PTPA1_YEAST
ID PTPA1_YEAST Reviewed; 393 AA.
AC P40454; D6VVD4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Serine/threonine-protein phosphatase 2A activator 1 {ECO:0000303|PubMed:11262194};
DE EC=5.2.1.8 {ECO:0000269|PubMed:16380387};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase PTPA-1 {ECO:0000303|PubMed:16380387};
DE Short=PPIase PTPA-1 {ECO:0000303|PubMed:16380387};
DE Short=Rotamase PTPA-1 {ECO:0000303|PubMed:16380387};
DE AltName: Full=Phosphotyrosyl phosphatase activator 1 {ECO:0000303|PubMed:11262194};
GN Name=RRD1; Synonyms=NCS1 {ECO:0000303|PubMed:11134337}, YPA1;
GN OrderedLocusNames=YIL153W;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 FUNCTION.
RX PubMed=11262194; DOI=10.1006/excr.2000.5144;
RA Van Hoof C., Janssens V., De Baere I., Stark M.J.R., de Winde J.H.,
RA Winderickx J., Thevelein J.M., Merlevede W., Goris J.;
RT "The Saccharomyces cerevisiae phosphotyrosyl phosphatase activator proteins
RT are required for a subset of the functions disrupted by protein phosphatase
RT 2A mutations.";
RL Exp. Cell Res. 264:372-387(2001).
RN [4]
RP FUNCTION, AND INTERACTION WITH SIT4.
RX PubMed=11134337; DOI=10.1128/mcb.21.2.488-500.2001;
RA Mitchell D.A., Sprague G.F. Jr.;
RT "The phosphotyrosyl phosphatase activator, Ncs1p (Rrd1p), functions with
RT Cla4p to regulate the G(2)/M transition in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 21:488-500(2001).
RN [5]
RP FUNCTION.
RX PubMed=12952889; DOI=10.1101/gad.259903;
RA Fellner T., Lackner D.H., Hombauer H., Piribauer P., Mudrak I.,
RA Zaragoza K., Juno C., Ogris E.;
RT "A novel and essential mechanism determining specificity and activity of
RT protein phosphatase 2A (PP2A) in vivo.";
RL Genes Dev. 17:2138-2150(2003).
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, SUBCELLULAR LOCATION, AND INTERACTION WITH SIT4.
RX PubMed=15150670; DOI=10.1007/s00294-004-0513-9;
RA Douville J., David J., Fortier P.K., Ramotar D.;
RT "The yeast phosphotyrosyl phosphatase activator protein, yPtpa1/Rrd1,
RT interacts with Sit4 phosphatase to mediate resistance to 4-nitroquinoline-
RT 1-oxide and UVA.";
RL Curr. Genet. 46:72-81(2004).
RN [9]
RP INTERACTION WITH PPG1; PPH3 AND SIT4.
RX PubMed=15447631; DOI=10.1042/bj20040887;
RA Van Hoof C., Martens E., Longin S., Jordens J., Stevens I., Janssens V.,
RA Goris J.;
RT "Specific interactions of PP2A and PP2A-like phosphatases with the yeast
RT PTPA homologues, Ypa1 and Ypa2.";
RL Biochem. J. 386:93-102(2005).
RN [10]
RP FUNCTION, AND INTERACTION WITH SIT4 AND TAP42.
RX PubMed=15689491; DOI=10.1091/mbc.e04-09-0797;
RA Zheng Y., Jiang Y.;
RT "The yeast phosphotyrosyl phosphatase activator is part of the Tap42-
RT phosphatase complexes.";
RL Mol. Biol. Cell 16:2119-2127(2005).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-205.
RX PubMed=16380387; DOI=10.1074/jbc.m507760200;
RA Jordens J., Janssens V., Longin S., Stevens I., Martens E., Bultynck G.,
RA Engelborghs Y., Lescrinier E., Waelkens E., Goris J., Van Hoof C.;
RT "The protein phosphatase 2A phosphatase activator is a novel peptidyl-
RT prolyl cis/trans-isomerase.";
RL J. Biol. Chem. 281:6349-6357(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND IDENTIFICATION BY
RP 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 [13]
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 [14]
RP DISRUPTION PHENOTYPE.
RX PubMed=32801125; DOI=10.1242/jcs.245555;
RA Uemura S., Mochizuki T., Amemiya K., Kurosaka G., Yazawa M., Nakamoto K.,
RA Ishikawa Y., Izawa S., Abe F.;
RT "Amino acid homeostatic control by TORC1 in Saccharomyces cerevisiae under
RT high hydrostatic pressure.";
RL J. Cell Sci. 133:jcs245555-jcs245555(2020).
RN [15] {ECO:0007744|PDB:2IXO, ECO:0007744|PDB:2IXP}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-319.
RX PubMed=16885030; DOI=10.1016/j.molcel.2006.07.008;
RA Leulliot N., Vicentini G., Jordens J., Quevillon-Cheruel S., Schiltz M.,
RA Barford D., van Tilbeurgh H., Goris J.;
RT "Crystal structure of the PP2A phosphatase activator: implications for its
RT PP2A-specific PPIase activity.";
RL Mol. Cell 23:413-424(2006).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Acts as a regulatory subunit for TAP42-associated PP2A-
CC like phosphatases modulating their activity or substrate specificity,
CC probably by inducing a conformational change in the catalytic subunit,
CC a direct target of the PPIase. Can reactivate inactive phosphatase
CC PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP
CC and Mg(2+) by dissociating the inactive form from the complex. Involved
CC in the regulation of cell cycle progression, mitotic spindle formation,
CC bud morphogenesis and DNA repair. {ECO:0000269|PubMed:11134337,
CC ECO:0000269|PubMed:11262194, ECO:0000269|PubMed:12952889,
CC ECO:0000269|PubMed:15150670, ECO:0000269|PubMed:15689491,
CC ECO:0000269|PubMed:16380387}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000269|PubMed:16380387};
CC -!- SUBUNIT: Interacts with the phosphatase PP2A-like catalytic subunits
CC PPG1, PPH3 and SIT4. Forms a ternary complex with SIT4-TAP42.
CC {ECO:0000269|PubMed:11134337, ECO:0000269|PubMed:15150670,
CC ECO:0000269|PubMed:15447631, ECO:0000269|PubMed:15689491}.
CC -!- INTERACTION:
CC P40454; P40164: PSY2; NbExp=3; IntAct=EBI-25278, EBI-29107;
CC P40454; P20604: SIT4; NbExp=4; IntAct=EBI-25278, EBI-13707;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- DISRUPTION PHENOTYPE: Sensitive to high hydrostatic pressure
CC (mechanical stress); simultaneous disruption of SCH9 exacerbates the
CC effect. {ECO:0000269|PubMed:32801125}.
CC -!- MISCELLANEOUS: Present with 4590 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PTPA-type PPIase family. {ECO:0000305}.
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DR EMBL; Z38059; CAA86125.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08400.1; -; Genomic_DNA.
DR PIR; S48381; S48381.
DR RefSeq; NP_012113.1; NM_001179501.1.
DR PDB; 2IXO; X-ray; 2.60 A; A/B=1-317.
DR PDB; 2IXP; X-ray; 2.80 A; A/B/C/D=1-317.
DR PDBsum; 2IXO; -.
DR PDBsum; 2IXP; -.
DR AlphaFoldDB; P40454; -.
DR SMR; P40454; -.
DR BioGRID; 34839; 302.
DR ComplexPortal; CPX-1863; TAP42-RRD1-SIT4 phosphatase complex.
DR DIP; DIP-5663N; -.
DR IntAct; P40454; 20.
DR MINT; P40454; -.
DR STRING; 4932.YIL153W; -.
DR iPTMnet; P40454; -.
DR MaxQB; P40454; -.
DR PaxDb; P40454; -.
DR PRIDE; P40454; -.
DR EnsemblFungi; YIL153W_mRNA; YIL153W; YIL153W.
DR GeneID; 854653; -.
DR KEGG; sce:YIL153W; -.
DR SGD; S000001415; RRD1.
DR VEuPathDB; FungiDB:YIL153W; -.
DR eggNOG; KOG2867; Eukaryota.
DR GeneTree; ENSGT00390000011500; -.
DR HOGENOM; CLU_030733_2_1_1; -.
DR InParanoid; P40454; -.
DR OMA; SWDRDPN; -.
DR BioCyc; YEAST:G3O-31402-MON; -.
DR ChiTaRS; RPP2B; yeast.
DR EvolutionaryTrace; P40454; -.
DR PRO; PR:P40454; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40454; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IPI:ComplexPortal.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:SGD.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IMP:SGD.
DR GO; GO:0008160; F:protein tyrosine phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IPI:SGD.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:SGD.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IMP:SGD.
DR GO; GO:0006970; P:response to osmotic stress; IMP:SGD.
DR GO; GO:0031929; P:TOR signaling; IC:ComplexPortal.
DR CDD; cd04087; PTPA; 1.
DR Gene3D; 1.20.120.1150; -; 1.
DR InterPro; IPR004327; Phstyr_phstse_ac.
DR InterPro; IPR043170; PTPA_C_lid.
DR InterPro; IPR037218; PTPA_sf.
DR PANTHER; PTHR10012; PTHR10012; 1.
DR Pfam; PF03095; PTPA; 1.
DR PIRSF; PIRSF016325; Phstyr_phstse_ac; 1.
DR SUPFAM; SSF140984; SSF140984; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isomerase; Nucleus; Phosphoprotein;
KW Reference proteome; Rotamase.
FT CHAIN 1..393
FT /note="Serine/threonine-protein phosphatase 2A activator 1"
FT /id="PRO_0000202955"
FT REGION 328..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 205
FT /note="D->G: Abolishes PPIase activity and fails to
FT activate PP2A phosphatases."
FT /evidence="ECO:0000269|PubMed:16380387"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 33..49
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 97..116
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 119..124
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:2IXO"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 146..161
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 170..190
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2IXP"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 210..218
FT /evidence="ECO:0007829|PDB:2IXO"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:2IXO"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 236..242
FT /evidence="ECO:0007829|PDB:2IXO"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 247..258
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 268..274
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 280..294
FT /evidence="ECO:0007829|PDB:2IXO"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:2IXO"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:2IXO"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:2IXO"
SQ SEQUENCE 393 AA; 45082 MW; 22F52B3359739B6E CRC64;
MSLDRVDWPH ATFSTPVKRI FDTQTTLDFQ SSLAIHRIKY HLHKYTTLIS HCSDPDPHAT
ASSIAMVNGL MGVLDKLAHL IDETPPLPGP RRYGNLACRE WHHKLDERLP QWLQEMLPSE
YHEVVPELQY YLGNSFGSST RLDYGTGHEL SFMATVAALD MLGMFPHMRG ADVFLLFNKY
YTIMRRLILT YTLEPAGSHG VWGLDDHFHL VYILGSSQWQ LLDAQAPLQP REILDKSLVR
EYKDTNFYCQ GINFINEVKM GPFEEHSPIL YDIAVTVPRW SKVCKGLLKM YSVEVLKKFP
VVQHFWFGTG FFPWVNIQNG TDLPVFEEKE EESIEQANAG SPGREQTSTR FPTSTSMPPP
GVPPSGNNIN YLLSHQNQSH RNQTSFSRDR LRR
