EDC4_MOUSE
ID EDC4_MOUSE Reviewed; 1406 AA.
AC Q3UJB9; Q3U6U8; Q7TS78; Q8R223;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Enhancer of mRNA-decapping protein 4 {ECO:0000305};
GN Name=Edc4 {ECO:0000312|MGI:MGI:2446249};
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Kidney;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon;
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-892, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680; THR-731; SER-745;
RP THR-879; SER-884; SER-892; SER-895 AND THR-906, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
RN [7]
RP INTERACTION WITH RC3H1.
RX PubMed=20639877; DOI=10.1038/ni.1902;
RA Glasmacher E., Hoefig K.P., Vogel K.U., Rath N., Du L., Wolf C.,
RA Kremmer E., Wang X., Heissmeyer V.;
RT "Roquin binds inducible costimulator mRNA and effectors of mRNA decay to
RT induce microRNA-independent post-transcriptional repression.";
RL Nat. Immunol. 11:725-733(2010).
RN [8]
RP INTERACTION WITH RC3H1.
RX PubMed=23583643; DOI=10.1016/j.immuni.2012.12.004;
RA Vogel K.U., Edelmann S.L., Jeltsch K.M., Bertossi A., Heger K., Heinz G.A.,
RA Zoller J., Warth S.C., Hoefig K.P., Lohs C., Neff F., Kremmer E.,
RA Schick J., Repsilber D., Geerlof A., Blum H., Wurst W., Heikenwalder M.,
RA Schmidt-Supprian M., Heissmeyer V.;
RT "Roquin paralogs 1 and 2 redundantly repress the Icos and Ox40 costimulator
RT mRNAs and control follicular helper T cell differentiation.";
RL Immunity 38:655-668(2013).
RN [9]
RP INTERACTION WITH TEX19.1.
RX PubMed=28254886; DOI=10.1242/jcs.188763;
RA Tarabay Y., Achour M., Teletin M., Ye T., Teissandier A., Mark M.,
RA Bourc'his D., Viville S.;
RT "Tex19 paralogs are new members of the piRNA pathway controlling
RT retrotransposon suppression.";
RL J. Cell Sci. 130:1463-1474(2017).
CC -!- FUNCTION: In the process of mRNA degradation, seems to play a role in
CC mRNA decapping. Component of a complex containing DCP2 and DCP1A which
CC functions in decapping of ARE-containing mRNAs. Promotes complex
CC formation between DCP1A and DCP2. Enhances the catalytic activity of
CC DCP2 (in vitro). {ECO:0000250|UniProtKB:Q6P2E9}.
CC -!- SUBUNIT: Part of a decapping complex consisting of DCP1A, DCP2, EDC3,
CC EDC4 and probably DDX6. Part of a complex consisting of DCP1A, EDC3,
CC EDC4 and DDX6. Part of a complex consisting of DCP1B, EDC3, EDC4 and
CC DDX6. Interacts with DCP2 (By similarity). Interacts with RC3H1
CC (PubMed:20639877, PubMed:23583643). Interacts with NBDY (By
CC similarity). Interacts with Tex19.1 and, probably, Tex19.2
CC (PubMed:28254886). Interacts with LSM14A (By similarity). Interacts
CC with DDX6 (By similarity). {ECO:0000250|UniProtKB:Q6P2E9,
CC ECO:0000269|PubMed:20639877, ECO:0000269|PubMed:23583643,
CC ECO:0000269|PubMed:28254886}.
CC -!- INTERACTION:
CC Q3UJB9; Q4VGL6: Rc3h1; NbExp=3; IntAct=EBI-2553526, EBI-2366263;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q6P2E9}.
CC Nucleus {ECO:0000250|UniProtKB:Q6P2E9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UJB9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UJB9-2; Sequence=VSP_023413;
CC -!- SIMILARITY: Belongs to the WD repeat EDC4 family. {ECO:0000305}.
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DR EMBL; AK146527; BAE27236.1; -; mRNA.
DR EMBL; AK152963; BAE31626.1; -; mRNA.
DR EMBL; BC022641; AAH22641.1; -; mRNA.
DR EMBL; BC053081; AAH53081.1; -; mRNA.
DR CCDS; CCDS52662.1; -. [Q3UJB9-2]
DR CCDS; CCDS80923.1; -. [Q3UJB9-1]
DR RefSeq; NP_001288029.1; NM_001301100.1.
DR RefSeq; NP_853625.1; NM_181594.3.
DR AlphaFoldDB; Q3UJB9; -.
DR SMR; Q3UJB9; -.
DR BioGRID; 231562; 30.
DR IntAct; Q3UJB9; 27.
DR STRING; 10090.ENSMUSP00000039134; -.
DR iPTMnet; Q3UJB9; -.
DR PhosphoSitePlus; Q3UJB9; -.
DR SwissPalm; Q3UJB9; -.
DR EPD; Q3UJB9; -.
DR jPOST; Q3UJB9; -.
DR MaxQB; Q3UJB9; -.
DR PaxDb; Q3UJB9; -.
DR PeptideAtlas; Q3UJB9; -.
DR PRIDE; Q3UJB9; -.
DR ProteomicsDB; 277677; -. [Q3UJB9-1]
DR ProteomicsDB; 277678; -. [Q3UJB9-2]
DR GeneID; 234699; -.
DR KEGG; mmu:234699; -.
DR UCSC; uc009nek.2; mouse. [Q3UJB9-2]
DR CTD; 23644; -.
DR MGI; MGI:2446249; Edc4.
DR eggNOG; KOG1916; Eukaryota.
DR InParanoid; Q3UJB9; -.
DR OrthoDB; 1424637at2759; -.
DR PhylomeDB; Q3UJB9; -.
DR Reactome; R-MMU-430039; mRNA decay by 5' to 3' exoribonuclease.
DR BioGRID-ORCS; 234699; 18 hits in 73 CRISPR screens.
DR ChiTaRS; Edc4; mouse.
DR PRO; PR:Q3UJB9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3UJB9; protein.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000932; C:P-body; ISO:MGI.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR Gene3D; 1.10.220.100; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045152; EDC4-like.
DR InterPro; IPR044938; EDC4_C.
DR InterPro; IPR032401; EDC4_WD40.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15598; PTHR15598; 1.
DR Pfam; PF16529; Ge1_WD40; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT CHAIN 2..1406
FT /note="Enhancer of mRNA-decapping protein 4"
FT /id="PRO_0000278963"
FT REPEAT 174..214
FT /note="WD 1"
FT REPEAT 230..277
FT /note="WD 2"
FT REPEAT 295..334
FT /note="WD 3"
FT REPEAT 342..393
FT /note="WD 4"
FT REGION 604..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 971..1030
FT /evidence="ECO:0000255"
FT COMPBIAS 667..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 125
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 731
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 826
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 849
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 879
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 880
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 897
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 906
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT VAR_SEQ 849..864
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023413"
FT CONFLICT 591
FT /note="E -> K (in Ref. 2; AAH53081)"
FT /evidence="ECO:0000305"
FT CONFLICT 772
FT /note="N -> D (in Ref. 2; AAH53081)"
FT /evidence="ECO:0000305"
FT CONFLICT 1152
FT /note="E -> G (in Ref. 1; BAE27236/BAE31626)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1406 AA; 152484 MW; F89969FDD9EF0725 CRC64;
MASCASIDIE DATQHLRDIL KLDRPAGGSN AESQRPSSAY NGDLNGLLVP DPLSSGDGNS
TNKPGIRTMP PINLQEKQVI CLSGDDSSTC IGILAKEVEI VASSDSSISS KARGSNKVKI
QPVAKYDWEQ KYYYGNLIAV SNSFLAYAIR AANNGSAMVR VISVSTSERT LLKGFTGSVA
DLAFAHLNSP QLACLDEAGN LFVWRLALVK GKIQEEILVH IRQPEGTALN HFRRIIWCPF
IPEESEDCCE ESSPTVALLH EDRAEVWDLD MLRSSHNTWP VDVSQIKQGF IVVKGHSTCL
SEGALSPDGT VLATASHDGF VKFWQIYIEG QDEPRCLHEW KPHDGRPLSC LLFCDNHKKQ
DPEVPFWRFL ITGADQNREL KMWCTVSWTC LQTIRFSPDI FSSVSVPPSL KVCLDLSAEY
LILSDVQRKV LYVMELLQNQ DEGRACFSSI SEFLLTHPVL SFGIQVVSRC RLRHTEVLPA
EEENDSLGTE SSHGAGALES AAGVLIKLFC VHTKALQDVQ IRFQPQLNPD VVAPLSTHTA
HEDFTFGESR PELGSEGLAS AAHGSQPDLR RIVELPAPAD FLSLSSETKP ELMTPDAFMT
PTASLQQISA SPSSSSSSSS SSSSSSSSSS SSLTAVSAVS SSSAMDPSLP RPPEELTLSP
KLQLDGSLTL NSSSSSLQAS PRSLLPGLLP GPADKLISKG PGQVSTAASA LSLDLQEVEP
LGLPQASPSR TRSPDVISSA STALSQDIPE IASEALSRGF GSSVPEGLIE PNSMASAASA
LHLLSPRPRQ GPELGSQLGL DGGPGDGDRH STPSLLEAAL TQEVATPDSQ VWPTAPDITR
ETCSTLTESP RNGLQEKHKS LAFHRPPYHL LQQRDSQDTS AEQSDHDDEV ASLASASGGF
GSKIPTPRLP SKDWKTKGSP RTSPKLKRKS KKDDGDSAVG SRLTEHQVAE PPEDWPALIW
QQQRELAELW HNQEELLQRL CAQLEGLQST VTDHVERALE TRHEQEQRRL ERALAEGQQR
GGQLQEQLTQ QLSQALSSAV AGRLERSVRD EIKKTVPPCV SRSLEPVAGQ LSNSVATKLT
AVEGSMKENI SKLLKSKNLT DAIARAAADT LQGPMQAAYR EAFQSVVLPA FEKSCQAMFQ
QINDSFRLGT QEYLQQLESH MKSRKAREQE AREPVLAQLR GLVSTLQSAT EQMAATVSSS
VRAEVQHQLH VAVGSLQESI LAQVQRIVKG EVSVALKEQQ ATVTSSIMQA MRSAAGTPVP
SAHLDCQAQQ AHILQLLQQG HLNQAFQQAL TAADLNLVLY VCETVDPAQV FGQPPCPLSQ
PVLLSLIQQL ASDLGTRSDL KLSYLEEAVM HLDHSDPITR DHMGSVMAQV RQKLFQFLQA
DPHNSLSKAA RRLSLMLHGL VTPSLP
