ID   FOSL_DROYA              Reviewed;         552 AA.
AC   B4PPK2;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Transcription factor kayak {ECO:0000250|UniProtKB:P21525};
GN   Name=kay {ECO:0000250|UniProtKB:P21525}; ORFNames=GE23884;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1] {ECO:0000312|EMBL:EDW98252.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW98252.1};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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 (By similarity).
CC       {ECO:0000250|UniProtKB:P21525}.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P21525,
CC       ECO:0000255|PROSITE-ProRule:PRU00978}.
CC   -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000255}.
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DR   EMBL; CM000160; EDW98252.1; -; Genomic_DNA.
DR   RefSeq; XP_002098540.1; XM_002098504.2.
DR   AlphaFoldDB; B4PPK2; -.
DR   SMR; B4PPK2; -.
DR   STRING; 7245.FBpp0268894; -.
DR   EnsemblMetazoa; FBtr0270402; FBpp0268894; FBgn0241033.
DR   GeneID; 6538005; -.
DR   eggNOG; KOG1414; Eukaryota.
DR   HOGENOM; CLU_020183_0_0_1; -.
DR   OMA; YQNGHIM; -.
DR   PhylomeDB; B4PPK2; -.
DR   ChiTaRS; kay; fly.
DR   Proteomes; UP000002282; Chromosome 3R.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
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   3: Inferred from homology;
KW   Activator; DNA-binding; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..552
FT                   /note="Transcription factor kayak"
FT                   /id="PRO_0000377393"
FT   DOMAIN          212..275
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          110..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..233
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          240..247
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          304..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..344
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21525"
SQ   SEQUENCE   552 AA;  58054 MW;  122F38CE2F90B076 CRC64;
     MTLDSYNIFN DEYLFNMPLS PLPKVLGSFE TVQSVLTLTT PTLTPTTTRN IEDTIGHLLS
     DTQPDRGAGC AGFAVPKVLP NAMGAIEALG MGIPSGVNSL PIQPAYDVNL AQGSDSEDSN
     ASYNDTQMNE EQDTTDTSSA HTDSTSYQAG QIMAGSVNGG GVNNFTNVLA AVSSTRGAAS
     VGSSNANTSN TPARRGGGRR PNRSTNMTPE EEQKRAVRRE RNKQAAARCR KRRVDQTNEL
     TEEVEQLEKR GDSMRKEIEA LTMSKNQLEY CLAAHRPTCQ KIRSDMLSVT TCNGLIAPAG
     LLSAGSSGSG ASSHHNHNSN DSSNGTITGM DATLNSTGRS NSPLDLKPAA NIDSLLLQHI
     KDEPLDGAID SGSSLDQDGP PPSKRITLPP MSTMPHVHMS TLMTPTGASS GSLQTPITST
     APVGFGSAFP VTTNGSSINT INSISQNNMN SPTLNALNKV PKERPNTLAF QRPVGHMHLT
     LANNNKPGGP TQIQGVPIQT PSTGTFNFDS LMDGGTGLTP VSGPLVPNSS SANKHPLELP
     TPTAEPSKLV SL