ID   EDC3_PONAB              Reviewed;         508 AA.
AC   Q5RDU9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Enhancer of mRNA-decapping protein 3;
DE   AltName: Full=YjeF domain-containing protein 1;
GN   Name=EDC3; Synonyms=YJDC;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR857796; CAH90058.1; -; mRNA.
DR   RefSeq; NP_001124985.1; NM_001131513.1.
DR   AlphaFoldDB; Q5RDU9; -.
DR   SMR; Q5RDU9; -.
DR   STRING; 9601.ENSPPYP00000007534; -.
DR   GeneID; 100171859; -.
DR   KEGG; pon:100171859; -.
DR   CTD; 80153; -.
DR   eggNOG; KOG2585; Eukaryota.
DR   InParanoid; Q5RDU9; -.
DR   OrthoDB; 870769at2759; -.
DR   Proteomes; UP000001595; 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_0000119057"
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          89..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        91..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;  56101 MW;  08AC0A1DF18745A7 CRC64;
     MATDWLGSIV SINCGDSLGV YQGRVSAVDQ VSQTISLTRP FHNGVKCLVP EVTFRAGDIT
     ELKILEIPGP GDNQHFGDLH QTELGPSGAG CQVGINQNGT GKLVKKPASS SSAPQNIPKR
     TDVKSQDVAV SPQQQQCSKS YVDRHMESLS QSKSFRRRHN SWSSSSRHPN QATPKKSGLK
     NGQMKNKDDE CFGDDIEEIP DTDFDFEGNL ALFDKAAVFE EIDTYERRSG TRSRGIPNER
     PTRYRHDENI LESEPIVYRR ITVPHNVSKE FCTDSGLVVP SISYELHKKL LSVAEKHGLT
     LERRLEMTGV CASQMALTLL GGPNRLNPKN VHQRPTVALL CGPHVKGAQG IRCGRHLANH
     DVQVILFLPN FVKMLESITN ELSLFSKTQG QQVSSLKDLP TSPVDLVINC LDCPENVFLR
     DQPWYKAAVA WANQNRAPVL SIDPPVHEVE QGIDAKWSLA LGLPLPLGEH AGRIYLCDIG
     IPQQVFQEVG INYHSPFGCK FVIPLHSA