E2F8_HUMAN
ID E2F8_HUMAN Reviewed; 867 AA.
AC A0AVK6; A8K9H3; Q2VPJ3; Q3C1U6; Q5BKY4; Q8N340; Q9H5M0;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Transcription factor E2F8;
DE Short=E2F-8;
GN Name=E2F8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Mammary gland, Skin, and Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-139.
RA Totoki Y., Yada T., Sakaki Y., Takeda T.;
RT "Identification of novel human genes predicted by combining multiple gene
RT finders.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=16179649; DOI=10.1093/nar/gki855;
RA Christensen J., Cloos P., Toftegaard U., Klinkenberg D., Bracken A.P.,
RA Trinh E., Heeran M., Di Stefano L., Helin K.;
RT "Characterization of E2F8, a novel E2F-like cell-cycle regulated repressor
RT of E2F-activated transcription.";
RL Nucleic Acids Res. 33:5458-5470(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-156 AND ARG-314.
RX PubMed=15897886; DOI=10.1038/sj.onc.1208703;
RA Logan N., Graham A., Zhao X., Fisher R., Maiti B., Leone G.,
RA La Thangue N.B.;
RT "E2F-8: an E2F family member with a similar organization of DNA-binding
RT domains to E2F-7.";
RL Oncogene 24:5000-5004(2005).
RN [7]
RP SUBUNIT.
RX PubMed=18194653; DOI=10.1016/j.devcel.2007.10.017;
RA Li J., Ran C., Li E., Gordon F., Comstock G., Siddiqui H., Cleghorn W.,
RA Chen H.-Z., Kornacker K., Liu C.-G., Pandit S.K., Khanizadeh M.,
RA Weinstein M., Leone G., de Bruin A.;
RT "Synergistic function of E2F7 and E2F8 is essential for cell survival and
RT embryonic development.";
RL Dev. Cell 14:62-75(2008).
RN [8]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF ARG-156 AND ARG-314.
RX PubMed=18202719; DOI=10.1038/sj.embor.7401158;
RA Zalmas L.P., Zhao X., Graham A.L., Fisher R., Reilly C., Coutts A.S.,
RA La Thangue N.B.;
RT "DNA-damage response control of E2F7 and E2F8.";
RL EMBO Rep. 9:252-259(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP FUNCTION, AND INTERACTION WITH HIF1A.
RX PubMed=22903062; DOI=10.1038/emboj.2012.231;
RA Weijts B.G., Bakker W.J., Cornelissen P.W., Liang K.H., Schaftenaar F.H.,
RA Westendorp B., de Wolf C.A., Paciejewska M., Scheele C.L., Kent L.,
RA Leone G., Schulte-Merker S., de Bruin A.;
RT "E2F7 and E2F8 promote angiogenesis through transcriptional activation of
RT VEGFA in cooperation with HIF1.";
RL EMBO J. 31:3871-3884(2012).
RN [11]
RP LACK OF RESPONSE TO DNA DAMAGE.
RX PubMed=22802528; DOI=10.1101/gad.184911.111;
RA Carvajal L.A., Hamard P.J., Tonnessen C., Manfredi J.J.;
RT "E2F7, a novel target, is up-regulated by p53 and mediates DNA damage-
RT dependent transcriptional repression.";
RL Genes Dev. 26:1533-1545(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-102; SER-413 AND
RP SER-417, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Atypical E2F transcription factor that participates in
CC various processes such as angiogenesis and polyploidization of
CC specialized cells. Mainly acts as a transcription repressor that binds
CC DNA independently of DP proteins and specifically recognizes the E2
CC recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of
CC classical E2F transcription factors such as E2F1: component of a
CC feedback loop in S phase by repressing the expression of E2F1, thereby
CC preventing p53/TP53-dependent apoptosis. Plays a key role in
CC polyploidization of cells in placenta and liver by regulating the
CC endocycle, probably by repressing genes promoting cytokinesis and
CC antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3).
CC Required for placental development by promoting polyploidization of
CC trophoblast giant cells. Acts as a promoter of sprouting angiogenesis,
CC possibly by acting as a transcription activator: associates with HIF1A,
CC recognizes and binds the VEGFA promoter, which is different from
CC canonical E2 recognition site, and activates expression of the VEGFA
CC gene. {ECO:0000269|PubMed:15897886, ECO:0000269|PubMed:16179649,
CC ECO:0000269|PubMed:18202719, ECO:0000269|PubMed:22903062}.
CC -!- SUBUNIT: Homodimer and heterodimer: mainly forms homodimers and, to a
CC lesser extent, heterodimers with E2F8. Dimerization is important for
CC DNA-binding. Interacts with HIF1A. {ECO:0000269|PubMed:18194653,
CC ECO:0000269|PubMed:18202719, ECO:0000269|PubMed:22903062}.
CC -!- INTERACTION:
CC A0AVK6; P07550: ADRB2; NbExp=3; IntAct=EBI-7779316, EBI-491169;
CC A0AVK6; Q92870-2: APBB2; NbExp=3; IntAct=EBI-7779316, EBI-21535880;
CC A0AVK6; P46379-2: BAG6; NbExp=3; IntAct=EBI-7779316, EBI-10988864;
CC A0AVK6; P55212: CASP6; NbExp=3; IntAct=EBI-7779316, EBI-718729;
CC A0AVK6; O14645: DNALI1; NbExp=3; IntAct=EBI-7779316, EBI-395638;
CC A0AVK6; Q96AV8: E2F7; NbExp=4; IntAct=EBI-7779316, EBI-1386765;
CC A0AVK6; P22607: FGFR3; NbExp=3; IntAct=EBI-7779316, EBI-348399;
CC A0AVK6; Q13643: FHL3; NbExp=3; IntAct=EBI-7779316, EBI-741101;
CC A0AVK6; Q14957: GRIN2C; NbExp=3; IntAct=EBI-7779316, EBI-8285963;
CC A0AVK6; P06396: GSN; NbExp=3; IntAct=EBI-7779316, EBI-351506;
CC A0AVK6; P01112: HRAS; NbExp=3; IntAct=EBI-7779316, EBI-350145;
CC A0AVK6; P42858: HTT; NbExp=12; IntAct=EBI-7779316, EBI-466029;
CC A0AVK6; O14901: KLF11; NbExp=3; IntAct=EBI-7779316, EBI-948266;
CC A0AVK6; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-7779316, EBI-16439278;
CC A0AVK6; Q7Z412: PEX26; NbExp=3; IntAct=EBI-7779316, EBI-752057;
CC A0AVK6; P37840: SNCA; NbExp=3; IntAct=EBI-7779316, EBI-985879;
CC A0AVK6; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-7779316, EBI-357085;
CC A0AVK6; Q12800: TFCP2; NbExp=3; IntAct=EBI-7779316, EBI-717422;
CC A0AVK6; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-7779316, EBI-741480;
CC A0AVK6; Q9Y649; NbExp=3; IntAct=EBI-7779316, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15897886}.
CC -!- INDUCTION: Following DNA damage (PubMed:18202719). Up-regulation in
CC response to DNA damage is not confirmed by PubMed:22802528.
CC {ECO:0000269|PubMed:18202719}.
CC -!- DOMAIN: In contrast to classical members of the E2F transcription
CC factor, atypical members contain 2 DNA-binding domains and regulate
CC transcription in a DP-independent manner. Both DNA-binding domains are
CC required for DNA-binding and are proposed to form an intramolecular
CC structure that is similar to the winged helix structure of the E2F-DP
CC heterodimer (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH28244.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15605.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK026964; BAB15605.1; ALT_INIT; mRNA.
DR EMBL; AK292688; BAF85377.1; -; mRNA.
DR EMBL; CH471064; EAW68354.1; -; Genomic_DNA.
DR EMBL; BC028244; AAH28244.2; ALT_INIT; mRNA.
DR EMBL; BC090877; AAH90877.1; -; mRNA.
DR EMBL; BC108700; AAI08701.1; -; mRNA.
DR EMBL; BC126400; AAI26401.1; -; mRNA.
DR EMBL; BC126402; AAI26403.1; -; mRNA.
DR EMBL; AB231781; BAE46901.1; -; mRNA.
DR CCDS; CCDS7849.1; -.
DR RefSeq; NP_001243300.1; NM_001256371.1.
DR RefSeq; NP_001243301.1; NM_001256372.1.
DR RefSeq; NP_078956.2; NM_024680.3.
DR PDB; 4YO2; X-ray; 3.07 A; A=110-341.
DR PDBsum; 4YO2; -.
DR AlphaFoldDB; A0AVK6; -.
DR SMR; A0AVK6; -.
DR BioGRID; 122847; 20.
DR IntAct; A0AVK6; 25.
DR MINT; A0AVK6; -.
DR STRING; 9606.ENSP00000481103; -.
DR ChEMBL; CHEMBL4630726; -.
DR GlyGen; A0AVK6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; A0AVK6; -.
DR PhosphoSitePlus; A0AVK6; -.
DR BioMuta; E2F8; -.
DR EPD; A0AVK6; -.
DR jPOST; A0AVK6; -.
DR MassIVE; A0AVK6; -.
DR MaxQB; A0AVK6; -.
DR PaxDb; A0AVK6; -.
DR PeptideAtlas; A0AVK6; -.
DR PRIDE; A0AVK6; -.
DR ProteomicsDB; 24; -.
DR Antibodypedia; 25218; 206 antibodies from 32 providers.
DR DNASU; 79733; -.
DR Ensembl; ENST00000250024.9; ENSP00000250024.4; ENSG00000129173.13.
DR Ensembl; ENST00000527884.5; ENSP00000434199.1; ENSG00000129173.13.
DR Ensembl; ENST00000620009.4; ENSP00000481103.1; ENSG00000129173.13.
DR GeneID; 79733; -.
DR KEGG; hsa:79733; -.
DR MANE-Select; ENST00000250024.9; ENSP00000250024.4; NM_024680.4; NP_078956.2.
DR UCSC; uc001mpm.4; human.
DR CTD; 79733; -.
DR DisGeNET; 79733; -.
DR GeneCards; E2F8; -.
DR HGNC; HGNC:24727; E2F8.
DR HPA; ENSG00000129173; Tissue enhanced (bone marrow, lymphoid tissue, skeletal muscle).
DR MIM; 612047; gene.
DR neXtProt; NX_A0AVK6; -.
DR OpenTargets; ENSG00000129173; -.
DR PharmGKB; PA142671918; -.
DR VEuPathDB; HostDB:ENSG00000129173; -.
DR eggNOG; KOG2578; Eukaryota.
DR GeneTree; ENSGT00940000158651; -.
DR HOGENOM; CLU_014845_2_0_1; -.
DR InParanoid; A0AVK6; -.
DR OMA; NGHTEMC; -.
DR OrthoDB; 145070at2759; -.
DR PhylomeDB; A0AVK6; -.
DR TreeFam; TF105567; -.
DR PathwayCommons; A0AVK6; -.
DR Reactome; R-HSA-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR SignaLink; A0AVK6; -.
DR BioGRID-ORCS; 79733; 26 hits in 1115 CRISPR screens.
DR ChiTaRS; E2F8; human.
DR GenomeRNAi; 79733; -.
DR Pharos; A0AVK6; Tbio.
DR PRO; PR:A0AVK6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; A0AVK6; protein.
DR Bgee; ENSG00000129173; Expressed in biceps brachii and 126 other tissues.
DR ExpressionAtlas; A0AVK6; baseline and differential.
DR Genevisible; A0AVK6; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0033301; P:cell cycle comprising mitosis without cytokinesis; ISS:UniProtKB.
DR GO; GO:0060718; P:chorionic trophoblast cell differentiation; ISS:UniProtKB.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0070365; P:hepatocyte differentiation; ISS:UniProtKB.
DR GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0001890; P:placenta development; ISS:UniProtKB.
DR GO; GO:0032877; P:positive regulation of DNA endoreduplication; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR015633; E2F.
DR InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12081; PTHR12081; 1.
DR Pfam; PF02319; E2F_TDP; 2.
DR SMART; SM01372; E2F_TDP; 2.
DR SUPFAM; SSF46785; SSF46785; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cell cycle; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..867
FT /note="Transcription factor E2F8"
FT /id="PRO_0000298909"
FT DNA_BIND 113..182
FT /evidence="ECO:0000255"
FT DNA_BIND 261..347
FT /evidence="ECO:0000255"
FT REGION 38..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 674
FT /note="I -> V (in dbSNP:rs793274)"
FT /id="VAR_034735"
FT MUTAGEN 156
FT /note="R->A: Loss of DNA-binding and inhibition of E2F1-
FT dependent activation. Impairs DNA-binding and dimerization;
FT when associated with A-314."
FT /evidence="ECO:0000269|PubMed:15897886,
FT ECO:0000269|PubMed:18202719"
FT MUTAGEN 314
FT /note="R->A: Loss of DNA-binding and inhibition of E2F1-
FT dependent activation. Impairs DNA-binding and dimerization;
FT when associated with A-156."
FT /evidence="ECO:0000269|PubMed:15897886,
FT ECO:0000269|PubMed:18202719"
FT CONFLICT 138
FT /note="N -> I (in Ref. 4; BAE46901)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="K -> R (in Ref. 1; BAB15605)"
FT /evidence="ECO:0000305"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4YO2"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:4YO2"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:4YO2"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:4YO2"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:4YO2"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:4YO2"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4YO2"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:4YO2"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:4YO2"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:4YO2"
FT HELIX 286..296
FT /evidence="ECO:0007829|PDB:4YO2"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:4YO2"
FT HELIX 308..321
FT /evidence="ECO:0007829|PDB:4YO2"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:4YO2"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:4YO2"
SQ SEQUENCE 867 AA; 94166 MW; AADBCFACB888BD93 CRC64;
MENEKENLFC EPHKRGLMKT PLKESTTANI VLAEIQPDFG PLTTPTKPKE GSQGEPWTPT
ANLKMLISAV SPEIRNRDQK RGLFDNRSGL PEAKDCIHEH LSGDEFEKSQ PSRKEKSLGL
LCHKFLARYP NYPNPAVNND ICLDEVAEEL NVERRRIYDI VNVLESLHMV SRLAKNRYTW
HGRHNLNKTL GTLKSIGEEN KYAEQIMMIK KKEYEQEFDF IKSYSIEDHI IKSNTGPNGH
PDMCFVELPG VEFRAASVNS RKDKSLRVMS QKFVMLFLVS TPQIVSLEVA AKILIGEDHV
EDLDKSKFKT KIRRLYDIAN VLSSLDLIKK VHVTEERGRK PAFKWTGPEI SPNTSGSSPV
IHFTPSDLEV RRSSKENCAK NLFSTRGKPN FTRHPSLIKL VKSIESDRRK INSAPSSPIK
TNKAESSQNS APFPSKMAQL AAICKMQLEE QSSESRQKVK VQLARSGPCK PVAPLDPPVN
AEMELTAPSL IQPLGMVPLI PSPLSSAVPL ILPQAPSGPS YAIYLQPTQA HQSVTPPQGL
SPTVCTTHSS KATGSKDSTD ATTEKAANDT SKASASTRPG SLLPAPERQG AKSRTREPAG
ERGSKRASML EDSGSKKKFK EDLKGLENVS ATLFPSGYLI PLTQCSSLGA ESILSGKENS
SALSPNHRIY SSPIAGVIPV TSSELTAVNF PSFHVTPLKL MVSPTSVAAV PVGNSPALAS
SHPVPIQNPS SAIVNFTLQH LGLISPNVQL SASPGSGIVP VSPRIESVNV APENAGTQQG
RATNYDSPVP GQSQPNGQSV AVTGAQQPVP VTPKGSQLVA ESFFRTPGGP TKPTSSSCMD
FEGANKTSLG TLFVPQRKLE VSTEDVH
