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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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