ID   EHF_HUMAN               Reviewed;         300 AA.
AC   Q9NZC4; D3DR08; D3DR10; E9PSB2; Q9H509; Q9UKF9; Q9Y5V4; Q9Y5V5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 183.
DE   RecName: Full=ETS homologous factor;
DE            Short=hEHF;
DE   AltName: Full=ETS domain-containing transcription factor;
DE   AltName: Full=Epithelium-specific Ets transcription factor 3;
DE            Short=ESE-3;
GN   Name=EHF {ECO:0000312|HGNC:HGNC:3246};
GN   Synonyms=ESE3, ESE3B {ECO:0000312|EMBL:AAW80658.1},
GN   ESEJ {ECO:0000312|EMBL:AAF61670.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAF06998.1, ECO:0000312|PIR:JC7115}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ALTERNATIVE SPLICING
RP   (ISOFORM 2), AND TISSUE SPECIFICITY.
RC   TISSUE=Prostate {ECO:0000312|EMBL:AAF06998.1};
RX   PubMed=10527851; DOI=10.1006/bbrc.1999.1493;
RA   Kleinbaum L.A., Duggan C., Ferreira E., Coffey G.P., Buttice G.,
RA   Burton F.H.;
RT   "Human chromosomal localization, tissue/tumor expression, and regulatory
RT   function of the ets family gene EHF.";
RL   Biochem. Biophys. Res. Commun. 264:119-126(1999).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAD30991.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Prostate {ECO:0000312|EMBL:AAD30991.1};
RX   PubMed=10644770; DOI=10.1074/jbc.275.4.2986;
RA   Kas K., Finger E., Grall F., Gu X., Akbarali Y., Boltax J., Weiss A.,
RA   Oettgen P., Kapeller R., Libermann T.A.;
RT   "ESE-3, a novel member of an epithelium-specific ets transcription factor
RT   subfamily, demonstrates different target gene specificity from ESE-1.";
RL   J. Biol. Chem. 275:2986-2998(2000).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:AAF61670.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=11259407; DOI=10.1074/jbc.m010930200;
RA   Tugores A., Le J., Sorokina I., Snijders A.J., Duyao M., Reddy P.S.,
RA   Carlee L., Ronshaugen M., Mushegian A., Watanaskul T., Chu S., Buckler A.,
RA   Emtage S., McCormick M.K.;
RT   "The epithelium-specific ETS protein EHF/ESE-3 is a context-dependent
RT   transcriptional repressor downstream of MAPK signaling cascades.";
RL   J. Biol. Chem. 276:20397-20406(2001).
RN   [4] {ECO:0000305, ECO:0000312|EMBL:AAG35644.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Mitchell S.C., Levin E., Hubert R., Yeramian C., Saffran D.C., Afar D.E.H.;
RT   "Up-regulation of the epithelial-specific transcription factor Genes hEHF
RT   and ESX in advanced prostate cancer.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000305, ECO:0000312|EMBL:AAG35644.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Lei W., Harrod K.S.;
RT   "New human ESE3B coding sequence from H441 cells.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Trachea;
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   [7] {ECO:0000312|EMBL:CAC12701.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [8] {ECO:0000305, ECO:0000312|EMBL:AAG35644.1}
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   [9] {ECO:0000305, ECO:0000312|EMBL:AAH38995.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Skin {ECO:0000312|EMBL:AAH38995.1};
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   [10] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=12444029; DOI=10.1165/rcmb.2002-0011oc;
RA   Silverman E.S., Baron R.M., Palmer L.J., Le L., Hallock A., Subramaniam V.,
RA   Riese R.J., McKenna M.D., Gu X., Libermann T.A., Tugores A., Haley K.J.,
RA   Shore S., Drazen J.M., Weiss S.T.;
RT   "Constitutive and cytokine-induced expression of the ETS transcription
RT   factor ESE-3 in the lung.";
RL   Am. J. Respir. Cell Mol. Biol. 27:697-704(2002).
RN   [11] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=17027647; DOI=10.1016/j.bbrc.2006.09.102;
RA   Lim J.H., Cho J.-Y., Park Y.B., Park J.-W., Kwon T.K.;
RT   "ESE-3 transcription factor is involved in the expression of death receptor
RT   (DR)-5 through putative Ets sites.";
RL   Biochem. Biophys. Res. Commun. 350:736-741(2006).
RN   [12] {ECO:0000305}
RP   INDUCTION.
RX   PubMed=16380452; DOI=10.1182/blood-2005-06-2480;
RA   Appel S., Bringmann A., Grunebach F., Weck M.M., Bauer J., Brossart P.;
RT   "Epithelial-specific transcription factor ESE-3 is involved in the
RT   development of monocyte-derived DCs.";
RL   Blood 107:3265-3270(2006).
CC   -!- FUNCTION: Transcriptional activator that may play a role in regulating
CC       epithelial cell differentiation and proliferation. May act as a
CC       repressor for a specific subset of ETS/AP-1-responsive genes and as a
CC       modulator of the nuclear response to mitogen-activated protein kinase
CC       signaling cascades. Binds to DNA sequences containing the consensus
CC       nucleotide core sequence GGAA. Involved in regulation of TNFRSF10B/DR5
CC       expression through Ets-binding sequences on the TNFRSF10B/DR5 promoter.
CC       May contribute to development and carcinogenesis by acting as a tumor
CC       suppressor gene or anti-oncogene. {ECO:0000269|PubMed:10527851,
CC       ECO:0000269|PubMed:10644770, ECO:0000269|PubMed:11259407,
CC       ECO:0000269|PubMed:12444029, ECO:0000269|PubMed:17027647}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237,
CC       ECO:0000269|PubMed:11259407, ECO:0000269|PubMed:12444029}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000269|PubMed:10527851, ECO:0000269|PubMed:10644770,
CC       ECO:0000269|PubMed:11259407}; Synonyms=ESE-3B
CC       {ECO:0000269|PubMed:10644770};
CC         IsoId=Q9NZC4-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:10644770}; Synonyms=ESE-3A
CC       {ECO:0000269|PubMed:10644770};
CC         IsoId=Q9NZC4-2; Sequence=VSP_052190;
CC       Name=3;
CC         IsoId=Q9NZC4-3; Sequence=VSP_046373;
CC   -!- TISSUE SPECIFICITY: Expressed exclusively in tissues with a high
CC       content of epithelial cells. Highly expressed in salivary gland,
CC       mammary gland, prostate, and lung. Weakly expressed in kidney and
CC       colon. Not detected in heart, brain, placenta, liver, skeletal muscle,
CC       spleen, thymus, testis, ovary, small intestine or peripheral blood
CC       leukocytes. {ECO:0000269|PubMed:10527851, ECO:0000269|PubMed:10644770,
CC       ECO:0000269|PubMed:11259407, ECO:0000269|PubMed:12444029}.
CC   -!- INDUCTION: By IL1B/interleukin-1 beta and TNF in bronchial smooth
CC       muscle cells and fibroblasts. By IL10/interleukin-10 and IFNG/IFN-gamma
CC       in monocyte-derived dendritic cells. {ECO:0000269|PubMed:12444029,
CC       ECO:0000269|PubMed:16380452}.
CC   -!- DOMAIN: The PNT domain acts as a transcriptional activator.
CC       {ECO:0000250|UniProtKB:O70273}.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000255}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/40421/EHF";
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DR   EMBL; AF170583; AAF06998.1; -; mRNA.
DR   EMBL; AF124438; AAD30990.1; -; mRNA.
DR   EMBL; AF124439; AAD30991.1; -; mRNA.
DR   EMBL; AF212848; AAF61670.1; -; mRNA.
DR   EMBL; AF203977; AAG35644.1; -; mRNA.
DR   EMBL; AY882601; AAW80658.1; -; mRNA.
DR   EMBL; AK310867; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC087783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL157952; CAC12700.1; -; Genomic_DNA.
DR   EMBL; AL157952; CAC12701.1; -; Genomic_DNA.
DR   EMBL; CH471064; EAW68162.1; -; Genomic_DNA.
DR   EMBL; CH471064; EAW68163.1; -; Genomic_DNA.
DR   EMBL; CH471064; EAW68164.1; -; Genomic_DNA.
DR   EMBL; CH471064; EAW68165.1; -; Genomic_DNA.
DR   EMBL; CH471064; EAW68166.1; -; Genomic_DNA.
DR   EMBL; BC038995; AAH38995.1; -; mRNA.
DR   CCDS; CCDS55752.1; -. [Q9NZC4-3]
DR   CCDS; CCDS55753.1; -. [Q9NZC4-2]
DR   CCDS; CCDS7894.1; -. [Q9NZC4-1]
DR   PIR; JC7115; JC7115.
DR   RefSeq; NP_001193544.1; NM_001206615.1. [Q9NZC4-2]
DR   RefSeq; NP_001193545.1; NM_001206616.1. [Q9NZC4-3]
DR   RefSeq; NP_036285.2; NM_012153.5. [Q9NZC4-1]
DR   RefSeq; XP_005252917.1; XM_005252860.1.
DR   RefSeq; XP_005252919.1; XM_005252862.1.
DR   RefSeq; XP_011518286.1; XM_011519984.1.
DR   RefSeq; XP_011518287.1; XM_011519985.1.
DR   AlphaFoldDB; Q9NZC4; -.
DR   SMR; Q9NZC4; -.
DR   BioGRID; 117675; 10.
DR   IntAct; Q9NZC4; 4.
DR   MINT; Q9NZC4; -.
DR   STRING; 9606.ENSP00000435835; -.
DR   iPTMnet; Q9NZC4; -.
DR   PhosphoSitePlus; Q9NZC4; -.
DR   BioMuta; EHF; -.
DR   DMDM; 74762761; -.
DR   EPD; Q9NZC4; -.
DR   jPOST; Q9NZC4; -.
DR   MassIVE; Q9NZC4; -.
DR   MaxQB; Q9NZC4; -.
DR   PaxDb; 9606-ENSP00000435835; -.
DR   PeptideAtlas; Q9NZC4; -.
DR   ProteomicsDB; 23565; -.
DR   ProteomicsDB; 83362; -. [Q9NZC4-1]
DR   ProteomicsDB; 83363; -. [Q9NZC4-2]
DR   Antibodypedia; 13027; 162 antibodies from 22 providers.
DR   DNASU; 26298; -.
DR   Ensembl; ENST00000257831.8; ENSP00000257831.3; ENSG00000135373.13. [Q9NZC4-1]
DR   Ensembl; ENST00000450654.6; ENSP00000399733.2; ENSG00000135373.13. [Q9NZC4-2]
DR   Ensembl; ENST00000530286.5; ENSP00000433508.1; ENSG00000135373.13. [Q9NZC4-1]
DR   Ensembl; ENST00000531794.5; ENSP00000435835.1; ENSG00000135373.13. [Q9NZC4-3]
DR   Ensembl; ENST00000533754.5; ENSP00000435837.1; ENSG00000135373.13. [Q9NZC4-1]
DR   GeneID; 26298; -.
DR   KEGG; hsa:26298; -.
DR   MANE-Select; ENST00000257831.8; ENSP00000257831.3; NM_012153.6; NP_036285.2.
DR   UCSC; uc001mvr.3; human. [Q9NZC4-1]
DR   AGR; HGNC:3246; -.
DR   CTD; 26298; -.
DR   DisGeNET; 26298; -.
DR   GeneCards; EHF; -.
DR   HGNC; HGNC:3246; EHF.
DR   HPA; ENSG00000135373; Tissue enhanced (salivary).
DR   MIM; 605439; gene.
DR   neXtProt; NX_Q9NZC4; -.
DR   OpenTargets; ENSG00000135373; -.
DR   PharmGKB; PA27681; -.
DR   VEuPathDB; HostDB:ENSG00000135373; -.
DR   eggNOG; KOG3804; Eukaryota.
DR   GeneTree; ENSGT00940000159310; -.
DR   HOGENOM; CLU_048172_0_0_1; -.
DR   InParanoid; Q9NZC4; -.
DR   OrthoDB; 3686750at2759; -.
DR   PhylomeDB; Q9NZC4; -.
DR   TreeFam; TF318679; -.
DR   PathwayCommons; Q9NZC4; -.
DR   SignaLink; Q9NZC4; -.
DR   SIGNOR; Q9NZC4; -.
DR   BioGRID-ORCS; 26298; 13 hits in 1167 CRISPR screens.
DR   ChiTaRS; EHF; human.
DR   GeneWiki; EHF_(gene); -.
DR   GenomeRNAi; 26298; -.
DR   Pharos; Q9NZC4; Tbio.
DR   PRO; PR:Q9NZC4; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9NZC4; Protein.
DR   Bgee; ENSG00000135373; Expressed in parotid gland and 146 other cell types or tissues.
DR   ExpressionAtlas; Q9NZC4; baseline and differential.
DR   Genevisible; Q9NZC4; HS.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd08539; SAM_PNT-ESE-3-like; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR033071; EHF_SAM_Pointed_dom.
DR   InterPro; IPR000418; Ets_dom.
DR   InterPro; IPR046328; ETS_fam.
DR   InterPro; IPR003118; Pointed_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11849; ETS; 1.
DR   PANTHER; PTHR11849:SF171; ETS HOMOLOGOUS FACTOR; 1.
DR   Pfam; PF00178; Ets; 1.
DR   Pfam; PF02198; SAM_PNT; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SMART; SM00251; SAM_PNT; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   PROSITE; PS51433; PNT; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..300
FT                   /note="ETS homologous factor"
FT                   /id="PRO_0000257969"
FT   DOMAIN          29..115
FT                   /note="PNT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT   DNA_BIND        207..289
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   REGION          183..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1
FT                   /note="M -> MGLPERRGLVLLLSLAEILFKIM (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046373"
FT   VAR_SEQ         159..181
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10644770"
FT                   /id="VSP_052190"
FT   VARIANT         96
FT                   /note="A -> V (in dbSNP:rs9804460)"
FT                   /id="VAR_048941"
FT   CONFLICT        40
FT                   /note="G -> S (in Ref. 2; AAD30990/AAD30991)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="S -> G (in Ref. 2; AAD30991)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169
FT                   /note="A -> V (in Ref. 2; AAD30991)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196
FT                   /note="K -> E (in Ref. 1; AAF06998)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   300 AA;  34892 MW;  5CABB38BAF852ED0 CRC64;
     MILEGGGVMN LNPGNNLLHQ PPAWTDSYST CNVSSGFFGG QWHEIHPQYW TKYQVWEWLQ
     HLLDTNQLDA NCIPFQEFDI NGEHLCSMSL QEFTRAAGTA GQLLYSNLQH LKWNGQCSSD
     LFQSTHNVIV KTEQTEPSIM NTWKDENYLY DTNYGSTVDL LDSKTFCRAQ ISMTTTSHLP
     VAESPDMKKE QDPPAKCHTK KHNPRGTHLW EFIRDILLNP DKNPGLIKWE DRSEGVFRFL
     KSEAVAQLWG KKKNNSSMTY EKLSRAMRYY YKREILERVD GRRLVYKFGK NARGWRENEN
//