FOSL_DROSE
ID FOSL_DROSE Reviewed; 549 AA.
AC B4HZE8;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Transcription factor kayak {ECO:0000250|UniProtKB:P21525};
GN Name=kay {ECO:0000250|UniProtKB:P21525}; ORFNames=GM12821;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1] {ECO:0000312|EMBL:EDW53405.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25 {ECO:0000312|EMBL:EDW53405.1};
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; CH480819; EDW53405.1; -; Genomic_DNA.
DR RefSeq; XP_002037246.1; XM_002037210.1.
DR AlphaFoldDB; B4HZE8; -.
DR SMR; B4HZE8; -.
DR STRING; 7238.B4HZE8; -.
DR EnsemblMetazoa; FBtr0195806; FBpp0194298; FBgn0167757.
DR GeneID; 6612743; -.
DR KEGG; dse:6612743; -.
DR HOGENOM; CLU_020183_0_0_1; -.
DR OMA; YQNGHIM; -.
DR PhylomeDB; B4HZE8; -.
DR ChiTaRS; kay; fly.
DR Proteomes; UP000001292; 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..549
FT /note="Transcription factor kayak"
FT /id="PRO_0000377389"
FT DOMAIN 212..275
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 108..143
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 367..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..192
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 519..535
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 549 AA; 57878 MW; E64F520D022F9621 CRC64;
MTLDSYNIFN DEYLFNMPLS PLPKVLGNFE TGQSVLTLTT PTLTPTTTRN IEDTLGHLLS
DTQTDRVAGC AGFAVPKVLP NAMGAIDALG MGIPTCVSSL PLQQTYDASL GQGSESEDSN
ASYNDTQMNE EQDTTDTSSA HTDSTSYQAG HIMVGSVNGG GVNNFTNVLA AVSSSRGSAS
VGSSNANTSN PPARRGGGRR PNRSTNMTPE EEQKRAVRRE RNKQAAARCR KRRVDQTNEL
TEEVEQLEKR RDSMRKEFEA LTNSKKQLEY LLATHRSTCQ KIRSDILSVA TCNGLIAPDG
LLSAGSSGSA ASSHHNHNSN DSSNGTITGM DATLNSTGRS NSPLDLKPAA NIDSLLLHIK
DEPLDGAIDS GSSLDQDGPP PSKRITLPPM STMPHVHLST LITPTGASSG SLQTPITSTA
PVGFGSAFPV TSNGSSINNI NSIGNSMNSP TLNALNKVPK ERPNTLAFQR PLGQMHLTMA
NNKAGGPTQI QGVPIQTPST GTFNFDSLMD GGTGLTPVSG PLVPNSSSTN KHPLELPTPT
AEPSKLVSL
