIRNR:PIRNR037646};
Name=APAF1 {ECO:0000313|Ensembl:ENSCAFP00000009806,
ECO:0000313|VGNC:VGNC:54194};
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000009806, ECO:0000313|Proteomes:UP000002254};
[1] {ECO:0000313|Ensembl:ENSCAFP00000009806, ECO:0000313|Proteomes:UP000002254}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000009806,
ECO:0000313|Proteomes:UP000002254};
PubMed=16341006; DOI=10.1038/nature04338;
Broad Sequencing Platform;
Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
"Genome sequence, comparative analysis and haplotype structure of the
domestic dog.";
Nature 438:803-819(2005).
[2] {ECO:0000313|Ensembl:ENSCAFP00000009806}
IDENTIFICATION.
STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000009806};
Ensembl;
Submitted (JUL-2011) to UniProtKB.
-!- FUNCTION: Oligomeric Apaf-1 mediates the cytochrome c-dependent
autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the
activation of caspase-3 and apoptosis. This activation requires
ATP. {ECO:0000256|PIRNR:PIRNR037646}.
-!- SUBUNIT: Monomer. Oligomerizes upon binding of cytochrome c and
dATP. {ECO:0000256|PIRNR:PIRNR037646}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR037646}.
-----------------------------------------------------------------------
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EMBL; AAEX03009966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
ProteinModelPortal; F1Q410; -.
Ensembl; ENSCAFT00000010576; ENSCAFP00000009806; ENSCAFG00000006556.
VGNC; VGNC:54194; APAF1.
eggNOG; KOG4155; Eukaryota.
eggNOG; KOG4658; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00920000149054; -.
OMA; SVNHCRF; -.
OrthoDB; EOG091G036U; -.
TreeFam; TF323866; -.
Reactome; R-CFA-111458; Formation of apoptosome.
Reactome; R-CFA-111459; Activation of caspases through apoptosome-mediated cleavage.
Reactome; R-CFA-6798695; Neutrophil degranulation.
Proteomes; UP000002254; Chromosome 15.
Bgee; ENSCAFG00000006556; Expressed in 3 organ(s), highest expression level in liver.
GO; GO:0043293; C:apoptosome; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0043531; F:ADP binding; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; IEA:Ensembl.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
GO; GO:1902510; P:regulation of apoptotic DNA fragmentation; IEA:Ensembl.
CDD; cd08323; CARD_APAF1; 1.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 2.130.10.10; -; 3.
InterPro; IPR017251; Apaf-1.
InterPro; IPR037963; APAF1_CARD_dom.
InterPro; IPR024977; Apc4_WD40_dom.
InterPro; IPR001315; CARD.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR002182; NB-ARC.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
InterPro; IPR036388; WH-like_DNA-bd_sf.
Pfam; PF12894; ANAPC4_WD40; 1.
Pfam; PF00619; CARD; 1.
Pfam; PF00931; NB-ARC; 1.
Pfam; PF00400; WD40; 8.
PIRSF; PIRSF037646; Apop_pept_activating-1; 1.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 13.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF50978; SSF50978; 2.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50209; CARD; 1.
PROSITE; PS00678; WD_REPEATS_1; 4.
PROSITE; PS50082; WD_REPEATS_2; 8.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
4: Predicted;
Apoptosis {ECO:0000256|PIRNR:PIRNR037646};
ATP-binding {ECO:0000256|PIRNR:PIRNR037646};
Complete proteome {ECO:0000313|Proteomes:UP000002254};
Cytoplasm {ECO:0000256|PIRNR:PIRNR037646};
Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037646};
Reference proteome {ECO:0000313|Proteomes:UP000002254};
Repeat {ECO:0000256|SAAS:SAAS00723881};
WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221,
ECO:0000256|SAAS:SAAS00723873}.
DOMAIN 1 90 CARD. {ECO:0000259|PROSITE:PS50209}.
DOMAIN 619 1222 WD_REPEATS_REGION.
{ECO:0000259|PROSITE:PS50294}.
REPEAT 619 660 WD. {ECO:0000256|PROSITE-
ProRule:PRU00221}.
REPEAT 661 702 WD. {ECO:0000256|PROSITE-
ProRule:PRU00221}.
REPEAT 703 746 WD. {ECO:0000256|PROSITE-
ProRule:PRU00221}.
REPEAT 747 788 WD. {ECO:0000256|PROSITE-
ProRule:PRU00221}.
REPEAT 886 918 WD. {ECO:0000256|PROSITE-
ProRule:PRU00221}.
REPEAT 1007 1048 WD. {ECO:0000256|PROSITE-
ProRule:PRU00221}.
REPEAT 1090 1124 WD. {ECO:0000256|PROSITE-
ProRule:PRU00221}.
REPEAT 1132 1173 WD. {ECO:0000256|PROSITE-
ProRule:PRU00221}.
SEQUENCE 1258 AA; 142749 MW; 63C8DA0C0DDA7036 CRC64;
MDAKARNCLL QYREALEKDI KTSYIMDRMI NDGVLTISEE EKVKNEPTQQ QRAALLIKTI
LKKDNYSYIS FYNALIHEGY KDLAALLHSG IPVISSSNGG KDSVGGITSH VKTVLCEGGV
PQRPVVFVTR KKLVNAIRQN LFKLSDEPGW VVIYGMAGCG KSVLAAEAVR DHFFLDVGCF
PGGVHWVSVG KQDKAGLLMK LQNLCTRLDQ DENFSQRPPL NIEEAKDRLR LLMLRKHPRI
RSLLILDDIW DSWILKAFDN QCQILLTTRD KSVTDSVMGP KYIVAVESDL GKEKGLEILS
LFVNMKKADL PEQAHSIIKE CKGSPLVVSL IGALLRDFPN RWDYYLRQLQ NKQFKRIRKS
SFYDYEALDE AMSISVEMLR EDIKDYYTDL SILQKDVKVP TKVIEGPTIL VIGYLWHVTF
DMVPKDIGRL RSISLRCREC KSLILVSIKG LILIFKFLKL FQDLHKKIVT QFQKHYQPHT
LSPDQEDCMY WYNFLAYHMA SASMHKELCA LMFSLDWIKA KTELVGPAHL IHEFVEYRHI
LDEKDCAVCE NFQEFLSLNG HLLGRQPFPN IVQLGLCEPE TSEVYQQAKL QAKQEVDHGM
LYLEWINKKN IKNLSRLVVR PHTDAVYHAC FSEDGQRIAS CGVDKTLQVF KAETGEKLLE
IKAHEDEVLC CAFSTDDRFI ATCSVDKKVK IWNSMTGGLV HVYDEHSEQV NCCHFTNNSH
YLLLATASSD CFLKLWDLNQ KECRNTMFGH TNSVNHCRFS PDDKLLASCS ADGTLKLWDV
KSANERKSIN VKQFFLNSEE PQEDMEVIVK CCSWSADGTR IMVAAKNKIF LFDIHTGGLL
AEIHTGHHST IQYCDFSPQN HLAVVALSQC CVELWNMDSC LKVADCRGHL SWVHCVMFSP
DGSSFLTSSD DQTIRLWETK KVCKNSAIVL KQEIDVVFQE NEVMVLAVDN IKRLQLINGK
TGQIDYLIEA QVSCCCLSPH LQYIAFGGED GAVEILELLN NRIFQSRIGH KKTVRHIQFT
DDGKTLISSS DDSSIQVWNW QSEEYVFLQA HQETVKDFKL LKNSKLLSWS FDGTVKKIWS
IITGRIEKDF VCHQDTVLSC DISPDATKFS STSADKTAKI WSFELLSPLH ELRGHKGCVR
CSVFSVDSTL LATGDDNGEI RIWNVSNGEL LHLCAPILVE EGAATHGGWV TDLCFSPDSK
MLVSAGGYLK WWNVVTGESS QTFYTNGTCL KKIHVSSDFK TYVTVDNLGI LYILQMLE


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