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Protein

N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D, mitochondrial

Gene

FMP30

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce N-acylethanolamines (NAEs).1 Publication

Catalytic activityi

An N-acylphosphatidylethanolamine + H2O = an N-acylethanolamine + a 1,2-diacylglycerol 3-phosphate.

Cofactori

Zn2+By similarityNote: Binds 1 or 2 zinc ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi265 – 2651Zinc 1Sequence analysis
Metal bindingi267 – 2671Zinc 1Sequence analysis
Metal bindingi269 – 2691Zinc 2Sequence analysis
Metal bindingi270 – 2701Zinc 2Sequence analysis
Metal bindingi332 – 3321Zinc 1Sequence analysis
Metal bindingi425 – 4251Zinc 2Sequence analysis

GO - Molecular functioni

  • N-acylphosphatidylethanolamine-specific phospholipase D activity Source: SGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • N-acylethanolamine metabolic process Source: SGD
  • N-acylphosphatidylethanolamine metabolic process Source: SGD
  • phospholipid catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism, Phospholipid degradation, Phospholipid metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-34005-MONOMER.

Chemistry

SwissLipidsiSLP:000000081.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D, mitochondrial (EC:3.1.4.54)
Short name:
NAPE-PLD
Short name:
NAPE-hydrolyzing phospholipase D
Alternative name(s):
Found in mitochondrial proteome protein 30
Gene namesi
Name:FMP30
Ordered Locus Names:YPL103C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL103C.
SGDiS000006024. FMP30.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei54 – 7623HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of mitochondrial inner membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3939MitochondrionSequence analysisAdd
BLAST
Chaini40 – 468429N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D, mitochondrialPRO_0000238633Add
BLAST

Proteomic databases

MaxQBiQ02883.

Expressioni

Inductioni

Expressed periodically during the glycolytic and respiratory oscillations cycles.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi36078. 64 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ02883.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NAPE-PLD family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000017990.
HOGENOMiHOG000246526.
InParanoidiQ02883.
OMAiHQKPRHI.
OrthoDBiEOG71K6CM.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Metallo-B-lactamas.
IPR024884. NAPE-PLD.
[Graphical view]
PfamiPF12706. Lactamase_B_2. 1 hit.
[Graphical view]
PIRSFiPIRSF038896. NAPE-PLD. 1 hit.
SUPFAMiSSF56281. SSF56281. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q02883-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFVTCHVQM RLLLQRRLVR LRESELFRPQ TSLSTFKRHA SQKTRPIQKC
60 70 80 90 100
SRKYARILLL SVLVPYTGYA FYVSLATVKQ IDLRNEMCQR LEENNNEVTY
110 120 130 140 150
KGSLLKYSPL EVLGRFENPF EEYRIQTVFE FFANRVFELF ERNRGGIPRD
160 170 180 190 200
VHQMNKLMPV HKPTWGPNLV DVDPAEETAL PLECKVLDEL HIPTAVEENE
210 220 230 240 250
GSKCPVYNTW LGQSCNYTVY NGLRILTDPL FSDFLIHKTL GPKRITQMPS
260 270 280 290 300
QITEVPKPDI ILVSHNHPDH LDLESLEYWS GKDSPLWIVP KGMKSYMTSN
310 320 330 340 350
GCDNVLELSW WETLQVKKNN EIYHISATPA MHWSGRSLLD TNKSLWCSFL
360 370 380 390 400
LTHHGNPILF HAGDTGYVKD LFVRIKERFG KGCKLALLPC GQYCPEWHQK
410 420 430 440 450
PRHINPQEVL KIMKDLEARN VLGVHWGTFV LSGEYFLEPK EKLEMLAEWG
460
GFKDRCYCPE LGKTECFD
Length:468
Mass (Da):54,368
Last modified:November 1, 1996 - v1
Checksum:iC5E6D8817C16791A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43281 Genomic DNA. Translation: AAB68197.1.
BK006949 Genomic DNA. Translation: DAA11330.1.
PIRiS61964.
RefSeqiNP_015222.1. NM_001183917.1.

Genome annotation databases

EnsemblFungiiYPL103C; YPL103C; YPL103C.
GeneIDi856001.
KEGGisce:YPL103C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43281 Genomic DNA. Translation: AAB68197.1.
BK006949 Genomic DNA. Translation: DAA11330.1.
PIRiS61964.
RefSeqiNP_015222.1. NM_001183917.1.

3D structure databases

ProteinModelPortaliQ02883.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36078. 64 interactions.

Chemistry

SwissLipidsiSLP:000000081.

Proteomic databases

MaxQBiQ02883.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL103C; YPL103C; YPL103C.
GeneIDi856001.
KEGGisce:YPL103C.

Organism-specific databases

EuPathDBiFungiDB:YPL103C.
SGDiS000006024. FMP30.

Phylogenomic databases

GeneTreeiENSGT00390000017990.
HOGENOMiHOG000246526.
InParanoidiQ02883.
OMAiHQKPRHI.
OrthoDBiEOG71K6CM.

Enzyme and pathway databases

BioCyciYEAST:G3O-34005-MONOMER.

Miscellaneous databases

NextBioi980872.
PROiQ02883.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Metallo-B-lactamas.
IPR024884. NAPE-PLD.
[Graphical view]
PfamiPF12706. Lactamase_B_2. 1 hit.
[Graphical view]
PIRSFiPIRSF038896. NAPE-PLD. 1 hit.
SUPFAMiSSF56281. SSF56281. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  5. "Presence and potential signaling function of N-acylethanolamines and their phospholipid precursors in the yeast Saccharomyces cerevisiae."
    Merkel O., Schmid P.C., Paltauf F., Schmid H.H.O.
    Biochim. Biophys. Acta 1734:215-219(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Logic of the yeast metabolic cycle: temporal compartmentalization of cellular processes."
    Tu B.P., Kudlicki A., Rowicka M., McKnight S.L.
    Science 310:1152-1158(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiFMP30_YEAST
AccessioniPrimary (citable) accession number: Q02883
Secondary accession number(s): D6W3R4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 178 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.