ID   EDC3_MACFA              Reviewed;         508 AA.
AC   Q4R8V9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Enhancer of mRNA-decapping protein 3;
DE   AltName: Full=YjeF domain-containing protein 1;
GN   Name=EDC3; Synonyms=YJDC; ORFNames=QtsA-11336;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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; AB168338; BAE00462.1; -; mRNA.
DR   RefSeq; NP_001272174.1; NM_001285245.1.
DR   AlphaFoldDB; Q4R8V9; -.
DR   SMR; Q4R8V9; -.
DR   STRING; 9541.XP_005560132.1; -.
DR   GeneID; 101926635; -.
DR   CTD; 80153; -.
DR   eggNOG; KOG2585; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR   GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..508
FT                   /note="Enhancer of mRNA-decapping protein 3"
FT                   /id="PRO_0000119055"
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:0000250|UniProtKB:Q96F86"
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"
SQ   SEQUENCE   508 AA;  55903 MW;  E20A36011558E082 CRC64;
     MAADWLGSIV SINCGDSLGV YQGRVSAVDQ VSQTISLTRP FHNGVKCLVP EVTFRAGDIT
     ELKILEIPGP GGNQHFGDVH QTELGPSGVG CQVGISQNGT GKLVKKPTSS SSAPQNIPKR
     TDVKSQDVAV SPQQQQCSKS YVDRHMESLS QSKSFRRRHN SWSSSSRHPN QATPKKSGLK
     NGQMKNKDDE CFGDDIEEIP DTDFDFEGNL ALFDKAAVFE EIGTYERRSG TRSRGIPNER
     PTRYRHDENI LESEPIVYRR ITVPHNVSKE FCTDSGLVVP SVSYEQHKKL LSVAEKHGLT
     LERRLEMTGV CASQMALTLL GGPNRLNPKN VHQRPTVALL CGPHVKGAQG ISCGRHLANH
     DVQVILFLPN FVKMLESITN ELSLFSKTQG QQVSSLKDLP TSPVDLVINC LDCPENVFLR
     DQPWYKAAVA WANQNRAPVL SIDPPVHEVE QGIDAKWSLA LGLPLPLGEH AGRIYLCDIG
     IPQQVFQEVG INYHSPFGCK FVIPLHSA