EDC4_RAT
ID EDC4_RAT Reviewed; 1407 AA.
AC Q3ZAV8;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Enhancer of mRNA-decapping protein 4;
GN Name=Edc4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-734 AND SER-850, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Interacts with NBDY. Interacts with Tex19.1
CC (By similarity). Interacts with LSM14A (By similarity). Interacts with
CC DDX6 (By similarity). {ECO:0000250|UniProtKB:Q3UJB9,
CC ECO:0000250|UniProtKB:Q6P2E9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q6P2E9}.
CC Nucleus {ECO:0000250|UniProtKB:Q6P2E9}.
CC -!- SIMILARITY: Belongs to the WD repeat EDC4 family. {ECO:0000305}.
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DR EMBL; BC103628; AAI03629.1; -; mRNA.
DR RefSeq; NP_001028240.3; NM_001033068.3.
DR AlphaFoldDB; Q3ZAV8; -.
DR BioGRID; 262648; 1.
DR IntAct; Q3ZAV8; 1.
DR STRING; 10116.ENSRNOP00000033608; -.
DR iPTMnet; Q3ZAV8; -.
DR PhosphoSitePlus; Q3ZAV8; -.
DR jPOST; Q3ZAV8; -.
DR PaxDb; Q3ZAV8; -.
DR PRIDE; Q3ZAV8; -.
DR GeneID; 361399; -.
DR KEGG; rno:361399; -.
DR UCSC; RGD:1562009; rat.
DR CTD; 23644; -.
DR RGD; 1562009; Edc4.
DR VEuPathDB; HostDB:ENSRNOG00000024025; -.
DR eggNOG; KOG1916; Eukaryota.
DR HOGENOM; CLU_005166_0_0_1; -.
DR InParanoid; Q3ZAV8; -.
DR OrthoDB; 1424637at2759; -.
DR Reactome; R-RNO-430039; mRNA decay by 5' to 3' exoribonuclease.
DR PRO; PR:Q3ZAV8; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000024025; Expressed in pancreas and 20 other tissues.
DR ExpressionAtlas; Q3ZAV8; baseline and differential.
DR Genevisible; Q3ZAV8; RN.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000932; C:P-body; ISO:RGD.
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; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT CHAIN 2..1407
FT /note="Enhancer of mRNA-decapping protein 4"
FT /id="PRO_0000278964"
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 547..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 972..1031
FT /evidence="ECO:0000255"
FT COMPBIAS 727..745
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 681
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UJB9"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 732
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 827
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 877
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 880
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3UJB9"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UJB9"
FT MOD_RES 896
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UJB9"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
FT MOD_RES 907
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3UJB9"
FT MOD_RES 1386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P2E9"
SQ SEQUENCE 1407 AA; 152596 MW; E9C551C47D199EA9 CRC64;
MASCASIDIE DATQHLRDIL KLDRPAGGSN VESQRPSSAY NGDLNGLLVP DPLSSGDGNS
TSKPGIRTMP PINLQEKQVI CLSGDDSSTC IGILAKEVEI VASSDSSISS KARGSNKVKI
QPVAKYDWEQ KYYYGNLIAV SNSFLAYAIR AANNGSAMVR VISVSTSERT LLKGFTGSVA
DLAFAHLNSP QLACLDEAGD LFVWRLALVK GKIQEEILVH IRQPEGTPLN HFRRIIWCPF
IPEESEDCCE ESSPTVALLH EDRAEVWDLD MLRSSHSTWP VDVSQIKQGF IVVKGHSTCL
SEGALSPDGT VLATASHDGF VKFWQIYIEG QDEPRCLHEW KPHDGRPLSC LLFCDNHKKQ
DPEVPFWRFL ITGADQNREL KMWCTVSWTC LQTIRFSPDI FSSVSVPPSL KVCLDLSAEY
LILSDVQRKV LYVMELLQNQ DEGRACFSSI SEFLLTHPVL SFGIQVVSRC RLRHTEVLPA
EEESDSLGTE SSHGAGTLES AAGVLIKLFC VHTKALQDVQ IRFQPQLNPD VVAPLSTHTA
HEDFTFGESR PELGSEGLAS APHGSQPDLR RIVELPAPAD FLSLSSETKP KLMTPDAFMT
PTASLQQISA SPSSSSSSSS SSSSSSSSSS SSSLTAVSAV SSSSAMDPSL PSRPPEELTL
SPKLQLDGSL TISSSSSLQA SPRSLLPGLL PGPADKLIPK GPGQVSSGTS ALSLDLQEVE
PLGLPQASPS RTRSPDVISS ASTALSQDIP EIASEALSRG FGSSVPEGLI EPDSMASAAS
ALHLLSPRPR QGPELSSQLG LDGGPGDGDR HSTPSLLEAA LTQEVATSDS QVWPTAPDIT
RETCSTLTES PRNGLQEKHK SLAFHRPPYH LLQQHDSQDT SAEQSDHDDE VASLASASGG
FGSKIPTPRL PAKDWKTKGS PRTSPKLKRK SKKDDGDSAV GSRLTEHQVV EPPEDWPALI
WQQQRELAEL WHNQEELLQR LCAQLEGLQS TVTDHVERAL ETRHEQEQRR LERALAEGQQ
RGGQLQEQLT QQLSQALSSA VAGRLERSIR DEIKKTVPPC VSRSLEPVAG QLSNSVATKL
TAVEGSMKEN ISKLLKSKNL TDAIARAAAD TLQGPMQAAY REAFQSVVLP AFEKSCQAMF
QQINDSFRLG TQEYLQQLDS HMKSRKAREQ EAREPVLAQL RGLVSTLQNA TEQMAATVSS
SVRAEVQHQL HVAVGSLQES ILAQVQRIVK GEVSVALKEQ QATVTSSIMQ AMRSAAGTPV
PSAHLDCQAQ QAHILQLLQQ GHLNQAFQQA LTAADLNLVL YVCETVDPAQ VFGQPPCPLS
QPVLLSLIQQ LASDLGTRSD LKLSYLEEAV MHLDHSDPIT RDHMGSVMAQ VRQKLFQFLQ
ADPHNSLGKA ARRLSLMLHG LVTPSLP
