APAF_MOUSE
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 03-AUG-2022, entry version 183.
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; O88879; -.
DR PeptideAtlas; O88879; -.
DR PRIDE; O88879; -.
DR ProteomicsDB; 281790; -. [O88879-1]
DR ProteomicsDB; 281791; -. [O88879-2]
DR Antibodypedia; 17738; 732 antibodies from 46 providers.
DR DNASU; 11783; -.
DR Ensembl; ENSMUST00000020157; ENSMUSP00000020157; ENSMUSG00000019979. [O88879-1]
DR Ensembl; ENSMUST00000159110; ENSMUSP00000125291; ENSMUSG00000019979. [O88879-1]
DR GeneID; 11783; -.
DR KEGG; mmu:11783; -.
DR UCSC; uc007gtg.1; mouse. [O88879-1]
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 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 71 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 242 other tissues.
DR ExpressionAtlas; O88879; baseline and differential.
DR Genevisible; O88879; MM.
DR GO; GO:0043293; C:apoptosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; 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:0097202; P:activation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
DR GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; ISO:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
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; IC: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 Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 1.10.8.430; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR017251; Apaf-1.
DR InterPro; IPR041452; APAF1_C.
DR InterPro; IPR037963; APAF1_CARD_dom.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR024977; Apc4_WD40_dom.
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; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF12894; ANAPC4_WD40; 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; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 13.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF50978; SSF50978; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
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.
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
