E4F1_MOUSE
ID E4F1_MOUSE Reviewed; 783 AA.
AC Q8CCE9; Q05BH7; Q3UNJ9; Q62065; Q6IR08; Q6PGI1; Q9QY56;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Transcription factor E4F1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q66K89};
DE AltName: Full=E4F transcription factor 1;
DE AltName: Full=Putative E3 ubiquitin-protein ligase E4F1;
DE AltName: Full=RING-type E3 ubiquitin transferase E4F1 {ECO:0000305};
DE AltName: Full=Transcription factor E4F;
DE AltName: Full=Transcription factor phi AP3;
DE AltName: Full=p120E4F;
GN Name=E4f1;
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).
RA Lebedeva T.V., Singh A.K.;
RT "Repression of the murine Il-1 beta expression by the murine analog of E4F
RT transcription factor.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 14-783 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic testis;
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 MRNA] (ISOFORMS 2 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 79-783 (ISOFORM 5).
RC STRAIN=C57BL/6J, FVB/N, and NMRI; TISSUE=Brain, and Mammary tumor;
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 [MRNA] OF 65-783 (ISOFORM 1), FUNCTION, DNA-BINDING,
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8262041; DOI=10.1002/j.1460-2075.1993.tb06192.x;
RA Fognani C., Della Valle G., Babiss L.E.;
RT "Repression of adenovirus E1A enhancer activity by a novel zinc finger-
RT containing DNA-binding protein related to the GLI-Kruppel protein.";
RL EMBO J. 12:4985-4992(1993).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9530632; DOI=10.1007/s003359900758;
RA Rooney R.J., Daniels R.R., Jenkins N.A., Gilbert D.J., Rothammer K.,
RA Morris S.W., Higgs D.R., Copeland N.G.;
RT "Chromosomal location and tissue expression of the gene encoding the
RT adenovirus E1A-regulated transcription factor E4F in humans and mice.";
RL Mamm. Genome 9:320-323(1998).
RN [6]
RP FUNCTION, AND INTERACTION WITH TP53.
RX PubMed=10644996; DOI=10.1038/sj.onc.1203250;
RA Sandy P., Gostissa M., Fogal V., Cecco L.D., Szalay K., Rooney R.J.,
RA Schneider C., Del Sal G.;
RT "p53 is involved in the p120E4F-mediated growth arrest.";
RL Oncogene 19:188-199(2000).
RN [7]
RP INTERACTION WITH RB1.
RX PubMed=10869426; DOI=10.1073/pnas.130198397;
RA Fajas L., Paul C., Zugasti O., Le Cam L., Polanowska J., Fabbrizio E.,
RA Medema R., Vignais M.-L., Sardet C.;
RT "pRB binds to and modulates the transrepressing activity of the E1A-
RT regulated transcription factor p120E4F.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:7738-7743(2000).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15226446; DOI=10.1128/mcb.24.14.6467-6475.2004;
RA Le Cam L., Lacroix M., Ciemerych M.A., Sardet C., Sicinski P.;
RT "The E4F protein is required for mitotic progression during embryonic cell
RT cycles.";
RL Mol. Cell. Biol. 24:6467-6475(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH ANP32A.
RX PubMed=17557114; DOI=10.1038/sj.embor.7400983;
RA Cvetanovic M., Rooney R.J., Garcia J.J., Toporovskaya N., Zoghbi H.Y.,
RA Opal P.;
RT "The role of LANP and ataxin 1 in E4F-mediated transcriptional
RT repression.";
RL EMBO Rep. 8:671-677(2007).
CC -!- FUNCTION: May function as a transcriptional repressor. May also
CC function as a ubiquitin ligase mediating ubiquitination of chromatin-
CC associated TP53. Functions in cell survival and proliferation through
CC control of the cell cycle. Functions in the p53 and pRB tumor
CC suppressor pathways and regulates the cyclin CCNA2 transcription.
CC {ECO:0000269|PubMed:10644996, ECO:0000269|PubMed:15226446,
CC ECO:0000269|PubMed:17557114, ECO:0000269|PubMed:8262041}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q66K89};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer; binds DNA as a dimer (By similarity). Forms a
CC complex with CDKN2A and TP53. Interacts with HDAC1, HMGA2 and RASSF1
CC (By similarity). Interactions with TP53, RB1, ANP32A and probably BMI1
CC and FHL2 regulate E4F1 activity. {ECO:0000250|UniProtKB:Q66K89,
CC ECO:0000269|PubMed:10644996, ECO:0000269|PubMed:10869426,
CC ECO:0000269|PubMed:17557114}.
CC -!- INTERACTION:
CC Q8CCE9; O35381: Anp32a; NbExp=2; IntAct=EBI-7450874, EBI-643140;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:15226446, ECO:0000269|PubMed:8262041}. Cytoplasm
CC {ECO:0000250}. Note=A small fraction is detected in the cytoplasm (By
CC similarity). Excluded from the nucleolus where it is targeted upon
CC CDKN2A overexpression. Localizes to the mitotic spindle during
CC embryogenesis. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8CCE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CCE9-2; Sequence=VSP_032196, VSP_032197;
CC Name=3;
CC IsoId=Q8CCE9-3; Sequence=VSP_032193;
CC Name=4;
CC IsoId=Q8CCE9-4; Sequence=VSP_032194, VSP_032195;
CC Name=5;
CC IsoId=Q8CCE9-5; Sequence=VSP_032192;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:8262041, ECO:0000269|PubMed:9530632}.
CC -!- DEVELOPMENTAL STAGE: Continuously expressed during embryogenesis.
CC {ECO:0000269|PubMed:9530632}.
CC -!- PTM: Phosphorylated; phosphorylation is cell cycle-dependent and
CC regulates DNA-binding activity and function.
CC {ECO:0000269|PubMed:8262041}.
CC -!- PTM: May be sumoylated by UBE2I upon interaction with CDKN2A.
CC {ECO:0000250|UniProtKB:Q66K89}.
CC -!- DISRUPTION PHENOTYPE: Death before 7.5 dpc probably at the peri-
CC implantation stage. Blastocysts display defects in mitotic progression
CC and chromosomal segregation and increased apoptosis.
CC {ECO:0000269|PubMed:15226446}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF22563.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH71228.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE25748.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA54188.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF126967; AAF22563.1; ALT_FRAME; mRNA.
DR EMBL; AK033285; BAC28222.1; -; mRNA.
DR EMBL; AK144176; BAE25748.1; ALT_INIT; mRNA.
DR EMBL; BC046459; AAH46459.1; -; mRNA.
DR EMBL; BC057011; AAH57011.1; -; mRNA.
DR EMBL; BC071228; AAH71228.1; ALT_FRAME; mRNA.
DR EMBL; X76858; CAA54188.1; ALT_INIT; mRNA.
DR CCDS; CCDS28481.1; -. [Q8CCE9-3]
DR PIR; S41688; S41688.
DR RefSeq; NP_001288713.1; NM_001301784.1. [Q8CCE9-1]
DR RefSeq; NP_031919.2; NM_007893.4. [Q8CCE9-3]
DR RefSeq; XP_011244570.1; XM_011246268.2. [Q8CCE9-5]
DR AlphaFoldDB; Q8CCE9; -.
DR SMR; Q8CCE9; -.
DR BioGRID; 199353; 4.
DR IntAct; Q8CCE9; 3.
DR MINT; Q8CCE9; -.
DR STRING; 10090.ENSMUSP00000062344; -.
DR iPTMnet; Q8CCE9; -.
DR PhosphoSitePlus; Q8CCE9; -.
DR EPD; Q8CCE9; -.
DR MaxQB; Q8CCE9; -.
DR PaxDb; Q8CCE9; -.
DR PRIDE; Q8CCE9; -.
DR ProteomicsDB; 277705; -. [Q8CCE9-1]
DR ProteomicsDB; 277706; -. [Q8CCE9-2]
DR ProteomicsDB; 277707; -. [Q8CCE9-3]
DR ProteomicsDB; 277708; -. [Q8CCE9-4]
DR ProteomicsDB; 277709; -. [Q8CCE9-5]
DR Antibodypedia; 23652; 112 antibodies from 18 providers.
DR DNASU; 13560; -.
DR Ensembl; ENSMUST00000056032; ENSMUSP00000062344; ENSMUSG00000024137. [Q8CCE9-3]
DR Ensembl; ENSMUST00000226941; ENSMUSP00000154444; ENSMUSG00000024137. [Q8CCE9-2]
DR GeneID; 13560; -.
DR KEGG; mmu:13560; -.
DR UCSC; uc008avy.2; mouse. [Q8CCE9-3]
DR UCSC; uc008awa.2; mouse. [Q8CCE9-1]
DR UCSC; uc008awb.2; mouse. [Q8CCE9-2]
DR UCSC; uc012ami.2; mouse. [Q8CCE9-5]
DR CTD; 1877; -.
DR MGI; MGI:109530; E4f1.
DR VEuPathDB; HostDB:ENSMUSG00000024137; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00840000129970; -.
DR HOGENOM; CLU_002678_50_0_1; -.
DR InParanoid; Q8CCE9; -.
DR OMA; MGNQIMK; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8CCE9; -.
DR TreeFam; TF315387; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 13560; 21 hits in 80 CRISPR screens.
DR ChiTaRS; E4f1; mouse.
DR PRO; PR:Q8CCE9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8CCE9; protein.
DR Bgee; ENSMUSG00000024137; Expressed in granulocyte and 272 other tissues.
DR ExpressionAtlas; Q8CCE9; baseline and differential.
DR Genevisible; Q8CCE9; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005819; C:spindle; IDA:MGI.
DR GO; GO:0035497; F:cAMP response element binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0010564; P:regulation of cell cycle process; IDA:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0009794; P:regulation of mitotic cell cycle, embryonic; IMP: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; TAS:MGI.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cytoplasm; DNA-binding;
KW Growth regulation; Metal-binding; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..783
FT /note="Transcription factor E4F1"
FT /id="PRO_0000324308"
FT ZN_FING 193..215
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 221..243
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 249..273
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 434..456
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 462..484
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 490..512
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 518..540
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 546..568
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 574..596
FT /note="C2H2-type 9; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 40..84
FT /note="Required for ubiquitin ligase activity"
FT /evidence="ECO:0000250"
FT REGION 185..264
FT /note="Mediates dimerization, DNA-binding, transcription
FT repression of CCNA2 and interaction with HMGA2"
FT /evidence="ECO:0000250"
FT REGION 368..565
FT /note="Mediates interaction with CDKN2A"
FT /evidence="ECO:0000250"
FT REGION 386..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..598
FT /note="Interaction with BMI1"
FT /evidence="ECO:0000250"
FT REGION 520..579
FT /note="Mediates interaction with TP53"
FT /evidence="ECO:0000250"
FT REGION 574..596
FT /note="Mediates interaction with RASSF1"
FT /evidence="ECO:0000250"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K89"
FT VAR_SEQ 244..274
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032192"
FT VAR_SEQ 422
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032193"
FT VAR_SEQ 458
FT /note="A -> VWQGLPQSLPAQEAPGGARARAPLPLWRLWEALQDHRSCAGPPACSL
FT RREAFPLSPVRQALQNQECPASTLPDTSGRKAPRVPVLQPRLPGEGLSGAACEAPHRRE
FT TFQVLQVWPWLRGAWHTQPAPAH (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032194"
FT VAR_SEQ 459..783
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032195"
FT VAR_SEQ 667..684
FT /note="DSHIMKVVQQIVHQAGAG -> RVWVRDGRITGLLGSPSG (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032196"
FT VAR_SEQ 685..783
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032197"
FT CONFLICT 13
FT /note="H -> D (in Ref. 2; BAE25748)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="R -> G (in Ref. 1; AAF22563, 2; BAE25748 and 3;
FT AAH46459/AAH71228)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="V -> VA (in Ref. 1; AAF22563 and 2; BAE25748)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="C -> F (in Ref. 2; BAE25748)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="V -> A (in Ref. 4; CAA54188)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="I -> V (in Ref. 4; CAA54188)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="V -> G (in Ref. 1; AAF22563, 2; BAE25748, 3;
FT AAH46459/AAH71228 and 4; CAA54188)"
FT /evidence="ECO:0000305"
FT CONFLICT 224..225
FT /note="KL -> NF (in Ref. 1; AAF22563)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="S -> N (in Ref. 1; AAF22563 and 2; BAE25748)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="V -> L (in Ref. 1; AAF22563)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="A -> V (in Ref. 1; AAF22563)"
FT /evidence="ECO:0000305"
FT CONFLICT 395..400
FT /note="PPSGSS -> LPFGST (in Ref. 1; AAF22563)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="P -> L (in Ref. 1; AAF22563)"
FT /evidence="ECO:0000305"
FT CONFLICT 479..480
FT /note="KH -> ND (in Ref. 4; CAA54188)"
FT /evidence="ECO:0000305"
FT CONFLICT 585..586
FT /note="EH -> DD (in Ref. 4; CAA54188)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="E -> Q (in Ref. 1; AAF22563, 2; BAE25748, 3;
FT AAH46459 and 4; CAA54188)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="T -> A (in Ref. 1; AAF22563, 2; BAE25748 and 4;
FT CAA54188)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 783 AA; 84296 MW; 59E47F7A64A224A4 CRC64;
MEGAMAVRVT AAHTAEARAE AGREAGEGGV AAAAALSSGG FLGLPAPFSE EDEDDVHRCG
RCQVEFTALE DFVQHKIQKT CHRAPQEALP TTPAATALLD QEVVPTAAEG GPDEPITVAH
IVVEATSLAE DISHAPDLVG SGHIKEVIVA AEAEPGDVEM AEAPGSPNHQ ELGLLGEGEQ
AHVKLLVNKE GRYVCMLCHK TFKTGSILKA HMVTHSSRKD HECKLCGASF RTKGSLIRHH
RRHTDERPYK CAKCGKSFRE SGALTRHLKS LTPCTEKIRF SISKDTAVGK EEVPAGSSAS
TVGTVTSSVA GDPMETSPVI HLVTDAKGTV IHEVHVQMQE LPLGMKALTP ESPDSEELPC
SSENSRENLL HQAMQNSGIV LERVAGEESA LEPAPPSGSS PQCLGDGSPE LPLLKVEQIE
TQVASEAATV PRTHPCPQCS ETFPTAATLE AHKRGHIAPR PFTCTQCGKA FPKAYLLKKH
QEVHVHERRF RCGDCGKLYK TIAHVRGHRR VHSDERPFPC PQCGKRYKTK NAQQVHFRTH
LEEKPHVCQF CSRGFREKGS LVRHVRHHTG EKPFKCYKCG RGFAEHGTLN RHLRTKGGCL
LEVEELLVSE ESPSAAATVL AEDPHTVLVE FSSVVADTQE YIIEATADDT ETSEATEIIE
GTQTEVDSHI MKVVQQIVHQ AGAGHQIIVQ NVTMDQETAL GSEATAADTI TIATPESLTE
QVAMTLASAI SEGTVLTARA GPNSTEQATV TMVSSEDIEI LEHGGELVIA SPEGQLEVQT
VIV
