DCP1_SCHPO
ID DCP1_SCHPO Reviewed; 127 AA.
AC Q9P805;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=mRNA-decapping enzyme subunit 1;
GN Name=dcp1; ORFNames=SPBC3B9.21;
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 FUNCTION.
RX PubMed=15671491; DOI=10.1093/jb/mvh190;
RA Sakuno T., Araki Y., Ohya Y., Kofuji S., Takahashi S., Hoshino S.,
RA Katada T.;
RT "Decapping reaction of mRNA requires Dcp1 in fission yeast: its
RT characterization in different species from yeast to human.";
RL J. Biochem. 136:805-812(2004).
RN [3]
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).
CC -!- FUNCTION: Component of the decapping complex necessary for the
CC degradation of mRNAs, both in normal mRNA turnover and in nonsense-
CC mediated mRNA decay. Removes the 7-methyl guanine cap structure from
CC mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP.
CC Decapping is the major pathway of mRNA degradation in yeast. It occurs
CC through deadenylation, decapping and subsequent 5' to 3' exonucleolytic
CC decay of the transcript body. {ECO:0000269|PubMed:15671491}.
CC -!- SUBUNIT: Component of the decapping complex composed of dcp1 and dcp2.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9P805; O13828: dcp2; NbExp=7; IntAct=EBI-7557105, EBI-3647323;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the DCP1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB69661.1; -; Genomic_DNA.
DR RefSeq; NP_596662.1; NM_001022584.2.
DR PDB; 2QKL; X-ray; 2.33 A; A=1-127.
DR PDB; 2QKM; X-ray; 2.80 A; A/C/E/G=1-127.
DR PDB; 5J3Q; X-ray; 1.87 A; A/C=1-127.
DR PDB; 5J3T; X-ray; 1.60 A; A=1-127.
DR PDB; 5J3Y; X-ray; 3.29 A; A/C=1-127.
DR PDB; 5JP4; X-ray; 2.04 A; A=1-127.
DR PDB; 5KQ1; X-ray; 3.00 A; A/D=1-127.
DR PDB; 5KQ4; X-ray; 2.56 A; A/D=1-127.
DR PDB; 5N2V; X-ray; 3.10 A; A/D=1-127.
DR PDBsum; 2QKL; -.
DR PDBsum; 2QKM; -.
DR PDBsum; 5J3Q; -.
DR PDBsum; 5J3T; -.
DR PDBsum; 5J3Y; -.
DR PDBsum; 5JP4; -.
DR PDBsum; 5KQ1; -.
DR PDBsum; 5KQ4; -.
DR PDBsum; 5N2V; -.
DR AlphaFoldDB; Q9P805; -.
DR SMR; Q9P805; -.
DR BioGRID; 277548; 18.
DR DIP; DIP-29008N; -.
DR IntAct; Q9P805; 3.
DR MINT; Q9P805; -.
DR STRING; 4896.SPBC3B9.21.1; -.
DR MaxQB; Q9P805; -.
DR PaxDb; Q9P805; -.
DR PRIDE; Q9P805; -.
DR EnsemblFungi; SPBC3B9.21.1; SPBC3B9.21.1:pep; SPBC3B9.21.
DR GeneID; 2541033; -.
DR KEGG; spo:SPBC3B9.21; -.
DR PomBase; SPBC3B9.21; dcp1.
DR VEuPathDB; FungiDB:SPBC3B9.21; -.
DR eggNOG; KOG2868; Eukaryota.
DR HOGENOM; CLU_152856_0_0_1; -.
DR InParanoid; Q9P805; -.
DR OMA; ILDQSAH; -.
DR PhylomeDB; Q9P805; -.
DR EvolutionaryTrace; Q9P805; -.
DR PRO; PR:Q9P805; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0098745; C:Dcp1-Dcp2 complex; IDA:PomBase.
DR GO; GO:0005845; C:mRNA cap binding complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000932; C:P-body; IDA:PomBase.
DR GO; GO:1990521; F:m7G(5')pppN diphosphatase activator activity; IDA:PomBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IDA:PomBase.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IMP:PomBase.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0034428; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 5'-3'; IMP:PomBase.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR010334; Dcp1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR16290; PTHR16290; 1.
DR Pfam; PF06058; DCP1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; mRNA processing; Nonsense-mediated mRNA decay;
KW Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..127
FT /note="mRNA-decapping enzyme subunit 1"
FT /id="PRO_0000339336"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:5J3T"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 23..39
FT /evidence="ECO:0007829|PDB:5J3T"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 44..59
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 64..74
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:5J3T"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:5J3T"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:5J3T"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:5J3T"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:5J3T"
SQ SEQUENCE 127 AA; 14983 MW; DD593F646C61EEC0 CRC64;
MEDENILRNA VNLQVLKFHY PEIESIIDIA SHVAVYQFDV GSQKWLKTSI EGTFFLVKDQ
RARVGYVILN RNSPENLYLF INHPSNVHLV DRYLIHRTEN QHVVGLWMFD PNDMSRIFNI
VKESLLR
