PTF1_SCHPO
ID PTF1_SCHPO Reviewed; 229 AA.
AC Q9P6N2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Pdp3-interacting factor 1 {ECO:0000303|PubMed:22184112};
DE EC=3.1.3.50 {ECO:0000250|UniProtKB:P53981};
GN Name=ptf1 {ECO:0000303|PubMed:22184112};
GN ORFNames=SPAC823.14 {ECO:0000312|PomBase:SPAC823.14};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MST2 COMPLEX,
RP AND FUNCTION.
RX PubMed=22184112; DOI=10.1074/jbc.m111.329417;
RA Wang Y., Kallgren S.P., Reddy B.D., Kuntz K., Lopez-Maury L., Thompson J.,
RA Watt S., Ma C., Hou H., Shi Y., Yates J.R. III, Bahler J., O'Connell M.J.,
RA Jia S.;
RT "Histone H3 lysine 14 acetylation is required for activation of a DNA
RT damage checkpoint in fission yeast.";
RL J. Biol. Chem. 287:4386-4393(2012).
CC -!- FUNCTION: Component of the mst2 complex which is a highly specific H3
CC lysine 14 (H3K14) acetyltransferase that functions together with gcn5
CC to regulate global levels of H3K14 acetylation (H3K14ac), critical for
CC DNA damage checkpoint activation. {ECO:0000269|PubMed:22184112}.
CC -!- FUNCTION: May also function as a sugar alcohol (polyol) phosphatase
CC that prevents accumulation of toxic levels of polyol phosphates, which
CC can impair glycolysis by inhibiting glucose-6-phosphate isomerase.
CC {ECO:0000250|UniProtKB:P53981}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribitol 5-phosphate + H2O = phosphate + ribitol;
CC Xref=Rhea:RHEA:47648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15963,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57695;
CC Evidence={ECO:0000250|UniProtKB:P53981};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47649;
CC Evidence={ECO:0000250|UniProtKB:P53981};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-sorbitol 6-phosphate + H2O = D-sorbitol + phosphate;
CC Xref=Rhea:RHEA:24580, ChEBI:CHEBI:15377, ChEBI:CHEBI:17924,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:60084; EC=3.1.3.50;
CC Evidence={ECO:0000250|UniProtKB:P53981};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24581;
CC Evidence={ECO:0000250|UniProtKB:P53981};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycerol 1-phosphate = glycerol + phosphate;
CC Xref=Rhea:RHEA:46084, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57685;
CC Evidence={ECO:0000250|UniProtKB:P53981};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46085;
CC Evidence={ECO:0000250|UniProtKB:P53981};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythrose 4-phosphate + H2O = D-erythrose + phosphate;
CC Xref=Rhea:RHEA:66376, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC ChEBI:CHEBI:27904, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000250|UniProtKB:P53981};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66377;
CC Evidence={ECO:0000250|UniProtKB:P53981};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q58989};
CC -!- SUBUNIT: Component of the mst2 complex composed of at least eaf6, mst2,
CC nto1, pdp3, ptf1, ptf2 and tfg3. {ECO:0000269|PubMed:22184112}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB90159.1; -; Genomic_DNA.
DR RefSeq; NP_593841.1; NM_001019270.2.
DR AlphaFoldDB; Q9P6N2; -.
DR SMR; Q9P6N2; -.
DR BioGRID; 279741; 27.
DR STRING; 4896.SPAC823.14.1; -.
DR MaxQB; Q9P6N2; -.
DR PaxDb; Q9P6N2; -.
DR EnsemblFungi; SPAC823.14.1; SPAC823.14.1:pep; SPAC823.14.
DR GeneID; 2543317; -.
DR KEGG; spo:SPAC823.14; -.
DR PomBase; SPAC823.14; ptf1.
DR VEuPathDB; FungiDB:SPAC823.14; -.
DR eggNOG; ENOG502QRU0; Eukaryota.
DR HOGENOM; CLU_058495_1_0_1; -.
DR InParanoid; Q9P6N2; -.
DR OMA; VPFHEFD; -.
DR PhylomeDB; Q9P6N2; -.
DR PRO; PR:Q9P6N2; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0036410; C:Mst2 histone acetyltransferase complex; TAS:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0110130; F:ribitol-5-phosphatase activity; IEA:RHEA.
DR GO; GO:0050286; F:sorbitol-6-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006384; HAD_hydro_PyrdxlP_Pase-like.
DR InterPro; IPR023214; HAD_sf.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01489; DKMTPPase-SF; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; DNA damage; Hydrolase; Magnesium;
KW Metal-binding; Nucleus; Reference proteome.
FT CHAIN 1..229
FT /note="Pdp3-interacting factor 1"
FT /id="PRO_0000339407"
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT ACT_SITE 14
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q58989"
SQ SEQUENCE 229 AA; 26272 MW; E7C00DA1AFDC04D6 CRC64;
MAQKKQLYVF SDFDGTITLQ DSNDYLTDNF GMGNANRVNL NQQVLDGSIS FRDAFAKMLD
SVHLSYDEAL EVLKKNVAID PSFKPFYEWC KSQDIRVIIL SSGMEPFIRA LFEQYLGKEE
ASSIEIVSND INVHPDGQWN IVYHDDSHFG HDKSLTIRPY AQLPESKRPH MVYCGDGVSD
LSAAKETEHL FAKKGRDLIK YCEREKISFS EFETFADIHK DLQKLFFSS
