DCR2_YEAST
ID DCR2_YEAST Reviewed; 578 AA.
AC Q05924; D6VYZ8;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Phosphatase DCR2;
DE EC=3.1.-.-;
DE AltName: Full=Dosage-dependent cell cycle regulator 2;
GN Name=DCR2; OrderedLocusNames=YLR361C;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
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 [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-338.
RX PubMed=15590836; DOI=10.1128/ec.3.6.1627-1638.2004;
RA Pathak R., Bogomolnaya L.M., Guo J., Polymenis M.;
RT "Gid8p (Dcr1p) and Dcr2p function in a common pathway to promote START
RT completion in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 3:1627-1638(2004).
CC -!- FUNCTION: Required for cell cycle progression. Has a role in the
CC completion of START. {ECO:0000269|PubMed:15590836}.
CC -!- INTERACTION:
CC Q05924; P32361: IRE1; NbExp=2; IntAct=EBI-3669144, EBI-9364;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15590836}.
CC -!- MISCELLANEOUS: Present with 1940 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U19103; AAB67574.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09664.1; -; Genomic_DNA.
DR PIR; S51379; S51379.
DR RefSeq; NP_013465.1; NM_001182250.1.
DR AlphaFoldDB; Q05924; -.
DR BioGRID; 31622; 148.
DR IntAct; Q05924; 1.
DR MINT; Q05924; -.
DR STRING; 4932.YLR361C; -.
DR MaxQB; Q05924; -.
DR PaxDb; Q05924; -.
DR PRIDE; Q05924; -.
DR EnsemblFungi; YLR361C_mRNA; YLR361C; YLR361C.
DR GeneID; 851075; -.
DR KEGG; sce:YLR361C; -.
DR SGD; S000004353; DCR2.
DR VEuPathDB; FungiDB:YLR361C; -.
DR eggNOG; KOG1432; Eukaryota.
DR GeneTree; ENSGT00940000176373; -.
DR HOGENOM; CLU_019692_4_2_1; -.
DR InParanoid; Q05924; -.
DR OMA; CEADPKT; -.
DR BioCyc; YEAST:G3O-32432-MON; -.
DR PRO; PR:Q05924; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q05924; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IMP:SGD.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1900102; P:negative regulation of endoplasmic reticulum unfolded protein response; IMP:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:SGD.
DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IMP:SGD.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cytoplasm; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..578
FT /note="Phosphatase DCR2"
FT /id="PRO_0000079819"
FT BINDING 116..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 338
FT /note="H->A: 20% phosphatase activity."
FT /evidence="ECO:0000269|PubMed:15590836"
SQ SEQUENCE 578 AA; 66463 MW; 8B9AECAEACF2564C CRC64;
MIRLPRLYQR YLLYLVVFVV IALFYFLQAP RVEEHIGFDL ALPISHVDNL WFQNKGLEGF
SNDDKLVVNI GYDECFHIGR FYEGCFNRHE LKSTLTDGHQ YLQRKRIHKD LRGSFGRRWF
GKSEYLYYDV LYPALVDYFG SNLEKLNVEA VTGISKYPKD KSLPFMDVSI TFEPISIELL
QKRSYISDIN ILFGVDCIQP IANWTLQKEF PLVKYRYSEP AYLTYKFVGT RPVDTGAQRL
QETDEGKFKI VQLADLHLGV GESECIDEYP KHEACKADPK TETFVQQVLD IEKPQLVVFT
GDQIMGDRSI QDSETVLLKA VAPVIARKIP WAMVWGNHDD EGSLTRWQLS EIASVLPYSL
FKFSPHDTHD NTFGVGNYIY QIFSNNDTEV PVGTLYFLDS HKYSTVGKIY PGYDWIKESQ
WKYIEDYHDV NLKFKTGLSM AFFHIPLPEY LNIESKTHPG EKNPLIGMYK EGVTAPKYNS
EGITTLDRLS VDVVSCGHDH CNDYCLRDDS TPNKIWLCYG GGGGEGGYAG YGGTERRIRI
YEINVNENNI HTWKRLNGSP KEIFDFQSML DGNSPESV
