PGC1_YEAST
ID PGC1_YEAST Reviewed; 321 AA.
AC Q08959; D6W3G4;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Phosphatidylglycerol phospholipase C;
DE EC=3.1.4.-;
GN Name=PGC1; OrderedLocusNames=YPL206C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 SUBCELLULAR LOCATION.
RX PubMed=12514182; DOI=10.1074/jbc.m212725200;
RA Beilharz T., Egan B., Silver P.A., Hofmann K., Lithgow T.;
RT "Bipartite signals mediate subcellular targeting of tail-anchored membrane
RT proteins in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:8219-8223(2003).
RN [4]
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 [5]
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 [6]
RP DOMAIN.
RX PubMed=16141200; DOI=10.1074/jbc.m507051200;
RA Fisher E., Almaguer C., Holic R., Griac P., Patton-Vogt J.;
RT "Glycerophosphocholine-dependent growth requires Gde1p (YPL110c) and Git1p
RT in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:36110-36117(2005).
RN [7]
RP FUNCTION.
RX PubMed=16172116; DOI=10.1074/jbc.m507700200;
RA Fernandez-Murray J.P., McMaster C.R.;
RT "Glycerophosphocholine catabolism as a new route for choline formation for
RT phosphatidylcholine synthesis by the Kennedy pathway.";
RL J. Biol. Chem. 280:38290-38296(2005).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18434318; DOI=10.1074/jbc.m800868200;
RA Simockova M., Holic R., Tahotna D., Patton-Vogt J., Griac P.;
RT "Yeast Pgc1p (YPL206c) controls the amount of phosphatidylglycerol via a
RT phospholipase C-type degradation mechanism.";
RL J. Biol. Chem. 283:17107-17115(2008).
RN [9]
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 [10]
RP SUBCELLULAR LOCATION.
RX PubMed=24868093; DOI=10.1194/jlr.m050229;
RA Currie E., Guo X., Christiano R., Chitraju C., Kory N., Harrison K.,
RA Haas J., Walther T.C., Farese R.V. Jr.;
RT "High-confidence proteomic analysis of yeast lipid droplets identifies
RT additional droplet proteins and reveals connections to dolichol synthesis
RT and sterol acetylation.";
RL J. Lipid Res. 55:1465-1477(2014).
CC -!- FUNCTION: Phosphatidylglycerol phospholipase required for the removal
CC of excess phosphatidylglycerol (PG) via a phospholipase C-type
CC degradation mechanism. {ECO:0000269|PubMed:16172116,
CC ECO:0000269|PubMed:18434318}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = a
CC 1,2-diacyl-sn-glycerol + H(+) + sn-glycerol 3-phosphate;
CC Xref=Rhea:RHEA:32927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57597, ChEBI:CHEBI:64716;
CC Evidence={ECO:0000269|PubMed:18434318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32928;
CC Evidence={ECO:0000305|PubMed:18434318};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:18434318}; Single-pass
CC type IV membrane protein {ECO:0000255}. Lipid droplet
CC {ECO:0000269|PubMed:12514182, ECO:0000269|PubMed:24868093}.
CC -!- DISRUPTION PHENOTYPE: Leads to the accumulation of phosphatidyl
CC glycerol. {ECO:0000269|PubMed:18434318}.
CC -!- MISCELLANEOUS: Present with 3270 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; Z73562; CAA97920.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11230.1; -; Genomic_DNA.
DR PIR; S65225; S65225.
DR RefSeq; NP_015118.1; NM_001184020.1.
DR AlphaFoldDB; Q08959; -.
DR SMR; Q08959; -.
DR BioGRID; 35979; 21.
DR IntAct; Q08959; 3.
DR STRING; 4932.YPL206C; -.
DR SwissLipids; SLP:000000075; -.
DR MaxQB; Q08959; -.
DR PaxDb; Q08959; -.
DR PRIDE; Q08959; -.
DR EnsemblFungi; YPL206C_mRNA; YPL206C; YPL206C.
DR GeneID; 855895; -.
DR KEGG; sce:YPL206C; -.
DR SGD; S000006127; PGC1.
DR VEuPathDB; FungiDB:YPL206C; -.
DR eggNOG; KOG2258; Eukaryota.
DR GeneTree; ENSGT00940000172471; -.
DR HOGENOM; CLU_030006_1_2_1; -.
DR InParanoid; Q08959; -.
DR OMA; YARHFFD; -.
DR BioCyc; MetaCyc:G3O-34097-MON; -.
DR BioCyc; YEAST:G3O-34097-MON; -.
DR PRO; PR:Q08959; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08959; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0034479; F:phosphatidylglycerol phospholipase C activity; IDA:SGD.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IMP:SGD.
DR GO; GO:0034478; P:phosphatidylglycerol catabolic process; IMP:SGD.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR Pfam; PF03009; GDPD; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS51704; GP_PDE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Lipid droplet; Lipid metabolism; Membrane; Mitochondrion;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..321
FT /note="Phosphatidylglycerol phospholipase C"
FT /id="PRO_0000234365"
FT TRANSMEM 297..315
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 2..251
FT /note="GP-PDE"
SQ SEQUENCE 321 AA; 37070 MW; AB64474D8E43D120 CRC64;
MVEIVGHRAF KARYPENTLL AFEKAYAAGA DVIETDLQMT SDGMVVVNHD SDTGRMWDKN
LVIGESTWEE VKRLRCKEDG SLAMMTLKEI LTWAVCHPGA KLMLDIKFTN EKIIMIKTFV
IMLEVKNDLK FWQERITWGL WLLDWYDFGI ETGVLKDFKV IVISLSLDIA SQFVKRSLTL
NDPHYKLFGI SVHFVSSWTS QFRLRLLPVL MKNDIKVYLW TVNKPIDFKY LCELPIHGAI
TDDPIKARKL CDGHTVAKKP TAEKKFVAPS LASVDGLRFH AFIKVYNILC TLLYSKWVHI
KLCGWSIAYV IFLFLRTIHF L
