FMP30_YEAST
ID FMP30_YEAST Reviewed; 468 AA.
AC Q02883; D6W3R4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D, mitochondrial;
DE Short=NAPE-PLD;
DE Short=NAPE-hydrolyzing phospholipase D;
DE EC=3.1.4.54;
DE AltName: Full=Found in mitochondrial proteome protein 30;
DE Flags: Precursor;
GN Name=FMP30; OrderedLocusNames=YPL103C;
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 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 [4]
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 [5]
RP FUNCTION.
RX PubMed=15878693; DOI=10.1016/j.bbalip.2005.03.004;
RA Merkel O., Schmid P.C., Paltauf F., Schmid H.H.O.;
RT "Presence and potential signaling function of N-acylethanolamines and their
RT phospholipid precursors in the yeast Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1734:215-219(2005).
RN [6]
RP INDUCTION.
RX PubMed=16254148; DOI=10.1126/science.1120499;
RA Tu B.P., Kudlicki A., Rowicka M., McKnight S.L.;
RT "Logic of the yeast metabolic cycle: temporal compartmentalization of
RT cellular processes.";
RL Science 310:1152-1158(2005).
CC -!- FUNCTION: Hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to
CC produce N-acylethanolamines (NAEs). {ECO:0000269|PubMed:15878693}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine = a
CC 1,2-diacyl-sn-glycero-3-phosphate + an N-acylethanolamine + H(+);
CC Xref=Rhea:RHEA:33159, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:52640, ChEBI:CHEBI:58608, ChEBI:CHEBI:62537; EC=3.1.4.54;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 or 2 zinc ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Expressed periodically during the glycolytic and respiratory
CC oscillations cycles. {ECO:0000269|PubMed:16254148}.
CC -!- MISCELLANEOUS: Present with 178 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NAPE-PLD family. {ECO:0000305}.
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DR EMBL; U43281; AAB68197.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11330.1; -; Genomic_DNA.
DR PIR; S61964; S61964.
DR RefSeq; NP_015222.1; NM_001183917.1.
DR AlphaFoldDB; Q02883; -.
DR SMR; Q02883; -.
DR BioGRID; 36078; 141.
DR STRING; 4932.YPL103C; -.
DR SwissLipids; SLP:000000081; -.
DR MaxQB; Q02883; -.
DR PaxDb; Q02883; -.
DR PRIDE; Q02883; -.
DR DNASU; 856001; -.
DR EnsemblFungi; YPL103C_mRNA; YPL103C; YPL103C.
DR GeneID; 856001; -.
DR KEGG; sce:YPL103C; -.
DR SGD; S000006024; FMP30.
DR VEuPathDB; FungiDB:YPL103C; -.
DR eggNOG; KOG3798; Eukaryota.
DR GeneTree; ENSGT00940000173847; -.
DR HOGENOM; CLU_020884_2_1_1; -.
DR InParanoid; Q02883; -.
DR OMA; CTPAMHW; -.
DR BioCyc; YEAST:G3O-34005-MON; -.
DR PRO; PR:Q02883; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02883; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0043227; C:membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0102200; F:N-acetylphosphatidylethanolamine-hydrolysing phospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; ISS:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0070291; P:N-acylethanolamine metabolic process; IMP:SGD.
DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; IMP:SGD.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR024884; NAPE-PLD.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR PIRSF; PIRSF038896; NAPE-PLD; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Metal-binding;
KW Mitochondrion; Phospholipid degradation; Phospholipid metabolism;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Zinc.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..468
FT /note="N-acyl-phosphatidylethanolamine-hydrolyzing
FT phospholipase D, mitochondrial"
FT /id="PRO_0000238633"
FT TRANSMEM 54..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 468 AA; 54368 MW; C5E6D8817C16791A CRC64;
MNFVTCHVQM RLLLQRRLVR LRESELFRPQ TSLSTFKRHA SQKTRPIQKC SRKYARILLL
SVLVPYTGYA FYVSLATVKQ IDLRNEMCQR LEENNNEVTY KGSLLKYSPL EVLGRFENPF
EEYRIQTVFE FFANRVFELF ERNRGGIPRD VHQMNKLMPV HKPTWGPNLV DVDPAEETAL
PLECKVLDEL HIPTAVEENE GSKCPVYNTW LGQSCNYTVY NGLRILTDPL FSDFLIHKTL
GPKRITQMPS QITEVPKPDI ILVSHNHPDH LDLESLEYWS GKDSPLWIVP KGMKSYMTSN
GCDNVLELSW WETLQVKKNN EIYHISATPA MHWSGRSLLD TNKSLWCSFL LTHHGNPILF
HAGDTGYVKD LFVRIKERFG KGCKLALLPC GQYCPEWHQK PRHINPQEVL KIMKDLEARN
VLGVHWGTFV LSGEYFLEPK EKLEMLAEWG GFKDRCYCPE LGKTECFD
