PP11_YEAST
ID PP11_YEAST Reviewed; 311 AA.
AC P20604; D6VRU8;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Serine/threonine-protein phosphatase PP1-1;
DE EC=3.1.3.16;
GN Name=SIT4; Synonyms=PPH1; OrderedLocusNames=YDL047W; ORFNames=D2693;
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].
RX PubMed=2537149; DOI=10.1016/0092-8674(89)90576-x;
RA Arndt K.T., Styles C.A., Fink G.R.;
RT "A suppressor of a HIS4 transcriptional defect encodes a protein with
RT homology to the catalytic subunit of protein phosphatases.";
RL Cell 56:527-537(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 CHARACTERIZATION.
RX PubMed=1848673; DOI=10.1128/mcb.11.4.2133-2148.1991;
RA Sutton A., Immanuel D., Arndt K.T.;
RT "The SIT4 protein phosphatase functions in late G1 for progression into S
RT phase.";
RL Mol. Cell. Biol. 11:2133-2148(1991).
RN [5]
RP INTERACTION WITH TAP42, AND MUTAGENESIS OF LEU-35; 37-GLU-GLU-38; GLU-38
RP AND ASN-40.
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 [6]
RP INTERACTION WITH TAP42.
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 [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 INTERACTION WITH PPE1 AND RRD1.
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 [9]
RP INTERACTION WITH RRD1 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).
CC -!- FUNCTION: Involved in the dephosphorylation of the large subunit of RNA
CC polymerase II. Is required in late G1 for normal G1 cyclin expression,
CC bud initiation and expression of certain genes that are periodically
CC expressed during late G1. Associates with the SAP proteins in a cell
CC cycle-dependent manner.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Inactivated in a complex with phosphatase methylesterase PPE1
CC (PP2Ai). Interacts with phosphatase 2A activator RRD1, which can
CC reactivate PP2Ai by dissociating the catalytic subunit from the
CC complex. Forms a ternary complex with RRD1-TAP42.
CC {ECO:0000269|PubMed:12820961, ECO:0000269|PubMed:14551259,
CC ECO:0000269|PubMed:15447631, ECO:0000269|PubMed:15689491}.
CC -!- INTERACTION:
CC P20604; P40454: RRD1; NbExp=4; IntAct=EBI-13707, EBI-25278;
CC P20604; P43612: SAP155; NbExp=9; IntAct=EBI-13707, EBI-16370;
CC P20604; P40856: SAP185; NbExp=9; IntAct=EBI-13707, EBI-16384;
CC P20604; P36123: SAP190; NbExp=4; IntAct=EBI-13707, EBI-16392;
CC P20604; Q04372: TAP42; NbExp=7; IntAct=EBI-13707, EBI-18926;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Functions in the late cell cycle G1 phase for
CC progression into the S phase, possibly associated in two separate
CC complexes with the phosphorylated forms of p155 and p190, two high MW
CC proteins.
CC -!- MISCELLANEOUS: Present with 3970 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-6 (PP-V)
CC subfamily. {ECO:0000305}.
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DR EMBL; M24395; AAA56864.1; -; Genomic_DNA.
DR EMBL; Z71781; CAA96442.1; -; Genomic_DNA.
DR EMBL; Z74095; CAA98609.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11808.1; -; Genomic_DNA.
DR PIR; A31874; PABY1.
DR RefSeq; NP_010236.1; NM_001180106.1.
DR AlphaFoldDB; P20604; -.
DR SMR; P20604; -.
DR BioGRID; 32011; 193.
DR ComplexPortal; CPX-1863; TAP42-RRD1-SIT4 phosphatase complex.
DR ComplexPortal; CPX-1864; SIT4-SAP155 phosphatase complex.
DR ComplexPortal; CPX-1865; SIT4-SAP185 phosphatase complex.
DR ComplexPortal; CPX-1866; SIT4-SAP190 phosphatase complex.
DR DIP; DIP-5850N; -.
DR IntAct; P20604; 99.
DR MINT; P20604; -.
DR STRING; 4932.YDL047W; -.
DR iPTMnet; P20604; -.
DR MaxQB; P20604; -.
DR PaxDb; P20604; -.
DR PRIDE; P20604; -.
DR EnsemblFungi; YDL047W_mRNA; YDL047W; YDL047W.
DR GeneID; 851513; -.
DR KEGG; sce:YDL047W; -.
DR SGD; S000002205; SIT4.
DR VEuPathDB; FungiDB:YDL047W; -.
DR eggNOG; KOG0373; Eukaryota.
DR GeneTree; ENSGT00550000074961; -.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; P20604; -.
DR OMA; CQNKYGN; -.
DR BioCyc; YEAST:G3O-29466-MON; -.
DR PRO; PR:P20604; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P20604; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:SGD.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; IPI:ComplexPortal.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:SGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:SGD.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0031929; P:TOR signaling; IC:ComplexPortal.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:SGD.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW Mitosis; Protein phosphatase; Reference proteome.
FT CHAIN 1..311
FT /note="Serine/threonine-protein phosphatase PP1-1"
FT /id="PRO_0000058881"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MUTAGEN 35
FT /note="L->A: Reduced interaction with TAP42."
FT /evidence="ECO:0000269|PubMed:14551259"
FT MUTAGEN 37..38
FT /note="EE->AA: Nearly no interaction with TAP42."
FT /evidence="ECO:0000269|PubMed:14551259"
FT MUTAGEN 38
FT /note="E->A: Normal interaction with TAP42."
FT /evidence="ECO:0000269|PubMed:14551259"
FT MUTAGEN 40
FT /note="N->A: Normal interaction with TAP42."
FT /evidence="ECO:0000269|PubMed:14551259"
SQ SEQUENCE 311 AA; 35538 MW; AF52BC65E4E715EC CRC64;
MVSRGPDEWL ETIKKCQALT ENEMKQLCEM VKELLMEESN IQPVQTPVTV CGDIHGQFHD
LLELFRTAGG FPDDINYIFL GDYVDRGYYS LETFTLLMCL KVKYPAKITL VRGNHESRQI
TQVYGFYEEC LNKYGSTTVW KYCCQVFDFL TLAAIIDGKI LCVHGGLSPE IRMLDQIRVL
SRAQEVPHEG GFSDLLWSDP DNVEAWQVSP RGAGWLFGSK VAREFNHVNG LNLIARAHQL
VMEGFKYHFP EKDVVTVWSA PNYCYRCGNV ASVMKVDEDL EPTFKIFSAV PDDYIRESTA
NHNNQRAGYF L
