EDC3_XENLA
ID EDC3_XENLA Reviewed; 505 AA.
AC Q5XH48;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, 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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-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 -!- 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 other proteins (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EDC3 family. {ECO:0000305}.
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DR EMBL; BC084225; AAH84225.1; -; mRNA.
DR RefSeq; NP_001088234.1; NM_001094765.1.
DR AlphaFoldDB; Q5XH48; -.
DR SMR; Q5XH48; -.
DR BioGRID; 105145; 1.
DR IntAct; Q5XH48; 1.
DR DNASU; 495065; -.
DR GeneID; 495065; -.
DR KEGG; xla:495065; -.
DR CTD; 495065; -.
DR Xenbase; XB-GENE-5890837; edc3.S.
DR OrthoDB; 870769at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 495065; Expressed in ovary and 19 other tissues.
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; Reference proteome; RNA-binding.
FT CHAIN 1..505
FT /note="Enhancer of mRNA-decapping protein 3"
FT /id="PRO_0000119060"
FT DOMAIN 187..223
FT /note="DFDF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT DOMAIN 280..484
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 84..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..293
FT /note="Required for interaction with DDX6"
FT /evidence="ECO:0000250"
FT REGION 219..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 55576 MW; C8BE6EF9D0F76E56 CRC64;
MAADWLGSIV SINCGNTLGV YQGCVSAVDR INQTISLSQP FHNGVKCLVP EVTFRAGDIS
ELKILEIPSE SLKYTSDQLN DHSTGFGYLP TRQQNGTGKQ KQTVAHNSAQ NIPGQEEGKA
SEPSSTSPQP CSKSFVDRHN EAVNQPKNFR RRHNSLGSSS SRYPNQVTPK KSGTKNGQLK
ARDDECFGDE LEEIPDTDFD FEGNLALFDK AAVFEEIDTH ERRGGGGTRS RGTPNERPPT
YRHDENILES EPIVYRKIVV PQSGGQEYCT DSGLVVPSIS YVLHKKLLCV AEKHGLSVER
RLEMSGVCAS QMALTLLGGP NRLNPKNVHQ RPTVALLCGP HVKGAQGISC GRHLANYDVD
IILFLPNFVK MLEPVTNELN LFCQTQGKQV SSVKDLPECP VDLVINCLDC NENAFLCDQP
WYRAAVDWAN HNRAPVLNID PPVGDHVQGI HAKWSLELGL PLALGEQAGR IYLCDIGIPQ
KVFREVGISY HSPFGCKFVI PLHSM