PHP_DROME
ID PHP_DROME Reviewed; 1589 AA.
AC P39769; O46097; Q9W521; Q9W522;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Polyhomeotic-proximal chromatin protein;
GN Name=ph-p; ORFNames=CG18412;
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].
RX PubMed=1937015; DOI=10.1016/0378-1119(91)90150-a;
RA Deatrick J., Daly M., Randsholt N.B., Brock H.W.;
RT "The complex genetic locus polyhomeotic in Drosophila melanogaster
RT potentially encodes two homologous zinc-finger proteins.";
RL Gene 105:185-195(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Imaginal disk;
RX PubMed=1346609; DOI=10.1101/gad.6.2.223;
RA Decamillis M., Cheng N.S., Pierre D., Brock H.W.;
RT "The polyhomeotic gene of Drosophila encodes a chromatin protein that
RT shares polytene chromosome-binding sites with Polycomb.";
RL Genes Dev. 6:223-232(1992).
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.
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 GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [6]
RP INTERACTION WITH SCM, AND MUTAGENESIS OF TRP-1513; LEU-1545; LEU-1553;
RP GLY-1562 AND ILE-1574.
RX PubMed=9343432; DOI=10.1128/mcb.17.11.6683;
RA Peterson A.J., Kyba M., Bornemann D., Morgan K., Brock H.W., Simon J.A.;
RT "A domain shared by the polycomb group proteins Scm and ph mediates
RT heterotypic and homotypic interactions.";
RL Mol. Cell. Biol. 17:6683-6692(1997).
RN [7]
RP IDENTIFICATION IN THE PRC1 COMPLEX WITH SCE; PC AND PSC.
RX PubMed=11493925; DOI=10.1038/35088096;
RA Saurin A.J., Shao Z., Erdjument-Bromage H., Tempst P., Kingston R.E.;
RT "A Drosophila Polycomb group complex includes Zeste and dTAFII proteins.";
RL Nature 412:655-660(2001).
RN [8]
RP IDENTIFICATION IN A PCG COMPLEX WITH SCE; PC AND PSC.
RX PubMed=11583617; DOI=10.1016/s1097-2765(01)00316-1;
RA Francis N.J., Saurin A.J., Shao Z., Kingston R.E.;
RT "Reconstitution of a functional core polycomb repressive complex.";
RL Mol. Cell 8:545-556(2001).
RN [9]
RP INTERACTION WITH TRL.
RX PubMed=12834867; DOI=10.1016/s0925-4773(03)00046-7;
RA Mishra K., Chopra V.S., Srinivasan A., Mishra R.K.;
RT "Trl-GAGA directly interacts with lola like and both are part of the
RT repressive complex of Polycomb group of genes.";
RL Mech. Dev. 120:681-689(2003).
RN [10]
RP INTERACTION WITH CORTO.
RX PubMed=12771214; DOI=10.1093/nar/gkg381;
RA Salvaing J., Lopez A., Boivin A., Deutsch J.S., Peronnet F.;
RT "The Drosophila Corto protein interacts with Polycomb-group proteins and
RT the GAGA factor.";
RL Nucleic Acids Res. 31:2873-2882(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1145 AND THR-1148, AND
RP 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).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1502-1577.
RX PubMed=11992127; DOI=10.1038/nsb802;
RA Kim C.A., Gingery M., Pilpa R.M., Bowie J.U.;
RT "The SAM domain of polyhomeotic forms a helical polymer.";
RL Nat. Struct. Biol. 9:453-457(2002).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1502-1577, AND INTERACTION WITH
RP SCM.
RX PubMed=15905166; DOI=10.1074/jbc.m503055200;
RA Kim C.A., Sawaya M.R., Cascio D., Kim W., Bowie J.U.;
RT "Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer.";
RL J. Biol. Chem. 280:27769-27775(2005).
CC -!- FUNCTION: Polycomb group (PcG) protein. PcG proteins act by forming
CC multiprotein complexes, which are required to maintain the
CC transcriptionally repressive state of homeotic genes throughout
CC development. PcG proteins are not required to initiate repression, but
CC to maintain it during later stages of development. Component of the PcG
CC multiprotein PRC1 complex, a complex that acts via chromatin remodeling
CC and modification of histones; it mediates monoubiquitination of histone
CC H2A 'Lys-118', rendering chromatin heritably changed in its
CC expressibility. Plays a role in regulating the expression of other
CC pair-rule genes such as eve, ftz, and H. {ECO:0000269|PubMed:1346609}.
CC -!- SUBUNIT: Component of PRC1 complex, which contains many PcG proteins
CC like Pc, ph, Scm, Psc, Sce and also chromatin-remodeling proteins such
CC as histone deacetylases. This complex is distinct from the Esc/E(z)
CC complex, at least composed of esc, E(z), Su(z)12, HDAC1/Rpd3 and Caf1-
CC 55. The 2 complexes however cooperate and interact together during the
CC first 3 hours of development to establish PcG silencing. Interacts with
CC the SAM domain of Scm via its SAM domain in vitro. Interacts with Trl
CC in vivo and with corto in vitro. {ECO:0000269|PubMed:11493925,
CC ECO:0000269|PubMed:11583617, ECO:0000269|PubMed:12771214,
CC ECO:0000269|PubMed:12834867, ECO:0000269|PubMed:15905166,
CC ECO:0000269|PubMed:9343432}.
CC -!- INTERACTION:
CC P39769; P41046: corto; NbExp=2; IntAct=EBI-300360, EBI-300379;
CC P39769; Q9VHA0: Scm; NbExp=6; IntAct=EBI-300360, EBI-89256;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Salivary glands. {ECO:0000269|PubMed:1346609}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305}.
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DR EMBL; M64750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X63672; CAA45211.1; -; mRNA.
DR EMBL; AE014298; AAF45727.3; -; Genomic_DNA.
DR EMBL; Z98269; CAB10975.1; -; Genomic_DNA.
DR PIR; T13606; T13606.
DR RefSeq; NP_476871.2; NM_057523.5.
DR PDB; 1KW4; X-ray; 1.75 A; A=1502-1577.
DR PDB; 1PK1; X-ray; 1.80 A; A/C=1502-1577.
DR PDBsum; 1KW4; -.
DR PDBsum; 1PK1; -.
DR AlphaFoldDB; P39769; -.
DR SMR; P39769; -.
DR BioGRID; 57724; 63.
DR DIP; DIP-19426N; -.
DR IntAct; P39769; 10.
DR MINT; P39769; -.
DR STRING; 7227.FBpp0070416; -.
DR iPTMnet; P39769; -.
DR PaxDb; P39769; -.
DR DNASU; 31181; -.
DR EnsemblMetazoa; FBtr0070432; FBpp0070416; FBgn0004861.
DR GeneID; 31181; -.
DR KEGG; dme:Dmel_CG18412; -.
DR CTD; 31181; -.
DR FlyBase; FBgn0004861; ph-p.
DR VEuPathDB; VectorBase:FBgn0004861; -.
DR eggNOG; ENOG502QS5Q; Eukaryota.
DR GeneTree; ENSGT00940000154964; -.
DR InParanoid; P39769; -.
DR OMA; DWANGRT; -.
DR PhylomeDB; P39769; -.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DME-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-DME-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-DME-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-DME-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; P39769; -.
DR BioGRID-ORCS; 31181; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; P39769; -.
DR GenomeRNAi; 31181; -.
DR PRO; PR:P39769; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004861; Expressed in wing disc and 27 other tissues.
DR ExpressionAtlas; P39769; baseline and differential.
DR Genevisible; P39769; DM.
DR GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0035102; C:PRC1 complex; IDA:FlyBase.
DR GO; GO:0051087; F:chaperone binding; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0044547; F:DNA topoisomerase binding; IPI:FlyBase.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:UniProtKB.
DR GO; GO:0021954; P:central nervous system neuron development; IMP:FlyBase.
DR GO; GO:0030708; P:germarium-derived female germ-line cyst encapsulation; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IGI:FlyBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0030713; P:ovarian follicle cell stalk formation; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0035075; P:response to ecdysone; IMP:FlyBase.
DR GO; GO:0035186; P:syncytial blastoderm mitotic cell cycle; IMP:FlyBase.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.30.60.160; -; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR012313; Znf_FCS.
DR InterPro; IPR038603; Znf_FCS_sf.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS51024; ZF_FCS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1589
FT /note="Polyhomeotic-proximal chromatin protein"
FT /id="PRO_0000058406"
FT DOMAIN 1513..1577
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 1356..1389
FT /note="FCS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 1368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 1383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT BINDING 1387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00367"
FT MOD_RES 1145
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1148
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 1513
FT /note="W->A: Significant loss of Scm-binding activity."
FT /evidence="ECO:0000269|PubMed:9343432"
FT MUTAGEN 1545
FT /note="L->A: Little effect on Scm-binding activity."
FT /evidence="ECO:0000269|PubMed:9343432"
FT MUTAGEN 1553
FT /note="L->A: Little effect on Scm-binding activity."
FT /evidence="ECO:0000269|PubMed:9343432"
FT MUTAGEN 1562
FT /note="G->A: Significant loss of Scm-binding activity."
FT /evidence="ECO:0000269|PubMed:9343432"
FT MUTAGEN 1574
FT /note="I->D: Little effect on Scm-binding activity."
FT /evidence="ECO:0000269|PubMed:9343432"
FT CONFLICT 253
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1011
FT /note="V -> A (in Ref. 5; CAB10975)"
FT /evidence="ECO:0000305"
FT CONFLICT 1193
FT /note="P -> L (in Ref. 2; CAA45211)"
FT /evidence="ECO:0000305"
FT CONFLICT 1275
FT /note="I -> T (in Ref. 5; CAB10975)"
FT /evidence="ECO:0000305"
FT HELIX 1510..1512
FT /evidence="ECO:0007829|PDB:1KW4"
FT HELIX 1515..1523
FT /evidence="ECO:0007829|PDB:1KW4"
FT HELIX 1529..1531
FT /evidence="ECO:0007829|PDB:1KW4"
FT HELIX 1532..1537
FT /evidence="ECO:0007829|PDB:1KW4"
FT HELIX 1542..1547
FT /evidence="ECO:0007829|PDB:1KW4"
FT HELIX 1550..1554
FT /evidence="ECO:0007829|PDB:1KW4"
FT TURN 1555..1557
FT /evidence="ECO:0007829|PDB:1KW4"
FT HELIX 1561..1574
FT /evidence="ECO:0007829|PDB:1KW4"
SQ SEQUENCE 1589 AA; 167281 MW; CF9B543DDBC79FBC CRC64;
MDRRALKFMQ KRADTESDTT TPVSTTASQG ISASAILAGG TLPLKDNSNI REKPLHHNYN
HNNNNSSQHS HSHQQQQQQQ VGGKQLERPL KCLETLAQKA GITFDEKYDV ASPPHPGIAQ
QQATSGTGPA TGSGSVTPTS HRHGTPPTGR RQTHTPSTPN RPSAPSTPNT NCNSIARHTS
LTLEKAQNPG QQVAATTTVP LQISPEQLQQ FYASNPYAIQ VKQEFPTHTT SGSGTELKHA
TNIMEVQQQL QLQQQLSEAN GGGAASAGAG GAASPANSQQ SQQQQHSTAI STMSPMQLAA
ATGGVGGDWT QGRTVQLMQP STSFLYPQMI VSGNLLHPGG LGQQPIQVIT AGKPFQGNGP
QMLTTTTQNA KQMIGGQAGF AGGNYATCIP TNHNQSPQTV LFSPMNVISP QQQQNLLQSM
AAAAQQQQLT QQQQQFNQQQ QQQLTQQQQQ LTAALAKVGV DAQGKLAQKV VQKVTTTSSA
VQAATGPGST GSTQTQQVQQ VQQQQQQTTQ TTQQCVQVSQ STLPVGVGGQ SVQTAQLLNA
GQAQQMQIPW FLQNAAGLQP FGPNQIILRN QPDGTQGMFI QQQPATQTLQ TQQNQIIQCN
VTQTPTKART QLDALAPKQQ QQQQQVGTTN QTQQQQLAVA TAQLQQQQQQ LTAAALQRPG
APVMPHNGTQ VRPASSVSTQ TAQNQSLLKA KMRNKQQPVR PALATLKTEI GQVAGQNKVV
GHLTTVQQQQ QATNLQQVVN AAGNKMVVMS TTGTPITLQN GQTLHAATAA GVDKQQQQLQ
LFQKQQILQQ QQMLQQQIAA IQMQQQQAAV QAQQQQQQQV SQQQQVNAQQ QQAVAQQQQA
VAQAQQQQRE QQQQVAQAQA QHQQALANAT QQILQVAPNQ FITSHQQQQQ QQLHNQLIQQ
QLQQQAQAQV QAQVQAQAQQ QQQQREQQQN IIQQIVVQQS GATSQQTSQQ QQHHQSGQLQ
LSSVPFSVSS STTPAGIATS SALQAALSAS GAIFQTAKPG TCSSSSPTSS VVTITNQSST
PLVTSSTVAS IQQAQTQSAQ VHQHQQLISA TIAGGTQQQP QGPPSLTPTT NPILAMTSMM
NATVGHLSTA PPVTVSVTST AVTSSPGQLV LLSTASSGGG GSIPATPTKE TPSKGPTATL
VPIGSPKTPV SGKDTCTTPK SSTPATVSAS VEASSSTGEA LSNGDASDRS STPSKGATTP
TSKQSNAAVQ PPSSTTPNSV SGKEEPKLAT CGSLTSATST STTTTITNGI GVARTTASTA
VSTASTTTTS SGTFITSCTS TTTTTTSSIS NGSKDLPKAM IKPNVLTHVI DGFIIQEANE
PFPVTRQRYA DKDVSDEPPK KKATMQEDIK LSGIASAPGS DMVACEQCGK MEHKAKLKRK
RYCSPGCSRQ AKNGIGGVGS GETNGLGTGG IVGVDAMALV DRLDEAMAEE KMQTEATPKL
SESFPILGAS TEVPPMSLPV QAAISAPSPL AMPLGSPLSV ALPTLAPLSV VTSGAAPKSS
EVNGTDRPPI SSWSVDDVSN FIRELPGCQD YVDDFIQQEI DGQALLLLKE KHLVNAMGMK
LGPALKIVAK VESIKEVPPP GEAKDPGAQ
