PSR2_YEAST
ID PSR2_YEAST Reviewed; 397 AA.
AC Q07949; D6VY21; Q06898; Q6B1J9;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Probable phosphatase PSR2;
DE EC=3.1.3.-;
DE AltName: Full=Plasma membrane sodium response protein 2;
GN Name=PSR2; OrderedLocusNames=YLR019W;
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:CAA97541.1}
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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] {ECO:0000312|EMBL:AAT93100.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-332.
RC STRAIN=ATCC 204508 / S288c;
RA Saville S.P., Atkinson S., Jamieson L., Pocklington M.J., Orr E.;
RT "A 7.8kb fragment from chromosome XII of Saccharomyces cerevisiae does not
RT harbour PKC2.";
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, AND PALMITOYLATION AT CYS-9 AND CYS-10.
RX PubMed=10777497; DOI=10.1074/jbc.m001314200;
RA Siniossoglou S., Hurt E.C., Pelham H.R.B.;
RT "Psr1p/Psr2p, two plasma membrane phosphatases with an essential DXDX(T/V)
RT motif required for sodium stress response in yeast.";
RL J. Biol. Chem. 275:19352-19360(2000).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=12090248; DOI=10.1046/j.1365-2443.2002.00538.x;
RA Kaida D., Yashiroda H., Toh-e A., Kikuchi Y.;
RT "Yeast Whi2 and Psr1-phosphatase form a complex and regulate STRE-mediated
RT gene expression.";
RL Genes Cells 7:543-552(2002).
RN [7]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Probable phosphatase. Involved in the response to sodium and
CC lithium ion stress (but not to potassium or sorbitol stress) by
CC inducing transcription of the sodium pump ENA1/PMR2. Acts through a
CC calcineurin-independent pathway and is functionally redundant with
CC PSR1. Also involved in the general stress response; acts together with
CC WHI2 to activate stress response element (STRE)-mediated gene
CC expression, possibly through dephosphorylation of MSN2.
CC {ECO:0000269|PubMed:10777497, ECO:0000269|PubMed:12090248,
CC ECO:0000303|PubMed:12090248}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA62154.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z73191; CAA97541.1; -; Genomic_DNA.
DR EMBL; AY693081; AAT93100.1; -; Genomic_DNA.
DR EMBL; X90564; CAA62154.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006945; DAA09337.1; -; Genomic_DNA.
DR PIR; S64841; S64841.
DR RefSeq; NP_013119.1; NM_001181906.1.
DR AlphaFoldDB; Q07949; -.
DR SMR; Q07949; -.
DR BioGRID; 31293; 90.
DR ComplexPortal; CPX-1318; WHI2-PSR2 phosphatase complex.
DR DIP; DIP-4181N; -.
DR IntAct; Q07949; 16.
DR MINT; Q07949; -.
DR STRING; 4932.YLR019W; -.
DR iPTMnet; Q07949; -.
DR SwissPalm; Q07949; -.
DR MaxQB; Q07949; -.
DR PaxDb; Q07949; -.
DR PRIDE; Q07949; -.
DR EnsemblFungi; YLR019W_mRNA; YLR019W; YLR019W.
DR GeneID; 850706; -.
DR KEGG; sce:YLR019W; -.
DR SGD; S000004009; PSR2.
DR VEuPathDB; FungiDB:YLR019W; -.
DR eggNOG; KOG1605; Eukaryota.
DR GeneTree; ENSGT01040000240451; -.
DR HOGENOM; CLU_020262_1_2_1; -.
DR InParanoid; Q07949; -.
DR BioCyc; YEAST:G3O-32180-MON; -.
DR PRO; PR:Q07949; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07949; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISA:SGD.
DR GO; GO:0071472; P:cellular response to salt stress; IGI:SGD.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IGI:SGD.
DR GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; IGI:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IGI:SGD.
DR GO; GO:0009651; P:response to salt stress; IGI:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02251; HIF-SF_euk; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Lipoprotein; Membrane; Palmitate;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..397
FT /note="Probable phosphatase PSR2"
FT /id="PRO_0000212577"
FT DOMAIN 223..381
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 13..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 9
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000303|PubMed:10777497"
FT LIPID 10
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000303|PubMed:10777497"
FT CONFLICT 59
FT /note="Y -> C (in Ref. 3; AAT93100)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 44772 MW; BEA0BB453C496B06 CRC64;
MGFIANILCC SSDTSKTHRQ RQPPETNHNR NRNRKHSSNK AQTQGRKQKA TPNGDKMQYS
TPEILLSSSD SGSNAGSKTM QENGNSGNGK LAPLSRDHSN NSYDEEKEYE DYNEGDVEMT
EVNNAGEEEE EDDEAKEKQD HVVHEYNVDA DRNSSINDEA PPQQGLYQVG QEDMNPQYVA
SSPDNDLNLI PTTEEDFSDL THLQPDQYHA PGYDTLLPPK LQEFQQKKCL ILDLDETLVH
SSFKYMHSAD FVLPVEIDDQ VHNVYVIKRP GVDEFLNRVS QLYEVVVFTA SVSRYANPLL
DTLDPNGTIH HRLFREACYN YEGNYIKNLS QIGRPLSETI ILDNSPASYI FHPQHAVPIS
SWFSDTHDNE LLDIIPLLED LSSGNVLDVG SVLDVTI
