TAP42_YEAST
ID TAP42_YEAST Reviewed; 366 AA.
AC Q04372; D6VZK2; Q05039;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Type 2A phosphatase-associated protein 42;
GN Name=TAP42; OrderedLocusNames=YMR028W; ORFNames=YM9711.18, YM9973.01C;
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=8756348; DOI=10.1101/gad.10.15.1904;
RA Di Como C.J., Arndt K.T.;
RT "Nutrients, via the Tor proteins, stimulate the association of Tap42 with
RT type 2A phosphatases.";
RL Genes Dev. 10:1904-1916(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
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 [5]
RP INTERACTION WITH PPH21 AND PPH22, PHOSPHORYLATION, AND DEPHOSPHORYLATION.
RX PubMed=10329624; DOI=10.1093/emboj/18.10.2782;
RA Jiang Y., Broach J.R.;
RT "Tor proteins and protein phosphatase 2A reciprocally regulate Tap42 in
RT controlling cell growth in yeast.";
RL EMBO J. 18:2782-2792(1999).
RN [6]
RP INTERACTION WITH TIP41.
RX PubMed=11741537; DOI=10.1016/s1097-2765(01)00386-0;
RA Jacinto E., Guo B., Arndt K.T., Schmelzle T., Hall M.N.;
RT "TIP41 interacts with TAP42 and negatively regulates the TOR signaling
RT pathway.";
RL Mol. Cell 8:1017-1026(2001).
RN [7]
RP FUNCTION, AND INTERACTION WITH PPG1; PPH21; PPH22; PPH3 AND SIT4.
RX PubMed=14551259; DOI=10.1091/mbc.e03-02-0072;
RA Wang H., Wang X., Jiang Y.;
RT "Interaction with Tap42 is required for the essential function of Sit4 and
RT type 2A phosphatases.";
RL Mol. Biol. Cell 14:4342-4351(2003).
RN [8]
RP FUNCTION, AND INTERACTION WITH SIT4.
RX PubMed=12820961; DOI=10.1016/s1097-2765(03)00228-4;
RA Duevel K., Santhanam A., Garrett S., Schneper L., Broach J.R.;
RT "Multiple roles of Tap42 in mediating rapamycin-induced transcriptional
RT changes in yeast.";
RL Mol. Cell 11:1467-1478(2003).
RN [9]
RP FUNCTION, AND INTERACTION WITH PPH21 AND PPH22.
RX PubMed=12697813; DOI=10.1128/mcb.23.9.3116-3125.2003;
RA Wang H., Jiang Y.;
RT "The Tap42-protein phosphatase type 2A catalytic subunit complex is
RT required for cell cycle-dependent distribution of actin in yeast.";
RL Mol. Cell. Biol. 23:3116-3125(2003).
RN [10]
RP FUNCTION.
RX PubMed=15470255; DOI=10.1128/ec.3.5.1261-1271.2004;
RA Santhanam A., Hartley A., Duevel K., Broach J.R., Garrett S.;
RT "PP2A phosphatase activity is required for stress and Tor kinase regulation
RT of yeast stress response factor Msn2p.";
RL Eukaryot. Cell 3:1261-1271(2004).
CC -!- FUNCTION: Involved in negative regulation of the TOR signaling pathway
CC in response to type of available nitrogen source. Inhibitor of PP2A
CC phosphatase SIT4, which results in inhibition of nuclear export of
CC MSN2, due to lack of dephosphorylation by SIT4. Also required for
CC rapamycin induced activation of expression of many nitrogen
CC discrimination pathway (NDP) genes. In complex with PPH21, required for
CC organization of the actin cytoskeletom during the cell cycle via a Rho
CC GTPase-dependent mechanism. {ECO:0000269|PubMed:12697813,
CC ECO:0000269|PubMed:12820961, ECO:0000269|PubMed:14551259,
CC ECO:0000269|PubMed:15470255}.
CC -!- SUBUNIT: Associates with the PP2a (PPH21 and PPH22) and SIT4 protein
CC phosphatase catalytic subunits. Interacts with PPG1, PPH3 and TIP41.
CC {ECO:0000269|PubMed:10329624, ECO:0000269|PubMed:11741537,
CC ECO:0000269|PubMed:12697813, ECO:0000269|PubMed:12820961,
CC ECO:0000269|PubMed:14551259}.
CC -!- INTERACTION:
CC Q04372; P23594: PPH21; NbExp=10; IntAct=EBI-18926, EBI-12745;
CC Q04372; P23595: PPH22; NbExp=5; IntAct=EBI-18926, EBI-12752;
CC Q04372; P20604: SIT4; NbExp=7; IntAct=EBI-18926, EBI-13707;
CC Q04372; P32600: TOR2; NbExp=4; IntAct=EBI-18926, EBI-19385;
CC -!- PTM: Phosphorylated by TOR kinases. Dephosphorylated by CDC55, TPD3 and
CC SIT4. {ECO:0000269|PubMed:10329624}.
CC -!- SIMILARITY: Belongs to the IGBP1/TAP42 family. {ECO:0000305}.
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DR EMBL; U43890; AAC49396.1; -; Genomic_DNA.
DR EMBL; Z49211; CAA89131.1; -; Genomic_DNA.
DR EMBL; Z49213; CAA89143.1; -; Genomic_DNA.
DR EMBL; AY558399; AAS56725.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09926.1; -; Genomic_DNA.
DR PIR; S54030; S54030.
DR RefSeq; NP_013741.1; NM_001182524.1.
DR PDB; 2V0P; X-ray; 1.80 A; A/B=1-234.
DR PDBsum; 2V0P; -.
DR AlphaFoldDB; Q04372; -.
DR SMR; Q04372; -.
DR BioGRID; 35200; 391.
DR ComplexPortal; CPX-1380; TAP42-RRD2-PPH21 phosphatase complex.
DR ComplexPortal; CPX-1382; TAP42-RRD2-PPH22 phosphatase complex.
DR ComplexPortal; CPX-1863; TAP42-RRD1-SIT4 phosphatase complex.
DR DIP; DIP-6380N; -.
DR IntAct; Q04372; 11.
DR MINT; Q04372; -.
DR STRING; 4932.YMR028W; -.
DR iPTMnet; Q04372; -.
DR MaxQB; Q04372; -.
DR PaxDb; Q04372; -.
DR PRIDE; Q04372; -.
DR EnsemblFungi; YMR028W_mRNA; YMR028W; YMR028W.
DR GeneID; 855043; -.
DR KEGG; sce:YMR028W; -.
DR SGD; S000004630; TAP42.
DR VEuPathDB; FungiDB:YMR028W; -.
DR eggNOG; KOG2830; Eukaryota.
DR GeneTree; ENSGT00390000002414; -.
DR HOGENOM; CLU_041824_2_2_1; -.
DR InParanoid; Q04372; -.
DR OMA; RAWDEFT; -.
DR BioCyc; YEAST:G3O-32733-MON; -.
DR EvolutionaryTrace; Q04372; -.
DR PRO; PR:Q04372; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04372; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IPI:ComplexPortal.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IBA:GO_Central.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IMP:SGD.
DR GO; GO:0035303; P:regulation of dephosphorylation; IBA:GO_Central.
DR GO; GO:0031929; P:TOR signaling; IC:ComplexPortal.
DR Gene3D; 1.25.40.540; -; 1.
DR InterPro; IPR038511; TAP42/TAP46-like_sf.
DR InterPro; IPR007304; TAP46-like.
DR PANTHER; PTHR10933; PTHR10933; 1.
DR Pfam; PF04177; TAP42; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1..366
FT /note="Type 2A phosphatase-associated protein 42"
FT /id="PRO_0000218623"
FT REGION 318..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:2V0P"
FT HELIX 29..50
FT /evidence="ECO:0007829|PDB:2V0P"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2V0P"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:2V0P"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:2V0P"
FT HELIX 93..120
FT /evidence="ECO:0007829|PDB:2V0P"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:2V0P"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:2V0P"
FT HELIX 156..186
FT /evidence="ECO:0007829|PDB:2V0P"
FT HELIX 199..231
FT /evidence="ECO:0007829|PDB:2V0P"
SQ SEQUENCE 366 AA; 42568 MW; 16F1E236BEC696DD CRC64;
MASVTEQFND IISLYSTKLE HTSLRQDSPE YQGLLLSTIK KLLNLKTAIF DRLALFSTNE
TIDDVSTASI KFLAVDYYLG LLISRRQSND SDVAQRQSMK LIYLKKSVES FINFLTLLQD
YKLLDPLVGE KLGNFKDRYN PQLSELYAQP KNNKDLSGAQ LKRKEKIELF QRNKEISTKL
HCLELELKNN DEDHDHDELL RELYLMRLHH FSLDTINNIE QNLFECEMLS NFLKNSVHEV
KSSGTQIRKE SNDDDSTGFT DKLENINKPL IDKKGQVLRN FTLVDKRQQL QQKVRGYGQY
GPTMSVEEFL DKEFEEGRVL QGGEEPEQAP DEENMDWQDR ETYKAREWDE FKESHAKGSG
NTMNRG
