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JRA_DROME
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   03-AUG-2022, entry version 212.
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; 14.
DR   STRING; 7227.FBpp0087498; -.
DR   iPTMnet; P18289; -.
DR   PaxDb; P18289; -.
DR   PRIDE; P18289; -.
DR   EnsemblMetazoa; FBtr0088410; FBpp0087498; FBgn0001291.
DR   EnsemblMetazoa; FBtr0088411; FBpp0087499; FBgn0001291.
DR   GeneID; 36057; -.
DR   KEGG; dme:Dmel_CG2275; -.
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   OrthoDB; 1090460at2759; -.
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   Reactome; R-DME-9018519; Estrogen-dependent gene expression.
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 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:0010259; P:multicellular organism aging; IMP:FlyBase.
DR   GO; GO:0008348; P:negative regulation of antimicrobial humoral response; IMP:FlyBase.
DR   GO; GO:0045823; P:positive regulation of heart contraction; 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   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR005643; JNK.
DR   InterPro; IPR029823; JunD.
DR   InterPro; IPR002112; Leuzip_Jun.
DR   InterPro; IPR008917; TF_DNA-bd_sf.
DR   PANTHER; PTHR11462:SF7; PTHR11462:SF7; 2.
DR   Pfam; PF00170; bZIP_1; 1.
DR   Pfam; PF03957; Jun; 1.
DR   PRINTS; PR00043; LEUZIPPRJUN.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF47454; SSF47454; 1.
DR   SUPFAM; SSF57959; SSF57959; 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
 
 
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