ID   EDC3_DANRE              Reviewed;         507 AA.
AC   Q502M5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Enhancer of mRNA-decapping protein 3;
DE   AltName: Full=LSM16 protein homolog;
DE   AltName: Full=YjeF domain-containing protein 1;
GN   Name=edc3; Synonyms=lsm16, yjdc; ORFNames=zgc:112006;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18307296; DOI=10.1021/pr700667w;
RA   Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA   Slijper M., Heck A.J.R.;
RT   "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT   analysis down to a single embryo.";
RL   J. Proteome Res. 7:1555-1564(2008).
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; BC095641; AAH95641.1; -; mRNA.
DR   AlphaFoldDB; Q502M5; -.
DR   SMR; Q502M5; -.
DR   STRING; 7955.ENSDARP00000106420; -.
DR   iPTMnet; Q502M5; -.
DR   PaxDb; Q502M5; -.
DR   ZFIN; ZDB-GENE-050522-287; edc3.
DR   eggNOG; KOG2585; Eukaryota.
DR   InParanoid; Q502M5; -.
DR   PhylomeDB; Q502M5; -.
DR   Reactome; R-DRE-430039; mRNA decay by 5' to 3' exoribonuclease.
DR   PRO; PR:Q502M5; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0000932; C:P-body; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR   GO; GO:0033962; P:P-body assembly; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN           1..507
FT                   /note="Enhancer of mRNA-decapping protein 3"
FT                   /id="PRO_0000119059"
FT   DOMAIN          189..225
FT                   /note="DFDF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT   DOMAIN          282..486
FT                   /note="YjeF N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00719"
FT   REGION          1..77
FT                   /note="Required for P-body targeting and interaction with
FT                   DCP1A"
FT                   /evidence="ECO:0000250"
FT   REGION          75..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..295
FT                   /note="Required for interaction with DDX6"
FT                   /evidence="ECO:0000250"
FT   REGION          220..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
SQ   SEQUENCE   507 AA;  54852 MW;  7DFBE3D9D4E4BA9B CRC64;
     MALDWVGNLV SIHCGPTLGV YQGEISSVDQ TSQTISLRNP FHNGVKCTVP EVTFSAMDIK
     DLKILEISKN SIEVSKQNGP ESSSTTLMPH VGRKDKGGGG GGGGAPANSA PVMVPNKAEP
     RLQEGGVSPV PHYSKSYGER HIDMAVQGKG FRRRHNSWSS SCRGPNQATP KKNGLKNGGH
     MKNKDDECFG DGMDDVLDED FDFEGNLALF DKAAVLSQIE SSERRGNGAR SRGTPGEQTP
     SRYRHDENIL EAKPVVYRQI TVPQNGSKEY STDSGLVVPS ISFELHKRLL AAAESHGLSL
     ERRLEMTGVC ASQMALTLLG GPNRLTPKNV HQRPTVALLC GPHVQGAQGI SCGRHLANHE
     VEVVLFLPNF VKMLEAITSE LALFGKTGGR LVSNVKDLPE TPVDLVINCL DSHENGFLRD
     QPWYKAAADW ANQNRAPVLS IDPPVSGQAH AVEAKWSLSL GLPLPLSEGA GRVYPCDIGI
     PRQVFQEVGI KYHSPFGCKF VIPLHSE