WEK_DROME
ID WEK_DROME Reviewed; 470 AA.
AC Q9VJN5;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Zinc finger protein weckle;
GN Name=wek {ECO:0000312|EMBL:AAF53484.1, ECO:0000312|FlyBase:FBgn0001990};
GN Synonyms=l(2)35Ea {ECO:0000312|EMBL:AAK93097.1}; ORFNames=CG4148;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:AAF53484.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF53484.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAK93097.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK93097.1}; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, SUBUNIT, INTERACTION WITH MYD88 AND TOLL, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16782008; DOI=10.1016/j.cub.2006.05.050;
RA Chen L.-Y., Wang J.-C., Hyvert Y., Lin H.-P., Perrimon N., Imler J.-L.,
RA Hsu J.-C.;
RT "Weckle is a zinc finger adaptor of the toll pathway in dorsoventral
RT patterning of the Drosophila embryo.";
RL Curr. Biol. 16:1183-1193(2006).
RN [5] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000269|PubMed:18327897};
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Acts as an adapter to assemble/stabilize a
CC Toll/wek/Myd88/tube complex; required for efficient recruitment of
CC Myd88 to Toll. Dispensable for innate immune response; plays a minimal
CC role, if any, in the immune defense against Gram-positive bacteria and
CC fungi. Involved in dorsoventral axis determination.
CC {ECO:0000269|PubMed:16782008}.
CC -!- SUBUNIT: Homodimer. Interacts with Myd88 and Toll.
CC {ECO:0000269|PubMed:16782008}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16782008}.
CC Note=Localizes to the plasma membrane in embryos when bound to Myd88.
CC {ECO:0000269|PubMed:16782008}.
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DR EMBL; AE014134; AAF53484.1; -; Genomic_DNA.
DR EMBL; AY051673; AAK93097.1; -; mRNA.
DR RefSeq; NP_001260472.1; NM_001273543.1.
DR RefSeq; NP_524930.1; NM_080191.3.
DR AlphaFoldDB; Q9VJN5; -.
DR SMR; Q9VJN5; -.
DR BioGRID; 71683; 32.
DR IntAct; Q9VJN5; 6.
DR STRING; 7227.FBpp0303719; -.
DR iPTMnet; Q9VJN5; -.
DR PaxDb; Q9VJN5; -.
DR DNASU; 48785; -.
DR EnsemblMetazoa; FBtr0080764; FBpp0080323; FBgn0001990.
DR EnsemblMetazoa; FBtr0331282; FBpp0303719; FBgn0001990.
DR GeneID; 48785; -.
DR KEGG; dme:Dmel_CG4148; -.
DR UCSC; CG4148-RA; d. melanogaster.
DR CTD; 48785; -.
DR FlyBase; FBgn0001990; wek.
DR VEuPathDB; VectorBase:FBgn0001990; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000167118; -.
DR HOGENOM; CLU_002678_94_14_1; -.
DR InParanoid; Q9VJN5; -.
DR OMA; CEECYSV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9VJN5; -.
DR Reactome; R-DME-214842; DL and DIF homodimers bind to TUB and phosphorylated PLL in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214844; DL and DIF homodimers complexed with CACT are all phosphorylated in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214862; Activated PLL kinase is autophosphorylated in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214863; Adaptor protein complex binds to TL receptor at the plasma membrane.
DR Reactome; R-DME-214869; Phosphorylated CACT, DL and DIF homodimers dissociate from the TL receptor 'signalling complex'.
DR Reactome; R-DME-214874; PLL kinase binds to TUB in the TL receptor 'signalling complex'.
DR BioGRID-ORCS; 48785; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 48785; -.
DR PRO; PR:Q9VJN5; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0001990; Expressed in egg cell and 21 other tissues.
DR ExpressionAtlas; Q9VJN5; baseline and differential.
DR Genevisible; Q9VJN5; DM.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0035591; F:signaling adaptor activity; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0007311; P:maternal specification of dorsal/ventral axis, oocyte, germ-line encoded; HMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0008063; P:Toll signaling pathway; IMP:FlyBase.
DR InterPro; IPR012934; Znf_AD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF07776; zf-AD; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00868; zf-AD; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS51915; ZAD; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..470
FT /note="Zinc finger protein weckle"
FT /id="PRO_0000351195"
FT DOMAIN 10..82
FT /note="ZAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT ZN_FING 271..294
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 300..322
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..350
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 355..377
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 383..405
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 411..434
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..103
FT /note="Required for homodimerization"
FT /evidence="ECO:0000269|PubMed:16782008"
FT REGION 156..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 470 AA; 53210 MW; E8B2E991E3657A73 CRC64;
MGVPTSDWIY WCRLCARDDV VYKVRERDDD LVRIISKCFD VEMTLEEPEL GSMLCEECYS
VIGQLITFSD SVSKVQAIFE LLRHSEPQDS QDLDALRLEY GLPPACKQDL EFLDIDDTED
RCSLVEELTI SDHSTSPSPD FEAQTVRTRA NLKQCNSDPK VLASPTASIP EVETKRSRRQ
QFAAKRNSKV YTATESDDEE AILDEDEAVS PPPLKRKRGR PKGSGKQKNV DDSDNVTSRE
PDDNAKSKQD DKTSELSMSP HGSQSSNFVD YPCKICNETF MSFMALRRHK HDMHGGPKKY
VCDHCGKGLK TFTSLVEHQL VHTEEKPCIC PVCNAGFKNK ARLRVHSQTH GEPKFECNVC
GKKLQTRAIL NKHKYVHTDE RRFKCEVCGS GCKNSTALKI HLLGHTGLRP YVCKYCGKAF
ASNTNCRSHK WKKHPELASK EDETESSRVP VPTLEELRAI TREMAKAKQD
