ID JRA_DROME Reviewed; 289 AA.
AC P18289; Q0E9D8; Q9V5G4;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 27-MAR-2024, entry version 220.
DE RecName: Full=Transcription factor Jra {ECO:0000305};
DE AltName: Full=Jun-related antigen;
DE AltName: Full=Transcription factor AP-1 subunit Jra {ECO:0000305};
DE AltName: Full=dJRA;
DE AltName: Full=dJun;
GN Name=Jra; Synonyms=jun; ORFNames=CG2275;
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], FUNCTION, INTERACTION WITH KAY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R;
RX PubMed=1696724; DOI=10.1073/pnas.87.16.6281;
RA Zhang K., Chaillet J.R., Perkins L.A., Halazonetis T.D., Perrimon N.;
RT "Drosophila homolog of the mammalian jun oncogene is expressed during
RT embryonic development and activates transcription in mammalian cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6281-6285(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION
RP WITH KAY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=2116361; DOI=10.1101/gad.4.5.822;
RA Perkins K.K., Admon A., Patel N., Tjian R.;
RT "The Drosophila Fos-related AP-1 protein is a developmentally regulated
RT transcription factor.";
RL Genes Dev. 4:822-834(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Oregon-R;
RX PubMed=9224723; DOI=10.1101/gad.11.13.1748;
RA Kockel L., Zeitlinger J., Staszewski L., Mlodzik M., Bohmann D.;
RT "Jun in Drosophila development: redundant and nonredundant functions and
RT regulation by two MAPK signal transduction pathways.";
RL Genes Dev. 11:1748-1758(1997).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [8]
RP INTERACTION WITH ATF3.
RX PubMed=20023169; DOI=10.1242/dev.037861;
RA Sekyrova P., Bohmann D., Jindra M., Uhlirova M.;
RT "Interaction between Drosophila bZIP proteins Atf3 and Jun prevents
RT replacement of epithelial cells during metamorphosis.";
RL Development 137:141-150(2010).
CC -!- FUNCTION: Transcription factor that recognizes and binds to the
CC enhancer heptamer motif 5'-TGA[CG]TCA-3' (PubMed:1696724,
CC PubMed:2116361). Plays a role in dorsal closure (PubMed:9224723).
CC {ECO:0000269|PubMed:1696724, ECO:0000269|PubMed:2116361,
CC ECO:0000269|PubMed:9224723}.
CC -!- SUBUNIT: Heterodimer with kay/Fra (PubMed:1696724, PubMed:2116361). The
CC kay-Jra complex is bound more stably to the AP-1 site than either of
CC the two proteins alone (PubMed:2116361). Interacts with Atf3; the
CC interaction enhances the DNA-binding activity of Atf3
CC (PubMed:20023169). {ECO:0000269|PubMed:1696724,
CC ECO:0000269|PubMed:20023169, ECO:0000269|PubMed:2116361}.
CC -!- INTERACTION:
CC P18289; A8MPH9: kay; NbExp=3; IntAct=EBI-159948, EBI-22062276;
CC P18289; P21525: kay; NbExp=3; IntAct=EBI-159948, EBI-195448;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9224723}.
CC -!- TISSUE SPECIFICITY: During embryogenesis, expression is elevated in the
CC amnioserosa, in the cells of the dorsolateral epidermis during and
CC following germ-band retraction, in the cells at the leading dorsal edge
CC of the epidermis and in the cells along the cephalic furrow (at protein
CC level). {ECO:0000269|PubMed:9224723}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryonic development.
CC {ECO:0000269|PubMed:1696724, ECO:0000269|PubMed:2116361,
CC ECO:0000269|PubMed:9224723}.
CC -!- DISRUPTION PHENOTYPE: Death in mid to late embryogenesis with large
CC anterior and dorsal holes. {ECO:0000269|PubMed:9224723}.
CC -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily. {ECO:0000305}.
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DR EMBL; M36181; AAA28650.1; -; Genomic_DNA.
DR EMBL; X54144; CAA38083.1; -; mRNA.
DR EMBL; Y12573; CAA73154.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58845.1; -; Genomic_DNA.
DR EMBL; AY058562; AAL13791.1; -; mRNA.
DR PIR; A36011; TVFFJD.
DR RefSeq; NP_476586.1; NM_057238.5.
DR RefSeq; NP_724882.1; NM_165739.2.
DR AlphaFoldDB; P18289; -.
DR SMR; P18289; -.
DR BioGRID; 61885; 68.
DR DIP; DIP-18982N; -.
DR IntAct; P18289; 15.
DR STRING; 7227.FBpp0303456; -.
DR GlyGen; P18289; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; P18289; -.
DR PaxDb; 7227-FBpp0087498; -.
DR EnsemblMetazoa; FBtr0088410; FBpp0087498; FBgn0001291.
DR EnsemblMetazoa; FBtr0088411; FBpp0087499; FBgn0001291.
DR GeneID; 36057; -.
DR KEGG; dme:Dmel_CG2275; -.
DR AGR; FB:FBgn0001291; -.
DR CTD; 36057; -.
DR FlyBase; FBgn0001291; Jra.
DR VEuPathDB; VectorBase:FBgn0001291; -.
DR eggNOG; KOG0837; Eukaryota.
DR GeneTree; ENSGT00940000169681; -.
DR HOGENOM; CLU_057007_0_0_1; -.
DR InParanoid; P18289; -.
DR OMA; HHQHMPA; -.
DR PhylomeDB; P18289; -.
DR Reactome; R-DME-209394; Transcriptional activtion and repression of REL-68 target genes.
DR Reactome; R-DME-209409; Formation of the nuclear AP-1 transcription factor 'scaffolding complex'.
DR Reactome; R-DME-209425; Transcriptional activtion by AP-1 transcription factor.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-2871796; FCERI mediated MAPK activation.
DR Reactome; R-DME-450341; Activation of the AP-1 family of transcription factors.
DR SignaLink; P18289; -.
DR BioGRID-ORCS; 36057; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36057; -.
DR PRO; PR:P18289; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0001291; Expressed in adult Malpighian tubule (Drosophila) and 25 other cell types or tissues.
DR ExpressionAtlas; P18289; baseline and differential.
DR Genevisible; P18289; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0035976; C:transcription factor AP-1 complex; IPI:FlyBase.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
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:0046844; P:chorion micropyle formation; IMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0046529; P:imaginal disc fusion, thorax closure; IMP:FlyBase.
DR GO; GO:0007254; P:JNK cascade; IMP:FlyBase.
DR GO; GO:0044827; P:modulation by host of viral genome replication; IMP:FlyBase.
DR GO; GO:0008348; P:negative regulation of antimicrobial humoral response; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0007464; P:R3/R4 cell fate commitment; TAS:FlyBase.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IGI:FlyBase.
DR GO; GO:0042060; P:wound healing; HMP:FlyBase.
DR CDD; cd14696; bZIP_Jun; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR005643; JNK.
DR InterPro; IPR002112; Leuzip_Jun.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR PANTHER; PTHR11462; JUN TRANSCRIPTION FACTOR-RELATED; 1.
DR PANTHER; PTHR11462:SF35; TRANSCRIPTION FACTOR JRA; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF03957; Jun; 1.
DR PRINTS; PR00043; LEUZIPPRJUN.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47454; A DNA-binding domain in eukaryotic transcription factors; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Activator; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..289
FT /note="Transcription factor Jra"
FT /id="PRO_0000076437"
FT DOMAIN 212..275
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 32..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..239
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 240..268
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 42..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT CONFLICT 267..268
FT /note="QL -> HV (in Ref. 1; AAA28650 and 3; CAA73154)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 31021 MW; FCCA13A6D2AF32BF CRC64;
MKTPVSAAAN LSIQNAGSSG ATAIQIIPKT EPVGEEGPMS LDFQSPNLNT STPNPNKRPG
SLDLNSKSAK NKRIFAPLVI NSPDLSSKTV NTPDLEKILL SNNLMQTPQP GKVFPTKAGP
VTVEQLDFGR GFEEALHNLH TNSQAFPSAN SAANSAANNT TAAAMTAVNN GISGGTFTYT
NMTEGFSVIK DEPVNQASSP TVNPIDMEAQ EKIKLERKRQ RNRVAASKCR KRKLERISKL
EDRVKVLKGE NVDLASIVKN LKDHVAQLKQ QVMEHIAAGC TVPPNSTDQ
//
