EDC4_DROME
ID EDC4_DROME Reviewed; 1354 AA.
AC Q9VKK1; Q8MZ42;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Enhancer of mRNA-decapping protein 4 homolog;
GN Name=Ge-1; ORFNames=CG6181;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 377-1354.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17901217; DOI=10.1101/gad.443107;
RA Eulalio A., Rehwinkel J., Stricker M., Huntzinger E., Yang S.-F.,
RA Doerks T., Dorner S., Bork P., Boutros M., Izaurralde E.;
RT "Target-specific requirements for enhancers of decapping in miRNA-mediated
RT gene silencing.";
RL Genes Dev. 21:2558-2570(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576 AND THR-581, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-561; THR-563;
RP SER-576; SER-759; SER-762; SER-763; SER-1207; THR-1211; THR-1317 AND
RP TYR-1320, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
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).
RN [8]
RP INTERACTION WITH GYF.
RX PubMed=31114929; DOI=10.1093/nar/gkz429;
RA Ruscica V., Bawankar P., Peter D., Helms S., Igreja C., Izaurralde E.;
RT "Direct role for the Drosophila GIGYF protein in 4EHP-mediated mRNA
RT repression.";
RL Nucleic Acids Res. 47:7035-7048(2019).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1220-1354, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18755833; DOI=10.1261/rna.1222908;
RA Jinek M., Eulalio A., Lingel A., Helms S., Conti E., Izaurralde E.;
RT "The C-terminal region of Ge-1 presents conserved structural features
RT required for P-body localization.";
RL RNA 14:1991-1998(2008).
CC -!- FUNCTION: In the process of mRNA degradation, seems to play a role in
CC mRNA decapping. Required for silencing a subset of endogenous miRNA
CC targets. {ECO:0000269|PubMed:17901217}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with Dcp1 and Dcp2
CC (PubMed:18755833). Interacts with Gyf (PubMed:31114929).
CC {ECO:0000269|PubMed:18755833, ECO:0000269|PubMed:31114929,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:17901217,
CC ECO:0000269|PubMed:18755833}.
CC -!- SIMILARITY: Belongs to the WD repeat EDC4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM29374.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF53066.2; -; Genomic_DNA.
DR EMBL; AE014134; AAF53067.2; -; Genomic_DNA.
DR EMBL; BT004479; AAO42643.1; -; mRNA.
DR EMBL; AY113369; AAM29374.1; ALT_INIT; mRNA.
DR RefSeq; NP_609486.2; NM_135642.3.
DR RefSeq; NP_723654.1; NM_164957.2.
DR PDB; 2VXG; X-ray; 1.90 A; A/B=1220-1354.
DR PDBsum; 2VXG; -.
DR AlphaFoldDB; Q9VKK1; -.
DR SMR; Q9VKK1; -.
DR BioGRID; 60603; 15.
DR IntAct; Q9VKK1; 7.
DR MINT; Q9VKK1; -.
DR STRING; 7227.FBpp0079818; -.
DR iPTMnet; Q9VKK1; -.
DR PaxDb; Q9VKK1; -.
DR PRIDE; Q9VKK1; -.
DR EnsemblMetazoa; FBtr0080231; FBpp0079818; FBgn0283682.
DR EnsemblMetazoa; FBtr0080232; FBpp0079819; FBgn0283682.
DR GeneID; 34541; -.
DR KEGG; dme:Dmel_CG6181; -.
DR UCSC; CG6181-RA; d. melanogaster.
DR CTD; 34541; -.
DR FlyBase; FBgn0283682; Ge-1.
DR VEuPathDB; VectorBase:FBgn0283682; -.
DR eggNOG; KOG1916; Eukaryota.
DR GeneTree; ENSGT00510000047791; -.
DR HOGENOM; CLU_005166_0_0_1; -.
DR InParanoid; Q9VKK1; -.
DR OMA; QQVNLMT; -.
DR OrthoDB; 1424637at2759; -.
DR PhylomeDB; Q9VKK1; -.
DR Reactome; R-DME-430039; mRNA decay by 5' to 3' exoribonuclease.
DR SignaLink; Q9VKK1; -.
DR EvolutionaryTrace; Q9VKK1; -.
DR GenomeRNAi; 34541; -.
DR PRO; PR:Q9VKK1; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0283682; Expressed in wing disc and 37 other tissues.
DR Genevisible; Q9VKK1; DM.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0045495; C:pole plasm; IDA:FlyBase.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IGI:FlyBase.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IMP:FlyBase.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IGI:FlyBase.
DR GO; GO:0006402; P:mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0033962; P:P-body assembly; IMP:FlyBase.
DR GO; GO:0045451; P:pole plasm oskar mRNA localization; IMP:FlyBase.
DR Gene3D; 1.10.220.100; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045152; EDC4-like.
DR InterPro; IPR044938; EDC4_C.
DR InterPro; IPR032401; EDC4_WD40.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15598; PTHR15598; 1.
DR Pfam; PF16529; Ge1_WD40; 1.
DR SMART; SM00320; WD40; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..1354
FT /note="Enhancer of mRNA-decapping protein 4 homolog"
FT /id="PRO_0000372649"
FT REPEAT 309..348
FT /note="WD 1"
FT REPEAT 363..406
FT /note="WD 2"
FT REGION 18..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 765..803
FT /evidence="ECO:0000255"
FT COILED 893..936
FT /evidence="ECO:0000255"
FT COILED 969..1036
FT /evidence="ECO:0000255"
FT COILED 1159..1188
FT /evidence="ECO:0000255"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 563
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 581
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1207
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1211
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1317
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1320
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT HELIX 1218..1228
FT /evidence="ECO:0007829|PDB:2VXG"
FT HELIX 1231..1240
FT /evidence="ECO:0007829|PDB:2VXG"
FT HELIX 1244..1253
FT /evidence="ECO:0007829|PDB:2VXG"
FT HELIX 1256..1259
FT /evidence="ECO:0007829|PDB:2VXG"
FT HELIX 1269..1281
FT /evidence="ECO:0007829|PDB:2VXG"
FT HELIX 1288..1300
FT /evidence="ECO:0007829|PDB:2VXG"
FT HELIX 1306..1329
FT /evidence="ECO:0007829|PDB:2VXG"
FT HELIX 1336..1349
FT /evidence="ECO:0007829|PDB:2VXG"
SQ SEQUENCE 1354 AA; 149251 MW; CA9E6E78D338CD2C CRC64;
MLIALFALAH LPIFRKTPLS ASSSPPPSVH RSPRCGKAST AYHPPPADAC ISITASAIDA
ASGMSNSAEQ DKPIAANGNA AEPQEIEVIH FQAQEKQCCR VIRSNKTKVL TSGGVHTRGS
SKVKLKNIVD YKWERKYYYP GHLVAVHRDG KHLAYAINVN NKATGMEGMV RVCNIATSMR
ALIKGMSGEV LDLQFAHTDC ERILAVIDVS SLFVYKVDQI EGNLLCNLVL KVEDPIANYV
PEYDMVSWCP YVCSSSATVP INDDDDENQL LIWSRSSQFQ CFQVKMIVSE HGRGKIQPAA
LESGYLKIEE DSLITCAALS PDGTTVAAAC ADGLVRFYQI YLFDVRNHRC LHEWKPHDGK
KVCSLFFLDN INKPVEESYW QHVITTSDAN TEIKLWNCSL WKCLQTINVV ASPSSLQPRN
FIAGIDRSAN YLVLSCLDSL AVYVMQIGST GGADSENRSS DSEGEGCDTS KRIQNVAEFK
LSSGILSFSI VNASMRRVKN SIESYYPIEE PDDFDDDSNS TSALVLHMFV VQAKSLQECQ
IIYQPCVAEK TERSSLNSKR SQTPEDNLLI KEEPESPNSG TVGAVQLDAL FAKSAKRAST
GSSSAMVAVA AAAAAAPSAI LQDATKEAAK SESPQLSSAY TQQVNLMTPD AFSASGTAAA
AAVFVSTSTT TSIGTDSSTT TSGQDRSIDS AVLQTIRMLA TVTSKTSENP NAEVLLNLMN
NTLIEDREQQ KLKEKLDARK KFIAIDRNPE RNVAENLASG SSSPSREVQE IMATQDDADA
YEAELENLDD DDDDEEEELA NSSPLPEAVD GTWPIVKLSS HSAELQNAAQ IMSQAVQNTN
NGNVPPTLGG GHNNNTSVGS NSNNNTATTL STSNTSSSNN AGGTCVDSSG TGELNAKMEL
LIDLVKAQSK QINKLENEVN KLQKQQEAAA ALHSKQDTSL EPKNLSQLAY KIEMQLSKLM
EQYLKRYENE HKKKLTEFLA ARESQNRELR DSVLQVLNQY VMNHFTDIIG NVLNMELQRQ
LLPRVNANMD QLQAQMQVEI VQKLSVFDKT VKENIAQVCK SKQFLDTFGK SVLIGVQTSL
QTAFIESMSS TLIPAYEKSS QNMFKQLHDA FSVGIKDFMV QFNTYLQHMP QPQAGSGNTE
EINNKLSMLK QLVESSLHKH RTELTDAMLE TQREVKSLEI LLARQVQETI RAELRKHMEA
QNVAMRSQAA TPAPPYDLRD SIKQLLMAGQ INKAFHQALL ANDLGLVEFT LRHTDSNQAF
APEGCRLEQK VLLSLIQQIS ADMTNHNELK QRYLNEALLA INMADPITRE HAPKVLTELY
RNCQQFIKNS PKNSQFSNVR LLMKAIITYR DQLK
