MGDP1_YEAST
ID MGDP1_YEAST Reviewed; 178 AA.
AC P40081; D3DM40;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Putative magnesium-dependent phosphatase YER134C;
DE EC=3.1.3.48;
GN OrderedLocusNames=YER134C;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
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 [5]
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).
CC -!- FUNCTION: Magnesium-dependent phosphatase which may act as a tyrosine
CC phosphatase. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 6190 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; U18916; AAC03232.1; -; Genomic_DNA.
DR EMBL; AY558562; AAS56888.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07794.1; -; Genomic_DNA.
DR PIR; S50637; S50637.
DR RefSeq; NP_011060.1; NM_001179024.1.
DR AlphaFoldDB; P40081; -.
DR SMR; P40081; -.
DR BioGRID; 36880; 107.
DR IntAct; P40081; 21.
DR STRING; 4932.YER134C; -.
DR iPTMnet; P40081; -.
DR MaxQB; P40081; -.
DR PaxDb; P40081; -.
DR PRIDE; P40081; -.
DR EnsemblFungi; YER134C_mRNA; YER134C; YER134C.
DR GeneID; 856873; -.
DR KEGG; sce:YER134C; -.
DR SGD; S000000936; YER134C.
DR VEuPathDB; FungiDB:YER134C; -.
DR eggNOG; KOG4549; Eukaryota.
DR GeneTree; ENSGT00940000165797; -.
DR HOGENOM; CLU_071162_0_1_1; -.
DR InParanoid; P40081; -.
DR OMA; RGVWAWR; -.
DR BioCyc; YEAST:G3O-30296-MON; -.
DR PRO; PR:P40081; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40081; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003993; F:acid phosphatase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030946; F:protein tyrosine phosphatase activity, metal-dependent; IDA:SGD.
DR CDD; cd07501; HAD_MDP-1_like; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR010033; HAD_SF_ppase_IIIC.
DR InterPro; IPR035679; MDP-1_euk.
DR InterPro; IPR010036; MDP_1_eu_arc.
DR PANTHER; PTHR17901; PTHR17901; 1.
DR Pfam; PF12689; Acid_PPase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01681; HAD-SF-IIIC; 1.
DR TIGRFAMs; TIGR01685; MDP-1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleus;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..178
FT /note="Putative magnesium-dependent phosphatase YER134C"
FT /id="PRO_0000202650"
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 13
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 13
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 178 AA; 20441 MW; F3F765AC0076CBFC CRC64;
MTGYPDVAAF DLDYTIWPCY CDTHLHGPFK PVKSSNGEVL TIICRDGYEL TIYKDIPRIL
GDLKDNGVKL MTASRTWAPE IAQEILKIFK VKYAGVVTPL ANLFDEFQWG ERSKIGHLRD
GLKDLYNTSD LKSKKICLFD DESRNKEVEK YGVKFVYVRD PENGPSWKLY QDYLSGKV
