2AAA_YEAST
ID 2AAA_YEAST Reviewed; 635 AA.
AC P31383; D6VPK2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Protein phosphatase PP2A regulatory subunit A;
DE AltName: Full=PR65;
GN Name=TPD3; OrderedLocusNames=YAL016W; ORFNames=FUN32;
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 204508 / S288c;
RX PubMed=1328868; DOI=10.1128/mcb.12.11.4946-4959.1992;
RA van Zyl W., Huang W., Sneddon A.A., Stark M., Camier S., Werner M.,
RA Marck C., Sentenac A., Broach J.R.;
RT "Inactivation of the protein phosphatase 2A regulatory subunit A results in
RT morphological and transcriptional defects in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 12:4946-4959(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8458570; DOI=10.1139/g93-005;
RA Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B.,
RA Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32
RT kb region between the LTE1 and SPO7 genes.";
RL Genome 36:32-42(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8144453; DOI=10.1128/jb.176.7.1872-1880.1994;
RA Barton A.B., Kaback D.B.;
RT "Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae:
RT analysis of the genes in the FUN38-MAK16-SPO7 region.";
RL J. Bacteriol. 176:1872-1880(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [5]
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 [6]
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 [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: Phosphatase 2A affects a variety of biological processes in
CC the cell such as transcription, cell cycle progression and cellular
CC morphogenesis, and provides an initial identification of critical
CC substrates for this phosphatase. The regulatory subunit may direct the
CC catalytic subunit to distinct, albeit overlapping, subsets of
CC substrates.
CC -!- SUBUNIT: PP2A exists in several trimeric forms, all of which consist of
CC a core composed of a catalytic subunit associated with a 65 kDa
CC regulatory subunit (PR65) (subunit A). The core complex associates with
CC a third, variable subunit (subunit B), which confers distinct
CC properties to the holoenzyme.
CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices joined
CC by a hydrophilic region, the intrarepeat loop. The repeat units may be
CC arranged laterally to form a rod-like structure.
CC -!- MISCELLANEOUS: Present with 16900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family.
CC {ECO:0000305}.
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DR EMBL; M98389; AAA35163.1; -; Genomic_DNA.
DR EMBL; L05146; AAC04941.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06972.1; -; Genomic_DNA.
DR PIR; S36718; S36718.
DR RefSeq; NP_009386.1; NM_001178161.1.
DR AlphaFoldDB; P31383; -.
DR SMR; P31383; -.
DR BioGRID; 31750; 68.
DR ComplexPortal; CPX-1856; Serine/threonine-protein phosphatase PP2A variant 1.
DR ComplexPortal; CPX-1857; Serine/threonine-protein phosphatase PP2A variant 2.
DR ComplexPortal; CPX-1858; Serine/threonine-protein phosphatase PP2A variant 4.
DR ComplexPortal; CPX-1859; Serine/threonine-protein phosphatase PP2A variant 3.
DR DIP; DIP-2010N; -.
DR IntAct; P31383; 47.
DR MINT; P31383; -.
DR STRING; 4932.YAL016W; -.
DR iPTMnet; P31383; -.
DR MaxQB; P31383; -.
DR PaxDb; P31383; -.
DR PRIDE; P31383; -.
DR EnsemblFungi; YAL016W_mRNA; YAL016W; YAL016W.
DR GeneID; 851217; -.
DR KEGG; sce:YAL016W; -.
DR SGD; S000000014; TPD3.
DR VEuPathDB; FungiDB:YAL016W; -.
DR eggNOG; KOG0211; Eukaryota.
DR GeneTree; ENSGT00950000183066; -.
DR HOGENOM; CLU_015533_2_1_1; -.
DR InParanoid; P31383; -.
DR OMA; SSLCMSW; -.
DR BioCyc; YEAST:G3O-28828-MON; -.
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P31383; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P31383; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:ComplexPortal.
DR GO; GO:0006417; P:regulation of translation; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021133; HEAT_type_2.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 9.
PE 1: Evidence at protein level;
KW Reference proteome; Repeat.
FT CHAIN 1..635
FT /note="Protein phosphatase PP2A regulatory subunit A"
FT /id="PRO_0000071414"
FT REPEAT 34..72
FT /note="HEAT 1"
FT REPEAT 73..111
FT /note="HEAT 2"
FT REPEAT 112..150
FT /note="HEAT 3"
FT REPEAT 151..189
FT /note="HEAT 4"
FT REPEAT 190..228
FT /note="HEAT 5"
FT REPEAT 229..273
FT /note="HEAT 6"
FT REPEAT 274..316
FT /note="HEAT 7"
FT REPEAT 317..356
FT /note="HEAT 8"
FT REPEAT 357..395
FT /note="HEAT 9"
FT REPEAT 396..434
FT /note="HEAT 10"
FT REPEAT 435..473
FT /note="HEAT 11"
FT REPEAT 474..512
FT /note="HEAT 12"
FT REPEAT 513..553
FT /note="HEAT 13"
FT REPEAT 554..598
FT /note="HEAT 14"
FT REPEAT 599..632
FT /note="HEAT 15"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 336
FT /note="V -> L (in Ref. 1; AAA35163)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="I -> T (in Ref. 1; AAA35163)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="Q -> E (in Ref. 1; AAA35163)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="C -> F (in Ref. 1; AAA35163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 635 AA; 70907 MW; 7ED350FB20633DC8 CRC64;
MSGARSTTAG AVPSAATTST TSTTSNSKDS DSNESLYPLA LLMDELKHDD IANRVEAMKK
LDTIALALGP ERTRNELIPF LTEVAQDDED EVFAVLAEQL GKFVPYIGGP QYATILLPVL
EILASAEETL VREKAVDSLN NVAQELSQEQ LFSDFVPLIE HLATADWFSS KVSACGLFKS
VIVRIKDDSL RKNILALYLQ LAQDDTPMVK RAVGKNLPIL IDLLTQNLGL STDEDWDYIS
NIFQKIINDN QDSVKFLAVD CLISILKFFN AKGDESHTQD LLNSAVKLIG DEAWRVRYMA
ADRFSDLASQ FSSNQAYIDE LVQPFLNLCE DNEGDVREAV AKQVSGFAKF LNDPSIILNK
ILPAVQNLSM DESETVRSAL ASKITNIVLL LNKDQVINNF LPILLNMLRD EFPDVRLNII
ASLKVVNDVI GIELLSDSLL PAITELAKDV NWRVRMAIIE YIPILAEQLG MQFFDQQLSD
LCLSWLWDTV YSIREAAVNN LKRLTEIFGS DWCRDEIISR LLKFDLQLLE NFVSRFTILS
ALTTLVPVVS LDVVTEQLLP FISHLADDGV PNIRFNVAKS YAVIVKVLIK DEAKYDALIK
NTILPSLQTL CQDEDVDVKY FAKKSLAECQ ELLKN
