ID Q9VYF3_DROME Unreviewed; 1252 AA. AC Q9VYF3; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 3. DT 27-MAR-2024, entry version 181. DE RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037911}; DE EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037911}; GN Name=HDAC4 {ECO:0000313|EMBL:AAF48245.3, GN ECO:0000313|FlyBase:FBgn0041210}; GN Synonyms=DHDAC4 {ECO:0000313|EMBL:AAF48245.3}, dHDAC4 GN {ECO:0000313|EMBL:AAF48245.3}, Dmel\CG1770 GN {ECO:0000313|EMBL:AAF48245.3}, dmHDA405 {ECO:0000313|EMBL:AAF48245.3}, GN GC1770 {ECO:0000313|EMBL:AAF48245.3}, HDAC GN {ECO:0000313|EMBL:AAF48245.3}, hdac4 {ECO:0000313|EMBL:AAF48245.3}, GN HDAC4-RD {ECO:0000313|EMBL:AFH55501.1}, HDAC4a GN {ECO:0000313|EMBL:AAF48245.3}; GN ORFNames=CG1770 {ECO:0000313|EMBL:AAF48245.3, GN ECO:0000313|FlyBase:FBgn0041210}, Dmel_CG1770 GN {ECO:0000313|EMBL:AAF48245.3}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF48245.3, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AAF48245.3, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A., RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:AAF48245.3, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster RT euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:AAF48245.3, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:AAF48245.3, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M., RA Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: a RT genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [5] {ECO:0000313|EMBL:AAF48245.3, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AAF48245.3, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [7] {ECO:0000313|EMBL:AAF48245.3} RP NUCLEOTIDE SEQUENCE. RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., RA Svirskas R., Rubin G.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:AAF48245.3, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin."; RL Science 316:1586-1591(2007). RN [9] {ECO:0000313|EMBL:AAF48245.3, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). RN [10] {ECO:0000313|EMBL:AFH55501.1} RP NUCLEOTIDE SEQUENCE. RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. RN [11] {ECO:0000313|EMBL:AAF48245.3} RP NUCLEOTIDE SEQUENCE. RX PubMed=26109357; DOI=.1534/g3.115.018929; RG FlyBase Consortium; RA Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E., RA Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M., RA Gelbart W.M., null; RT "Gene Model Annotations for Drosophila melanogaster: Impact of High- RT Throughput Data."; RL G3 (Bethesda) 5:1721-1736(2015). RN [12] {ECO:0000313|EMBL:AAF48245.3} RP NUCLEOTIDE SEQUENCE. RX PubMed=26109356; DOI=.1534/g3.115.018937; RG FlyBase Consortium; RA Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E., RA Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M., RA null; RT "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders."; RL G3 (Bethesda) 5:1737-1749(2015). RN [13] {ECO:0000313|EMBL:AAF48245.3} RP NUCLEOTIDE SEQUENCE. RX PubMed=25589440; RA Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E., RA Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M., RA Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M., RA de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M., RA Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M., RA Karpen G.H., Celniker S.E.; RT "The Release 6 reference sequence of the Drosophila melanogaster genome."; RL Genome Res. 25:445-458(2015). RN [14] {ECO:0000313|EMBL:AAF48245.3} RP NUCLEOTIDE SEQUENCE. RG Berkeley Drosophila Genome Project; RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C., RA Rubin G.; RT "Drosophila melanogaster release 4 sequence."; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. RN [15] {ECO:0000313|EMBL:AAF48245.3} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Responsible for the deacetylation of lysine residues on the CC N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone CC deacetylation gives a tag for epigenetic repression and plays an CC important role in transcriptional regulation, cell cycle progression CC and developmental events. {ECO:0000256|PIRNR:PIRNR037911}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl- CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA- CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, CC ChEBI:CHEBI:61930; EC=3.5.1.98; CC Evidence={ECO:0000256|ARBA:ARBA00001028, CC ECO:0000256|PIRNR:PIRNR037911}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037911}. CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2 CC subfamily. {ECO:0000256|ARBA:ARBA00007738, CC ECO:0000256|PIRNR:PIRNR037911}. 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; AE014298; AAF48245.3; -; Genomic_DNA. DR EMBL; BT133402; AFH55501.1; -; mRNA. DR RefSeq; NP_572868.3; NM_132640.6. DR AlphaFoldDB; Q9VYF3; -. DR SMR; Q9VYF3; -. DR IntAct; Q9VYF3; 3. DR EnsemblMetazoa; FBtr0301298; FBpp0290513; FBgn0041210. DR GeneID; 32278; -. DR UCSC; CG1770-RA; d. melanogaster. DR AGR; FB:FBgn0041210; -. DR CTD; 9759; -. DR FlyBase; FBgn0041210; HDAC4. DR VEuPathDB; VectorBase:FBgn0041210; -. DR GeneTree; ENSGT00940000169192; -. DR OrthoDB; 124800at2759; -. DR BioGRID-ORCS; 32278; 0 hits in 3 CRISPR screens. DR ChiTaRS; HDAC4; fly. DR GenomeRNAi; 32278; -. DR Proteomes; UP000000803; Chromosome X. DR Bgee; FBgn0041210; Expressed in brain and 20 other cell types or tissues. DR ExpressionAtlas; Q9VYF3; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase. DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule. DR GO; GO:0005634; C:nucleus; IDA:FlyBase. DR GO; GO:0004407; F:histone deacetylase activity; IDA:FlyBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007616; P:long-term memory; IMP:FlyBase. DR GO; GO:0007613; P:memory; IMP:FlyBase. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:FlyBase. DR CDD; cd11681; HDAC_classIIa; 1. DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1. DR InterPro; IPR046949; HDAC4/5/7/9. DR InterPro; IPR000286; His_deacetylse. DR InterPro; IPR023801; His_deacetylse_dom. DR InterPro; IPR037138; His_deacetylse_dom_sf. DR InterPro; IPR023696; Ureohydrolase_dom_sf. DR PANTHER; PTHR10625:SF15; HISTONE DEACETYLASE; 1. DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1. DR Pfam; PF00850; Hist_deacetyl; 1. DR PIRSF; PIRSF037911; HDAC_II_euk; 3. DR PRINTS; PR01270; HDASUPER. DR SUPFAM; SSF52768; Arginase/deacetylase; 1. PE 1: Evidence at protein level; KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR037911, ECO:0000313|EMBL:AAF48245.3}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2}; KW Proteomics identification {ECO:0007829|PeptideAtlas:Q9VYF3}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}; KW Repressor {ECO:0000256|PIRNR:PIRNR037911}; KW Transcription {ECO:0000256|PIRNR:PIRNR037911}; KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037911}; KW Zinc {ECO:0000256|PIRSR:PIRSR037911-2}. FT DOMAIN 843..1158 FT /note="Histone deacetylase" FT /evidence="ECO:0000259|Pfam:PF00850" FT REGION 114..151 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 178..222 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 276..345 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 507..541 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 759..778 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1231..1252 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 589..616 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 178..208 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 276..298 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 315..345 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 519..539 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 761..778 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1236..1252 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 968 FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1" FT BINDING 835 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2" FT BINDING 837 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2" FT BINDING 843 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2" FT BINDING 916 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2" SQ SEQUENCE 1252 AA; 134162 MW; C6FE30273DDC1EC5 CRC64; MSSPDDRIPI HDLPSEAGSD ERLLHITPAT LTLDFKPHPA VDIDQQIMEL KKSQELQKQR LINSFQEQSK QMELEHKLQL EHKYQFAVNS HGAFQELRNE SMVTAAAAAV AQEQHRQQLH QQQQQHQQQQ QQQQHQQQQQ QQQARGRDGM KLKQNCSANA SPEVKQILNC FILSRKSQAA ASNGTTTTSP YRNRGVVKSS SGESLPAGTV TSAHPYKIPQ PPPSLLKYES DFPLRKTASE PNLLKIRLKQ SVIERKARIG GPAGARRHER LLQAAQRRQQ KNSVLTNCNS TPDSGPNSPP SAAALAVGVV GSRGSPTSAP IQEENEEGSQ YQPGQRSSIN DLPLFSSPSL PNISLGRPHL PNSAQAHAQV NAQVAAQAQA QAQAQAQAHA MFAALAAAQG GCGQPGYYNP LGMAFVGRQP APLAMIPATG IAPQQPSPVV RSASATSTSS SQASLVGDVA PPQAHAASTI LPSSSSYMQQ LGSVAGSGVN LHAAAVAAAA AAAAAAGSLP PTNSHGHGHG SHAHPHPHAH GHGHGHGHGI YAGHQHNVPI TDAQVAQVHL HKQGHRPLGR TQSAPLPLGH PMLTGAVQLN VVQTHYENSE AERQAYEHQV VNQKVRQTVL TRSGAAAAAA AAAGVSVVRE AQLKEEDDDS AAEVMDLTDK KKPPKTVLTS TIATSTSQNL PEALAAAAAA AAYRAPHNAS SNSASATKSG IKLRDQEYLQ QQREQLLLLQ QEEELAKSLM RPLSRTLSSP LVPLGPHGLS QIPDTGQQPA PIATSSSADH IPPVNLSLPH RQHRQLMSTL YASQLRNHQP SASGSPPHKV TTGLAYDPLM LKHSCICGDN AQHPEHSGRL QSVWARLNET DLVKRCDRLR ARKATQEELQ TVHTEAHAML FGSNQCQLSR PKLENTLSAS FVRLSCGGLG VDLDTTWNEH HTATAARMAA GCVIDLALKT AKGDLRNGFA VVRPPGHHAE ANLAMGFCFF NSIAIAAKLL RQRMPEVRRI LIVDWDVHHG NGTQQAFYQS PDILYLSIHR HDDGNFFPGT GGPTECGSGA GLGFNVNISW SGALNPPLGD AEYIAAFRTV VMPIARSFNP DIVLVSSGFD AATGHPAPLG GYHVSPACFG FMTRELLQLA NGKVVLALEG GYDLAAICDS AQECVRALLG DPAAPIAKAE LERPPCQNAI NTLQKTIAIQ QTHWPCVRML EHTVGLSALE TLKVEHDESE TINAMAGLSM QSMHRTLSRD DSEEPMDQDE TK //