GenomeNet

Database: UniProt
Entry: Q01842
LinkDB: Q01842
Original site: Q01842 
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   07-OCT-2020, entry version 205.
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; Holometabola; 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};
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   SMR; Q01842; -.
DR   BioGRID; 59621; 62.
DR   DIP; DIP-20916N; -.
DR   IntAct; Q01842; 2.
DR   STRING; 7227.FBpp0077522; -.
DR   iPTMnet; Q01842; -.
DR   PaxDb; Q01842; -.
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   eggNOG; KOG3804; Eukaryota.
DR   HOGENOM; CLU_325474_0_0_1; -.
DR   InParanoid; Q01842; -.
DR   KO; K03211; -.
DR   OMA; IESHMMQ; -.
DR   OrthoDB; 827924at2759; -.
DR   PhylomeDB; Q01842; -.
DR   SignaLink; Q01842; -.
DR   BioGRID-ORCS; 33392; 1 hit in 5 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 saliva-secreting gland and 20 other tissues.
DR   ExpressionAtlas; Q01842; baseline and differential.
DR   Genevisible; Q01842; DM.
DR   GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR   GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
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:0001751; P:compound eye photoreceptor cell differentiation; 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:0048747; P:muscle fiber development; IMP:FlyBase.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; 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; 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: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   COMPBIAS        313..322
FT                   /note="Poly-Gln"
FT   COMPBIAS        332..349
FT                   /note="Gln-rich"
FT   COMPBIAS        528..539
FT                   /note="Gln-rich"
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:0000244|PDB:1SV0"
FT   HELIX           56..69
FT                   /evidence="ECO:0000244|PDB:1SV0"
FT   HELIX           77..80
FT                   /evidence="ECO:0000244|PDB:1SV0"
FT   HELIX           84..87
FT                   /evidence="ECO:0000244|PDB:1SV0"
FT   HELIX           92..98
FT                   /evidence="ECO:0000244|PDB:1SV0"
FT   TURN            100..102
FT                   /evidence="ECO:0000244|PDB:1SV0"
FT   HELIX           103..118
FT                   /evidence="ECO:0000244|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
//
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