FOSL_DROGR
ID FOSL_DROGR Reviewed; 796 AA.
AC B4JYN3;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Transcription factor kayak {ECO:0000250|UniProtKB:P21525};
GN Name=kay {ECO:0000250|UniProtKB:P21525}; ORFNames=GH14331;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1] {ECO:0000312|EMBL:EDV90795.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00 {ECO:0000312|EMBL:EDV90795.1};
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; CH916377; EDV90795.1; -; Genomic_DNA.
DR RefSeq; XP_001996137.1; XM_001996101.1.
DR AlphaFoldDB; B4JYN3; -.
DR SMR; B4JYN3; -.
DR STRING; 7222.FBpp0148237; -.
DR GeneID; 6569643; -.
DR KEGG; dgr:6569643; -.
DR eggNOG; KOG1414; Eukaryota.
DR HOGENOM; CLU_020183_0_0_1; -.
DR InParanoid; B4JYN3; -.
DR OMA; YQNGHIM; -.
DR PhylomeDB; B4JYN3; -.
DR ChiTaRS; kay; fly.
DR Proteomes; UP000001070; 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..796
FT /note="Transcription factor kayak"
FT /id="PRO_0000377384"
FT DOMAIN 478..541
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 109..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..499
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 506..534
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 569..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21525"
SQ SEQUENCE 796 AA; 86674 MW; 81038DC30A83DC37 CRC64;
MKNLNGRAHN ACYHPYYQQQ LQQQQQQQQQ HQQQQLLQQQ QQQLLQQQQQ QLQQQLQLPY
ATQYTQQQQQ QQQQYNQQQY YNQQLQQQQQ QQQQQHLLRQ QQLLPTQSAY QQQQSKQSYN
NNNNSNSNSN TSAANMTAMT ARVNMHAATV ATAHSNGNSN ANANATTAAM AAMCQMQSFL
SHQQQQQQQQ QQQQQYNNNC AHINYNQQQQ QQQQQQQQQQ QLPTATTATT TNGDKLALDS
ASEIANFLAS ELFMQQLVTF DGIQSAPTLT TPTLTPTTLR TIEETIFELT TETQNVPFQA
GFKPPPLTSL CNVTVVNNNN NNNNNNNNNS SNNNNNNSNT VTTTAAAAGN LTLASPMSTM
STLNTNPQLD LLGFNCGSVP ESDSEQSNVS WNVGGPHDDQ STTDTSSAAT DSTSYQNGGH
MFGNNGSNGS GVNNFTGSLA GVGSAGRGTS STSNNATPAR RGGGRRPNKS ANMSPEEEEK
RRVRRERNKL AAARCRKRRV DQTNELSEEV DGLLKKNEDL KKEIEILTNT RHQLNFVLEA
HRPTCQKVRD DLLSVTTCNG LIAPTAMLSS GSNGSHHHNS NSNNSNNNNS NNNNNSNSND
SSCGTITGFD ASLNSTGRSN SPLDLKPVLI DDQLLVNIKH EPHDAGLDSS SSLDQDGPPA
AKRFALPDIA TLKPHSASLT TPTGPVASLN TPMSGMAPTA FGIHAKPMPK TRPNTLNVNQ
SLAQPGNIAI GKTPMQIEGV PIQTPSAGNF NFDSLMAGGT GLTPVSGPLV PTCSSQNKHP
LELPTPTSEP SKLVSL
