PNR_DROME
ID PNR_DROME Reviewed; 540 AA.
AC P52168;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=GATA-binding factor A;
DE AltName: Full=Protein pannier;
DE AltName: Full=Transcription factor GATA-A;
DE AltName: Full=dGATA-A;
GN Name=pnr; Synonyms=GATA-A; ORFNames=CG3978;
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=7916677; DOI=10.1242/dev.119.4.1055;
RA Winick J., Abel T., Leonard M.W., Michelson A.M., Chardon-Loriaux I.,
RA Holmgren R.A., Maniatis T., Engel J.D.;
RT "A GATA family transcription factor is expressed along the embryonic
RT dorsoventral axis in Drosophila melanogaster.";
RL Development 119:1055-1065(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANTS PNRD1; PNRD2; PNRD3 AND
RP PNRD4.
RX PubMed=7916679; DOI=10.1242/dev.119.4.1277;
RA Ramain P., Heitzler P., Haenlin M., Simpson P.;
RT "Pannier, a negative regulator of achaete and scute in Drosophila, encodes
RT a zinc finger protein with homology to the vertebrate transcription factor
RT GATA-1.";
RL Development 119:1277-1291(1993).
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 INTERACTION WITH OSA.
RX PubMed=12629041; DOI=10.1101/gad.255703;
RA Heitzler P., Vanolst L., Biryukova I., Ramain P.;
RT "Enhancer-promoter communication mediated by Chip during Pannier-driven
RT proneural patterning is regulated by Osa.";
RL Genes Dev. 17:591-596(2003).
CC -!- FUNCTION: Transcriptional regulator involved in several developmental
CC processes during embryonic and imaginal disks development. Involved in
CC determining dorsal cell fate. Acts as an essential transcriptional
CC regulator of proneural achaete-scute complex (AS-C) and is required for
CC its spatial regulation during development of the adult peripheral
CC nervous system, and hence for the positioning of neural precursors. It
CC is the only factor to directly activate AS-C genes.
CC -!- SUBUNIT: Interacts with OSA. {ECO:0000269|PubMed:12629041}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DEVELOPMENTAL STAGE: It is first seen in the dorsal portion of the
CC embryo just after cellularization and is expressed at high levels
CC during early embryogenesis and as development progresses high levels
CC are seen in the dorsal epidermis.
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DR EMBL; S68798; AAB29874.1; -; Genomic_DNA.
DR EMBL; S68909; AAB29874.1; JOINED; Genomic_DNA.
DR EMBL; S68793; AAB29874.1; JOINED; Genomic_DNA.
DR EMBL; S68795; AAB29874.1; JOINED; Genomic_DNA.
DR EMBL; S68803; AAB29876.2; -; Genomic_DNA.
DR EMBL; S68802; AAB29876.2; JOINED; Genomic_DNA.
DR EMBL; AE014297; AAN13693.1; -; Genomic_DNA.
DR RefSeq; NP_476685.1; NM_057337.3.
DR AlphaFoldDB; P52168; -.
DR SMR; P52168; -.
DR BioGRID; 69326; 110.
DR IntAct; P52168; 2.
DR STRING; 7227.FBpp0082675; -.
DR PaxDb; P52168; -.
DR PRIDE; P52168; -.
DR DNASU; 44849; -.
DR EnsemblMetazoa; FBtr0083221; FBpp0082675; FBgn0003117.
DR GeneID; 44849; -.
DR KEGG; dme:Dmel_CG3978; -.
DR UCSC; CG3978-RA; d. melanogaster.
DR CTD; 44849; -.
DR FlyBase; FBgn0003117; pnr.
DR VEuPathDB; VectorBase:FBgn0003117; -.
DR eggNOG; KOG1601; Eukaryota.
DR GeneTree; ENSGT00940000160139; -.
DR InParanoid; P52168; -.
DR PhylomeDB; P52168; -.
DR Reactome; R-DME-5683826; Surfactant metabolism.
DR Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P52168; -.
DR BioGRID-ORCS; 44849; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 44849; -.
DR PRO; PR:P52168; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003117; Expressed in spermathecum and 18 other tissues.
DR ExpressionAtlas; P52168; baseline and differential.
DR Genevisible; P52168; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007350; P:blastoderm segmentation; IMP:FlyBase.
DR GO; GO:0007510; P:cardioblast cell fate determination; IMP:FlyBase.
DR GO; GO:0010002; P:cardioblast differentiation; IMP:FlyBase.
DR GO; GO:0035051; P:cardiocyte differentiation; IMP:FlyBase.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0022416; P:chaeta development; IGI:FlyBase.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:FlyBase.
DR GO; GO:0060047; P:heart contraction; IMP:FlyBase.
DR GO; GO:0048542; P:lymph gland development; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:FlyBase.
DR GO; GO:0061320; P:pericardial nephrocyte differentiation; IMP:FlyBase.
DR GO; GO:0042440; P:pigment metabolic process; IMP:FlyBase.
DR GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR CDD; cd00202; ZnF_GATA; 2.
DR Gene3D; 3.30.50.10; -; 2.
DR InterPro; IPR039355; Transcription_factor_GATA.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR10071; PTHR10071; 1.
DR Pfam; PF00320; GATA; 2.
DR PRINTS; PR00619; GATAZNFINGER.
DR SMART; SM00401; ZnF_GATA; 2.
DR PROSITE; PS00344; GATA_ZN_FINGER_1; 2.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..540
FT /note="GATA-binding factor A"
FT /id="PRO_0000083460"
FT ZN_FING 169..193
FT /note="GATA-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT ZN_FING 226..250
FT /note="GATA-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 168
FT /note="E->K: In pnrD4; abolishes DNA-binding."
FT MUTAGEN 169
FT /note="C->Y: In pnrD1; abolishes DNA-binding."
FT MUTAGEN 186
FT /note="G->E: In pnrD2; abolishes DNA-binding."
FT MUTAGEN 190
FT /note="C->S: In pnrD3; abolishes DNA-binding."
FT CONFLICT 413
FT /note="Y -> S (in Ref. 2; AAB29876)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 57036 MW; 46557C0754BEEB59 CRC64;
MGILLSDGDS TSDQQSTRDY PHFSGDYQNV TLSAASASTS ASASATHVAA VKMYHSSAVA
AYTDLAAAGS AASAGVGVGV SGYHQQAVNA PVYVPSNRQY NHVAAHFGSA AAQNAWTTEG
FGSAHAQFYS PNAAVMMGSW RSAYDPSGFQ RSSPYESAMD FQFGEGRECV NCGAISTPLW
RRDGTGHYLC NACGLYHKMN GMNRPLIKPS KRLVSATATR RMGLCCTNCG TRTTTLWRRN
NDGEPVCNAC GLYYKLHGVN RPLAMRKDGI QTRKRKPKKT GSGSAVGAGT GSGTGSTLEA
IKECKEEHDL KPSLSLERHS LSKLHTDMKS GTSSSSTLMG HHSAQQQQQQ QQQQQQQQQQ
QQQQSAHQQC FPLYGQTTTQ QQHQQHGHSM TSSSGQAHLS ARHLHGAAGT QLYTPGSSSG
GGSASAYTSH SAETPALSNG TPSPHYQHHH HLGGTHGHHV TAAAAHHHFH AAAAVAAYGV
KTEASATNYD YVNNCYFGGT FGALGGAATT TAMAGGAASE LAGYHHQHNV IQAAKLMATS
