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FOSL_DROMO
ID   FOSL_DROMO              Reviewed;         784 AA.
AC   B4K617;
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=GI10426;
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230;
RN   [1] {ECO:0000312|EMBL:EDW16254.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22 {ECO:0000312|EMBL:EDW16254.1};
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; CH933806; EDW16254.1; -; Genomic_DNA.
DR   RefSeq; XP_002000793.2; XM_002000757.2.
DR   AlphaFoldDB; B4K617; -.
DR   SMR; B4K617; -.
DR   STRING; 7230.FBpp0159643; -.
DR   EnsemblMetazoa; FBtr0428490; FBpp0386028; FBgn0133190.
DR   GeneID; 6574764; -.
DR   eggNOG; KOG1414; Eukaryota.
DR   HOGENOM; CLU_020183_0_0_1; -.
DR   InParanoid; B4K617; -.
DR   OMA; YQNGHIM; -.
DR   OrthoDB; 1378696at2759; -.
DR   PhylomeDB; B4K617; -.
DR   ChiTaRS; kay; fly.
DR   Proteomes; UP000009192; 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..784
FT                   /note="Transcription factor kayak"
FT                   /id="PRO_0000377386"
FT   DOMAIN          459..522
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          97..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          461..463
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          464..471
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          616..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          759..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         594
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21525"
SQ   SEQUENCE   784 AA;  85158 MW;  C9E7BC2EDFABCEED CRC64;
     MMKNLNGRAH NVCYQPYYQQ QLQHQQLHQQ QHQQQQQQQQ QQQHLQQQQL QLQLPYAAQY
     NQLQQQQLQY NQQQYYQQQL QQQQQQQQQQ QLLRQQQPTQ SAYQQQNAKQ SYGHNNNNNS
     NNNANMARSN MHATTVAAVN ANGNSHANAA NANTATAAMA AMCQMQSFLS QQQQQQRQQQ
     QQQQQQYSNN SAHINYNQQQ QQSQQQQQSQ QQQQSQQQQQ SQQQQQQHLP TVATTNGDKL
     TLDSANEIAN FLANELFMQQ LVTFDGMQSA PTLTTPTLTP TTLRTIEDTI YELTTDSHVP
     FQAGFKPPPL TSLGNITNNN TITSTTAGGA TLPGINANLI NTNPQFDLIA LNCAGSVPGS
     DTEESNGSWN EGQLNDDQST TDTSSAATDS TSYQNGGHMM GNGSNGGVNN FAAALSGVNT
     SGRGSGLAAN STTSNSATPA RRGGGRRPNK AANMSPEEEE KRRIRRERNK LAAARCRKRR
     VDQTNELTEE VDALMKKSED LKKEIESLTA TKSQLEYVLQ THSSTCQKVR DDLLTVATCN
     GLIGPTTLLN ACNTSSVSLH NSNNSNNNSN SNDSSNGTIT GFDATLNSTG RSNSPLDLKP
     VLIDEQLLQH IKHEPQDGAI DSGSSLDQDG PTPAKRFALP NIATFNASLQ TPTGPAAGAA
     LNTPISSTAP SSFAHFSSAI SSPTLNAHAL NKLPKPRPNT LNVNAQRPFG VAAAAGDGKA
     PPTQIQGVPI QTPSTGTFNF DSLMDGGTGL TPVSGPLMPT CSSQNKHPLE LPTPTSEPSK
     LVSL
 
 
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