JIL1_DROME
ID JIL1_DROME Reviewed; 1207 AA.
AC Q9V3I5; B5RJL0; Q0E8F9; Q95RY3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Chromosomal serine/threonine-protein kinase JIL-1;
DE EC=2.7.11.1;
GN Name=JIL-1 {ECO:0000312|FlyBase:FBgn0020412}; ORFNames=CG6297;
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] {ECO:0000305, ECO:0000312|EMBL:AAD48407.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND AUTOPHOSPHORYLATION.
RX PubMed=10445035; DOI=10.1016/s1097-2765(00)80195-1;
RA Jin Y., Wang Y., Walker D.L., Dong H., Conley C., Johansen J.,
RA Johansen K.M.;
RT "JIL-1: a novel chromosomal tandem kinase implicated in transcriptional
RT regulation in Drosophila.";
RL Mol. Cell 4:129-135(1999).
RN [2] {ECO:0000312|EMBL:AAF50105.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAF50105.1}
RP GENOME REANNOTATION.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAL28591.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 962-1207.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28591.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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] {ECO:0000305}
RP ASSOCIATION WITH THE MSL DOSAGE COMPENSATION COMPLEX.
RX PubMed=10831604; DOI=10.1083/jcb.149.5.1005;
RA Jin Y., Wang Y., Johansen J., Johansen K.M.;
RT "JIL-1, a chromosomal kinase implicated in regulation of chromatin
RT structure, associates with the male specific lethal (MSL) dosage
RT compensation complex.";
RL J. Cell Biol. 149:1005-1010(2000).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=11371341; DOI=10.1016/s0092-8674(01)00325-7;
RA Wang Y., Zhang W., Jin Y., Johansen J., Johansen K.M.;
RT "The JIL-1 tandem kinase mediates histone H3 phosphorylation and is
RT required for maintenance of chromatin structure in Drosophila.";
RL Cell 105:433-443(2001).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=14668387; DOI=10.1093/genetics/165.3.1341;
RA Zhang W., Jin Y., Ji Y., Girton J., Johansen J., Johansen K.M.;
RT "Genetic and phenotypic analysis of alleles of the Drosophila chromosomal
RT JIL-1 kinase reveals a functional requirement at multiple developmental
RT stages.";
RL Genetics 165:1341-1354(2003).
RN [9] {ECO:0000305}
RP INTERACTION WITH LOLA.
RX PubMed=12538650; DOI=10.1074/jbc.m213269200;
RA Zhang W., Wang Y., Long J., Girton J., Johansen J., Johansen K.M.;
RT "A developmentally regulated splice variant from the complex lola locus
RT encoding multiple different zinc finger domain proteins interacts with the
RT chromosomal kinase JIL-1.";
RL J. Biol. Chem. 278:11696-11704(2003).
RN [10]
RP FUNCTION.
RX PubMed=15574598; DOI=10.1101/gad.323004;
RA Ebert A., Schotta G., Lein S., Kubicek S., Krauss V., Jenuwein T.,
RA Reuter G.;
RT "Su(var) genes regulate the balance between euchromatin and heterochromatin
RT in Drosophila.";
RL Genes Dev. 18:2973-2983(2004).
RN [11]
RP FUNCTION.
RX PubMed=15986206; DOI=10.1007/s00412-005-0006-8;
RA Deng H., Zhang W., Bao X., Martin J.N., Girton J., Johansen J.,
RA Johansen K.M.;
RT "The JIL-1 kinase regulates the structure of Drosophila polytene
RT chromosomes.";
RL Chromosoma 114:173-182(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-31; SER-424; THR-588;
RP THR-1045 AND SER-1047, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Phosphorylates 'Ser-10' of histone H3. May regulate gene
CC expression by establishing or maintaining the structure of more open
CC chromatin regions. Also required for normal polytene chromosome
CC structure, for oogenesis and for viability throughout development.
CC Regulates the structure of polytene chromosomes in salivary glands. May
CC phosphorylate 'Ser-1' of histone H2A. {ECO:0000269|PubMed:10445035,
CC ECO:0000269|PubMed:11371341, ECO:0000269|PubMed:14668387,
CC ECO:0000269|PubMed:15574598, ECO:0000269|PubMed:15986206}.
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=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:10445035};
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=2.7.11.1; Evidence={ECO:0000269|PubMed:10445035};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10445035};
CC -!- SUBUNIT: Interacts with lola. Interacts with proteins of the male
CC specific lethal (MSL) dosage compensation complex; this interaction is
CC mediated by the kinase domains. {ECO:0000269|PubMed:10831604,
CC ECO:0000269|PubMed:12538650}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10445035}. Chromosome
CC {ECO:0000269|PubMed:10445035}. Note=Associates with chromosomes
CC throughout the cell cycle. Localizes to interband regions along the
CC polytene chromosomes and is enriched almost two-fold on the male X
CC chromosome compared to the autosome.
CC -!- PTM: Autophosphorylated in vitro. {ECO:0000269|PubMed:10445035,
CC ECO:0000269|PubMed:18327897}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28591.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF142061; AAD48407.1; -; mRNA.
DR EMBL; AE014296; AAF50105.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11898.1; -; Genomic_DNA.
DR EMBL; BT044484; ACH95258.1; -; mRNA.
DR EMBL; AY061043; AAL28591.1; ALT_INIT; mRNA.
DR RefSeq; NP_001261697.1; NM_001274768.1.
DR RefSeq; NP_648432.1; NM_140175.3.
DR RefSeq; NP_729661.1; NM_168439.2.
DR AlphaFoldDB; Q9V3I5; -.
DR SMR; Q9V3I5; -.
DR BioGRID; 64615; 14.
DR IntAct; Q9V3I5; 106.
DR STRING; 7227.FBpp0304953; -.
DR iPTMnet; Q9V3I5; -.
DR PaxDb; Q9V3I5; -.
DR PRIDE; Q9V3I5; -.
DR DNASU; 39241; -.
DR EnsemblMetazoa; FBtr0076236; FBpp0075965; FBgn0020412.
DR EnsemblMetazoa; FBtr0076237; FBpp0075966; FBgn0020412.
DR EnsemblMetazoa; FBtr0332707; FBpp0304953; FBgn0020412.
DR GeneID; 39241; -.
DR KEGG; dme:Dmel_CG6297; -.
DR CTD; 39241; -.
DR FlyBase; FBgn0020412; JIL-1.
DR VEuPathDB; VectorBase:FBgn0020412; -.
DR eggNOG; KOG0603; Eukaryota.
DR GeneTree; ENSGT00940000167362; -.
DR HOGENOM; CLU_003357_0_0_1; -.
DR InParanoid; Q9V3I5; -.
DR OMA; MRRDNHC; -.
DR OrthoDB; 1132245at2759; -.
DR PhylomeDB; Q9V3I5; -.
DR Reactome; R-DME-198753; ERK/MAPK targets.
DR Reactome; R-DME-199920; CREB phosphorylation.
DR Reactome; R-DME-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-DME-5621575; CD209 (DC-SIGN) signaling.
DR BioGRID-ORCS; 39241; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39241; -.
DR PRO; PR:Q9V3I5; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0020412; Expressed in brain and 23 other tissues.
DR ExpressionAtlas; Q9V3I5; baseline and differential.
DR Genevisible; Q9V3I5; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005705; C:polytene chromosome interband; IDA:UniProtKB.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
DR GO; GO:0016456; C:X chromosome located dosage compensation complex, transcription activating; IPI:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035175; F:histone kinase activity (H3-S10 specific); IMP:UniProtKB.
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:0006325; P:chromatin organization; IMP:UniProtKB.
DR GO; GO:0051276; P:chromosome organization; IMP:FlyBase.
DR GO; GO:0033696; P:heterochromatin boundary formation; IMP:FlyBase.
DR GO; GO:0016572; P:histone phosphorylation; IBA:GO_Central.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0043687; P:post-translational protein modification; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IMP:FlyBase.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Chromosome; Developmental protein;
KW Kinase; Magnesium; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..1207
FT /note="Chromosomal serine/threonine-protein kinase JIL-1"
FT /id="PRO_0000086039"
FT DOMAIN 261..530
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 531..599
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 623..886
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 389
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 739
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 267..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 629..637
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 652
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 588
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1045
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1047
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 1207 AA; 137045 MW; BD99FB932D708743 CRC64;
MSRLQKQNYE ILSGTSTSRL KNHQHPRESE SLAYEEPDQM VRNHLNGQLV ANGNGKTRKN
SNSETMTNGK KSKLNTEGSG SGSGKTLNYN NNNNNNNSIS ATNGQYTNSS SKTTSASARD
YTYRETISPP TPPSPPTTNV ADIVCISDAE SEDGRDPERE YYDQDMEEDE PNGIEIDESS
SSLSKAKSNN AAAAAAAAAA AAAAAASKAS SSTTPSYAMP TSNSTPLDLD NEAHQRDLEA
VTDLKYYVKL YSDEAVSLND FKIIRVLGTG AYGRVFLVRK LTRHDAGKLY AMKVLNKITV
VQKRKTAEHT KTERVVLEAI QRNPFLVSLH YAFQSSSKLY LVLDFANGGE LFTHLYHSEN
FEESRVRVYI AEVVLALEQL HQLGIIYRDI KLENILLDGE GHIVLSDFGL SKILTAENEY
RAHSFCGTLE YMAPEIIRTG PPGHDSAVDW WSVGVLTFEL LTGASPFATS DGQVQQSEIS
RRIQKEQPMI PSSFSANARD FVLKMLEKNP KRRLGGNHRD ASEIKEHPFF NGINWQELRT
KRRKAPYKPT LTAEDDVQNF SNEFTDQVPE DPECDAPPSR IRLFRGYTYV APEHLEQMRR
DNHCEIQYFN TGLQNIPCRP DDLELGTRTS NGAYGTCHFV VDSSTDLVFL AKIIPLSKFR
PSEVDALISC ALDTTNHKNI VSYHGTFREK CETWIVMEYL SGPELTASIR MDEDSCREIF
LQLVMAVRHI HSKHFIHGDL KPENIMFENR EDRTVKLIDF GSACYNNRFK SWKDKPRYTL
DYAPPEMLAD ANLVTYSPAV DIYGLGATLY TMLVGHRPYR QNEDDVDHSA AAHHELRKRM
RRGTFNQRSM RWESASPAFR HLVSWCLQRD PADRPTLSDI LDSEWLQYGS NDPDVDIILP
QQMVVDLSED TMEQPTGGMF DDQQQLEFMH DKSAEDEGIT LVSEPMDTTV ATHESRRNAA
AFSSVVAPTT DDEIVHERFD PAFEVQADFY GFDENAPPLP LPEEYYSELP LPEEDRQYIP
PPPALIPVEP ETTFRRPRTR QQRRTESQLV QPVSVATYED SKASLRVLMQ QLPPPGDNVV
ARIPKRTHRV VRTLPPTFGT TKREENFYGF SKTAISWRKT RASWRHFCLL INGVQQVLKV
RFKKARRVYC LPHIKEEKLD HAYEKPLTFP RPKAQLKRTK REPKVPRPPT RVQPERARAM
RQLYQFQ
