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 27-MAR-2024, entry version 81.
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.B4M5T7; -.
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; HMSTLMT; -.
DR OrthoDB; 5399209at2759; -.
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:0007297; P:follicle cell of egg chamber migration; IEA:EnsemblMetazoa.
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:0040013; P:negative regulation of locomotion; 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 CDD; cd14721; bZIP_Fos; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR23351; FOS TRANSCRIPTION FACTOR-RELATED; 1.
DR PANTHER; PTHR23351:SF24; TRANSCRIPTION FACTOR KAYAK, ISOFORMS A_B_F; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PRINTS; PR00042; LEUZIPPRFOS.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 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
//
