EDC3_MOUSE
ID EDC3_MOUSE Reviewed; 508 AA.
AC Q8K2D3; Q3THV7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Enhancer of mRNA-decapping protein 3;
DE AltName: Full=YjeF domain-containing protein 1;
GN Name=Edc3; Synonyms=Yjdc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Mammary gland, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Binds single-stranded RNA. Involved in the process of mRNA
CC degradation and in the positive regulation of mRNA decapping (By
CC similarity). {ECO:0000250|UniProtKB:Q96F86}.
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. Interacts with ZFP36.
CC {ECO:0000250|UniProtKB:Q96F86}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250}. Note=Processing
CC bodies (PB). {ECO:0000250}.
CC -!- DOMAIN: The DFDF domain is unstructured by itself. It assumes a helical
CC fold upon interaction with DDX6 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EDC3 family. {ECO:0000305}.
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DR EMBL; AK146804; BAE27445.1; -; mRNA.
DR EMBL; AK166286; BAE38683.1; -; mRNA.
DR EMBL; AK168118; BAE40089.1; -; mRNA.
DR EMBL; BC031725; AAH31725.1; -; mRNA.
DR EMBL; BC033484; AAH33484.1; -; mRNA.
DR CCDS; CCDS23231.1; -.
DR RefSeq; NP_722494.1; NM_153799.3.
DR RefSeq; XP_011241062.1; XM_011242760.2.
DR AlphaFoldDB; Q8K2D3; -.
DR SMR; Q8K2D3; -.
DR BioGRID; 237268; 3.
DR IntAct; Q8K2D3; 2.
DR MINT; Q8K2D3; -.
DR STRING; 10090.ENSMUSP00000049146; -.
DR iPTMnet; Q8K2D3; -.
DR PhosphoSitePlus; Q8K2D3; -.
DR EPD; Q8K2D3; -.
DR jPOST; Q8K2D3; -.
DR MaxQB; Q8K2D3; -.
DR PaxDb; Q8K2D3; -.
DR PRIDE; Q8K2D3; -.
DR ProteomicsDB; 277676; -.
DR Antibodypedia; 27003; 198 antibodies from 29 providers.
DR Ensembl; ENSMUST00000043990; ENSMUSP00000049146; ENSMUSG00000038957.
DR GeneID; 353190; -.
DR KEGG; mmu:353190; -.
DR UCSC; uc009pvp.1; mouse.
DR CTD; 80153; -.
DR MGI; MGI:2142951; Edc3.
DR VEuPathDB; HostDB:ENSMUSG00000038957; -.
DR eggNOG; KOG2585; Eukaryota.
DR GeneTree; ENSGT00390000016435; -.
DR HOGENOM; CLU_026194_0_0_1; -.
DR InParanoid; Q8K2D3; -.
DR OMA; KNRDDEC; -.
DR OrthoDB; 870769at2759; -.
DR PhylomeDB; Q8K2D3; -.
DR TreeFam; TF324695; -.
DR Reactome; R-MMU-430039; mRNA decay by 5' to 3' exoribonuclease.
DR BioGRID-ORCS; 353190; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Edc3; mouse.
DR PRO; PR:Q8K2D3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8K2D3; protein.
DR Bgee; ENSMUSG00000038957; Expressed in embryonic brain and 225 other tissues.
DR ExpressionAtlas; Q8K2D3; baseline and differential.
DR Genevisible; Q8K2D3; MM.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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 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 Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..508
FT /note="Enhancer of mRNA-decapping protein 3"
FT /id="PRO_0000119056"
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 98..194
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 98..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:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96F86"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96F86"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96F86"
FT CONFLICT 237
FT /note="P -> T (in Ref. 1; BAE40089)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="Q -> R (in Ref. 1; BAE40089)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 55957 MW; DD1F449BEF1341C8 CRC64;
MAMDWLGSIV SINCGDSLGV YQGRVSAVDQ VSQTISLTRP FHNGVKCLVP EVTFRAGDIT
ELKILEIPGP GDNQQVGDLH QTELGPSGVG YQMSISQNGT GKVVKKPASS SSAPQSIPKR
TDVKSQDVAI SPQQQQCSKS YVDRHMESLS QSKSFRRRHN SWSSSSRHPN QATPKKSGLK
NGQMKNKDDE CFGDDIEELP DTDFDFEGNL ALFDKAAVFE EIDTYERRSG SRSRGVPNER
PARYRHDENI LESEPIVYRR ITVPHSVSKE FCTDSGLVVP SVSYELHKKL LSVAEKHGLT
LERRLEMTGV CASQMALTLL GGPNRLNPKN VHQRPTVALL CGPHVKGAQG ISCGRHLANH
DVQVILFLPN FVKMLESITN ELSLFSKTQG QQVSSLRDLP ASPVDLVINC LDCPENAFLR
DQPWYKAAVA WANQNRAPVL SIDPPVHEVE QGIDAKWSLA LGLPLPLGEH AGRVYLCDIG
IPQQVFQEVG INYHSPFGCK FVIPLHSA
