EDC3_DROME
ID EDC3_DROME Reviewed; 680 AA.
AC Q9VVI2; Q8T042; Q95SZ2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Enhancer of mRNA-decapping protein 3;
GN Name=Edc3; ORFNames=CG6311;
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] OF 126-680.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND THR-188, AND
RP 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 [5]
RP INTERACTION WITH DCP1 AND DDX6/ME31B.
RX PubMed=18765641; DOI=10.1128/mcb.00759-08;
RA Tritschler F., Eulalio A., Helms S., Schmidt S., Coles M.,
RA Weichenrieder O., Izaurralde E., Truffault V.;
RT "Similar modes of interaction enable Trailer Hitch and EDC3 to associate
RT with DCP1 and Me31B in distinct protein complexes.";
RL Mol. Cell. Biol. 28:6695-6708(2008).
RN [6]
RP INTERACTION WITH DDX6/ME31B, AND MUTAGENESIS OF PHE-345 AND PHE-347.
RX PubMed=19285948; DOI=10.1016/j.molcel.2009.02.014;
RA Tritschler F., Braun J.E., Eulalio A., Truffault V., Izaurralde E.,
RA Weichenrieder O.;
RT "Structural basis for the mutually exclusive anchoring of P body components
RT EDC3 and Tral to the DEAD box protein DDX6/Me31B.";
RL Mol. Cell 33:661-668(2009).
RN [7]
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 [8]
RP STRUCTURE BY NMR OF 1-101, SUBUNIT, SUBCELLULAR LOCATION, CHARACTERIZATION
RP OF N-TERMINAL DOMAIN, MUTAGENESIS OF GLN-25; PHE-42 AND ASN-44, AND
RP INTERACTION WITH DCP1A; DCP2 AND ME31B.
RX PubMed=17923697; DOI=10.1128/mcb.01506-07;
RA Tritschler F., Eulalio A., Truffault V., Hartmann M.D., Helms S.,
RA Schmidt S., Coles M., Izaurralde E., Weichenrieder O.;
RT "A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body
RT targeting.";
RL Mol. Cell. Biol. 27:8600-8611(2007).
CC -!- FUNCTION: In the process of mRNA degradation, may play a role in mRNA
CC decapping.
CC -!- SUBUNIT: Forms a complex with DCP1A, DCP2, Me31B/DDX6 and EDC4/HEDLS
CC (By similarity). Within this complex directly interacts with DCP1A,
CC DCP2 and Me31B/DDX6 (PubMed:17923697, PubMed:18765641,
CC PubMed:19285948). Homooligomer (PubMed:17923697). Interacts with Gyf
CC (PubMed:31114929). {ECO:0000250|UniProtKB:Q96F86,
CC ECO:0000269|PubMed:17923697, ECO:0000269|PubMed:18765641,
CC ECO:0000269|PubMed:19285948, ECO:0000269|PubMed:31114929}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:17923697}.
CC Note=Processing bodies (PB).
CC -!- SIMILARITY: Belongs to the EDC3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL25455.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL39717.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014296; AAF49329.1; -; Genomic_DNA.
DR EMBL; AY069572; AAL39717.1; ALT_INIT; mRNA.
DR EMBL; AY060416; AAL25455.1; ALT_INIT; mRNA.
DR RefSeq; NP_648992.1; NM_140735.3.
DR PDB; 2RM4; NMR; -; A=1-101.
DR PDBsum; 2RM4; -.
DR AlphaFoldDB; Q9VVI2; -.
DR BMRB; Q9VVI2; -.
DR SMR; Q9VVI2; -.
DR BioGRID; 65245; 7.
DR IntAct; Q9VVI2; 3.
DR MINT; Q9VVI2; -.
DR STRING; 7227.FBpp0074970; -.
DR iPTMnet; Q9VVI2; -.
DR PaxDb; Q9VVI2; -.
DR PRIDE; Q9VVI2; -.
DR EnsemblMetazoa; FBtr0075208; FBpp0074970; FBgn0036735.
DR GeneID; 39957; -.
DR KEGG; dme:Dmel_CG6311; -.
DR CTD; 80153; -.
DR FlyBase; FBgn0036735; Edc3.
DR VEuPathDB; VectorBase:FBgn0036735; -.
DR eggNOG; KOG2585; Eukaryota.
DR GeneTree; ENSGT00390000016435; -.
DR HOGENOM; CLU_026194_0_0_1; -.
DR InParanoid; Q9VVI2; -.
DR OMA; NHQWPKI; -.
DR OrthoDB; 870769at2759; -.
DR PhylomeDB; Q9VVI2; -.
DR Reactome; R-DME-430039; mRNA decay by 5' to 3' exoribonuclease.
DR BioGRID-ORCS; 39957; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; Q9VVI2; -.
DR GenomeRNAi; 39957; -.
DR PRO; PR:Q9VVI2; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036735; Expressed in spermathecum and 26 other tissues.
DR ExpressionAtlas; Q9VVI2; baseline and differential.
DR Genevisible; Q9VVI2; DM.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0006402; P:mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0033962; P:P-body assembly; IBA:GO_Central.
DR CDD; cd01737; LSm16_N; 1.
DR Gene3D; 3.40.50.10260; -; 1.
DR InterPro; IPR025762; DFDF.
DR InterPro; IPR019050; FDF_dom.
DR InterPro; IPR025609; Lsm14-like_N.
DR InterPro; IPR034107; Lsm16_N.
DR InterPro; IPR004443; YjeF_N_dom.
DR InterPro; IPR036652; YjeF_N_dom_sf.
DR SMART; SM01199; FDF; 1.
DR SMART; SM01271; LSM14; 1.
DR PROSITE; PS51512; DFDF; 1.
DR PROSITE; PS51385; YJEF_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..680
FT /note="Enhancer of mRNA-decapping protein 3"
FT /id="PRO_0000330730"
FT DOMAIN 333..369
FT /note="DFDF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT DOMAIN 430..658
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00719"
FT REGION 1..101
FT /note="Required for P-body targeting and interaction with
FT DCP1A"
FT /evidence="ECO:0000269|PubMed:17923697"
FT REGION 73..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..338
FT /note="Required for interaction with DCP2"
FT /evidence="ECO:0000269|PubMed:17923697"
FT REGION 120..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..440
FT /note="Required for interaction with Me31B"
FT COMPBIAS 138..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 188
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 25
FT /note="Q->A: Strongly reduced interaction with DCP1A. No
FT effect on P-body targeting."
FT /evidence="ECO:0000269|PubMed:17923697"
FT MUTAGEN 42
FT /note="F->A: Strongly reduced interaction with DCP1A, but
FT no effect on P-body targeting; when associated with A-44."
FT /evidence="ECO:0000269|PubMed:17923697"
FT MUTAGEN 44
FT /note="N->A: Strongly reduced interaction with DCP1A, but
FT no effect on P-body targeting; when associated with A-42."
FT /evidence="ECO:0000269|PubMed:17923697"
FT MUTAGEN 345
FT /note="F->A: Strongly reduced interaction with DDX6."
FT /evidence="ECO:0000269|PubMed:19285948"
FT MUTAGEN 347
FT /note="F->A: Minor effect on interaction with DDX6."
FT /evidence="ECO:0000269|PubMed:19285948"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:2RM4"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:2RM4"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:2RM4"
FT STRAND 23..32
FT /evidence="ECO:0007829|PDB:2RM4"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:2RM4"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2RM4"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2RM4"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2RM4"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:2RM4"
SQ SEQUENCE 680 AA; 73415 MW; 10B567618DF26CB6 CRC64;
MGPTDQDWIG CAVSIACDEV LGVFQGLIKQ ISAEEITIVR AFRNGVPLRK QNAEVVLKCT
DIRSIDLIEP AKQDLDGHTA PPPVVNKPTP VKLPHFSNIL GKQQQLQLQQ QQQQLQLQQQ
QKQQFQEQER EQDLPSTPRS RANDNGRVAA GGASSSSGPR GNFNSALSDK MHQLKLIETN
GSNGTLRTPQ TSRASSAQQQ PQISTTPNSV AAFFGNMIPP KVEVKLGSYV SNTRESYCSS
SGDSGEATGL SLGSSKPIDI VSNGDGFYKQ TAASSYGNTN GNVRRNGNAN NNGNGTGNGS
YTNGNGNGNG KNKRNRVRRE SSMRQQQVQL TFGSEADDPL IHEDFDFEGN LALFDKQAIW
DDIESTTQKP DVVRHIVNNH HHKPEQKYRH DENILASKPL QLRQIESMFG GSQDFVTDDG
LIIPTIPAYV RNKIEISADK AGLSLQRQID ILARGASDLA ITLLGGARRL TPANNHQWPK
IAIICDGGKN MRTINIGAAT GRQLASHGLT VLLYVEQAKL LEQNSSSPEI SLFKATDNVI
VHSVDALPTP DLVILSTNTA NLSDAIRKWL SVNRASVLAI DPPPCGINEV AIKYSILPIL
PLNGISTATT SSSSSAAATP TPIASTSAAA SATKSAASTN NCGKLYLCNL GIPDKFYRDC
GIKYKSPYGH KYVIPIHSKD
