DCS2_YEAST
ID DCS2_YEAST Reviewed; 353 AA.
AC Q12123; D6W2M9;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Inactive diphosphatase DCS2;
DE AltName: Full=Histidine triad protein;
DE AltName: Full=Protein Dcs2p;
GN Name=DCS2 {ECO:0000312|SGD:S000005699}; OrderedLocusNames=YOR173W;
GN ORFNames=O3625;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB47418.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1678 {ECO:0000312|EMBL:AAB47418.1};
RX PubMed=8972579;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1563::aid-yea44>3.0.co;2-m;
RA Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P.;
RT "Analysis of a 22,956 bp region on the right arm of Saccharomyces
RT cerevisiae chromosome XV.";
RL Yeast 12:1563-1573(1996).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAA99381.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-11, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=15240832; DOI=10.1093/nar/gkh687;
RA Malys N., Carroll K., Miyan J., Tollervey D., McCarthy J.E.G.;
RT "The 'scavenger' m7GpppX pyrophosphatase activity of Dcs1 modulates
RT nutrient-induced responses in yeast.";
RL Nucleic Acids Res. 32:3590-3600(2004).
RN [5]
RP LACK OF ENZYME ACTIVITY.
RX PubMed=12198172; DOI=10.1093/emboj/cdf448;
RA Liu H., Rodgers N.D., Jiao X., Kiledjian M.;
RT "The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of
RT pyrophosphatases.";
RL EMBO J. 21:4699-4708(2002).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=16963086; DOI=10.1016/j.jmb.2006.08.015;
RA Malys N., McCarthy J.E.;
RT "Dcs2, a novel stress-induced modulator of m7GpppX pyrophosphatase activity
RT that locates to P bodies.";
RL J. Mol. Biol. 363:370-382(2006).
RN [9]
RP LACK OF CATALYTIC ACTIVITY.
RX PubMed=15273322; DOI=10.1261/rna.7660804;
RA Liu S.-W., Jiao X., Liu H., Gu M., Lima C.D., Kiledjian M.;
RT "Functional analysis of mRNA scavenger decapping enzymes.";
RL RNA 10:1412-1422(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Plays a role in the cleavage of a residual cap structure
CC following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA
CC decay pathway. Stress-induced regulatory protein that modulates the
CC m7GpppX diphosphatase activity of DCS1. {ECO:0000269|PubMed:15240832,
CC ECO:0000269|PubMed:16963086}.
CC -!- SUBUNIT: Homodimer. Forms heterodimer with DCS2; the interaction
CC inhibits the DCS1 scavenger decapping activity during post-diauxic
CC growth. {ECO:0000269|PubMed:15240832, ECO:0000269|PubMed:16963086}.
CC -!- INTERACTION:
CC Q12123; Q06151: DCS1; NbExp=8; IntAct=EBI-38701, EBI-38973;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC Cytoplasm, P-body. Note=Predominantly cytoplasmic. Localizes close to
CC the perinuclear space before the diauxic growth shift. Recruited to the
CC P-body after the post-diauxic growth shift. Colocalizes with the
CC decapping activator protein LSM1 at P-body.
CC -!- INDUCTION: By nutrient, osmotic, oxidative and heat stress. Up-
CC regulated during the diauxic shift. {ECO:0000269|PubMed:15240832}.
CC -!- MISCELLANEOUS: Present with 1870 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HIT family. {ECO:0000255}.
CC -!- CAUTION: Although strongly related to the DcpS enzyme, it has
CC apparently no scavenger mRNA-decapping activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB47418.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA99381.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U55021; AAB47418.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z75081; CAA99381.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006948; DAA10945.1; -; Genomic_DNA.
DR PIR; S67061; S67061.
DR RefSeq; NP_014816.2; NM_001183592.1.
DR AlphaFoldDB; Q12123; -.
DR SMR; Q12123; -.
DR BioGRID; 34567; 50.
DR ComplexPortal; CPX-1185; DCS1-DCS2 regulator of decapping scavenger complex.
DR DIP; DIP-4135N; -.
DR IntAct; Q12123; 4.
DR MINT; Q12123; -.
DR STRING; 4932.YOR173W; -.
DR iPTMnet; Q12123; -.
DR MaxQB; Q12123; -.
DR PaxDb; Q12123; -.
DR PRIDE; Q12123; -.
DR EnsemblFungi; YOR173W_mRNA; YOR173W; YOR173W.
DR GeneID; 854344; -.
DR KEGG; sce:YOR173W; -.
DR SGD; S000005699; DCS2.
DR VEuPathDB; FungiDB:YOR173W; -.
DR eggNOG; KOG3969; Eukaryota.
DR GeneTree; ENSGT00390000003924; -.
DR HOGENOM; CLU_041045_0_1_1; -.
DR InParanoid; Q12123; -.
DR OMA; LIYPCTD; -.
DR BioCyc; YEAST:G3O-33686-MON; -.
DR PRO; PR:Q12123; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12123; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
DR GO; GO:0031670; P:cellular response to nutrient; IDA:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IGI:SGD.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IDA:SGD.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IDA:ComplexPortal.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:1903398; P:regulation of m7G(5')pppN diphosphatase activity; IDA:ComplexPortal.
DR GO; GO:0009408; P:response to heat; IDA:UniProtKB.
DR GO; GO:0007584; P:response to nutrient; IDA:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR Gene3D; 3.30.200.40; -; 1.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR008594; DcpS/DCS2.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR011145; Scavenger_mRNA_decap_enz_N.
DR PANTHER; PTHR12978; PTHR12978; 1.
DR Pfam; PF05652; DcpS; 1.
DR PIRSF; PIRSF028973; Scavenger_mRNA_decap_enz; 1.
DR SUPFAM; SSF102860; SSF102860; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS00892; HIT_1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Nonsense-mediated mRNA decay;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15240832"
FT CHAIN 2..353
FT /note="Inactive diphosphatase DCS2"
FT /id="PRO_0000109799"
FT REGION 333..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 265..269
FT /note="Histidine triad motif"
FT /evidence="ECO:0000250"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 353 AA; 40941 MW; B76D89C0816019A4 CRC64;
MGSQDLASLI GRFKYVRVLD SNPHTKVISL LGSIDGKDAV LTAEKTHFIF DETVRRPSQS
GRSTPIFFHR EIDEYSFLNG ITDLKELTSN DIYYWGLSVL KQHILHNPTA KVNLIWPASQ
FHIKGYDQQD LHVVRETPDM YRNIVVPFIQ EMCTSERMKW VNNILYEGAE DDRVVYKEYS
SRNKEDGFVI LPDMKWDGIN IDSLYLVAIV YRDDIKSLRD LNPNHRDWLI RLNKKIKTII
PQHYDYNVNP DELRVFIHYQ PSYYHFHVHI VNIRHPGVGE ERGSGMTILL EDVIEALGFL
GPEGYMKKTL TYVIGENHDL WKKGFKEEVE KQLKHDGIAT SPEKGSGFNT NLG
