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Enhancer of mRNA-decapping protein 3

 
Known also as: LSM16 homolog, YjeF N-terminal domain-containing protein 2, YjeF domain-containing protein 1

Known abbreviations: EDC3, LSM16, YJDC, YJEFN2, PP844

 

FUNCTION:
 
Binds single-stranded RNA. In the process of mRNA degradation, may play a role in mRNA decapping. May play a role in spermiogenesis and oogenesis. 
 
SUBUNIT STRUCTURE:
 
Homodimer (via YjeF N-terminal domain). Forms a complex with DCP1A, DCP2, DDX6 and EDC4/HEDLS, within this complex directly interacts with DCP1A and DDX6. Interacts with ZFP36.
 
CELLULAR LOCALIZATION:
 
Cytoplasm › P-body. Note: Processing bodies (PB). 
 
TISSUE SPECIFICITY:
 
Expressed in theca and granulosa cells in ovary, and in spermatids of the meiotic division part II and apical membrane of Sertoli cells in testis (at protein level). Also expressed in brain and mammary gland. 
 
DOMAIN:
 
The DFDF domain is unstructured by itself. It assumes a helical fold upon interaction with DDX6. 



This protein can be a part of a given complexes: Activities in which Enhancer of mRNA-decapping protein 3 is involved: Pathways in which Enhancer of mRNA-decapping protein 3 is involved:

NCBI GI number(s): 215598545
215598544
215598560
215598561
19923613
215598515
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q96F86 Q96F86
BRENDA - -
KEGG hsa:80153 hsa:80153
PFAM: PF09532
PF12701
PF03853
PF09532
PF12701
PF03853
InterPro: IPR019050
IPR025609
IPR004443
IPR019050
IPR025609
IPR004443
CATH: - -
SCOP: - -
Solved crystal structures: 3D3J
2VC8
3D3K
2WAX
2WAY
[PDB] [details]
[PDB] [details]
[PDB] [details]
[PDB] [details]
[PDB] [details]


Protein sequence:
MATDWLGSIVSINCGDSLGVYQGRVSAVDQVSQTISLTRPFHNGVKCLVP
EVTFRAGDITELKILEIPGPGDNQHFGDLHQTELGPSGAGCQVGINQNGT
GKFVKKPASSSSAPQNIPKRTDVKSQDVAVSPQQQQCSKSYVDRHMESLS
QSKSFRRRHNSWSSSSRHPNQATPKKSGLKNGQMKNKDDECFGDDIEEIP
DTDFDFEGNLALFDKAAVFEEIDTYERRSGTRSRGIPNERPTRYRHDENI
LESEPIVYRRIIVPHNVSKEFCTDSGLVVPSISYELHKKLLSVAEKHGLT
LERRLEMTGVCASQMALTLLGGPNRLNPKNVHQRPTVALLCGPHVKGAQG
ISCGRHLANHDVQVILFLPNFVKMLESITNELSLFSKTQGQQVSSLKDLP
TSPVDLVINCLDCPENVFLRDQPWYKAAVAWANQNRAPVLSIDPPVHEVE
QGIDAKWSLALGLPLPLGEHAGRIYLCDIGIPQQVFQEVGINYHSPFGCK
FVIPLHSA

Enhancer of mRNA-decapping protein 3 (Homo sapiens) is product of expression of EDC3 gene.

References:

Title Authors Journal Publication date (Issue) PubMed ID
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, K Genome Res 2004-10-01 (14) 15489334
Complete sequencing and characterization of 21,243 full-length human cDNAs. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K Nat Genet 2004-02-01 (36) 14702039
Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Fenger-Gron M, Fillman C, Norrild B, Lykke-Andersen J Mol Cell 2005-12-22 (20) 16364915
Structural basis for the mutually exclusive anchoring of P body components EDC3 and Tral to the DEAD box protein DDX6/Me31B. Tritschler F, Braun JE, Eulalio A, Truffault V, Izaurralde E, Weichenrieder O Mol Cell 2009-03-13 (33) 19285948
A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP Nat Biotechnol 2006-10-01 (24) 16964243
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S Anal Chem 2009-06-01 (81) 19413330
Initial characterization of the human central proteome. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J BMC Syst Biol 2011-01-01 (5) 21269460
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A 2008-08-05 (105) 18669648
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal 2009-01-01 (2) 19690332
Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd J Proteome Res 2008-03-01 (7) 18220336
Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A Proc Natl Acad Sci U S A 2007-01-13 (104) 17287340
Large-scale cDNA transfection screening for genes related to cancer development and progression. Wan D, Gong Y, Qin W, Zhang P, Li J, Wei L, Zhou X, Li H, Qiu X, Zhong F, He L, Yu J, Yao G, Jiang H, Qian L, Yu Y, Shu H, Chen X, Xu H, Guo M, Pan Z, Chen Y, Ge C, Yang S, Gu J Proc Natl Acad Sci U S A 2004-11-02 (101) 15498874
ApoA-I-binding protein (AI-BP) and its homologues hYjeF_N2 and hYjeF_N3 comprise the YjeF_N domain protein family in humans with a role in spermiogenesis and oogenesis. Rudolph C, Sigruener A, Hartmann A, Orso E, Bals-Pratsch M, Gronwald W, Seifert B, Kalbitzer HR, Verdorfer I, Luetjens CM, Ortmann O, Bornstein SR, Schmitz G Horm Metab Res 2007-05-01 (39) 17533573
A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting. Tritschler F, Eulalio A, Truffault V, Hartmann MD, Helms S, Schmidt S, Coles M, Izaurralde E, Weichenrieder O Mol Cell Biol 2007-12-01 (27) 17923697



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Last modification of this entry: Sept. 25, 2012.

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