GEP4_YEAST
ID GEP4_YEAST Reviewed; 185 AA.
AC P38812; D3DL50;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Phosphatidylglycerophosphatase GEP4, mitochondrial;
DE EC=3.1.3.27;
DE AltName: Full=Genetic interactor of prohibitins 4;
DE AltName: Full=PGP phosphatase GEP4;
GN Name=GEP4; OrderedLocusNames=YHR100C;
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 [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 [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [5]
RP FUNCTION.
RX PubMed=19221197; DOI=10.1083/jcb.200810189;
RA Osman C., Haag M., Potting C., Rodenfels J., Dip P.V., Wieland F.T.,
RA Brugger B., Westermann B., Langer T.;
RT "The genetic interactome of prohibitins: coordinated control of cardiolipin
RT and phosphatidylethanolamine by conserved regulators in mitochondria.";
RL J. Cell Biol. 184:583-596(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-45 AND ASP-47.
RX PubMed=20485265; DOI=10.1038/emboj.2010.98;
RA Osman C., Haag M., Wieland F.T., Brugger B., Langer T.;
RT "A mitochondrial phosphatase required for cardiolipin biosynthesis: the PGP
RT phosphatase Gep4.";
RL EMBO J. 29:1976-1987(2010).
RN [7]
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).
CC -!- FUNCTION: Phosphatidylglycerophosphatase involved in the biosynthesis
CC of cardiolipin (CL), a unique dimeric phosphoglycerolipid predominantly
CC present in mitochondrial membranes and which has important functions
CC for cellular energy metabolism, mitochondrial dynamics and the
CC initiation of apoptotic pathways. Required for the stability of
CC respiratory chain supercomplexes and for growth at elevated
CC temperature, in presence of ethidium bromide or in absence of
CC prohibitins. {ECO:0000269|PubMed:19221197,
CC ECO:0000269|PubMed:20485265}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) +
CC H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate;
CC Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27;
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:20485265}; Peripheral
CC membrane protein {ECO:0000269|PubMed:16823961,
CC ECO:0000269|PubMed:20485265}; Matrix side {ECO:0000269|PubMed:16823961,
CC ECO:0000269|PubMed:20485265}.
CC -!- SIMILARITY: Belongs to the GEP4 family. {ECO:0000305}.
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DR EMBL; U00059; AAB68862.1; -; Genomic_DNA.
DR EMBL; AY692650; AAT92669.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06794.1; -; Genomic_DNA.
DR PIR; S48943; S48943.
DR RefSeq; NP_011968.1; NM_001179230.1.
DR AlphaFoldDB; P38812; -.
DR SMR; P38812; -.
DR BioGRID; 36533; 48.
DR DIP; DIP-1343N; -.
DR IntAct; P38812; 1.
DR MINT; P38812; -.
DR STRING; 4932.YHR100C; -.
DR SwissLipids; SLP:000000061; -.
DR SwissLipids; SLP:000000220; -.
DR MaxQB; P38812; -.
DR PaxDb; P38812; -.
DR PRIDE; P38812; -.
DR EnsemblFungi; YHR100C_mRNA; YHR100C; YHR100C.
DR GeneID; 856500; -.
DR KEGG; sce:YHR100C; -.
DR SGD; S000001142; GEP4.
DR VEuPathDB; FungiDB:YHR100C; -.
DR eggNOG; KOG2961; Eukaryota.
DR HOGENOM; CLU_056221_3_2_1; -.
DR InParanoid; P38812; -.
DR OMA; DMLMANM; -.
DR BioCyc; YEAST:G3O-31145-MON; -.
DR UniPathway; UPA00084; UER00504.
DR PRO; PR:P38812; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38812; protein.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0008962; F:phosphatidylglycerophosphatase activity; IDA:SGD.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IMP:SGD.
DR GO; GO:0046838; P:phosphorylated carbohydrate dephosphorylation; IMP:SGD.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR027706; PGP_Pase.
DR InterPro; IPR010021; PGPP1/Gep4.
DR PANTHER; PTHR19288:SF25; PTHR19288:SF25; 1.
DR Pfam; PF09419; PGP_phosphatase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01668; YqeG_hyp_ppase; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome.
FT CHAIN 1..185
FT /note="Phosphatidylglycerophosphatase GEP4, mitochondrial"
FT /id="PRO_0000202908"
FT MOTIF 45..49
FT /note="Phosphoryl acceptor"
FT MUTAGEN 45
FT /note="D->N: Abolishes phosphatase activity and impairs
FT cardiolipin biosynthesis."
FT /evidence="ECO:0000269|PubMed:20485265"
FT MUTAGEN 47
FT /note="D->N: Abolishes phosphatase activity and impairs
FT cardiolipin biosynthesis."
FT /evidence="ECO:0000269|PubMed:20485265"
SQ SEQUENCE 185 AA; 20945 MW; 1E3D8F936C2EF7EC CRC64;
MNISGTLNTL RLLYNPSLCK PSLVVPTFND LPIPIHDSIK AVVLDKDNCI AFPHDDKIWP
DYLQHWETLR SKYSNKALLI VSNTAGSNSD KDYSQAKLLE DKTGIPVLRH STKKPGCHNE
ILDYFYRNKT ITNPKEVAVV GDRLFTDILM ANLMGSYGVW IRDGVKVSAN PLSKFEKKLY
NFLGF