E2F7_MOUSE
ID E2F7_MOUSE Reviewed; 904 AA.
AC Q6S7F2; B2RWZ8; Q8BRE2; Q8BSQ3; Q8C9R3;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Transcription factor E2F7;
DE Short=E2F-7;
GN Name=E2f7;
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), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=12893818; DOI=10.1074/jbc.m308105200;
RA de Bruin A., Maiti B., Jakoi L., Timmers C., Buerki R., Leone G.;
RT "Identification and characterization of E2F7, a novel mammalian E2F family
RT member capable of blocking cellular proliferation.";
RL J. Biol. Chem. 278:42041-42049(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Forelimb, Spleen, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [6]
RP FUNCTION.
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 [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22516201; DOI=10.1016/j.devcel.2012.01.013;
RA Ouseph M.M., Li J., Chen H.Z., Pecot T., Wenzel P., Thompson J.C.,
RA Comstock G., Chokshi V., Byrne M., Forde B., Chong J.L., Huang K.,
RA Machiraju R., de Bruin A., Leone G.;
RT "Atypical E2F repressors and activators coordinate placental development.";
RL Dev. Cell 22:849-862(2012).
RN [8]
RP FUNCTION.
RX PubMed=22802529; DOI=10.1101/gad.196238.112;
RA Aksoy O., Chicas A., Zeng T., Zhao Z., McCurrach M., Wang X., Lowe S.W.;
RT "The atypical E2F family member E2F7 couples the p53 and RB pathways during
RT cellular senescence.";
RL Genes Dev. 26:1546-1557(2012).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=23064264; DOI=10.1038/ncb2585;
RA Pandit S.K., Westendorp B., Nantasanti S., van Liere E., Tooten P.C.,
RA Cornelissen P.W., Toussaint M.J., Lamers W.H., de Bruin A.;
RT "E2F8 is essential for polyploidization in mammalian cells.";
RL Nat. Cell Biol. 14:1181-1191(2012).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23064266; DOI=10.1038/ncb2595;
RA Chen H.Z., Ouseph M.M., Li J., Pecot T., Chokshi V., Kent L., Bae S.,
RA Byrne M., Duran C., Comstock G., Trikha P., Mair M., Senapati S.,
RA Martin C.K., Gandhi S., Wilson N., Liu B., Huang Y.W., Thompson J.C.,
RA Raman S., Singh S., Leone M., Machiraju R., Huang K., Mo X., Fernandez S.,
RA Kalaszczynska I., Wolgemuth D.J., Sicinski P., Huang T., Jin V., Leone G.;
RT "Canonical and atypical E2Fs regulate the mammalian endocycle.";
RL Nat. Cell Biol. 14:1192-1202(2012).
RN [11]
RP FUNCTION, DNA-BINDING, AND DEVELOPMENTAL STAGE.
RX PubMed=22180533; DOI=10.1093/nar/gkr1203;
RA Westendorp B., Mokry M., Groot Koerkamp M.J., Holstege F.C., Cuppen E.,
RA de Bruin A.;
RT "E2F7 represses a network of oscillating cell cycle genes to control S-
RT phase progression.";
RL Nucleic Acids Res. 40:3511-3523(2012).
CC -!- FUNCTION: Atypical E2F transcription factor that participates in
CC various processes such as angiogenesis, polyploidization of specialized
CC cells and DNA damage response. Mainly acts as a transcription repressor
CC that binds DNA independently of DP proteins and specifically recognizes
CC the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses
CC transcription of classical E2F transcription factors such as E2F1. Acts
CC as a regulator of S-phase by recognizing and binding the E2-related
CC site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes.
CC Plays a key role in polyploidization of cells in placenta and liver by
CC regulating the endocycle, probably by repressing genes promoting
CC cytokinesis and antagonizing action of classical E2F proteins (E2F1,
CC E2F2 and/or E2F3). Required for placental development by promoting
CC polyploidization of trophoblast giant cells. Also involved in DNA
CC damage response: up-regulated by p53/TP53 following genotoxic stress
CC and acts as a downstream effector of p53/TP53-dependent repression by
CC mediating repression of indirect p53/TP53 target genes involved in DNA
CC replication. Acts as a promoter of sprouting angiogenesis, possibly by
CC acting as a transcription activator: associates with HIF1A, recognizes
CC and binds the VEGFA promoter, which is different from canonical E2
CC recognition site, and activates expression of the VEGFA gene. Acts as a
CC negative regulator of keratinocyte differentiation.
CC {ECO:0000269|PubMed:12893818, ECO:0000269|PubMed:18194653,
CC ECO:0000269|PubMed:22180533, ECO:0000269|PubMed:22516201,
CC ECO:0000269|PubMed:22802529, ECO:0000269|PubMed:22903062,
CC ECO:0000269|PubMed:23064264, ECO:0000269|PubMed:23064266}.
CC -!- SUBUNIT: Interacts with HIF1A (By similarity). Homodimer and
CC heterodimer: mainly forms homodimers and, to a lesser extent,
CC heterodimers with E2F8. Dimerization is important for DNA-binding.
CC Interacts with MN1 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q96AV8}.
CC -!- INTERACTION:
CC Q6S7F2; Q16665: HIF1A; Xeno; NbExp=3; IntAct=EBI-8030813, EBI-447269;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12893818}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6S7F2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6S7F2-2; Sequence=VSP_044618, VSP_044619;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in skin and
CC thymus and very low levels in brain, muscle and stomach. Expressed in
CC trophoblast giant cells throughout placenta development (at protein
CC level). {ECO:0000269|PubMed:12893818, ECO:0000269|PubMed:22516201,
CC ECO:0000269|PubMed:23064266}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during mid to late S-phase.
CC {ECO:0000269|PubMed:22180533}.
CC -!- INDUCTION: Induced at the onset of hepatocyte polyploidization.
CC {ECO:0000269|PubMed:23064264}.
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 (PubMed:12893818). {ECO:0000269|PubMed:12893818}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; mice develop normally and
CC live to old age. E2f7 and E2f8 double knockout embryos die by 11.5 dpc
CC of massive apoptosis and dilation of blood vessels and show increased
CC expression of E2f1 and Tp53, as well as many stress-related genes.
CC {ECO:0000269|PubMed:18194653}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32193.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY463359; AAR26542.1; -; mRNA.
DR EMBL; AK031078; BAC27243.1; -; mRNA.
DR EMBL; AK045040; BAC32193.1; ALT_FRAME; mRNA.
DR EMBL; AK041481; BAC30958.1; -; mRNA.
DR EMBL; AK143686; BAE25497.1; -; mRNA.
DR EMBL; CH466539; EDL21712.1; -; Genomic_DNA.
DR EMBL; BC145429; AAI45430.1; -; mRNA.
DR EMBL; BC150772; AAI50773.1; -; mRNA.
DR CCDS; CCDS36055.1; -. [Q6S7F2-1]
DR RefSeq; NP_848724.2; NM_178609.4. [Q6S7F2-1]
DR RefSeq; XP_006513945.1; XM_006513882.3.
DR AlphaFoldDB; Q6S7F2; -.
DR SMR; Q6S7F2; -.
DR IntAct; Q6S7F2; 1.
DR MINT; Q6S7F2; -.
DR STRING; 10090.ENSMUSP00000073453; -.
DR iPTMnet; Q6S7F2; -.
DR PhosphoSitePlus; Q6S7F2; -.
DR EPD; Q6S7F2; -.
DR MaxQB; Q6S7F2; -.
DR PaxDb; Q6S7F2; -.
DR PRIDE; Q6S7F2; -.
DR ProteomicsDB; 277702; -. [Q6S7F2-1]
DR ProteomicsDB; 277703; -. [Q6S7F2-2]
DR Antibodypedia; 29706; 181 antibodies from 32 providers.
DR DNASU; 52679; -.
DR Ensembl; ENSMUST00000073781; ENSMUSP00000073453; ENSMUSG00000020185. [Q6S7F2-1]
DR Ensembl; ENSMUST00000173471; ENSMUSP00000133494; ENSMUSG00000020185. [Q6S7F2-1]
DR GeneID; 52679; -.
DR KEGG; mmu:52679; -.
DR UCSC; uc007gzo.1; mouse. [Q6S7F2-2]
DR UCSC; uc007gzp.1; mouse. [Q6S7F2-1]
DR CTD; 144455; -.
DR MGI; MGI:1289147; E2f7.
DR VEuPathDB; HostDB:ENSMUSG00000020185; -.
DR eggNOG; KOG2578; Eukaryota.
DR GeneTree; ENSGT00940000157713; -.
DR HOGENOM; CLU_014845_1_0_1; -.
DR InParanoid; Q6S7F2; -.
DR OMA; EPDCTSA; -.
DR OrthoDB; 145070at2759; -.
DR PhylomeDB; Q6S7F2; -.
DR TreeFam; TF105567; -.
DR Reactome; R-MMU-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR BioGRID-ORCS; 52679; 4 hits in 73 CRISPR screens.
DR ChiTaRS; E2f7; mouse.
DR PRO; PR:Q6S7F2; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6S7F2; protein.
DR Bgee; ENSMUSG00000020185; Expressed in ear vesicle and 138 other tissues.
DR ExpressionAtlas; Q6S7F2; baseline and differential.
DR Genevisible; Q6S7F2; MM.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IDA: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; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0060718; P:chorionic trophoblast cell differentiation; IMP:UniProtKB.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0070365; P:hepatocyte differentiation; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0032466; P:negative regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0071930; P:negative regulation of transcription involved in G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0001890; P:placenta development; IMP:UniProtKB.
DR GO; GO:0032877; P:positive regulation of DNA endoreduplication; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IMP: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 Activator; Alternative splicing; Cell cycle; DNA damage; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..904
FT /note="Transcription factor E2F7"
FT /id="PRO_0000298908"
FT DNA_BIND 143..212
FT /evidence="ECO:0000255"
FT DNA_BIND 283..368
FT /evidence="ECO:0000255"
FT REGION 61..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AV8"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AV8"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AV8"
FT VAR_SEQ 376..421
FT /note="DEELLDVSASILPELKKEAYGQIRVCAKERLVRYGSFNTVHTSEKI -> GK
FT EMRSFDKDLWYIPFPSSTCRQQNWPFPVLPVTRNLRLMTSLLEQ (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_044618"
FT VAR_SEQ 422..904
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_044619"
FT CONFLICT 73
FT /note="V -> D (in Ref. 2; BAC27243)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="Y -> H (in Ref. 2; BAC32193)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="H -> L (in Ref. 3; AAI50773/AAI45430)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="L -> H (in Ref. 2; BAC27243)"
FT /evidence="ECO:0000305"
FT CONFLICT 776
FT /note="N -> D (in Ref. 2; BAC32193)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 904 AA; 99535 MW; 1EABCD1805FF80D2 CRC64;
MEVNCLTLKD LISPRQTRLD FAIEDAENAQ KENIFVDRSR MTPKTPMKNE PIDLSKQRIF
TPDRNPITPV KPVDRQPQVE PWTPTANLKM LISAASPDIR DREKKKELFR PIENKEDAFV
NSLQLDVAGD GAVDEYEKQR PSRKQKSLGL LCQKFLARYP SYPLSTEKTT ISLDEVAVSL
GVERRRIYDI VNVLESLHLV SRVAKNQYGW HGRHSLPKTL RTLQRLGEEQ KYEEQMACLQ
QKELDLMGYR FGERRKDGSP DPRDPHLLDF SEADYPSSSA NSRKDKSLRI MSQKFVMLFL
VSKTKIVTLD VAAKILIEES QDTPDHSKFK TKVRRLYDIA NVLTSLALIK KVHVTEERGR
KPAFKWIGPV DFSSIDEELL DVSASILPEL KKEAYGQIRV CAKERLVRYG SFNTVHTSEK
IQRKVSSEPS SPQGERQGSA YSLEIGSLAA IYRQKVEDNS QEEAFVSNTA VPPASILDPA
LSMDSEYCVK PLAQPVFSVA QTDLPAFSAQ NGPSGQVGVP VPSAASDTEN LKPALLAGQP
LVYVPSTQLF MLYGSVQEGL SPESRSEEDG GGSDVPADLS VTPSAQKRLC EERDPQEEED
EPAMKRQSQE FEDSPLSLVM PKKPSSSTDL ACPVTMGNGS SPPLEDACVK GQLPAAEEVT
GKAAPNCYVA SECGNPARNP DTEKPSNENE ITKDPSLMQY LYVQSPAGLN GFNMVLPGTQ
TPHTVAPSPA QLPSFGVPCM FLQSPGLGPF PVLYSPAIPG PISSAPGTHP NPGPMNFGLS
TLASASHLLI SPAAMVNPKP STLPCTDPQL RCQPSLNLNP VMPGSHGVIH PESPCYVRHP
VSMVKAEQSP APATPKSIQR RHRETFFKTP GSLGDPVFRR KERNQSRNTS SAQRRLEISS
SGPD
