EDC3_HUMAN
ID EDC3_HUMAN Reviewed; 508 AA.
AC Q96F86; B3KPH0; D3DW61; Q9H797;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Enhancer of mRNA-decapping protein 3;
DE AltName: Full=LSM16 homolog;
DE AltName: Full=YjeF N-terminal domain-containing protein 2;
DE Short=YjeF_N2;
DE Short=hYjeF_N2;
DE AltName: Full=YjeF domain-containing protein 1;
GN Name=EDC3; Synonyms=LSM16, YJDC, YJEFN2; ORFNames=PP844;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DCP1A; DCP2; DDX6;
RP EDC4 AND ZFP36, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16364915; DOI=10.1016/j.molcel.2005.10.031;
RA Fenger-Groen M., Fillman C., Norrild B., Lykke-Andersen J.;
RT "Multiple processing body factors and the ARE binding protein TTP activate
RT mRNA decapping.";
RL Mol. Cell 20:905-915(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17533573; DOI=10.1055/s-2007-977699;
RA Rudolph C., Sigruener A., Hartmann A., Orso E., Bals-Pratsch M.,
RA Gronwald W., Seifert B., Kalbitzer H.R., Verdorfer I., Luetjens C.M.,
RA Ortmann O., Bornstein S.R., Schmitz G.;
RT "ApoA-I-binding protein (AI-BP) and its homologues hYjeF_N2 and hYjeF_N3
RT comprise the YjeF_N domain protein family in humans with a role in
RT spermiogenesis and oogenesis.";
RL Horm. Metab. Res. 39:322-335(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-140, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-161, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP FUNCTION, INVOLVEMENT IN MRT50, VARIANT MRT50 SER-54, AND CHARACTERIZATION
RP OF VARIANT MRT50 SER-54.
RX PubMed=25701870; DOI=10.1093/hmg/ddv069;
RA Ahmed I., Buchert R., Zhou M., Jiao X., Mittal K., Sheikh T.I.,
RA Scheller U., Vasli N., Rafiq M.A., Brohi M.Q., Mikhailov A., Ayaz M.,
RA Bhatti A., Sticht H., Nasr T., Carter M.T., Uebe S., Reis A., Ayub M.,
RA John P., Kiledjian M., Vincent J.B., Jamra R.A.;
RT "Mutations in DCPS and EDC3 in autosomal recessive intellectual disability
RT indicate a crucial role for mRNA decapping in neurodevelopment.";
RL Hum. Mol. Genet. 24:3172-3180(2015).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
RP INTERACTION WITH DDX6.
RX PubMed=31422817; DOI=10.1016/j.ajhg.2019.07.010;
RA Balak C., Benard M., Schaefer E., Iqbal S., Ramsey K., Ernoult-Lange M.,
RA Mattioli F., Llaci L., Geoffroy V., Courel M., Naymik M., Bachman K.K.,
RA Pfundt R., Rump P., Ter Beest J., Wentzensen I.M., Monaghan K.G.,
RA McWalter K., Richholt R., Le Bechec A., Jepsen W., De Both M., Belnap N.,
RA Boland A., Piras I.S., Deleuze J.F., Szelinger S., Dollfus H., Chelly J.,
RA Muller J., Campbell A., Lal D., Rangasamy S., Mandel J.L., Narayanan V.,
RA Huentelman M., Weil D., Piton A.;
RT "Rare de novo missense variants in RNA helicase DDX6 cause intellectual
RT disability and dysmorphic features and lead to P-body defects and RNA
RT dysregulation.";
RL Am. J. Hum. Genet. 105:509-525(2019).
RN [19]
RP INTERACTION WITH DDX6.
RX PubMed=31439631; DOI=10.1101/gad.329219.119;
RA Peter D., Ruscica V., Bawankar P., Weber R., Helms S., Valkov E.,
RA Igreja C., Izaurralde E.;
RT "Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated
RT translational repression.";
RL Genes Dev. 33:1355-1360(2019).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.31 ANGSTROMS) OF 1-82.
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).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 250-508, FUNCTION, RNA-BINDING,
RP SUBUNIT, CIRCULAR DICHROISM, AND MUTAGENESIS OF GLU-306 AND VAL-310.
RX PubMed=18678652; DOI=10.1128/mcb.00761-08;
RA Ling S.H., Decker C.J., Walsh M.A., She M., Parker R., Song H.;
RT "Crystal structure of human Edc3 and its functional implications.";
RL Mol. Cell. Biol. 28:5965-5976(2008).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 192-228 IN COMPLEX WITH DDX6,
RP INTERACTION WITH DDX6, MUTAGENESIS OF PHE-204 AND PHE-206, AND DOMAIN.
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).
CC -!- FUNCTION: Binds single-stranded RNA. Involved in the process of mRNA
CC degradation and in the positive regulation of mRNA decapping. May play
CC a role in spermiogenesis and oogenesis. {ECO:0000269|PubMed:16364915,
CC ECO:0000269|PubMed:17533573, ECO:0000269|PubMed:18678652,
CC ECO:0000269|PubMed:25701870}.
CC -!- SUBUNIT: Homodimer (via YjeF N-terminal domain). Forms a complex with
CC DCP1A, DCP2, DDX6 and EDC4/HEDLS, within this complex directly
CC interacts with DCP1A and DDX6 (PubMed:16364915, PubMed:31422817,
CC PubMed:19285948, PubMed:31439631). Interacts with ZFP36.
CC {ECO:0000269|PubMed:16364915, ECO:0000269|PubMed:18678652,
CC ECO:0000269|PubMed:19285948, ECO:0000269|PubMed:31422817,
CC ECO:0000269|PubMed:31439631}.
CC -!- INTERACTION:
CC Q96F86; Q9UJ72: ANXA10; NbExp=11; IntAct=EBI-997311, EBI-8648654;
CC Q96F86; Q9NPI6: DCP1A; NbExp=14; IntAct=EBI-997311, EBI-374238;
CC Q96F86; Q8IZD4: DCP1B; NbExp=8; IntAct=EBI-997311, EBI-521595;
CC Q96F86; P26196: DDX6; NbExp=15; IntAct=EBI-997311, EBI-351257;
CC Q96F86; Q96F86: EDC3; NbExp=8; IntAct=EBI-997311, EBI-997311;
CC Q96F86; Q5JST6: EFHC2; NbExp=7; IntAct=EBI-997311, EBI-2349927;
CC Q96F86; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-997311, EBI-739832;
CC Q96F86; O75928-2: PIAS2; NbExp=3; IntAct=EBI-997311, EBI-348567;
CC Q96F86; P47897: QARS1; NbExp=3; IntAct=EBI-997311, EBI-347462;
CC Q96F86; P26651: ZFP36; NbExp=2; IntAct=EBI-997311, EBI-374248;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16364915}.
CC Note=Processing bodies (PB).
CC -!- TISSUE SPECIFICITY: Expressed in theca and granulosa cells in ovary,
CC and in spermatids of the meiotic division part II and apical membrane
CC of Sertoli cells in testis (at protein level). Also expressed in brain
CC and mammary gland. {ECO:0000269|PubMed:17533573}.
CC -!- DOMAIN: The DFDF domain is unstructured by itself. It assumes a helical
CC fold upon interaction with DDX6. {ECO:0000269|PubMed:19285948}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 50
CC (MRT50) [MIM:616460]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRT50
CC patients show mild intellectual disability and microcephaly.
CC {ECO:0000269|PubMed:25701870}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the EDC3 family. {ECO:0000305}.
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DR EMBL; AF193058; AAG22486.1; -; mRNA.
DR EMBL; AK024781; BAB15001.1; -; mRNA.
DR EMBL; AK056339; BAG51682.1; -; mRNA.
DR EMBL; CH471136; EAW99316.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99317.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99318.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99319.1; -; Genomic_DNA.
DR EMBL; BC011534; AAH11534.1; -; mRNA.
DR EMBL; BC021271; AAH21271.1; -; mRNA.
DR CCDS; CCDS10267.1; -.
DR RefSeq; NP_001135915.1; NM_001142443.1.
DR RefSeq; NP_001135916.1; NM_001142444.1.
DR RefSeq; NP_079359.2; NM_025083.3.
DR PDB; 2VC8; X-ray; 1.31 A; A=1-82.
DR PDB; 2WAX; X-ray; 2.30 A; B/D=192-228.
DR PDB; 2WAY; X-ray; 2.30 A; B/D=192-228.
DR PDB; 3D3J; X-ray; 2.80 A; A=203-508.
DR PDB; 3D3K; X-ray; 2.20 A; A/B/C/D=250-508.
DR PDB; 6S8S; X-ray; 2.21 A; B/D=192-228.
DR PDBsum; 2VC8; -.
DR PDBsum; 2WAX; -.
DR PDBsum; 2WAY; -.
DR PDBsum; 3D3J; -.
DR PDBsum; 3D3K; -.
DR PDBsum; 6S8S; -.
DR AlphaFoldDB; Q96F86; -.
DR SMR; Q96F86; -.
DR BioGRID; 123144; 142.
DR CORUM; Q96F86; -.
DR DIP; DIP-35516N; -.
DR IntAct; Q96F86; 47.
DR MINT; Q96F86; -.
DR STRING; 9606.ENSP00000320503; -.
DR GlyGen; Q96F86; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96F86; -.
DR PhosphoSitePlus; Q96F86; -.
DR BioMuta; EDC3; -.
DR DMDM; 74731669; -.
DR EPD; Q96F86; -.
DR jPOST; Q96F86; -.
DR MassIVE; Q96F86; -.
DR MaxQB; Q96F86; -.
DR PaxDb; Q96F86; -.
DR PeptideAtlas; Q96F86; -.
DR PRIDE; Q96F86; -.
DR ProteomicsDB; 76503; -.
DR Antibodypedia; 27003; 198 antibodies from 29 providers.
DR DNASU; 80153; -.
DR Ensembl; ENST00000315127.9; ENSP00000320503.4; ENSG00000179151.13.
DR Ensembl; ENST00000426797.7; ENSP00000401343.3; ENSG00000179151.13.
DR Ensembl; ENST00000568176.5; ENSP00000455580.1; ENSG00000179151.13.
DR Ensembl; ENST00000647659.1; ENSP00000497737.1; ENSG00000179151.13.
DR GeneID; 80153; -.
DR KEGG; hsa:80153; -.
DR MANE-Select; ENST00000315127.9; ENSP00000320503.4; NM_025083.5; NP_079359.2.
DR UCSC; uc002aym.4; human.
DR CTD; 80153; -.
DR DisGeNET; 80153; -.
DR GeneCards; EDC3; -.
DR HGNC; HGNC:26114; EDC3.
DR HPA; ENSG00000179151; Low tissue specificity.
DR MalaCards; EDC3; -.
DR MIM; 609842; gene.
DR MIM; 616460; phenotype.
DR neXtProt; NX_Q96F86; -.
DR OpenTargets; ENSG00000179151; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR PharmGKB; PA142670551; -.
DR VEuPathDB; HostDB:ENSG00000179151; -.
DR eggNOG; KOG2585; Eukaryota.
DR GeneTree; ENSGT00390000016435; -.
DR HOGENOM; CLU_026194_0_0_1; -.
DR InParanoid; Q96F86; -.
DR OMA; KNRDDEC; -.
DR OrthoDB; 870769at2759; -.
DR PhylomeDB; Q96F86; -.
DR TreeFam; TF324695; -.
DR PathwayCommons; Q96F86; -.
DR Reactome; R-HSA-430039; mRNA decay by 5' to 3' exoribonuclease.
DR SignaLink; Q96F86; -.
DR SIGNOR; Q96F86; -.
DR BioGRID-ORCS; 80153; 15 hits in 1074 CRISPR screens.
DR ChiTaRS; EDC3; human.
DR EvolutionaryTrace; Q96F86; -.
DR GeneWiki; EDC3; -.
DR GenomeRNAi; 80153; -.
DR Pharos; Q96F86; Tbio.
DR PRO; PR:Q96F86; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q96F86; protein.
DR Bgee; ENSG00000179151; Expressed in left testis and 123 other tissues.
DR ExpressionAtlas; Q96F86; baseline and differential.
DR Genevisible; Q96F86; HS.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0033962; P:P-body assembly; IBA:GO_Central.
DR CDD; cd01737; LSm16_N; 1.
DR DisProt; DP02253; -.
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 Pfam; PF09532; FDF; 1.
DR Pfam; PF12701; LSM14; 1.
DR Pfam; PF03853; YjeF_N; 1.
DR SMART; SM01199; FDF; 1.
DR SMART; SM01271; LSM14; 1.
DR SUPFAM; SSF64153; SSF64153; 1.
DR PROSITE; PS51512; DFDF; 1.
DR PROSITE; PS51385; YJEF_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disease variant; Intellectual disability;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..508
FT /note="Enhancer of mRNA-decapping protein 3"
FT /id="PRO_0000119054"
FT DOMAIN 192..228
FT /note="DFDF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT DOMAIN 283..487
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00719"
FT REGION 1..79
FT /note="Required for P-body targeting and interaction with
FT DCP1A"
FT /evidence="ECO:0000250"
FT REGION 95..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..296
FT /note="Required for interaction with DDX6"
FT /evidence="ECO:0000250"
FT COMPBIAS 95..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VARIANT 54
FT /note="F -> S (in MRT50; does not enhance DCP2 decapping
FT activity; dbSNP:rs1057517676)"
FT /evidence="ECO:0000269|PubMed:25701870"
FT /id="VAR_073963"
FT MUTAGEN 204
FT /note="F->A: Abolishes interaction with DDX6; when
FT associated with A-206."
FT /evidence="ECO:0000269|PubMed:19285948"
FT MUTAGEN 206
FT /note="F->A: Abolishes interaction with DDX6; when
FT associated with A-204."
FT /evidence="ECO:0000269|PubMed:19285948"
FT MUTAGEN 306
FT /note="E->A: Abolishes homodimerization and RNA binding;
FT when associated with A-310."
FT /evidence="ECO:0000269|PubMed:18678652"
FT MUTAGEN 310
FT /note="V->A: Abolishes homodimerization and RNA binding;
FT when associated with A-306."
FT /evidence="ECO:0000269|PubMed:18678652"
FT CONFLICT 74
FT /note="Q -> R (in Ref. 2; BAB15001)"
FT /evidence="ECO:0000305"
FT TURN 4..7
FT /evidence="ECO:0007829|PDB:2VC8"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:2VC8"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:2VC8"
FT STRAND 20..29
FT /evidence="ECO:0007829|PDB:2VC8"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:2VC8"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:2VC8"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:2VC8"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2VC8"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2VC8"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:6S8S"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:6S8S"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:6S8S"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:3D3K"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:3D3K"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:3D3K"
FT HELIX 301..319
FT /evidence="ECO:0007829|PDB:3D3K"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:3D3K"
FT HELIX 345..359
FT /evidence="ECO:0007829|PDB:3D3K"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:3D3K"
FT HELIX 376..385
FT /evidence="ECO:0007829|PDB:3D3K"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:3D3K"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:3D3K"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:3D3K"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:3D3K"
FT HELIX 423..435
FT /evidence="ECO:0007829|PDB:3D3K"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:3D3K"
FT STRAND 456..463
FT /evidence="ECO:0007829|PDB:3D3K"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:3D3K"
FT STRAND 473..477
FT /evidence="ECO:0007829|PDB:3D3K"
FT HELIX 483..488
FT /evidence="ECO:0007829|PDB:3D3K"
FT TURN 496..499
FT /evidence="ECO:0007829|PDB:3D3J"
FT STRAND 501..506
FT /evidence="ECO:0007829|PDB:3D3K"
SQ SEQUENCE 508 AA; 56078 MW; 95346F484FCFC3EA CRC64;
MATDWLGSIV SINCGDSLGV YQGRVSAVDQ VSQTISLTRP FHNGVKCLVP EVTFRAGDIT
ELKILEIPGP GDNQHFGDLH QTELGPSGAG CQVGINQNGT GKFVKKPASS SSAPQNIPKR
TDVKSQDVAV SPQQQQCSKS YVDRHMESLS QSKSFRRRHN SWSSSSRHPN QATPKKSGLK
NGQMKNKDDE CFGDDIEEIP DTDFDFEGNL ALFDKAAVFE EIDTYERRSG TRSRGIPNER
PTRYRHDENI LESEPIVYRR IIVPHNVSKE FCTDSGLVVP SISYELHKKL LSVAEKHGLT
LERRLEMTGV CASQMALTLL GGPNRLNPKN VHQRPTVALL CGPHVKGAQG ISCGRHLANH
DVQVILFLPN FVKMLESITN ELSLFSKTQG QQVSSLKDLP TSPVDLVINC LDCPENVFLR
DQPWYKAAVA WANQNRAPVL SIDPPVHEVE QGIDAKWSLA LGLPLPLGEH AGRIYLCDIG
IPQQVFQEVG INYHSPFGCK FVIPLHSA
