POK_DROME
ID POK_DROME Reviewed; 732 AA.
AC Q01842; Q6AWH6; Q6NR43; Q9VQ81;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Ets DNA-binding protein pokkuri;
DE AltName: Full=Protein anterior open;
DE AltName: Full=Protein yan;
GN Name=aop; Synonyms=pok, Yan; ORFNames=CG3166;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=1505027; DOI=10.1016/0092-8674(92)90430-k;
RA Lai Z.C., Rubin G.M.;
RT "Negative control of photoreceptor development in Drosophila by the product
RT of the yan gene, an ETS domain protein.";
RL Cell 70:609-620(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=1495974; DOI=10.1073/pnas.89.15.6856;
RA Tei H., Nihonmatsu I., Yokokura T., Ueda R., Sano Y., Okuda T., Sato K.,
RA Hirata K., Fujita S.C., Yamamoto D.;
RT "Pokkuri, a Drosophila gene encoding an E-26-specific (Ets) domain protein,
RT prevents overproduction of the R7 photoreceptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6856-6860(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 MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=8033205; DOI=10.1016/0092-8674(94)90580-0;
RA O'Neill E.M., Rebay I., Tjian R., Rubin G.M.;
RT "The activities of two Ets-related transcription factors required for
RT Drosophila eye development are modulated by the Ras/MAPK pathway.";
RL Cell 78:137-147(1994).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543; SER-677; SER-682 AND
RP SER-696, 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: Ets-related protein that functions as a negative regulator of
CC photoreceptor development acting antagonistically to pnt and the
CC proneural signal mediated by RAS (PubMed:1505027, PubMed:1495974,
CC PubMed:8033205). It acts upstream of SINA to inhibit R7 development
CC (PubMed:1505027, PubMed:1495974). {ECO:0000269|PubMed:1495974,
CC ECO:0000269|PubMed:1505027, ECO:0000269|PubMed:8033205}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237,
CC ECO:0000269|PubMed:1505027}. Note=In undifferentiated cells during the
CC early stages of eye development.
CC -!- TISSUE SPECIFICITY: Expressed in R7 and cone cells of the eye.
CC {ECO:0000269|PubMed:1505027}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryo.
CC {ECO:0000269|PubMed:1505027}.
CC -!- PTM: Phosphorylated in response to MAPK signaling. May be
CC phosphorylated by rl. {ECO:0000269|PubMed:8033205}.
CC -!- MISCELLANEOUS: 'Pokkuri' means 'dropping dead' in Japanese. Flies
CC lacking aop result in the differentiation of supernumerary
CC photoreceptors in the eye.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA01080.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M97693; AAA29023.1; -; mRNA.
DR EMBL; D10228; BAA01080.1; ALT_FRAME; mRNA.
DR EMBL; AE014134; AAF51297.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10445.1; -; Genomic_DNA.
DR EMBL; BT010237; AAQ23555.1; -; mRNA.
DR EMBL; BT015272; AAT94501.1; -; mRNA.
DR PIR; A43315; A43315.
DR PIR; A46193; A46193.
DR RefSeq; NP_001259908.1; NM_001272979.1.
DR RefSeq; NP_001259909.1; NM_001272980.1.
DR RefSeq; NP_001259910.1; NM_001272981.1.
DR RefSeq; NP_523455.2; NM_078731.3.
DR RefSeq; NP_722766.1; NM_164457.2.
DR PDB; 1SV0; X-ray; 2.07 A; A/B=42-118.
DR PDB; 1SV4; X-ray; 2.15 A; A/B=42-118.
DR PDBsum; 1SV0; -.
DR PDBsum; 1SV4; -.
DR AlphaFoldDB; Q01842; -.
DR SMR; Q01842; -.
DR BioGRID; 59621; 64.
DR DIP; DIP-20916N; -.
DR IntAct; Q01842; 2.
DR STRING; 7227.FBpp0077522; -.
DR iPTMnet; Q01842; -.
DR PaxDb; Q01842; -.
DR DNASU; 33392; -.
DR EnsemblMetazoa; FBtr0077850; FBpp0077522; FBgn0000097.
DR EnsemblMetazoa; FBtr0077851; FBpp0077523; FBgn0000097.
DR EnsemblMetazoa; FBtr0330658; FBpp0303508; FBgn0000097.
DR EnsemblMetazoa; FBtr0330659; FBpp0303509; FBgn0000097.
DR EnsemblMetazoa; FBtr0330660; FBpp0303510; FBgn0000097.
DR GeneID; 33392; -.
DR KEGG; dme:Dmel_CG3166; -.
DR CTD; 33392; -.
DR FlyBase; FBgn0000097; aop.
DR VEuPathDB; VectorBase:FBgn0000097; -.
DR eggNOG; KOG3804; Eukaryota.
DR HOGENOM; CLU_325474_0_0_1; -.
DR InParanoid; Q01842; -.
DR OMA; GHHFMAP; -.
DR OrthoDB; 827924at2759; -.
DR PhylomeDB; Q01842; -.
DR SignaLink; Q01842; -.
DR BioGRID-ORCS; 33392; 1 hit in 3 CRISPR screens.
DR ChiTaRS; aop; fly.
DR EvolutionaryTrace; Q01842; -.
DR GenomeRNAi; 33392; -.
DR PRO; PR:Q01842; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000097; Expressed in eye disc (Drosophila) and 24 other tissues.
DR ExpressionAtlas; Q01842; baseline and differential.
DR Genevisible; Q01842; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0019904; F:protein domain specific binding; IPI:FlyBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0001709; P:cell fate determination; IMP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; TAS:FlyBase.
DR GO; GO:0006897; P:endocytosis; IMP:FlyBase.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0008406; P:gonad development; IMP:FlyBase.
DR GO; GO:0055001; P:muscle cell development; IMP:FlyBase.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0110118; P:negative regulation of compound eye photoreceptor cell differentiation; IMP:FlyBase.
DR GO; GO:0035157; P:negative regulation of fusion cell fate specification; IMP:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IGI:FlyBase.
DR GO; GO:0045677; P:negative regulation of R7 cell differentiation; IMP:FlyBase.
DR GO; GO:0035155; P:negative regulation of terminal cell fate specification, open tracheal system; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0060233; P:oenocyte delamination; IMP:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IMP:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0007464; P:R3/R4 cell fate commitment; IMP:FlyBase.
DR GO; GO:0090175; P:regulation of establishment of planar polarity; IGI:FlyBase.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045500; P:sevenless signaling pathway; IDA:FlyBase.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IDA:FlyBase.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR003118; Pointed_dom.
DR InterPro; IPR033077; Pokkuri.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR PANTHER; PTHR11849:SF201; PTHR11849:SF201; 1.
DR Pfam; PF00178; Ets; 1.
DR Pfam; PF02198; SAM_PNT; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SMART; SM00251; SAM_PNT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR PROSITE; PS51433; PNT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..732
FT /note="Ets DNA-binding protein pokkuri"
FT /id="PRO_0000204131"
FT DOMAIN 33..117
FT /note="PNT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT DNA_BIND 396..479
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 133..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 27
FT /note="R -> C (in Ref. 2; BAA01080)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="G -> S (in Ref. 2; BAA01080)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="P -> A (in Ref. 2; BAA01080)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="P -> R (in Ref. 5; AAQ23555)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="P -> S (in Ref. 2; BAA01080)"
FT /evidence="ECO:0000305"
FT CONFLICT 693
FT /note="S -> P (in Ref. 5; AAQ23555)"
FT /evidence="ECO:0000305"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1SV0"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:1SV0"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:1SV0"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:1SV0"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:1SV0"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:1SV0"
FT HELIX 103..118
FT /evidence="ECO:0007829|PDB:1SV0"
SQ SEQUENCE 732 AA; 78574 MW; 25D36A652BA67176 CRC64;
MSKMKMLPVQ LSLNSLNPGI WSDVLWRCPP APSSQLAELK TQLPPSLPSD PRLWSREDVL
VFLRFCVREF DLPKLDFDLF QMNGKALCLL TRADFGHRCP GAGDVLHNVL QMLIIESHMM
QWHLPNSPVT PTSRYPLSPH SHPPTPTWPP LNAPPENSPF HSSAHSLAGH HFMAPNSVTL
SPPPSVDSQA SSPPQAPYQN GGATGAAPGS AGGSAPAAGG ATNTSNPTSS SASSTGSNGS
QPNIMPMKGI SSASSNHSDS EEEYSETSGG VSKMPPAPLS YSTASPPGTP ILKDIKPNWT
QQLTNSFVNS WSQQQQQQQQ QQAAAVAAVA AQAQQHQLQQ QQQQQQLPQK LTLDNTAGPV
VTPAGGSISA PTTPSYMYKA KREFFPENSE PNTNGRLLWD FLQQLLNDRN QKYSDLIAWK
CRDTGVFKIV DPAGLAKLWG IQKNHLSMNY DKMSRALRYY YRVNILRKVQ GERHCYQFLR
NPTELKNIKN ISLLRQSTPA NGNGGSPSMP QGSSQAPGSP AGQNWNPQQQ SQQQQQSPQR
PASRNGPMSL PAVAAVAAAA AAAYGPPPTS PLFMHAINGA FHYLSAAAAG PPPNSPALNT
PSAVGGPDKF QFHPLKLENG SGSGSESAGE DLKPTDLSVS SKSTATSNED CYPLIRNADG
LTTIKLIRYN EHQVAASPAG QSPKHDDQQA GASNASSSPR PMDQASEQAQ PVPMESDCNG
GESEDSFRHM QQ
