PSR1_YEAST
ID PSR1_YEAST Reviewed; 427 AA.
AC Q07800; D6VXZ2;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Phosphatase PSR1;
DE EC=3.1.3.-;
DE AltName: Full=Plasma membrane sodium response protein 1;
GN Name=PSR1; OrderedLocusNames=YLL010C; ORFNames=L1341;
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:0000312|EMBL:CAA62782.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90840 / EAY235 / FY23;
RX PubMed=8810043;
RX DOI=10.1002/(sici)1097-0061(19960615)12:7<693::aid-yea956>3.0.co;2-g;
RA Miosga T., Zimmermann F.K.;
RT "Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a
RT 43.7 kb fragment of chromosome XII including an open reading frame
RT homologous to the human cystic fibrosis transmembrane conductance regulator
RT protein CFTR.";
RL Yeast 12:693-708(1996).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAA97454.1}
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 [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 FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-9 AND CYS-10,
RP PHOSPHORYLATION, AND MUTAGENESIS OF GLY-2; 9-CYS-CYS-10; ASP-263 AND
RP ASP-265.
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 [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH WHI2.
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 [6] {ECO:0000305}
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, 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 [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-154, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Has phosphatase activity in vitro. Involved in the response
CC to sodium and lithium ion stress (but not to potassium or sorbitol
CC stress) by inducing transcription of the sodium pump ENA1/PMR2. Acts
CC through a calcineurin-independent pathway and is functionally redundant
CC with PSR2. Also involved in the general stress response; acts together
CC with 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 -!- SUBUNIT: Interacts with WHI2. {ECO:0000269|PubMed:12090248}.
CC -!- INTERACTION:
CC Q07800; P12611: WHI2; NbExp=4; IntAct=EBI-31129, EBI-20530;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10777497,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 5620 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X91488; CAA62782.1; -; Genomic_DNA.
DR EMBL; Z73115; CAA97454.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09308.1; -; Genomic_DNA.
DR PIR; S64752; S64752.
DR RefSeq; NP_013091.1; NM_001181830.1.
DR AlphaFoldDB; Q07800; -.
DR SMR; Q07800; -.
DR BioGRID; 31241; 129.
DR ComplexPortal; CPX-1317; WHI2-PSR1 phosphatase complex.
DR DIP; DIP-4182N; -.
DR IntAct; Q07800; 3.
DR MINT; Q07800; -.
DR STRING; 4932.YLL010C; -.
DR iPTMnet; Q07800; -.
DR SwissPalm; Q07800; -.
DR MaxQB; Q07800; -.
DR PaxDb; Q07800; -.
DR PRIDE; Q07800; -.
DR EnsemblFungi; YLL010C_mRNA; YLL010C; YLL010C.
DR GeneID; 850650; -.
DR KEGG; sce:YLL010C; -.
DR SGD; S000003933; PSR1.
DR VEuPathDB; FungiDB:YLL010C; -.
DR eggNOG; KOG1605; Eukaryota.
DR GeneTree; ENSGT01040000240451; -.
DR HOGENOM; CLU_020262_1_2_1; -.
DR InParanoid; Q07800; -.
DR OMA; RTRGVHQ; -.
DR BioCyc; YEAST:G3O-32115-MON; -.
DR PRO; PR:Q07800; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07800; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:1903293; C:phosphatase complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:SGD.
DR GO; GO:0071472; P:cellular response to salt stress; IGI:SGD.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP: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; IMP:UniProtKB.
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; Isopeptide bond; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Protein phosphatase; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..427
FT /note="Phosphatase PSR1"
FT /id="PRO_0000212576"
FT DOMAIN 253..411
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 14..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT LIPID 9
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:10777497"
FT LIPID 10
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:10777497"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 2
FT /note="G->A: No effect on membrane association."
FT /evidence="ECO:0000269|PubMed:10777497"
FT MUTAGEN 9..10
FT /note="CC->GG: Impairs membrane association."
FT /evidence="ECO:0000269|PubMed:10777497"
FT MUTAGEN 263
FT /note="D->E: Low residual phosphatase activity. Loss of
FT stress response functions."
FT /evidence="ECO:0000269|PubMed:10777497"
FT MUTAGEN 265
FT /note="D->E: Low residual phosphatase activity. Loss of
FT stress response functions."
FT /evidence="ECO:0000269|PubMed:10777497"
SQ SEQUENCE 427 AA; 47931 MW; 402F5C395132A080 CRC64;
MGFISSILCC SSETTQSNSN SAYRQQQSSS LNKNRSVKHS NTKSRTRGVH QTNSPPSKTN
SAATFSSTER STGKSGISTN DNEKKKPSSP TAAVTATTTN NMTKVEKRIS KDDLYEEKYE
VDEDEEIDDE DNRRSRGIVQ EKGDAVKDTS RQKKQQQQQQ QQSQPQPQPQ SQSQSQSQSQ
SQQRGPTVQV SSDHLIQDMN LSRVSSSSQA SETSNDADDE DDEDEEYIDL TLLQQGQYHA
PGYNTLLPPQ DESTKGKKCL ILDLDETLVH SSFKYLRSAD FVLSVEIDDQ VHNVYVIKRP
GVEEFLERVG KLFEVVVFTA SVSRYGDPLL DILDTDKVIH HRLFREACYN YEGNYIKNLS
QIGRPLSDII ILDNSPASYI FHPQHAIPIS SWFSDTHDNE LLDIIPLLED LSVKTSLDVG
KILDVTI
