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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
 
 
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