ID   FOSL_DROAN              Reviewed;         529 AA.
AC   B3MTI9;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Transcription factor kayak {ECO:0000250|UniProtKB:P21525};
GN   Name=kay {ECO:0000250|UniProtKB:P21525}; ORFNames=GF23375;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1] {ECO:0000312|EMBL:EDV30579.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13 {ECO:0000312|EMBL:EDV30579.1};
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. Is able to carry out its function either
CC       independently of or in conjunction with Jra (By similarity).
CC       {ECO:0000250}.
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; CH902623; EDV30579.1; -; Genomic_DNA.
DR   RefSeq; XP_001964783.1; XM_001964747.2.
DR   AlphaFoldDB; B3MTI9; -.
DR   SMR; B3MTI9; -.
DR   STRING; 7217.FBpp0126567; -.
DR   EnsemblMetazoa; FBtr0128075; FBpp0126567; FBgn0100369.
DR   GeneID; 6506017; -.
DR   KEGG; dan:6506017; -.
DR   eggNOG; KOG1414; Eukaryota.
DR   HOGENOM; CLU_020183_0_0_1; -.
DR   InParanoid; B3MTI9; -.
DR   OMA; YQNGHIM; -.
DR   PhylomeDB; B3MTI9; -.
DR   ChiTaRS; kay; fly.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
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; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..529
FT                   /note="Transcription factor kayak"
FT                   /id="PRO_0000377382"
FT   DOMAIN          219..282
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          118..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..240
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          247..275
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          311..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         349
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21525"
SQ   SEQUENCE   529 AA;  56221 MW;  8C9C99F056B10689 CRC64;
     MTLDNYNIFN DEYLFGMPLS PLPKVLGTFD GIQLAPTLTT PTLTPTTTRS LQEAFFELTN
     DPGTPYQATF KPPPLGLMPG GNNGNGVTNV PTTTATATVV GVVNPMISQL PYEVNSALQG
     TDSDNSNASW ADAQNNEDQD TTDTSSAHTD STSYQNGHMA GSSVNGGGAN NFTNVLAGIN
     AGRGSTQGSN TNTSNSATPA RRGGGRRPNR NTNMSPEEEE KRRIRRERNK QAAARCRKRR
     VDQTNELTYE VEQLEKKRDG LKKEMETLTD VKNQLEFFLR AHHSSCQKIR TDLLSVTTCN
     GLIAPVGLPS AGSCDSGSSS HHNNNSNDSS NGTITGLDAS LNSTGRSNSP LDLKPQIKDE
     PLDGGLDSSC LLDQDGPPPS KRFPLPPMST LMTPTGVSSG SLQTPIASTA PGGFGSAYPI
     TTTKGSMNSP TLNELNKPKE RPNTLAVQRP FVPQMHLNLT SNHNKMPGSG PTHIQGVPIQ
     TPTTGFNFDS LMDGGTGLTP VSGPLVPSQN KHPLELPTPT AEPSKLVSL