PTPA2_YEAST
ID PTPA2_YEAST Reviewed; 358 AA.
AC Q12461; D6W3L7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Serine/threonine-protein phosphatase 2A activator 2;
DE EC=5.2.1.8 {ECO:0000269|PubMed:16380387};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase PTPA-2;
DE Short=PPIase PTPA-2;
DE Short=Rotamase PTPA-2;
DE AltName: Full=Phosphotyrosyl phosphatase activator 2;
GN Name=RRD2; Synonyms=NOH1, YPA2; OrderedLocusNames=YPL152W;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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]
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 [5]
RP FUNCTION.
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 [6]
RP FUNCTION, AND INTERACTION WITH PPH21.
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 [7]
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 [8]
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 [9]
RP FUNCTION, AND INTERACTION WITH PPH21 AND PPH22.
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 PPH21 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, AND CATALYTIC ACTIVITY.
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).
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. Acts
CC also inhibitory at high concentrations. Involved in the regulation of
CC cell cycle progression, mitotic spindle formation and bud
CC morphogenesis. {ECO:0000269|PubMed:11134337,
CC ECO:0000269|PubMed:11262194, ECO:0000269|PubMed:12952889,
CC ECO:0000269|PubMed:15447631, 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 catalytic subunits PPH21
CC and PPH22. Forms a ternary complex with PPH21-TAP42.
CC {ECO:0000269|PubMed:12952889, ECO:0000269|PubMed:15447631,
CC ECO:0000269|PubMed:15689491}.
CC -!- INTERACTION:
CC Q12461; P23594: PPH21; NbExp=7; IntAct=EBI-32784, EBI-12745;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2430 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X96770; CAA65569.1; -; Genomic_DNA.
DR EMBL; Z73508; CAA97857.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11283.1; -; Genomic_DNA.
DR PIR; S65163; S65163.
DR RefSeq; NP_015173.1; NM_001183966.1.
DR PDB; 2IXN; X-ray; 2.80 A; A/B=1-304.
DR PDBsum; 2IXN; -.
DR AlphaFoldDB; Q12461; -.
DR SMR; Q12461; -.
DR BioGRID; 36031; 225.
DR ComplexPortal; CPX-1380; TAP42-RRD2-PPH21 phosphatase complex.
DR ComplexPortal; CPX-1382; TAP42-RRD2-PPH22 phosphatase complex.
DR DIP; DIP-2558N; -.
DR IntAct; Q12461; 4.
DR MINT; Q12461; -.
DR STRING; 4932.YPL152W; -.
DR MaxQB; Q12461; -.
DR PaxDb; Q12461; -.
DR PRIDE; Q12461; -.
DR EnsemblFungi; YPL152W_mRNA; YPL152W; YPL152W.
DR GeneID; 855951; -.
DR KEGG; sce:YPL152W; -.
DR SGD; S000006073; RRD2.
DR VEuPathDB; FungiDB:YPL152W; -.
DR eggNOG; KOG2867; Eukaryota.
DR GeneTree; ENSGT00390000011500; -.
DR HOGENOM; CLU_030733_0_0_1; -.
DR InParanoid; Q12461; -.
DR OMA; YMFLGCI; -.
DR BioCyc; YEAST:G3O-34049-MON; -.
DR EvolutionaryTrace; Q12461; -.
DR PRO; PR:Q12461; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12461; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:SGD.
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:0007052; P:mitotic spindle organization; 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; Reference proteome; Rotamase.
FT CHAIN 1..358
FT /note="Serine/threonine-protein phosphatase 2A activator 2"
FT /id="PRO_0000226120"
FT TURN 10..13
FT /evidence="ECO:0007829|PDB:2IXN"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:2IXN"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:2IXN"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:2IXN"
FT HELIX 50..66
FT /evidence="ECO:0007829|PDB:2IXN"
FT HELIX 84..103
FT /evidence="ECO:0007829|PDB:2IXN"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:2IXN"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:2IXN"
FT HELIX 133..148
FT /evidence="ECO:0007829|PDB:2IXN"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:2IXN"
FT HELIX 165..180
FT /evidence="ECO:0007829|PDB:2IXN"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:2IXN"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:2IXN"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:2IXN"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:2IXN"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:2IXN"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:2IXN"
FT HELIX 233..244
FT /evidence="ECO:0007829|PDB:2IXN"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:2IXN"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:2IXN"
FT HELIX 255..260
FT /evidence="ECO:0007829|PDB:2IXN"
FT HELIX 266..280
FT /evidence="ECO:0007829|PDB:2IXN"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:2IXN"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:2IXN"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:2IXN"
SQ SEQUENCE 358 AA; 41452 MW; E0BE8A7EDD54E306 CRC64;
MLPEKRLLTP DDMKLWEESP TRAHFTKFII DLAESVKGHE NSQYKEPISE SINSMMNLLS
QIKDITQKHP VIKDADSSRF GKVEFRDFYD EVSRNSRKIL RSEFPSLTDE QLEQLSIYLD
ESWGNKRRID YGSGHELNFM CLLYGLYSYG IFNLSNDSTN LVLKVFIEYL KIMRILETKY
WLEPAGSHGV WGLDDYHFLP FLFGAFQLTT HKHLKPISIH NNELVEMFAH RYLYFGCIAF
INKVKSSASL RWHSPMLDDI SGVKTWSKVA EGMIKMYKAE VLSKLPIMQH FYFSEFLPCP
DGVSPPRGHI HDGTDKDDEC NFEGHVHTTW GDCCGIKLPS AIAATEMNKK HHKPIPFD
