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FOSL_DROPE
ID   FOSL_DROPE              Reviewed;         526 AA.
AC   B4G652;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-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=GL23721;
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234;
RN   [1] {ECO:0000312|EMBL:EDW23811.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479179; EDW23811.1; -; Genomic_DNA.
DR   RefSeq; XP_002012825.1; XM_002012789.1.
DR   AlphaFoldDB; B4G652; -.
DR   SMR; B4G652; -.
DR   STRING; 7234.FBpp0187828; -.
DR   EnsemblMetazoa; FBtr0189336; FBpp0187828; FBgn0161311.
DR   eggNOG; KOG1414; Eukaryota.
DR   HOGENOM; CLU_020183_0_0_1; -.
DR   OMA; YQNGHIM; -.
DR   PhylomeDB; B4G652; -.
DR   ChiTaRS; kay; fly.
DR   Proteomes; UP000008744; 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..526
FT                   /note="Transcription factor kayak"
FT                   /id="PRO_0000377387"
FT   DOMAIN          208..271
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          71..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..229
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          236..264
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          301..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..340
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         339
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21525"
SQ   SEQUENCE   526 AA;  55860 MW;  1A39D854374ECA4F CRC64;
     MTLDNYNIFG DEYLFSMPLS PLPKVLGTFD GIQSAPTLTT PTLTPTTLRS IEETFFEMTN
     DAPYQAGFKP PPLAPLVNNN NNNNNNGNGN GNGNGNQQQQ QVFDCGASVM PGSDTEESNG
     SWADGQMNED QSISDTSSGA TDSTSYQNGH MMGNSGGGNG GGTGGANNFS NVLAAAGRNT
     NTSNSATPAR RGGGRRPNRS ANMTPEEEEK RRIRRERNKQ AAARCRKRRV DQTNELTEEV
     ELLEKRGENL KKEMELLNET KNQLEYFLQA HRPTCQKVRA DMLSVTTCNG LIGPPALLSA
     GSCGSGSSHH NNNSNSNDSS SGTITGLDAT LNSTGRSNSP LDLKPVPIDE DLLLHIKDEP
     LDGALDSSSS LDQDGPPPHK RFALPNIATL MTPTGPAGSL QTPVSGTAPH GFGSFPTTIS
     NISSIHNGPT LNSLNKMPKE RPNTLAFQRP FGGQMQLSVS GRAPTQIQGV PIQTPSTGTF
     NFDSLMDGGT GLTPVSGPLI PNCTSQNKHP LELPTPTTEP SKLVSL
 
 
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