ID   FOSL_DROSI              Reviewed;         498 AA.
AC   B4R090;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Transcription factor kayak {ECO:0000250|UniProtKB:P21525};
GN   Name=kay {ECO:0000250|UniProtKB:P21525}; ORFNames=GD21465;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1] {ECO:0000312|EMBL:EDX14896.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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; CM000364; EDX14896.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4R090; -.
DR   SMR; B4R090; -.
DR   STRING; 7240.B4R090; -.
DR   HOGENOM; CLU_020183_0_0_1; -.
DR   OMA; YQNGHIM; -.
DR   PhylomeDB; B4R090; -.
DR   ChiTaRS; kay; fly.
DR   Proteomes; UP000000304; 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; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..498
FT                   /note="Transcription factor kayak"
FT                   /id="PRO_0000377390"
FT   DOMAIN          212..275
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          108..144
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..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          465..498
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        468..484
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   498 AA;  52725 MW;  3DDEE737636F284E CRC64;
     MTLDSYNIFN DEYLFNMPLS PLPKVLGNFE TGQSVLTLTT PTLTPTTTRN IEDTLGHLLS
     DTQTDRVAGC AGFAVPKVLP NAMGAIDALG MGIPTCVSSL PLQQTYDASL GQGSESEDSN
     ASYNDTQMNE EQDTTDTSSA HTDSTSYQAG HIMAGSVNGG GVNNFTNVLA AVSSSRGSAS
     VGSSNANTSN TPARRGGGRR PNRSTNMTPE EEQKRAVRRE RNKQAAARCR KRRVDQTNEL
     TEEVEQLEKR RDSMRKEFEA LTNSKKQLEY LLATHRSTCQ KIRSDMLSVA TCNGLIAPAG
     LLSAGSSGSG ASSHHNHNSN DSSNGTITGM DATLNSTGRS NSPLDLKPAA NIDSLLLHIK
     DEPLDGAIDS GSSLDRFPVT SNGSSINNIN SIGNNMNSPT LNALNKVPKE RPNTLAFQRP
     LGQMHLSMAN NKAGGPTQIQ GVPIQTPSTG TFNLVSLMDG GTGLTPVSGP LVPNSSSTNK
     HPLELPTPTA EPSKLVSL