PP2C7_YEAST
ID PP2C7_YEAST Reviewed; 343 AA.
AC P38797; A2TBN2; D3DL26; Q06HN3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Protein phosphatase 2C homolog 7, mitochondrial;
DE Short=PP2C-7;
DE EC=3.1.3.16 {ECO:0000269|PubMed:23940037, ECO:0000269|PubMed:28076776, ECO:0000269|PubMed:30267671};
DE Flags: Precursor;
GN Name=PTC7; OrderedLocusNames=YHR076W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-125.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17244705; DOI=10.1073/pnas.0610354104;
RA Juneau K., Palm C., Miranda M., Davis R.W.;
RT "High-density yeast-tiling array reveals previously undiscovered introns
RT and extensive regulation of meiotic splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-113.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17351133; DOI=10.1101/gr.6049107;
RA Zhang Z., Hesselberth J.R., Fields S.;
RT "Genome-wide identification of spliced introns using a tiling microarray.";
RL Genome Res. 17:503-509(2007).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11327310; DOI=10.1080/713803741;
RA Ramos C.W., Gueldener U., Klein S., Hegemann J.H., Gonzalez S.,
RA Rodriguez-Medina J.R.;
RT "Molecular analysis of the Saccharomyces cerevisiae YHR076w gene.";
RL IUBMB Life 50:371-377(2000).
RN [6]
RP FUNCTION.
RX PubMed=12220683; DOI=10.1016/s0014-5793(02)03247-7;
RA Jiang L., Whiteway M., Ramos C.W., Rodriguez-Medina J.R., Shen S.-H.;
RT "The YHR076w gene encodes a type 2C protein phosphatase and represents the
RT seventh PP2C gene in budding yeast.";
RL FEBS Lett. 527:323-325(2002).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23940037; DOI=10.1074/jbc.m113.474494;
RA Martin-Montalvo A., Gonzalez-Mariscal I., Pomares-Viciana T.,
RA Padilla-Lopez S., Ballesteros M., Vazquez-Fonseca L., Gandolfo P.,
RA Brautigan D.L., Navas P., Santos-Ocana C.;
RT "The phosphatase Ptc7 induces coenzyme Q biosynthesis by activating the
RT hydroxylase Coq7 in yeast.";
RL J. Biol. Chem. 288:28126-28137(2013).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-109 AND ASP-265.
RX PubMed=28076776; DOI=10.1016/j.celrep.2016.12.049;
RA Guo X., Niemi N.M., Hutchins P.D., Condon S.G.F., Jochem A., Ulbrich A.,
RA Higbee A.J., Russell J.D., Senes A., Coon J.J., Pagliarini D.J.;
RT "Ptc7p Dephosphorylates Select Mitochondrial Proteins to Enhance Metabolic
RT Function.";
RL Cell Rep. 18:307-313(2017).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=30267671; DOI=10.1016/j.bbabio.2018.09.369;
RA Gonzalez-Mariscal I., Martin-Montalvo A., Vazquez-Fonseca L.,
RA Pomares-Viciana T., Sanchez-Cuesta A., Fernandez-Ayala D.J., Navas P.,
RA Santos-Ocana C.;
RT "The mitochondrial phosphatase PPTC7 orchestrates mitochondrial metabolism
RT regulating coenzyme Q10 biosynthesis.";
RL Biochim. Biophys. Acta 1859:1235-1248(2018).
CC -!- FUNCTION: Protein phosphatase which positively regulates biosynthesis
CC of the ubiquinone, coenzyme Q (PubMed:12220683, PubMed:23940037,
CC PubMed:28076776, PubMed:30267671). Dephosphorylates and activates the
CC ubiquinone biosynthesis protein CAT5/COQ7 (PubMed:23940037,
CC PubMed:30267671). Also dephosphorylates CIT1 on 'Ser-462', which leads
CC to its activation (PubMed:28076776). {ECO:0000269|PubMed:12220683,
CC ECO:0000269|PubMed:23940037, ECO:0000269|PubMed:28076776,
CC ECO:0000269|PubMed:30267671}.
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 Evidence={ECO:0000269|PubMed:23940037, ECO:0000269|PubMed:28076776};
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 Evidence={ECO:0000269|PubMed:23940037, ECO:0000269|PubMed:30267671};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:23940037, ECO:0000269|PubMed:28076776};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:23940037, ECO:0000269|PubMed:28076776};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU01082};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=155.7 uM for phosphorylated CIT1 {ECO:0000269|PubMed:28076776};
CC Vmax=218.6 umol/min/ug enzyme {ECO:0000269|PubMed:28076776};
CC -!- INTERACTION:
CC P38797; P24280: SEC14; NbExp=4; IntAct=EBI-24588, EBI-16535;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11327310,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:30267671}.
CC -!- INDUCTION: By the presence of non-fermentable carbon sources and
CC oxidative stress. {ECO:0000269|PubMed:23940037}.
CC -!- DISRUPTION PHENOTYPE: Decreased growth in non-fermentable sugar mediums
CC (PubMed:23940037, PubMed:28076776). This is caused by a decrease in
CC COQ6 levels, which results in a severe decrease in complex II, NADH-
CC coenzyme Q dehydrogenase to complex III, and complex II to complex III
CC activities in the electron transport chain (PubMed:23940037). Impaired
CC antioxidant defenses (PubMed:23940037). Decreased phosphorylation of
CC CAT5/COQ7 (PubMed:23940037). Increased phosphorylation of CIT1 and
CC decreased citrate synthase activity (PubMed:28076776).
CC {ECO:0000269|PubMed:23940037, ECO:0000269|PubMed:28076776}.
CC -!- CAUTION: There are conflicting reports on the effect the deletion of
CC PTC7 causes in cells (PubMed:23940037, PubMed:28076776). In one report,
CC deletion of PTC7 causes decreases in COQ6 levels, and mitochondrial
CC defects observed are thought to be caused by disruption of the COQ6
CC pathway (PubMed:23940037). In another report, deletion of PTC7 causes
CC no change in COQ6 levels and mitochondrial defects observed in mutants
CC are not thought to be caused by changes in the COQ6 pathway
CC (PubMed:28076776). {ECO:0000269|PubMed:23940037,
CC ECO:0000269|PubMed:28076776}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB68888.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U10556; AAB68888.1; ALT_SEQ; Genomic_DNA.
DR EMBL; EF123135; ABM97479.1; -; mRNA.
DR EMBL; DQ881450; ABI95877.1; -; mRNA.
DR EMBL; BK006934; DAA06770.1; -; Genomic_DNA.
DR PIR; S46810; S46810.
DR RefSeq; NP_011943.2; NM_001179206.1.
DR AlphaFoldDB; P38797; -.
DR SMR; P38797; -.
DR BioGRID; 36510; 129.
DR DIP; DIP-6369N; -.
DR IntAct; P38797; 8.
DR MINT; P38797; -.
DR STRING; 4932.YHR076W; -.
DR MaxQB; P38797; -.
DR PaxDb; P38797; -.
DR PRIDE; P38797; -.
DR DNASU; 856475; -.
DR EnsemblFungi; YHR076W_mRNA; YHR076W; YHR076W.
DR GeneID; 856475; -.
DR KEGG; sce:YHR076W; -.
DR SGD; S000001118; PTC7.
DR VEuPathDB; FungiDB:YHR076W; -.
DR eggNOG; KOG1379; Eukaryota.
DR GeneTree; ENSGT00390000011937; -.
DR HOGENOM; CLU_029404_7_0_1; -.
DR InParanoid; P38797; -.
DR OMA; MQSIYWT; -.
DR BioCyc; YEAST:G3O-31123-MON; -.
DR SABIO-RK; P38797; -.
DR PRO; PR:P38797; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38797; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
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:0004721; F:phosphoprotein phosphatase activity; IDA:SGD.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:SGD.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:SGD.
DR GO; GO:0010795; P:regulation of ubiquinone biosynthetic process; IMP:UniProtKB.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR InterPro; IPR039123; PPTC7.
DR PANTHER; PTHR12320; PTHR12320; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW Protein phosphatase; Reference proteome; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..343
FT /note="Protein phosphatase 2C homolog 7, mitochondrial"
FT /id="PRO_0000057779"
FT DOMAIN 76..342
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 109
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28076776"
FT BINDING 109
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28076776"
FT BINDING 110
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 265
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28076776"
FT MUTAGEN 109
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:28076776"
FT MUTAGEN 265
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:28076776"
SQ SEQUENCE 343 AA; 37782 MW; FCCC729800371B24 CRC64;
MFANVGFRTL RVSRGPLYGS CSQIISFSKR TFYSSAKSGY QSNNSHGDAY SSGSQSGPFT
YKTAVAFQPK DRDDLIYQKL KDSIRSPTGE DNYFVTSNNV HDIFAGVADG VGGWAEHGYD
SSAISRELCK KMDEISTALA ENSSKETLLT PKKIIGAAYA KIRDEKVVKV GGTTAIVAHF
PSNGKLEVAN LGDSWCGVFR DSKLVFQTKF QTVGFNAPYQ LSIIPEEMLK EAERRGSKYI
LNTPRDADEY SFQLKKKDII ILATDGVTDN IATDDIELFL KDNAARTNDE LQLLSQKFVD
NVVSLSKDPN YPSVFAQEIS KLTGKNYSGG KEDDITVVVV RVD
