ID DOA_DROME Reviewed; 832 AA. AC P49762; Q8IMM0; Q8T041; Q95RC9; Q9VAR8; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2003, sequence version 2. DT 27-MAR-2024, entry version 202. DE RecName: Full=Serine/threonine-protein kinase Doa; DE EC=2.7.12.1; DE AltName: Full=Protein darkener of apricot; GN Name=Doa; ORFNames=CG42320; 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; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RX PubMed=7926721; DOI=10.1101/gad.8.10.1160; RA Yun B., Farkas R., Lee K., Rabinow L.; RT "The Doa locus encodes a member of a new protein kinase family and is RT essential for eye and embryonic development in Drosophila melanogaster."; RL Genes Dev. 8:1160-1173(1994). RN [2] RP SEQUENCE REVISION. RA Rabinow L.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; 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.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., 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.A., 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.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J.H., 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.C., Scheeler F., RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., RA Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING. RC STRAIN=Berkeley; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C). RC STRAIN=Berkeley; TISSUE=Embryo; RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., RA Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP FUNCTION, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-508. RX PubMed=8910305; DOI=10.1074/jbc.271.44.27299; RA Lee K., Du C., Horn M., Rabinow L.; RT "Activity and autophosphorylation of LAMMER protein kinases."; RL J. Biol. Chem. 271:27299-27303(1996). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, RP AND DEVELOPMENTAL STAGE. RX PubMed=11014821; DOI=10.1093/genetics/156.2.749; RA Yun B., Lee K., Farkas R., Hitte C., Rabinow L.; RT "The LAMMER protein kinase encoded by the Doa locus of Drosophila is RT required in both somatic and germline cells and is expressed as both RT nuclear and cytoplasmic isoforms throughout development."; RL Genetics 156:749-761(2000). CC -!- FUNCTION: Negative regulator of the copia retrotransposon element of CC the white (w) gene. In the eye, it is required for normal pigmentation, CC photoreceptor cell development and for organization of interommatidial CC bristles. Also essential for embryonic segmentation and differentiation CC of the nervous system. Functions in the control of alternative splicing CC by phosphorylating the arginine/serine-rich splicing factors, SR CC proteins. {ECO:0000269|PubMed:11014821, ECO:0000269|PubMed:7926721, CC ECO:0000269|PubMed:8910305}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.12.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SUBCELLULAR LOCATION: [Isoform C]: Cytoplasm, cytosol. CC -!- SUBCELLULAR LOCATION: [Isoform A]: Nucleus. Note=Mainly nuclear with CC only low levels present in the cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist.; CC Name=C; Synonyms=105 kDa isoform; CC IsoId=P49762-1; Sequence=Displayed; CC Name=A; Synonyms=55 kDa isoform; CC IsoId=P49762-2; Sequence=VSP_008268, VSP_008270, VSP_008272; CC Name=B; CC IsoId=P49762-3; Sequence=VSP_008269, VSP_008271, VSP_008272; CC -!- TISSUE SPECIFICITY: Ubiquitous expression in embryos. Stage 17 embryos CC show elevated expression in CNS and brain. Ubiquitous expression in CC larval imaginal disks. Increased expression posterior to the eye- CC antennal disk morphogenetic furrow. {ECO:0000269|PubMed:11014821, CC ECO:0000269|PubMed:7926721}. CC -!- DEVELOPMENTAL STAGE: Expressed both maternally (isoform C) and CC zygotically (isoforms A and C) in all developmental stages. CC {ECO:0000269|PubMed:11014821, ECO:0000269|PubMed:7926721}. CC -!- PTM: Autophosphorylated on serine, threonine and tyrosine residues. CC -!- MISCELLANEOUS: [Isoform C]: May correspond to the described 105 kDa CC isoform although there is no translation sequence evidence for this. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. Lammer subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA55367.1; Type=Miscellaneous discrepancy; Note=Chimera. Chimera of genomic DNA and cDNA.; 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; X78715; CAA55367.1; ALT_SEQ; Genomic_DNA. DR EMBL; AE014297; AAF56832.3; -; Genomic_DNA. DR EMBL; AE014297; AAF56833.2; -; Genomic_DNA. DR EMBL; AE014297; AAN14305.1; -; Genomic_DNA. DR EMBL; AY061474; AAL29022.1; -; mRNA. DR EMBL; AY069573; AAL39718.1; -; mRNA. DR PIR; A54099; A54099. DR RefSeq; NP_001014679.1; NM_001014679.2. [P49762-1] DR RefSeq; NP_001014680.1; NM_001014680.4. [P49762-2] DR RefSeq; NP_001014682.1; NM_001014682.3. [P49762-3] DR RefSeq; NP_001036765.1; NM_001043300.3. [P49762-2] DR RefSeq; NP_001138120.1; NM_001144648.3. [P49762-2] DR RefSeq; NP_001138121.1; NM_001144649.2. [P49762-2] DR RefSeq; NP_001138122.1; NM_001144650.1. [P49762-3] DR AlphaFoldDB; P49762; -. DR SMR; P49762; -. DR BioGRID; 68286; 59. DR IntAct; P49762; 50. DR STRING; 7227.FBpp0289029; -. DR PaxDb; 7227-FBpp0289029; -. DR DNASU; 43415; -. DR EnsemblMetazoa; FBtr0299742; FBpp0289020; FBgn0265998. [P49762-2] DR EnsemblMetazoa; FBtr0299743; FBpp0289021; FBgn0265998. [P49762-1] DR EnsemblMetazoa; FBtr0299745; FBpp0289023; FBgn0265998. [P49762-2] DR EnsemblMetazoa; FBtr0299748; FBpp0289026; FBgn0265998. [P49762-3] DR EnsemblMetazoa; FBtr0299749; FBpp0289027; FBgn0265998. [P49762-2] DR EnsemblMetazoa; FBtr0299750; FBpp0289028; FBgn0265998. [P49762-2] DR EnsemblMetazoa; FBtr0299752; FBpp0289030; FBgn0265998. [P49762-3] DR GeneID; 43415; -. DR KEGG; dme:Dmel_CG42320; -. DR AGR; FB:FBgn0265998; -. DR CTD; 43415; -. DR FlyBase; FBgn0265998; Doa. DR VEuPathDB; VectorBase:FBgn0265998; -. DR eggNOG; KOG0671; Eukaryota. DR GeneTree; ENSGT00940000154947; -. DR HOGENOM; CLU_000482_0_0_1; -. DR InParanoid; P49762; -. DR OMA; GQEDGYR; -. DR BRENDA; 2.7.11.1; 1994. DR BRENDA; 2.7.12.1; 1994. DR SignaLink; P49762; -. DR BioGRID-ORCS; 43415; 2 hits in 3 CRISPR screens. DR ChiTaRS; Doa; fly. DR GenomeRNAi; 43415; -. DR PRO; PR:P49762; -. DR Proteomes; UP000000803; Chromosome 3R. DR Bgee; FBgn0265998; Expressed in egg cell and 32 other cell types or tissues. DR ExpressionAtlas; P49762; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase. DR GO; GO:0005634; C:nucleus; IDA:FlyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IDA:FlyBase. DR GO; GO:0004672; F:protein kinase activity; IDA:FlyBase. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0007350; P:blastoderm segmentation; IMP:FlyBase. DR GO; GO:0048749; P:compound eye development; IMP:FlyBase. DR GO; GO:0042051; P:compound eye photoreceptor development; IMP:FlyBase. DR GO; GO:2000255; P:negative regulation of male germ cell proliferation; IMP:FlyBase. DR GO; GO:0007399; P:nervous system development; IMP:FlyBase. DR GO; GO:0002225; P:positive regulation of antimicrobial peptide production; IMP:FlyBase. DR GO; GO:0010508; P:positive regulation of autophagy; IMP:FlyBase. DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IMP:FlyBase. DR GO; GO:0046777; P:protein autophosphorylation; IDA:FlyBase. DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase. DR GO; GO:0009306; P:protein secretion; IMP:FlyBase. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; HMP:FlyBase. DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central. DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW. DR GO; GO:0007548; P:sex differentiation; IMP:FlyBase. DR GO; GO:0018993; P:somatic sex determination; IMP:FlyBase. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR CDD; cd14134; PKc_CLK; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR45646; SERINE/THREONINE-PROTEIN KINASE DOA-RELATED; 1. DR PANTHER; PTHR45646:SF11; SERINE_THREONINE-PROTEIN KINASE DOA; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; P49762; DM. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cytoplasm; Developmental protein; KW Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Sensory transduction; Serine/threonine-protein kinase; Transferase; KW Tyrosine-protein kinase; Vision. FT CHAIN 1..832 FT /note="Serine/threonine-protein kinase Doa" FT /id="PRO_0000085926" FT DOMAIN 479..799 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..86 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 135..158 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 179..215 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 258..419 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 809..832 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..19 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 20..34 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 36..59 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 71..86 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 179..213 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 258..318 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 348..369 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 380..419 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 812..832 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 605 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 485..493 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 508 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT VAR_SEQ 1..315 FT /note="Missing (in isoform B)" FT /evidence="ECO:0000305" FT /id="VSP_008269" FT VAR_SEQ 1..252 FT /note="Missing (in isoform A)" FT /evidence="ECO:0000303|PubMed:12537569" FT /id="VSP_008268" FT VAR_SEQ 253..453 FT /note="APQQQSKIGYPRTGAPLTHSASFSSAQRPTALQFHQQHQQQQHLQQQQQHPQ FT QQQHQHSSFGVGMMSRNYYNMPKQPERKPLQTFDPYAYPKPNQMQPVKYQQQQQHPHTQ FT FQNASAGGGGGGAAGLQYDPNTNTQLFYASPASSSSNKQPQQPQQQQQQQQSQLQQSNS FT VIFNHSGQQHQPHQQQQNEMSKSALGLHFIE -> MQLPSLKDKLMPSGSVQQAKANFS FT WQSLTQLLSGLWQRLYLPRSPFLALPAPPLATPPANTTQRRAKKEMPRTRRLHHSRDRS FT SAGTRDKRRRHDTADHSPPLAEAPSPPRITNTHHTRSAAKRRRHELDAKKAQISKEPTF FT DDSISTRRRKERSKRSHRKSPAASRRQHKYRYRDETSHSSSRRRHRDRAKDERDSGRNN FT RQSQAK (in isoform A)" FT /evidence="ECO:0000303|PubMed:12537569" FT /id="VSP_008270" FT VAR_SEQ 316..453 FT /note="GMMSRNYYNMPKQPERKPLQTFDPYAYPKPNQMQPVKYQQQQQHPHTQFQNA FT SAGGGGGGAAGLQYDPNTNTQLFYASPASSSSNKQPQQPQQQQQQQQSQLQQSNSVIFN FT HSGQQHQPHQQQQNEMSKSALGLHFIE -> MPRTRRLHHSRDRSSAGTRDKRRRHDTA FT DHSPPLAEAPSPPRITNTHHTRSAAKRRRHELDAKKAQISKEPTFDDSISTRRRKERSK FT RSHRKSPAASRRQHKYRYRDETSHSSSRRRHRDRAKDERDSGRNNRQSQAK (in FT isoform B)" FT /evidence="ECO:0000305" FT /id="VSP_008271" FT VAR_SEQ 722..727 FT /note="Missing (in isoform A and isoform B)" FT /evidence="ECO:0000303|PubMed:12537569" FT /id="VSP_008272" FT MUTAGEN 508 FT /note="K->R: Loss of activity." FT /evidence="ECO:0000269|PubMed:8910305" SQ SEQUENCE 832 AA; 95723 MW; 6EC90CB1A031DD68 CRC64; MVAANLEVPT SSSSSAATKR QKDVDNKLEK CLNDMLKLKT SSNNNSTSNS NNNAIMSHSL TGEHKDPKTA LEGPTSSSSS SSSKYIGESQ IPVPVQLYDP QKPLLQQQQQ QQRICYPIGK SNSTSQLPMG GYQRLLQHQQ QQHHQQQQQQ HQEQQQYPQH KRPFLNWNSF ACSAMNGASD PFMQQQHMPA HQQQQHLPHK LQQSYSSSHV PKQAPKSGLA MFLQKNTNKE NKFGQPMQQQ PPGMMPQMYG YQAPQQQSKI GYPRTGAPLT HSASFSSAQR PTALQFHQQH QQQQHLQQQQ QHPQQQQHQH SSFGVGMMSR NYYNMPKQPE RKPLQTFDPY AYPKPNQMQP VKYQQQQQHP HTQFQNASAG GGGGGAAGLQ YDPNTNTQLF YASPASSSSN KQPQQPQQQQ QQQQSQLQQS NSVIFNHSGQ QHQPHQQQQN EMSKSALGLH FIETAKPVIQ DDADGHLIYH TGDILHHRYK IMATLGEGTF GRVVKVKDME RDYCMALKII KNVEKYREAA KLEINALEKI AQKDPHCDHL CVKMIDWFDY HGHMCIVFEM LGLSVFDFLR ENNYEPYPLD QVRHMAYQLC YSVKFLHDNR LTHTDLKPEN ILFVDSDYTS HYNHKINREV RRVKNTDVRL IDFGSATFDH EHHSTIVSTR HYRAPEVILE LGWSQPCDVW SIGCILFELY LGITLFQTHD NREHLAMMER ILGQIPYRMA RNHTLYSKTK TKYFYHGKLD WDEKSSAGRY VRDHCKPLFL CQLSDSEDHC ELFSLIKKML EYEPSSRITL GEALHHPFFD RLPPHHRVGE VSNKQPLSSG SSSRERSHSL SR //