ID   FOSL_DROVI              Reviewed;         792 AA.
AC   B4M5T7;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Transcription factor kayak {ECO:0000250|UniProtKB:P21525};
GN   Name=kay {ECO:0000250|UniProtKB:P21525}; ORFNames=GJ10642;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1] {ECO:0000312|EMBL:EDW59013.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW59013.1};
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; CH940652; EDW59013.1; -; Genomic_DNA.
DR   RefSeq; XP_002055901.2; XM_002055865.2.
DR   AlphaFoldDB; B4M5T7; -.
DR   SMR; B4M5T7; -.
DR   STRING; 7244.FBpp0225059; -.
DR   EnsemblMetazoa; FBtr0442597; FBpp0399057; FBgn0197920.
DR   GeneID; 6632814; -.
DR   KEGG; dvi:6632814; -.
DR   eggNOG; KOG1414; Eukaryota.
DR   HOGENOM; CLU_020183_0_0_1; -.
DR   InParanoid; B4M5T7; -.
DR   OMA; YQNGHIM; -.
DR   OrthoDB; 1378696at2759; -.
DR   PhylomeDB; B4M5T7; -.
DR   ChiTaRS; kay; fly.
DR   Proteomes; UP000008792; 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..792
FT                   /note="Transcription factor kayak"
FT                   /id="PRO_0000377391"
FT   DOMAIN          450..513
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          96..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..454
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          455..462
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          545..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          623..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         602
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21525"
SQ   SEQUENCE   792 AA;  85832 MW;  0A01908FD9A368D8 CRC64;
     MMKNLNGRTH NACYQPYYQQ QLQLQQQHQQ QQQLQQQQQL LQQQQQLQLP YAAPYNQLQQ
     QQYTQQQYYQ QQLQQQQQQQ QQQQQQLLRQ QQPTLSVYQQ QQHAKQSYGH NNSNNNANMT
     QTARSNMQTA SIATVSANGN NSSSSSSNAN AANSATAAMA AMCQMQSFLS QQQQQQQQQQ
     QQQQQQQQQQ YHNNCAHINY NQQQQQQQQQ LQQQQLSTAA TTNGDKLALD NASEIANFLA
     SELFMQQLVT FDGMQSAPTL TTPTLTPTTL RTIEETIYEL TTEPQIVPFQ AGFKPPPLTS
     LGAITNNNTV TPTTAAAAAA ATLAVVNANP INANPQFDLL GLNCNSVRGS DTEDSNGSWN
     DGQLNDDQST TDTSSAATDS TSYQNGGHML GNGSNGGVNN FTVALAAVNN AGRASGQAGG
     NSTTSNSGTP ARRGGGRRPN KAANMSPEEE EKRRIRRERN KLAAARCRKR RVDQTNELTE
     EVDALIKKGE DMKKEIENLN ATKNQLEYVL QAHRPTCQKV RNDLLSVVTC NGLIAPTTLL
     SAGSCTGTGS QHSNNNNNNS SNNNNSNSSN NNNNNSNSND SSSGGTITGF DATLNSTGRS
     NSPLDLKPVL TDEQLLQHIK NEPQDVGLDS SSSLDQDGPP PAKRCFALPN IAALTASLTT
     PTDPGSCSLN TPITSTAPNI FANFGGDLNS PTLNALNKLP KARPNTLNVQ QLQRPFVVQQ
     LGNDGNKAPP TQIQGVPIQT PSTGTFNFDS LMDGGTGLTP VSGPLVPTCS SQNKHPLELP
     TPTSEPSKLV SL