ID   APAF_MOUSE              Reviewed;        1249 AA.
AC   O88879; A2RRK8;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   24-JAN-2024, entry version 190.
DE   RecName: Full=Apoptotic protease-activating factor 1;
DE            Short=APAF-1;
GN   Name=Apaf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RX   PubMed=9753320; DOI=10.1016/s0092-8674(00)81732-8;
RA   Cecconi F., Alvarez-Bolado G., Meyer B.I., Roth K.A., Gruss P.;
RT   "Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian
RT   development.";
RL   Cell 94:727-737(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Spleen;
RX   PubMed=11119689; DOI=10.1016/s0006-8993(00)02916-4;
RA   Walke D.W., Morgan J.I.;
RT   "A comparison of the expression and properties of Apaf-1 and Apaf-1L.";
RL   Brain Res. 886:73-81(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH APIP, AND DOMAIN.
RX   PubMed=15262985; DOI=10.1074/jbc.m405747200;
RA   Cho D.-H., Hong Y.-M., Lee H.-J., Woo H.-N., Pyo J.-O., Mak T.W.,
RA   Jung Y.-K.;
RT   "Induced inhibition of ischemic/hypoxic injury by APIP, a novel Apaf-1-
RT   interacting protein.";
RL   J. Biol. Chem. 279:39942-39950(2004).
RN   [5]
RP   INTERACTION WITH UACA.
RX   PubMed=15271982; DOI=10.1074/jbc.m402902200;
RA   Sakai T., Liu L., Teng X., Mukai-Sakai R., Shimada H., Kaji R., Mitani T.,
RA   Matsumoto M., Toida K., Ishimura K., Shishido Y., Mak T.W., Fukui K.;
RT   "Nucling recruits Apaf-1/pro-caspase-9 complex for the induction of stress-
RT   induced apoptosis.";
RL   J. Biol. Chem. 279:41131-41140(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), WD REPEATS, SUBUNIT, AND MUTAGENESIS
RP   OF ARG-265.
RX   PubMed=21827944; DOI=10.1016/j.str.2011.05.013;
RA   Reubold T.F., Wohlgemuth S., Eschenburg S.;
RT   "Crystal structure of full-length Apaf-1: how the death signal is relayed
RT   in the mitochondrial pathway of apoptosis.";
RL   Structure 19:1074-1083(2011).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Oligomerizes to a heptameric ring, known as the
CC       apoptosome, upon binding of cytochrome c and dATP. Oligomeric Apaf-1
CC       and pro-caspase-9 bind to each other via their respective NH2-terminal
CC       CARD domains and consecutively mature caspase-9 is released from the
CC       complex (By similarity). Interacts with UACA. It may also interact with
CC       Bcl-XL. Interacts with APIP. Interacts (via CARD and NACHT domains)
CC       with NAIP/BIRC1 (via NACHT domain) (By similarity). Interacts with
CC       CIAO2A (By similarity). {ECO:0000250|UniProtKB:O14727}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Apaf-1L;
CC         IsoId=O88879-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O88879-2; Sequence=VSP_006763;
CC   -!- TISSUE SPECIFICITY: Highly expressed in lung and spleen, weakly in
CC       brain and kidney and not detectable in liver.
CC   -!- DEVELOPMENTAL STAGE: High levels in embryonic brain and liver from 11.5
CC       dpc to 17.5 dpc.
CC   -!- DOMAIN: The CARD domain mediates interaction with APIP.
CC       {ECO:0000269|PubMed:15262985}.
CC   -!- DOMAIN: The monomeric form is autoinhibited in a closed conformation
CC       through a bound ADP at the nucleotide binding site. Exchange of ADP for
CC       ATP and binding of cytochrome c trigger a large conformational change
CC       where the first WD repeat region swings out, allowing the NB-ARC domain
CC       to rotate and expose the contact areas for oligomerization.
CC       {ECO:0000269|PubMed:15262985}.
CC   -!- MISCELLANEOUS: Physiological concentrations of calcium ions negatively
CC       affect the assembly of apoptosome by inhibiting nucleotide exchange in
CC       the monomeric form. {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform 1]: Major isoform.
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DR   EMBL; AF064071; AAC62458.1; -; mRNA.
DR   EMBL; BC131683; AAI31684.1; -; mRNA.
DR   EMBL; BC131684; AAI31685.1; -; mRNA.
DR   CCDS; CCDS36030.1; -. [O88879-1]
DR   CCDS; CCDS70095.1; -. [O88879-2]
DR   RefSeq; NP_001036023.1; NM_001042558.1. [O88879-1]
DR   RefSeq; NP_033814.2; NM_009684.2. [O88879-1]
DR   PDB; 3SFZ; X-ray; 3.00 A; A=1-1249.
DR   PDB; 3SHF; X-ray; 3.55 A; A=1-1249.
DR   PDBsum; 3SFZ; -.
DR   PDBsum; 3SHF; -.
DR   AlphaFoldDB; O88879; -.
DR   SMR; O88879; -.
DR   BioGRID; 198139; 3.
DR   ComplexPortal; CPX-3824; Apoptosome.
DR   CORUM; O88879; -.
DR   IntAct; O88879; 1.
DR   STRING; 10090.ENSMUSP00000020157; -.
DR   iPTMnet; O88879; -.
DR   PhosphoSitePlus; O88879; -.
DR   EPD; O88879; -.
DR   MaxQB; O88879; -.
DR   PaxDb; 10090-ENSMUSP00000020157; -.
DR   PeptideAtlas; O88879; -.
DR   ProteomicsDB; 281790; -. [O88879-1]
DR   ProteomicsDB; 281791; -. [O88879-2]
DR   Pumba; O88879; -.
DR   Antibodypedia; 17738; 846 antibodies from 46 providers.
DR   DNASU; 11783; -.
DR   Ensembl; ENSMUST00000020157.13; ENSMUSP00000020157.7; ENSMUSG00000019979.13. [O88879-1]
DR   Ensembl; ENSMUST00000159110.8; ENSMUSP00000125291.2; ENSMUSG00000019979.13. [O88879-1]
DR   GeneID; 11783; -.
DR   KEGG; mmu:11783; -.
DR   UCSC; uc007gtg.1; mouse. [O88879-1]
DR   AGR; MGI:1306796; -.
DR   CTD; 317; -.
DR   MGI; MGI:1306796; Apaf1.
DR   VEuPathDB; HostDB:ENSMUSG00000019979; -.
DR   eggNOG; KOG4155; Eukaryota.
DR   eggNOG; KOG4658; Eukaryota.
DR   GeneTree; ENSGT00940000157710; -.
DR   InParanoid; O88879; -.
DR   OMA; YHMANAN; -.
DR   OrthoDB; 2995530at2759; -.
DR   PhylomeDB; O88879; -.
DR   TreeFam; TF323866; -.
DR   Reactome; R-MMU-111458; Formation of apoptosome.
DR   Reactome; R-MMU-111459; Activation of caspases through apoptosome-mediated cleavage.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-9627069; Regulation of the apoptosome activity.
DR   BioGRID-ORCS; 11783; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; Apaf1; mouse.
DR   PRO; PR:O88879; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; O88879; Protein.
DR   Bgee; ENSMUSG00000019979; Expressed in granulocyte and 246 other cell types or tissues.
DR   ExpressionAtlas; O88879; baseline and differential.
DR   GO; GO:0043293; C:apoptosome; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IDA:MGI.
DR   GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0010659; P:cardiac muscle cell apoptotic process; ISO:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:Ensembl.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0097193; P:intrinsic apoptotic signaling pathway; NAS:ComplexPortal.
DR   GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0051402; P:neuron apoptotic process; IGI:MGI.
DR   GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IGI:MGI.
DR   GO; GO:1902510; P:regulation of apoptotic DNA fragmentation; IGI:MGI.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
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; 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; SSF50978; WD40 repeat-like; 2.
DR   PROSITE; PS50209; CARD; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 4.
DR   PROSITE; PS50082; WD_REPEATS_2; 9.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   Genevisible; O88879; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Apoptosis; ATP-binding; Calcium;
KW   Cytoplasm; Nucleotide-binding; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..1249
FT                   /note="Apoptotic protease-activating factor 1"
FT                   /id="PRO_0000050845"
FT   DOMAIN          1..90
FT                   /note="CARD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT   DOMAIN          106..415
FT                   /note="NB-ARC"
FT   REPEAT          613..652
FT                   /note="WD 1-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT                   ECO:0000269|PubMed:21827944"
FT   REPEAT          655..694
FT                   /note="WD 1-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT                   ECO:0000269|PubMed:21827944"
FT   REPEAT          697..738
FT                   /note="WD 1-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT                   ECO:0000269|PubMed:21827944"
FT   REPEAT          741..780
FT                   /note="WD 1-4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT                   ECO:0000269|PubMed:21827944"
FT   REPEAT          796..837
FT                   /note="WD 1-5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT                   ECO:0000269|PubMed:21827944"
FT   REPEAT          838..877
FT                   /note="WD 1-6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT                   ECO:0000269|PubMed:21827944"
FT   REPEAT          880..910
FT                   /note="WD 1-7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT                   ECO:0000269|PubMed:21827944"
FT   REPEAT          922..958
FT                   /note="WD 2-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT                   ECO:0000269|PubMed:21827944"
FT   REPEAT          959..998
FT                   /note="WD 2-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT                   ECO:0000269|PubMed:21827944"
FT   REPEAT          1001..1040
FT                   /note="WD 2-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT                   ECO:0000269|PubMed:21827944"
FT   REPEAT          1042..1080
FT                   /note="WD 2-4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT                   ECO:0000269|PubMed:21827944"
FT   REPEAT          1083..1122
FT                   /note="WD 2-5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT                   ECO:0000269|PubMed:21827944"
FT   REPEAT          1125..1164
FT                   /note="WD 2-6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT                   ECO:0000269|PubMed:21827944"
FT   REPEAT          1176..1213
FT                   /note="WD 2-7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT                   ECO:0000269|PubMed:21827944"
FT   REPEAT          1214..1249
FT                   /note="WD 2-8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT                   ECO:0000269|PubMed:21827944"
FT   REGION          910..921
FT                   /note="Interpropeller linker"
FT   BINDING         154..161
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         265
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   VAR_SEQ         99..110
FT                   /note="GKDTDGGITSFV -> A (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11119689"
FT                   /id="VSP_006763"
FT   MUTAGEN         265
FT                   /note="R->S: No stimulation of CASP9 activity."
FT                   /evidence="ECO:0000269|PubMed:21827944"
FT   CONFLICT        209
FT                   /note="E -> D (in Ref. 1; AAC62458)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        592
FT                   /note="R -> P (in Ref. 1; AAC62458)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        710
FT                   /note="K -> S (in Ref. 1; AAC62458)"
FT                   /evidence="ECO:0000305"
FT   HELIX           109..116
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           130..141
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   TURN            142..145
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          148..153
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           160..167
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           171..174
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   TURN            175..177
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          182..186
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           192..206
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   TURN            207..209
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           220..230
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          232..235
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          239..244
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           248..251
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          259..266
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   TURN            267..272
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           288..299
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           309..316
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   TURN            317..319
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           321..333
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          334..336
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           338..346
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           361..373
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   TURN            377..379
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           380..385
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           386..388
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           397..404
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           408..420
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          425..436
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           439..448
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           450..452
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           453..465
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   TURN            470..472
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           480..493
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           497..504
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           507..517
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           520..528
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   TURN            529..532
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           540..552
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   TURN            553..556
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          557..559
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           563..568
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           575..585
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          589..591
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           598..600
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          608..611
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          618..623
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          627..634
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          639..643
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   TURN            644..646
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          649..653
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          660..665
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          669..676
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          679..685
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   TURN            686..688
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          691..696
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          702..707
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          709..712
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          715..720
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          725..729
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          732..739
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          746..751
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          757..771
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           772..774
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          777..782
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          810..817
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          820..825
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   TURN            826..828
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          831..836
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          838..841
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          845..848
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          854..858
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          860..862
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          864..868
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   TURN            869..872
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          873..878
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          885..890
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          894..901
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          906..910
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   HELIX           911..915
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          919..931
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          934..953
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          956..959
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          964..969
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          973..980
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          986..989
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   TURN            990..992
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          996..998
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1009..1011
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1013..1016
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1018..1021
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1023..1030
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   TURN            1032..1034
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1047..1052
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1054..1071
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   TURN            1072..1075
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1079..1082
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1091..1093
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1095..1099
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1101..1103
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1114..1118
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1130..1135
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1137..1146
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1153..1159
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1183..1186
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1193..1203
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1205..1207
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1228..1230
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1233..1236
FT                   /evidence="ECO:0007829|PDB:3SFZ"
FT   STRAND          1242..1245
FT                   /evidence="ECO:0007829|PDB:3SFZ"
SQ   SEQUENCE   1249 AA;  141003 MW;  AA639E407F9ABC24 CRC64;
     MDAKARNCLL QHREALEKDI KTSYIMDHMI SNGVLSVIEE EKVKSQATQY QRAAALIKMI
     LNKDNCAYIS FYNALLHEGY KDLAALLQSG LPLVSSSSGK DTDGGITSFV RTVLCEGGVP
     QRPVIFVTRK KLVHAIQQKL WKLNGEPGWV TIYGMAGCGK SVLAAEAVRD HSLLEGCFSG
     GVHWVSIGKQ DKSGLLMKLQ NLCMRLDQEE SFSQRLPLNI EEAKDRLRVL MLRKHPRSLL
     ILDDVWDPWV LKAFDNQCQI LLTTRDKSVT DSVMGPKHVV PVESGLGREK GLEILSLFVN
     MKKEDLPAEA HSIIKECKGS PLVVSLIGAL LRDFPNRWAY YLRQLQNKQF KRIRKSSSYD
     YEALDEAMSI SVEMLREDIK DYYTDLSILQ KDVKVPTKVL CVLWDLETEE VEDILQEFVN
     KSLLFCNRNG KSFCYYLHDL QVDFLTEKNR SQLQDLHRKM VTQFQRYYQP HTLSPDQEDC
     MYWYNFLAYH MASANMHKEL CALMFSLDWI KAKTELVGPA HLIHEFVAYR HILDEKDCAV
     CENFQEFLSL NGHLLGRQPF PNIVQLGLCE PETSEVYRQA KLQAKQEGDT GRLYLEWINK
     KTIKNLSRLV VRPHTDAVYH ACFSQDGQRI ASCGADKTLQ VFKAETGEKL LDIKAHEDEV
     LCCAFSSDDS YIATCSADKK VKIWDSATGK LVHTYDEHSE QVNCCHFTNK SNHLLLATGS
     NDFFLKLWDL NQKECRNTMF GHTNSVNHCR FSPDDELLAS CSADGTLRLW DVRSANERKS
     INVKRFFLSS EDPPEDVEVI VKCCSWSADG DKIIVAAKNK VLLFDIHTSG LLAEIHTGHH
     STIQYCDFSP YDHLAVIALS QYCVELWNID SRLKVADCRG HLSWVHGVMF SPDGSSFLTA
     SDDQTIRVWE TKKVCKNSAI VLKQEIDVVF QENETMVLAV DNIRGLQLIA GKTGQIDYLP
     EAQVSCCCLS PHLEYVAFGD EDGAIKIIEL PNNRVFSSGV GHKKAVRHIQ FTADGKTLIS
     SSEDSVIQVW NWQTGDYVFL QAHQETVKDF RLLQDSRLLS WSFDGTVKVW NVITGRIERD
     FTCHQGTVLS CAISSDATKF SSTSADKTAK IWSFDLLSPL HELKGHNGCV RCSAFSLDGI
     LLATGDDNGE IRIWNVSDGQ LLHSCAPISV EEGTATHGGW VTDVCFSPDS KTLVSAGGYL
     KWWNVATGDS SQTFYTNGTN LKKIHVSPDF RTYVTVDNLG ILYILQVLE
//