EDC3_SCHPO
ID EDC3_SCHPO Reviewed; 454 AA.
AC O94752;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Enhancer of mRNA-decapping protein 3;
GN Name=edc3; ORFNames=SPBC18E5.11c, SPBC23G7.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP STRUCTURE BY NMR OF 1-121 IN COMPLEX WITH DCP2, AND FUNCTION.
RX PubMed=22085934; DOI=10.1038/emboj.2011.408;
RA Fromm S.A., Truffault V., Kamenz J., Braun J.E., Hoffmann N.A.,
RA Izaurralde E., Sprangers R.;
RT "The structural basis of Edc3- and Scd6-mediated activation of the
RT Dcp1:Dcp2 mRNA decapping complex.";
RL EMBO J. 31:279-290(2012).
CC -!- FUNCTION: Stimulates decapping of both stable and unstable mRNA during
CC mRNA decay. Stimulates decapping presumably by preventing the DCP1-DCP2
CC decapping complex from adopting an inactive conformation.
CC {ECO:0000269|PubMed:22085934}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with dcp2. {ECO:0000250,
CC ECO:0000269|PubMed:22085934}.
CC -!- INTERACTION:
CC O94752; O13828: dcp2; NbExp=5; IntAct=EBI-7556871, EBI-3647323;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16823372}.
CC Note=Is concentrated in several cytoplasmic foci called P bodies (or
CC cytoplasmic processing bodies) which represent sites of mRNA decapping
CC and 5' to 3' exonucleotidic decay. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EDC3 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA22671.1; -; Genomic_DNA.
DR PIR; T39762; T39762.
DR RefSeq; NP_595858.1; NM_001021762.2.
DR PDB; 4A53; NMR; -; A=1-121.
DR PDB; 4A54; NMR; -; A=1-94.
DR PDBsum; 4A53; -.
DR PDBsum; 4A54; -.
DR AlphaFoldDB; O94752; -.
DR BMRB; O94752; -.
DR SMR; O94752; -.
DR BioGRID; 277164; 4.
DR IntAct; O94752; 2.
DR MINT; O94752; -.
DR STRING; 4896.SPBC18E5.11c.1; -.
DR iPTMnet; O94752; -.
DR MaxQB; O94752; -.
DR PaxDb; O94752; -.
DR PRIDE; O94752; -.
DR EnsemblFungi; SPBC18E5.11c.1; SPBC18E5.11c.1:pep; SPBC18E5.11c.
DR GeneID; 2540639; -.
DR KEGG; spo:SPBC18E5.11c; -.
DR PomBase; SPBC18E5.11c; edc3.
DR VEuPathDB; FungiDB:SPBC18E5.11c; -.
DR eggNOG; KOG2585; Eukaryota.
DR HOGENOM; CLU_622814_0_0_1; -.
DR InParanoid; O94752; -.
DR OMA; KNRDDEC; -.
DR PhylomeDB; O94752; -.
DR PRO; PR:O94752; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:PomBase.
DR GO; GO:0000932; C:P-body; IDA:PomBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IMP:PomBase.
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; IPR034107; Lsm16_N.
DR InterPro; IPR004443; YjeF_N_dom.
DR InterPro; IPR036652; YjeF_N_dom_sf.
DR Pfam; PF09532; FDF; 1.
DR Pfam; PF03853; YjeF_N; 1.
DR SMART; SM01199; FDF; 1.
DR SUPFAM; SSF64153; SSF64153; 1.
DR PROSITE; PS51512; DFDF; 1.
DR PROSITE; PS51385; YJEF_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome.
FT CHAIN 1..454
FT /note="Enhancer of mRNA-decapping protein 3"
FT /id="PRO_0000119063"
FT DOMAIN 87..123
FT /note="DFDF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT DOMAIN 222..431
FT /note="YjeF N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00719"
FT REGION 173..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:4A53"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:4A53"
FT STRAND 20..29
FT /evidence="ECO:0007829|PDB:4A53"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:4A53"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:4A53"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:4A53"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:4A53"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:4A53"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:4A53"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4A54"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4A53"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4A53"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:4A53"
SQ SEQUENCE 454 AA; 49219 MW; F488C398D2550275 CRC64;
MSVADFYGSN VEVLLNNDSK ARGVITNFDS SNSILQLRLA NDSTKSIVTK DIKDLRILPK
NEIMPKNGTK SPSTNSTKLK SAETYSSKNK WSMDCDEEFD FAANLEKFDK KQVFAEFREK
DKKDPAKLLV SHNKSPNRNY HHKQNVLGPS VKDEFVDLPS AGSQINGIDA VLSSSSNGHV
TPGSKKGSRE TLKKKPFVDE NIPAELHTTT GDILKPITPE QLSQGIALAI AKTSTDIVVE
NAAQLLSQFV FSVLGGHKRL SSRNHNSQPL VCILVGSHDH ASAAVAAGRR LCAIGIKVVL
RLLTPFNVDN RQLLMFQAAG GYIPTENFDQ FLNKLTSPIE LVVDVLTGFH PSIDKNSHAL
IQWANDLNVL ILSVDIPSGY TVQKKNTAIL PKWTLALGAV TTTLAQAALV KQAAGVSVFV
GNLGTGSQTW AELGILESQV TGQYLAQISC TSTN
