FOSLD_DROME
ID FOSLD_DROME Reviewed; 722 AA.
AC A8MPH9; A8MPH8;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Transcription factor kayak, isoforms D/sro {ECO:0000250|UniProtKB:P21525, ECO:0000303|PubMed:18571877, ECO:0000312|EMBL:ABI74757.1};
DE AltName: Full=AP-1 {ECO:0000250|UniProtKB:P21525};
DE AltName: Full=Fos-related antigen {ECO:0000250|UniProtKB:P21525};
DE Short=Dfos {ECO:0000250|UniProtKB:P21525};
DE Short=dFra {ECO:0000250|UniProtKB:P21525};
GN Name=kay {ECO:0000303|PubMed:18571877};
GN Synonyms=Fra {ECO:0000250|UniProtKB:P21525}; ORFNames=CG15509;
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] {ECO:0000305, ECO:0000312|EMBL:ABI74757.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SRO), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 1-215 (ISOFORM D), ALTERNATIVE PROMOTER USAGE, ALTERNATIVE SPLICING,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=18571877; DOI=10.1016/j.gene.2008.05.001;
RA Hudson S.G., Goldstein E.S.;
RT "The gene structure of the Drosophila melanogaster proto-oncogene, kayak,
RT and its nested gene, fos-intronic gene.";
RL Gene 420:76-81(2008).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [3] {ECO:0000305}
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 [4] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000269|PubMed:18327897};
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).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH JRA, AND SUBCELLULAR LOCATION.
RC TISSUE=Embryo {ECO:0000269|PubMed:2116361};
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).
CC -!- FUNCTION: Developmentally regulated transcription factor AP-1 binds and
CC recognizes the enhancer DNA sequence: 5'-TGA[CG]TCA-3'. May play a role
CC in the function or determination of a particular subset of cells in the
CC developing embryo. It is able to carry out its function either
CC independently of or in conjunction with Jra.
CC {ECO:0000269|PubMed:2116361}.
CC -!- SUBUNIT: Homodimer. Heterodimer with Jra. The kay-Jra heterodimer binds
CC more stably to the AP-1 site than either of the two proteins alone.
CC -!- INTERACTION:
CC A8MPH9; P18289: Jra; NbExp=3; IntAct=EBI-22062276, EBI-159948;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:2116361}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
CC Name=D {ECO:0000269|PubMed:10731132}; Synonyms=alpha
CC {ECO:0000269|PubMed:18571877};
CC IsoId=A8MPH9-1; Sequence=Displayed;
CC Name=sro {ECO:0000269|PubMed:18571877}; Synonyms=shroud
CC {ECO:0000269|PubMed:18571877};
CC IsoId=A8MPH9-2; Sequence=VSP_053112, VSP_053113;
CC Name=A {ECO:0000269|PubMed:10731132}; Synonyms=beta
CC {ECO:0000269|PubMed:18571877};
CC IsoId=P21525-2; Sequence=External;
CC Name=B {ECO:0000269|PubMed:10731132}; Synonyms=gamma
CC {ECO:0000269|PubMed:18571877};
CC IsoId=P21525-3; Sequence=External;
CC Name=F {ECO:0000269|PubMed:10731132};
CC IsoId=P21525-5; Sequence=External;
CC -!- DEVELOPMENTAL STAGE: Isoform D and isoform sro are expressed both
CC maternally and zygotically. Zygotic expression is present throughout
CC embryogenesis, fading by second larval instar. Isoform D has higher
CC expression level than isoform sro. {ECO:0000269|PubMed:18571877}.
CC -!- DISRUPTION PHENOTYPE: Loss of isoform D causes embryonic lethality.
CC {ECO:0000269|PubMed:18571877}.
CC -!- MISCELLANEOUS: Mammals typically have four copies of fos, Drosophila
CC has a single gene with multiple transcription start sites giving rise
CC to multiple protein isoforms.
CC -!- MISCELLANEOUS: [Isoform D]: Produced by alternative promoter usage.
CC {ECO:0000269|PubMed:18571877}.
CC -!- MISCELLANEOUS: [Isoform sro]: May perform a regulatory function, acting
CC as a dominant negative regulator of isoform alpha. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000255}.
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DR EMBL; DQ858474; ABI74756.1; -; mRNA.
DR EMBL; DQ858475; ABI74757.1; -; mRNA.
DR EMBL; AE014297; AAZ83991.1; -; Genomic_DNA.
DR RefSeq; NP_001027580.1; NM_001032408.3. [A8MPH9-1]
DR AlphaFoldDB; A8MPH9; -.
DR SMR; A8MPH9; -.
DR BioGRID; 533679; 67.
DR IntAct; A8MPH9; 1.
DR iPTMnet; A8MPH9; -.
DR PRIDE; A8MPH9; -.
DR DNASU; 3772082; -.
DR EnsemblMetazoa; FBtr0099988; FBpp0099941; FBgn0001297. [A8MPH9-1]
DR GeneID; 3772082; -.
DR CTD; 3772082; -.
DR FlyBase; FBgn0001297; kay.
DR VEuPathDB; VectorBase:FBgn0001297; -.
DR SignaLink; A8MPH9; -.
DR BioGRID-ORCS; 3772082; 2 hits in 3 CRISPR screens.
DR ChiTaRS; kay; fly.
DR GenomeRNAi; 3772082; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0001297; Expressed in wing disc and 50 other tissues.
DR ExpressionAtlas; A8MPH9; baseline and differential.
DR Genevisible; A8MPH9; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035976; C:transcription factor AP-1 complex; IPI:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI: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:0048674; P:collateral sprouting of injured axon; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0007281; P:germ cell development; IMP:FlyBase.
DR GO; GO:0046529; P:imaginal disc fusion, thorax closure; IMP:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0007297; P:ovarian follicle cell migration; IMP:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IGI: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; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009611; P:response to wounding; IMP:FlyBase.
DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IGI:FlyBase.
DR GO; GO:0042060; P:wound healing; IMP:FlyBase.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PRINTS; PR00042; LEUZIPPRFOS.
DR SMART; SM00338; BRLZ; 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; Alternative promoter usage; Alternative splicing; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..722
FT /note="Transcription factor kayak, isoforms D/sro"
FT /id="PRO_0000377385"
FT DOMAIN 385..448
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 173..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..406
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 413..420
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 477..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 202..210
FT /note="LGNFETGQS -> VSGLVKCVR (in isoform sro)"
FT /evidence="ECO:0000303|PubMed:18571877"
FT /id="VSP_053112"
FT VAR_SEQ 211..722
FT /note="Missing (in isoform sro)"
FT /evidence="ECO:0000303|PubMed:18571877"
FT /id="VSP_053113"
SQ SEQUENCE 722 AA; 78320 MW; F7BD3A403A1E8770 CRC64;
MIALKATEMQ HNNNALQQQQ QLQHQLLQQH QQQHQQQLQQ QLNSPDNNYI WATTHNANIS
RNNAMLQLQQ QQLRAPWITD CNKQHHINNN NSMNVNYNQQ LTQQPQQQQQ QTQYMQHNYN
NYTQQQQQQH LVPATTSQSN SHFYQCNQQQ QQQQFLAPTT TTAAVVVAAA HQQHQTQQQH
QSQQQQQHQR QDYASLQMGR QLGNFETGQS VLTLTTPTLT PTTTRNIEDT LGHLLSDTQT
DRVAGCAGFA VPKVLPNAID VLGMGIPTGV SSLPLQQTFD LSLGQGSESE DSNASYNDTQ
MNEEQDTTDT SSAHTDSTSY QAGHIMAGSV NGGGVNNFSN VLAAVSSSRG SASVGSSNAN
TSNTPARRGG GRRPNRSTNM TPEEEQKRAV RRERNKQAAA RCRKRRVDQT NELTEEVEQL
EKRGESMRKE IEVLTNSKNQ LEYLLATHRA TCQKIRSDML SVVTCNGLIA PAGLLSAGSS
GSGASSHHNH NSNDSSNGTI TGMDATLNST GRSNSPLDLK PAANIDSLLM HIKDEPLDGA
IDSGSSLDQD GPPPSKRITL PPMSTMPHVH LSTILTPTGA SSGSLQTPIT STAPGGFGSA
FPVTSNGSSI NNINSIGNNM NSPTLNAHNK VPKERPNTLA FQRPLGQMHL TMANNKAGGP
TQIQGVPIQT PSTGTFNFDS LMDGGTGLTP VSGPLVPNSS STNKHPLELP TPTAEPSKLV
SL
