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FOSL_DROWI
ID   FOSL_DROWI              Reviewed;         620 AA.
AC   B4NBL5;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Transcription factor kayak {ECO:0000250|UniProtKB:P21525};
GN   Name=kay {ECO:0000250|UniProtKB:P21525}; ORFNames=GK11924;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1] {ECO:0000312|EMBL:EDW81179.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24 {ECO:0000312|EMBL:EDW81179.1};
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; CH964232; EDW81179.1; -; Genomic_DNA.
DR   RefSeq; XP_002070193.2; XM_002070157.2.
DR   AlphaFoldDB; B4NBL5; -.
DR   SMR; B4NBL5; -.
DR   STRING; 7260.FBpp0241067; -.
DR   GeneID; 6647957; -.
DR   KEGG; dwi:6647957; -.
DR   eggNOG; KOG1414; Eukaryota.
DR   HOGENOM; CLU_020183_0_0_1; -.
DR   InParanoid; B4NBL5; -.
DR   OMA; YQNGHIM; -.
DR   OrthoDB; 1378696at2759; -.
DR   PhylomeDB; B4NBL5; -.
DR   ChiTaRS; kay; fly.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblMetazoa.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0035976; C:transcription factor AP-1 complex; IEA:EnsemblMetazoa.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:EnsemblMetazoa.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:EnsemblMetazoa.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:EnsemblMetazoa.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:EnsemblMetazoa.
DR   GO; GO:0048674; P:collateral sprouting of injured axon; IEA:EnsemblMetazoa.
DR   GO; GO:0048813; P:dendrite morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0007391; P:dorsal closure; IEA:EnsemblMetazoa.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; ISS:UniProtKB.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:EnsemblMetazoa.
DR   GO; GO:0046529; P:imaginal disc fusion, thorax closure; IEA:EnsemblMetazoa.
DR   GO; GO:0045475; P:locomotor rhythm; IEA:EnsemblMetazoa.
DR   GO; GO:0007297; P:ovarian follicle cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IEA:EnsemblMetazoa.
DR   GO; GO:1903688; P:positive regulation of border follicle cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:0007464; P:R3/R4 cell fate commitment; IEA:EnsemblMetazoa.
DR   GO; GO:0016330; P:second mitotic wave involved in compound eye morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IEA:EnsemblMetazoa.
DR   GO; GO:0035220; P:wing disc development; IEA:EnsemblMetazoa.
DR   GO; GO:0042060; P:wound healing; IEA:EnsemblMetazoa.
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..620
FT                   /note="Transcription factor kayak"
FT                   /id="PRO_0000377392"
FT   DOMAIN          284..347
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..305
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          312..340
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          375..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..264
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..608
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         422
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21525"
SQ   SEQUENCE   620 AA;  64962 MW;  8B3AB6157D3457BD CRC64;
     MKVKVERTTI TKKTTTTKPK PDEEDNNDDN SSSNGVEVTA TATATRETSD QLDFLPADLS
     ATISTTTTPT ATRATTTRNL ILHPFDGMQS APTLTTPTLT PTTLRSIDEA FYELTGETNN
     SVNAPFQAGF KPPPLALLPN SGPVVGIGSA VEAIVPAGNT LEIGHQPNLD VLSKLNYSNS
     IVGSDTDDSN ASWNDQHRIN GDTTDTSSGA TDSTSYQNNS MLGNGSNGSG ANNFTGALAA
     NQSTGGRGAN NNSNTNTSNS ATPAARRGGG RRPNKAFNMT PEEEEKRRIR RERNKAAAAR
     CRKRRVDQTN DLTEEVDALV KKGDTLKAEI TTLTELRNQL KYVIEAHLPT CPKVRDDILS
     VSTCNGLIGP AALHSTGGSS CGSVHSNHSH NNNNNNNNSN DSSSGTITGF DATLNSTGRS
     HSPLDLKPVH IDENLLLAIK HEPLDNGLDS ESSSLDQDGP PPAKRAVPLP TIAQLTASLT
     TPTNPNGGSL NTPIVSQAPV SFAAFAANAN NPNSPTLNLL NKGPKARPNT LAVQRPFAAP
     MQLNASGTGG VVDGKGAPIQ IQGVPIQTPS TGVFNFDSLM DGGTGLTPVS GPLIPNCSSQ
     NKHPLELPTP TTEPSKLCPL
 
 
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