DOA_DROME
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 03-AUG-2022, entry version 195.
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};
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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; P49762; -.
DR PRIDE; P49762; -.
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 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 OrthoDB; 74406at2759; -.
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 tissues.
DR ExpressionAtlas; P49762; baseline and differential.
DR Genevisible; P49762; DM.
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 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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
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
