ID ELF2_HUMAN Reviewed; 593 AA. AC Q15723; E9PCX3; Q15724; Q15725; Q6P1K5; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 2. DT 27-MAR-2024, entry version 197. DE RecName: Full=ETS-related transcription factor Elf-2; DE AltName: Full=E74-like factor 2; DE AltName: Full=New ETS-related factor; GN Name=ELF2 {ECO:0000312|EMBL:AAF67195.1}; GN Synonyms=NERF {ECO:0000303|PubMed:8756667}; 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:AAB37759.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 5), FUNCTION, AND TISSUE RP SPECIFICITY. RC TISSUE=Fetal brain {ECO:0000269|PubMed:8756667}, Fetal liver RC {ECO:0000269|PubMed:8756667}, and Spleen RC {ECO:0000312|EMBL:AAB37759.1}; RX PubMed=8756667; DOI=10.1128/mcb.16.9.5091; RA Oettgen P., Akbarali Y., Boltax J., Best J., Kunsch C., Libermann T.A.; RT "Characterization of NERF, a novel transcription factor related to the Ets RT factor ELF-1."; RL Mol. Cell. Biol. 16:5091-5106(1996). RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF67195.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Chronic myeloid leukemia cell; RA Wilkinson D.A., Neale G.A.M., Mao S., Fernandes E.R., Davenport J.W., RA Naeve C.W., Goorha R.M.; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH34951.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4). RC TISSUE=Testis {ECO:0000312|EMBL:AAH34951.1}; 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 [5] {ECO:0000305} RP INTERACTION WITH RUNX1. RX PubMed=10207087; DOI=10.1128/mcb.19.5.3635; RA Mao S., Frank R.C., Zhang J., Miyazaki Y., Nimer S.D.; RT "Functional and physical interactions between AML1 proteins and an ETS RT protein, MEF: implications for the pathogenesis of t(8;21)-positive RT leukemias."; RL Mol. Cell. Biol. 19:3635-3644(1999). RN [6] {ECO:0000305} RP FUNCTION, AND INTERACTION WITH RUNX1. RX PubMed=14970218; DOI=10.1074/jbc.m309074200; RA Cho J.-Y., Akbarali Y., Zerbini L.F., Gu X., Boltax J., Wang Y., RA Oettgen P., Zhang D.-E., Libermann T.A.; RT "Isoforms of the Ets transcription factor NERF/ELF-2 physically interact RT with AML1 and mediate opposing effects on AML1-mediated transcription of RT the B cell-specific blk gene."; RL J. Biol. Chem. 279:19512-19522(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-430, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-185; SER-191; RP SER-363 AND THR-521, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-494, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-536, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). CC -!- FUNCTION: Isoform 1 transcriptionally activates the LYN and BLK CC promoters and acts synergistically with RUNX1 to transactivate the BLK CC promoter. CC -!- FUNCTION: Isoform 2 may function in repression of RUNX1-mediated CC transactivation. CC -!- SUBUNIT: Interacts with the LIM domains of LMO2 (By similarity). CC Interacts via its N-terminal region with RUNX1. CC {ECO:0000250|UniProtKB:Q9JHC9, ECO:0000269|PubMed:10207087, CC ECO:0000269|PubMed:14970218}. CC -!- INTERACTION: CC Q15723; Q01196: RUNX1; NbExp=2; IntAct=EBI-956941, EBI-925904; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=5 {ECO:0000269|PubMed:8756667}; Synonyms=NERF-2b CC {ECO:0000303|PubMed:8756667}; CC IsoId=Q15723-5; Sequence=Displayed; CC Name=1 {ECO:0000269|PubMed:8756667}; Synonyms=NERF-2 CC {ECO:0000303|PubMed:8756667}, NERF-2a {ECO:0000303|PubMed:8756667}; CC IsoId=Q15723-1; Sequence=VSP_014155; CC Name=2 {ECO:0000269|PubMed:8756667}; Synonyms=NERF-1a CC {ECO:0000303|PubMed:8756667}; CC IsoId=Q15723-2; Sequence=VSP_014154, VSP_014155; CC Name=3 {ECO:0000269|PubMed:8756667}; Synonyms=NERF-1b CC {ECO:0000303|PubMed:8756667}; CC IsoId=Q15723-3; Sequence=VSP_014154; CC Name=4 {ECO:0000305}; CC IsoId=Q15723-4; Sequence=VSP_014154, VSP_014156; CC -!- TISSUE SPECIFICITY: Expressed in all fetal and adult tissues examined. CC Among fetal tissues, highest levels of expression detected in heart, CC lung, liver and kidney, and lower levels in brain. Among adult tissues, CC highest levels of expression detected in heart, placenta, lung, CC skeletal muscle, spleen, thymus, testis and ovary. Moderate expression CC in prostate, small intestine, kidney, liver and pancreas, and weak CC expression in colon, brain and peripheral blood lymphocytes. CC {ECO:0000269|PubMed:8756667}. CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000255}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH65025.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U43188; AAB37759.1; -; mRNA. DR EMBL; U43189; AAB37760.1; -; mRNA. DR EMBL; U43189; AAB37761.1; -; mRNA. DR EMBL; AF256222; AAF67195.1; -; mRNA. DR EMBL; AF256223; AAF67196.1; -; mRNA. DR EMBL; AC024032; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC093602; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC034951; AAH34951.1; -; mRNA. DR EMBL; BC065025; AAH65025.1; ALT_FRAME; mRNA. DR CCDS; CCDS3744.1; -. [Q15723-1] DR CCDS; CCDS3745.1; -. [Q15723-3] DR CCDS; CCDS64062.1; -. [Q15723-2] DR CCDS; CCDS64063.1; -. [Q15723-4] DR CCDS; CCDS82954.1; -. [Q15723-5] DR PIR; G02318; G02318. DR RefSeq; NP_001263386.1; NM_001276457.1. [Q15723-4] DR RefSeq; NP_001263387.1; NM_001276458.1. [Q15723-2] DR RefSeq; NP_001263388.1; NM_001276459.1. DR RefSeq; NP_001317965.1; NM_001331036.1. [Q15723-5] DR RefSeq; NP_006865.1; NM_006874.3. [Q15723-3] DR RefSeq; NP_973728.1; NM_201999.2. [Q15723-1] DR RefSeq; XP_005262861.1; XM_005262804.2. DR AlphaFoldDB; Q15723; -. DR SMR; Q15723; -. DR BioGRID; 108313; 145. DR IntAct; Q15723; 117. DR MINT; Q15723; -. DR STRING; 9606.ENSP00000368868; -. DR GlyCosmos; Q15723; 23 sites, 2 glycans. DR GlyGen; Q15723; 28 sites, 2 O-linked glycans (28 sites). DR iPTMnet; Q15723; -. DR PhosphoSitePlus; Q15723; -. DR BioMuta; ELF2; -. DR DMDM; 68052029; -. DR EPD; Q15723; -. DR jPOST; Q15723; -. DR MassIVE; Q15723; -. DR MaxQB; Q15723; -. DR PaxDb; 9606-ENSP00000377782; -. DR PeptideAtlas; Q15723; -. DR ProteomicsDB; 19535; -. DR ProteomicsDB; 60718; -. [Q15723-5] DR ProteomicsDB; 60719; -. [Q15723-1] DR ProteomicsDB; 60720; -. [Q15723-2] DR ProteomicsDB; 60721; -. [Q15723-3] DR ProteomicsDB; 60722; -. [Q15723-4] DR Pumba; Q15723; -. DR Antibodypedia; 896; 171 antibodies from 26 providers. DR DNASU; 1998; -. DR Ensembl; ENST00000358635.7; ENSP00000351458.2; ENSG00000109381.21. [Q15723-3] DR Ensembl; ENST00000379549.7; ENSP00000368867.2; ENSG00000109381.21. [Q15723-4] DR Ensembl; ENST00000379550.5; ENSP00000368868.1; ENSG00000109381.21. [Q15723-5] DR Ensembl; ENST00000394235.6; ENSP00000377782.1; ENSG00000109381.21. [Q15723-1] DR Ensembl; ENST00000510408.5; ENSP00000426997.1; ENSG00000109381.21. [Q15723-2] DR Ensembl; ENST00000686138.1; ENSP00000510098.1; ENSG00000109381.21. [Q15723-5] DR GeneID; 1998; -. DR KEGG; hsa:1998; -. DR MANE-Select; ENST00000686138.1; ENSP00000510098.1; NM_001331036.3; NP_001317965.1. DR UCSC; uc003ihm.3; human. [Q15723-5] DR AGR; HGNC:3317; -. DR CTD; 1998; -. DR DisGeNET; 1998; -. DR GeneCards; ELF2; -. DR HGNC; HGNC:3317; ELF2. DR HPA; ENSG00000109381; Low tissue specificity. DR MIM; 619798; gene. DR neXtProt; NX_Q15723; -. DR OpenTargets; ENSG00000109381; -. DR PharmGKB; PA27745; -. DR VEuPathDB; HostDB:ENSG00000109381; -. DR eggNOG; KOG3804; Eukaryota. DR GeneTree; ENSGT00940000154953; -. DR HOGENOM; CLU_027279_2_0_1; -. DR InParanoid; Q15723; -. DR OMA; SSHVHCT; -. DR OrthoDB; 4245771at2759; -. DR PhylomeDB; Q15723; -. DR TreeFam; TF318679; -. DR PathwayCommons; Q15723; -. DR Reactome; R-HSA-8939245; RUNX1 regulates transcription of genes involved in BCR signaling. DR SignaLink; Q15723; -. DR SIGNOR; Q15723; -. DR BioGRID-ORCS; 1998; 61 hits in 1193 CRISPR screens. DR ChiTaRS; ELF2; human. DR GeneWiki; ELF2; -. DR GenomeRNAi; 1998; -. DR Pharos; Q15723; Tbio. DR PRO; PR:Q15723; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q15723; Protein. DR Bgee; ENSG00000109381; Expressed in calcaneal tendon and 195 other cell types or tissues. DR ExpressionAtlas; Q15723; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. 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; IDA:NTNU_SB. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR000418; Ets_dom. DR InterPro; IPR046328; ETS_fam. DR InterPro; IPR022084; TF_Elf_N. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR11849; ETS; 1. DR PANTHER; PTHR11849:SF10; ETS-RELATED TRANSCRIPTION FACTOR ELF-2; 1. DR Pfam; PF12310; Elf-1_N; 1. DR Pfam; PF00178; Ets; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS00345; ETS_DOMAIN_1; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. DR Genevisible; Q15723; HS. PE 1: Evidence at protein level; KW Activator; Alternative splicing; DNA-binding; Isopeptide bond; Methylation; KW Nucleus; Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..593 FT /note="ETS-related transcription factor Elf-2" FT /id="PRO_0000204087" FT DNA_BIND 208..290 FT /note="ETS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237" FT REGION 146..201 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 146..165 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 107 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 182 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9JHC9" FT MOD_RES 185 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 191 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 363 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 372 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 376 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9JHC9" FT MOD_RES 430 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 494 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 521 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 536 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447" FT VAR_SEQ 1..79 FT /note="MTSAVVDSGGTILELSSNGVENQEESEKVSEYPAVIVEPVPSARLEQGYAAQ FT VLVYDDETYMMQDVAEEQEVETENVET -> MATSLHEGPTNQLDLLIRA (in FT isoform 2, isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8756667, ECO:0000303|Ref.2" FT /id="VSP_014154" FT VAR_SEQ 117..129 FT /note="PVEVFVPPCVSTP -> P (in isoform 1 and isoform 2)" FT /evidence="ECO:0000303|PubMed:8756667, ECO:0000303|Ref.2" FT /id="VSP_014155" FT VAR_SEQ 175..203 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014156" SQ SEQUENCE 593 AA; 63967 MW; B67013B453559910 CRC64; MTSAVVDSGG TILELSSNGV ENQEESEKVS EYPAVIVEPV PSARLEQGYA AQVLVYDDET YMMQDVAEEQ EVETENVETV EASVHSSNAH CTDKTIEAAE ALLHMESPTC LRDSRSPVEV FVPPCVSTPE FIHAAMRPDV ITETVVEVST EESEPMDTSP IPTSPDSHEP MKKKKVGRKP KTQQSPISNG SPELGIKKKP REGKGNTTYL WEFLLDLLQD KNTCPRYIKW TQREKGIFKL VDSKAVSKLW GKHKNKPDMN YETMGRALRY YYQRGILAKV EGQRLVYQFK DMPKNIVVID DDKSETCNED LAGTTDEKSL ERVSLSAESL LKAASSVRSG KNSSPINCSR AEKGVARVVN ITSPGHDASS RSPTTTASVS ATAAPRTVRV AMQVPVVMTS LGQKISTVAV QSVNAGAPLI TSTSPTTATS PKVVIQTIPT VMPASTENGD KITMQPAKII TIPATQLAQC QLQTKSNLTG SGSINIVGTP LAVRALTPVS IAHGTPVMRL SMPTQQASGQ TPPRVISAVI KGPEVKSEAV AKKQEHDVKT LQLVEEKPAD GNKTVTHVVV VSAPSAIALP VTMKTEGLVT CEK //