ID   FOSL_DROER              Reviewed;         549 AA.
AC   B3P5D2;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Transcription factor kayak {ECO:0000250|UniProtKB:P21525};
GN   Name=kay {ECO:0000250|UniProtKB:P21525}; ORFNames=GG11694;
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220;
RN   [1] {ECO:0000312|EMBL:EDV53182.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14021-0224.01 {ECO:0000312|EMBL:EDV53182.1};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH954182; EDV53182.1; -; Genomic_DNA.
DR   RefSeq; XP_001981312.1; XM_001981276.2.
DR   AlphaFoldDB; B3P5D2; -.
DR   SMR; B3P5D2; -.
DR   STRING; 7220.FBpp0130240; -.
DR   EnsemblMetazoa; FBtr0131748; FBpp0130240; FBgn0103990.
DR   GeneID; 6554552; -.
DR   KEGG; der:6554552; -.
DR   eggNOG; KOG1414; Eukaryota.
DR   HOGENOM; CLU_020183_0_0_1; -.
DR   OMA; YQNGHIM; -.
DR   PhylomeDB; B3P5D2; -.
DR   ChiTaRS; kay; fly.
DR   Proteomes; UP000008711; 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; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..549
FT                   /note="Transcription factor kayak"
FT                   /id="PRO_0000377383"
FT   DOMAIN          211..274
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          177..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..232
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          239..246
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          363..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..379
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..535
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21525"
SQ   SEQUENCE   549 AA;  57985 MW;  6D5E70709EB04193 CRC64;
     MTLDNYNIFN DEYLFNMPLS PLPKVLGSFE AQSVLTLTTP TLTPTTTRNI EDTIGHLLSD
     TQADRGAGCA GFAVPKVLPN AMGAIEALGM GIPSGVTTIP IQTSYDMSLA QASESEDSNA
     SYNDMQMNEE QDTTDTSSAH TDSTSYQTGH IMAGSVNGGG ANNFTNVLAA VNSSRGVASA
     GSSNANTSNT PARRGGGRRP NRSTNMTPEE EQKRAVRRER NKQAAARCRK RRVDQTNELT
     EEVEQLEKRG DAMRKEIEAL TNSKSELEYL LIAHRSTCQK IRSDMLSVNT CNGLIAPTGL
     LSAGSNGSGA SSHHNHNSND SSNGTITGMD ATLNSTGRSN SPLDLKPSAN IESLMLHIKD
     EPLDSTIDSG SSLDQNGPPP SKRVTLPPMS TMPHMSTLMT PTGASSGSLQ TPITSTAPVA
     FGSAFPVTTN GSSINCITIN SISNNNMNSP TLNALNKVPK ERPNTLAFQR PMAQMHLTLP
     NNKAGGPTQI QGVPIQTPST GTFNFDSLMD GGTGLTPVSG PLVPNSSSTN KHPLELPTPT
     AEPSKLVSL