Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Enhancer of mRNA-decapping protein 3

Gene

Edc3

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In the process of mRNA degradation, may play a role in mRNA decapping.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-DME-430039. mRNA decay by 5' to 3' exoribonuclease.

Names & Taxonomyi

Protein namesi
Recommended name:
Enhancer of mRNA-decapping protein 3
Gene namesi
Name:Edc3
ORF Names:CG6311
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0036735. Edc3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic mRNA processing body Source: UniProtKB
  • microtubule associated complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi25 – 251Q → A: Strongly reduced interaction with DCP1A. No effect on P-body targeting. 1 Publication
Mutagenesisi42 – 421F → A: Strongly reduced interaction with DCP1A, but no effect on P-body targeting; when associated with A-44. 1 Publication
Mutagenesisi44 – 441N → A: Strongly reduced interaction with DCP1A, but no effect on P-body targeting; when associated with A-42. 1 Publication
Mutagenesisi345 – 3451F → A: Strongly reduced interaction with DDX6. 1 Publication
Mutagenesisi347 – 3471F → A: Minor effect on interaction with DDX6. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 680680Enhancer of mRNA-decapping protein 3PRO_0000330730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei136 – 1361Phosphoserine1 Publication
Modified residuei188 – 1881Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VVI2.
PRIDEiQ9VVI2.

PTM databases

iPTMnetiQ9VVI2.

Expressioni

Gene expression databases

BgeeiQ9VVI2.
ExpressionAtlasiQ9VVI2. differential.
GenevisibleiQ9VVI2. DM.

Interactioni

Subunit structurei

Forms a complex with DCP1A, DCP2, Me31B/DDX6 and EDC4/HEDLS (By similarity). Within this complex directly interacts with DCP1A, DCP2 and Me31B/DDX6. Homooligomer.By similarity3 Publications

Protein-protein interaction databases

BioGridi65245. 2 interactions.
IntActiQ9VVI2. 3 interactions.
MINTiMINT-903966.
STRINGi7227.FBpp0074970.

Structurei

Secondary structure

1
680
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Beta strandi12 – 176Combined sources
Turni19 – 213Combined sources
Beta strandi23 – 3210Combined sources
Beta strandi35 – 439Combined sources
Beta strandi51 – 533Combined sources
Beta strandi55 – 584Combined sources
Turni59 – 613Combined sources
Beta strandi62 – 698Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RM4NMR-A1-101[»]
ProteinModelPortaliQ9VVI2.
SMRiQ9VVI2. Positions 1-101, 340-366, 412-678.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9VVI2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini333 – 36937DFDFPROSITE-ProRule annotationAdd
BLAST
Domaini430 – 658229YjeF N-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 101101Required for P-body targeting and interaction with DCP1AAdd
BLAST
Regioni102 – 338237Required for interaction with DCP2Add
BLAST
Regioni331 – 440110Required for interaction with Me31BAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi103 – 13230Gln-richAdd
BLAST
Compositional biasi278 – 31538Asn/Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the EDC3 family.Curated
Contains 1 DFDF domain.PROSITE-ProRule annotation
Contains 1 YjeF N-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2585. Eukaryota.
COG0062. LUCA.
GeneTreeiENSGT00390000016435.
InParanoidiQ9VVI2.
KOiK12615.
OMAiPANNHQW.
OrthoDBiEOG7H793B.
PhylomeDBiQ9VVI2.

Family and domain databases

InterProiIPR025762. DFDF.
IPR019050. FDF_dom.
IPR025609. Lsm14_N.
IPR004443. YjeF_N_dom.
[Graphical view]
SMARTiSM01199. FDF. 1 hit.
SM01271. LSM14. 1 hit.
[Graphical view]
PROSITEiPS51512. DFDF. 1 hit.
PS51385. YJEF_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VVI2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPTDQDWIG CAVSIACDEV LGVFQGLIKQ ISAEEITIVR AFRNGVPLRK
60 70 80 90 100
QNAEVVLKCT DIRSIDLIEP AKQDLDGHTA PPPVVNKPTP VKLPHFSNIL
110 120 130 140 150
GKQQQLQLQQ QQQQLQLQQQ QKQQFQEQER EQDLPSTPRS RANDNGRVAA
160 170 180 190 200
GGASSSSGPR GNFNSALSDK MHQLKLIETN GSNGTLRTPQ TSRASSAQQQ
210 220 230 240 250
PQISTTPNSV AAFFGNMIPP KVEVKLGSYV SNTRESYCSS SGDSGEATGL
260 270 280 290 300
SLGSSKPIDI VSNGDGFYKQ TAASSYGNTN GNVRRNGNAN NNGNGTGNGS
310 320 330 340 350
YTNGNGNGNG KNKRNRVRRE SSMRQQQVQL TFGSEADDPL IHEDFDFEGN
360 370 380 390 400
LALFDKQAIW DDIESTTQKP DVVRHIVNNH HHKPEQKYRH DENILASKPL
410 420 430 440 450
QLRQIESMFG GSQDFVTDDG LIIPTIPAYV RNKIEISADK AGLSLQRQID
460 470 480 490 500
ILARGASDLA ITLLGGARRL TPANNHQWPK IAIICDGGKN MRTINIGAAT
510 520 530 540 550
GRQLASHGLT VLLYVEQAKL LEQNSSSPEI SLFKATDNVI VHSVDALPTP
560 570 580 590 600
DLVILSTNTA NLSDAIRKWL SVNRASVLAI DPPPCGINEV AIKYSILPIL
610 620 630 640 650
PLNGISTATT SSSSSAAATP TPIASTSAAA SATKSAASTN NCGKLYLCNL
660 670 680
GIPDKFYRDC GIKYKSPYGH KYVIPIHSKD
Length:680
Mass (Da):73,415
Last modified:May 1, 2000 - v1
Checksum:i10B567618DF26CB6
GO

Sequence cautioni

The sequence AAL25455.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAL39717.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF49329.1.
AY069572 mRNA. Translation: AAL39717.1. Different initiation.
AY060416 mRNA. Translation: AAL25455.1. Different initiation.
RefSeqiNP_648992.1. NM_140735.3.
UniGeneiDm.2069.

Genome annotation databases

EnsemblMetazoaiFBtr0075208; FBpp0074970; FBgn0036735.
GeneIDi39957.
KEGGidme:Dmel_CG6311.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF49329.1.
AY069572 mRNA. Translation: AAL39717.1. Different initiation.
AY060416 mRNA. Translation: AAL25455.1. Different initiation.
RefSeqiNP_648992.1. NM_140735.3.
UniGeneiDm.2069.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RM4NMR-A1-101[»]
ProteinModelPortaliQ9VVI2.
SMRiQ9VVI2. Positions 1-101, 340-366, 412-678.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65245. 2 interactions.
IntActiQ9VVI2. 3 interactions.
MINTiMINT-903966.
STRINGi7227.FBpp0074970.

PTM databases

iPTMnetiQ9VVI2.

Proteomic databases

PaxDbiQ9VVI2.
PRIDEiQ9VVI2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0075208; FBpp0074970; FBgn0036735.
GeneIDi39957.
KEGGidme:Dmel_CG6311.

Organism-specific databases

CTDi80153.
FlyBaseiFBgn0036735. Edc3.

Phylogenomic databases

eggNOGiKOG2585. Eukaryota.
COG0062. LUCA.
GeneTreeiENSGT00390000016435.
InParanoidiQ9VVI2.
KOiK12615.
OMAiPANNHQW.
OrthoDBiEOG7H793B.
PhylomeDBiQ9VVI2.

Enzyme and pathway databases

ReactomeiR-DME-430039. mRNA decay by 5' to 3' exoribonuclease.

Miscellaneous databases

EvolutionaryTraceiQ9VVI2.
GenomeRNAii39957.
PROiQ9VVI2.

Gene expression databases

BgeeiQ9VVI2.
ExpressionAtlasiQ9VVI2. differential.
GenevisibleiQ9VVI2. DM.

Family and domain databases

InterProiIPR025762. DFDF.
IPR019050. FDF_dom.
IPR025609. Lsm14_N.
IPR004443. YjeF_N_dom.
[Graphical view]
SMARTiSM01199. FDF. 1 hit.
SM01271. LSM14. 1 hit.
[Graphical view]
PROSITEiPS51512. DFDF. 1 hit.
PS51385. YJEF_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 126-680.
    Strain: Berkeley.
    Tissue: Embryo.
  4. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND THR-188, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  5. "Similar modes of interaction enable Trailer Hitch and EDC3 to associate with DCP1 and Me31B in distinct protein complexes."
    Tritschler F., Eulalio A., Helms S., Schmidt S., Coles M., Weichenrieder O., Izaurralde E., Truffault V.
    Mol. Cell. Biol. 28:6695-6708(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCP1 AND DDX6/ME31B.
  6. "Structural basis for the mutually exclusive anchoring of P body components EDC3 and Tral to the DEAD box protein DDX6/Me31B."
    Tritschler F., Braun J.E., Eulalio A., Truffault V., Izaurralde E., Weichenrieder O.
    Mol. Cell 33:661-668(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX6/ME31B, MUTAGENESIS OF PHE-345 AND PHE-347.
  7. Cited for: STRUCTURE BY NMR OF 1-101, SUBUNIT, SUBCELLULAR LOCATION, CHARACTERIZATION OF N-TERMINAL DOMAIN, MUTAGENESIS OF GLN-25; PHE-42 AND ASN-44, INTERACTION WITH DCP1A; DCP2 AND ME31B.

Entry informationi

Entry nameiEDC3_DROME
AccessioniPrimary (citable) accession number: Q9VVI2
Secondary accession number(s): Q8T042, Q95SZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.