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Q04958 (NTE1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysophospholipase NTE1

EC=3.1.1.5
Alternative name(s):
Intracellular phospholipase B
Neuropathy target esterase homolog
Gene names
Name:NTE1
Ordered Locus Names:YML059C
ORF Names:YM9958.03C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1679 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Intracellular phospholipase B that catalyzes the double deacylation of phosphatidylcholine (PC) to glycerophosphocholine (GroPCho). Plays an important role in membrane lipid homeostasis. Responsible for the rapid PC turnover in response to inositol, elevated temperatures, or when choline is present in the growth medium. Ref.5 Ref.6 Ref.7

Catalytic activity

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

Enzyme regulation

Positively regulated by SEC14. Inhibited by organophosphorus esters in the order phenyl saligenin phosphate (PSP) > phenyldipentyl phosphinate (PDPP) = diisopropyl fluorophosphate (DFP) > and paraoxon (PXN). Ref.5 Ref.6

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.3 Ref.5.

Miscellaneous

Present with 521 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the NTE family.

Contains 2 cyclic nucleotide-binding domains.

Contains 1 patatin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16791679Lysophospholipase NTE1
PRO_0000172528

Regions

Topological domain1 – 4949Cytoplasmic Potential
Transmembrane50 – 7021Helical; Potential
Topological domain71 – 10333Lumenal Potential
Transmembrane104 – 12421Helical; Potential
Topological domain125 – 16791555Cytoplasmic Potential
Domain1373 – 1537165Patatin
Nucleotide binding803 – 947145cNMP 1
Nucleotide binding943 – 1074132cNMP 2
Motif1404 – 14085GXSXG
Compositional bias259 – 29739Asp-rich
Compositional bias713 – 7186Poly-Ser

Sites

Active site14061

Amino acid modifications

Modified residue3001Phosphoserine Ref.11
Modified residue3121Phosphoserine Ref.11
Modified residue6321Phosphoserine Ref.11
Modified residue6341Phosphoserine Ref.9 Ref.10 Ref.11
Modified residue6531Phosphoserine Ref.11
Modified residue6611Phosphoserine Ref.11
Modified residue6701Phosphoserine Ref.11
Modified residue6801Phosphoserine Ref.11
Modified residue7391Phosphoserine Ref.11
Modified residue8031Phosphothreonine Ref.10

Experimental info

Mutagenesis14061S → A: Loss of esterase activity. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q04958 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 550FFCD4ACAF8E25

FASTA1,679187,133
        10         20         30         40         50         60 
MRSMNCTTNN TNNTGQNTKN SLGSSFNSSN YTSYRFQTCL TDQIISEAQT WSLSSLFNFS 

        70         80         90        100        110        120 
WVVSYFVMGA SRMIFRYGWY LATLSLLRIP KWIFFKLHHV QFTLSFWLIL FALAVIVFVT 

       130        140        150        160        170        180 
YTIMKERILS QYKRLTPEFL PLENTGKSGS SANINAASTQ SANAPPAIGS STTGASSIID 

       190        200        210        220        230        240 
SKKHSLKDGN ENETFLSSYL DQFLSAIKIF GYLEKPVFHD LTKNMKTQKM DEGEILLLDS 

       250        260        270        280        290        300 
TIGFAIVVEG TLQLYHEVDH SDKDHGDETD HSDTDGLDDQ DRDEEDEEED DDIDNYDTKS 

       310        320        330        340        350        360 
CSSNLIDEED ESVGYIHLKN GLGNFQLLNT VKPGNPLTSL VSILNLFTHS MSSYGNSNFP 

       370        380        390        400        410        420 
SELSSPIDTT VSVNNMFCSS EQNFSNTDSM TNSTNSFPTF PSSMPKLVAR AATDCTIGII 

       430        440        450        460        470        480 
PPQSFAKLTA KYPRSASHII QMVLTKLYHV TFQTAHDYLG LTKEIMDIEV LLNKSIVYEL 

       490        500        510        520        530        540 
PYYLKEAVIR KFKTVDKSSG SADLEPKPKN SNASSKLKKP PKAKPSDGII QSLKIANANA 

       550        560        570        580        590        600 
NTSSNSLSLK PEFTHHPSSR HVVLGSRDQF NPGDLLSNVP LSRTMDILSP NPIHNNNRNK 

       610        620        630        640        650        660 
SNGINTSTSN QHKRSSRSSS NNASVHSKKF SSLSPELRNA QLSTSPLSLD NTSVHDHIHP 

       670        680        690        700        710        720 
SPVHLKGRVS PRPNLLPTTS FSAAQEETED SALRMALVEA MLTYLGVNKS NMSVSSSSIA 

       730        740        750        760        770        780 
NMSSLNSPQL NEMYSRRPSN ASFLMSPHCT PSDISVASSF ASPQTQPTML RILPKEYTIS 

       790        800        810        820        830        840 
NKRHNKSKSQ DKKKPRAYKE ELTPNLDFED VKKDFAQGIQ LKFFKKGTTI VEQNARGKGL 

       850        860        870        880        890        900 
FYIISGKVNV TTNSSSSVVS SMSKPEQVSA QSSHKGENPH HTQHLLYSVG SGGIVGYLSS 

       910        920        930        940        950        960 
LIGYKSFVNI VAKSDVYVGF LSSATLERLF DKYFLIYLRI SDSLTKLLSS RLLKLDHALE 

       970        980        990       1000       1010       1020 
WVHLRASETL FSQGDSANGI YVVLNGRLRQ LQQQSLSNSN TSSEEVETQN IILGELAQGE 

      1030       1040       1050       1060       1070       1080 
SFGEVEVLTA MNRYSTIVAV RDSELARIPR TLFELLALEH PSIMIRVSRL VAKKIVGDRT 

      1090       1100       1110       1120       1130       1140 
VPALTGDPLS IKENDFTSLI PPTKASYSSS LSHKPQNITS GTITFRTITI LPITSGLPVE 

      1150       1160       1170       1180       1190       1200 
AFAMKLVQAF KQVGRTTIGL NQRTTLTHLG RHAFDRLSKL KQSGYFAELE EMYQTVVYIS 

      1210       1220       1230       1240       1250       1260 
DTPVKSNWTR TCIAQGDCIL LLADARSPSA EIGEYEKLLL NSKTTARTEL ILLHPERYVE 

      1270       1280       1290       1300       1310       1320 
PGLTHKWLRY RPWVHSHHHI QFSLTGTTLM NEGKMHVLNN GALALMDKLI QTEFSRKTQQ 

      1330       1340       1350       1360       1370       1380 
NISKLLPDSI KNTVENFSSR FMKSKRQYYT PVHRHKNDFL RLARILSGQA IGLVLGGGGA 

      1390       1400       1410       1420       1430       1440 
RGISHLGVIQ AIEEQGIPVD VIGGTSIGSF VGGLYAKDYD LVPIYGRVKK FAGRISSIWR 

      1450       1460       1470       1480       1490       1500 
MLTDLTWPVT SYTTGHEFNR GIWKTFGDTR IEDFWIQYYC NSTNITDSVQ EIHSFGYAWR 

      1510       1520       1530       1540       1550       1560 
YIRASMSLAG LLPPLEENGS MLLDGGYVDN LPVTEMRARG CQTIFAVDVG SADDRTPMEY 

      1570       1580       1590       1600       1610       1620 
GDSLNGFWII FNRWNPFSSH PNIPNMAEIQ VRLGYVASVN ALEKAKNTPG VVYVRPPIEE 

      1630       1640       1650       1660       1670 
YATLDFSKFE EIYHVGVDYG RIFLQGLIDD DKMPYIPGSQ ETTLNSQVPE FLLHRRNSI 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"Neuropathy target esterase and its yeast homologue degrade phosphatidylcholine to glycerophosphocholine in living cells."
Zaccheo O., Dinsdale D., Meacock P.A., Glynn P.
J. Biol. Chem. 279:24024-24033(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, MUTAGENESIS OF SER-1406.
[6]"Nte1p-mediated deacylation of phosphatidylcholine functionally interacts with Sec14p."
Fernandez-Murray J.P., McMaster C.R.
J. Biol. Chem. 280:8544-8552(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[7]"Inositol induces a profound alteration in the pattern and rate of synthesis and turnover of membrane lipids in Saccharomyces cerevisiae."
Gaspar M.L., Aregullin M.A., Jesch S.A., Henry S.A.
J. Biol. Chem. 281:22773-22785(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[9]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634 AND THR-803, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-312; SER-632; SER-634; SER-653; SER-661; SER-670; SER-680 AND SER-739, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z46729 Genomic DNA. Translation: CAA86716.1.
BK006946 Genomic DNA. Translation: DAA09838.1.
PIRS49802.
RefSeqNP_013652.1. NM_001182418.1.

3D structure databases

ProteinModelPortalQ04958.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35107. 24 interactions.
DIPDIP-5949N.
IntActQ04958. 16 interactions.
MINTMINT-653305.
STRING4932.YML059C.

Proteomic databases

PaxDbQ04958.
PeptideAtlasQ04958.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYML059C; YML059C; YML059C.
GeneID854943.
KEGGsce:YML059C.

Organism-specific databases

CYGDYML059c.
SGDS000004524. NTE1.

Phylogenomic databases

eggNOGCOG0664.
GeneTreeENSGT00390000002533.
HOGENOMHOG000048680.
KOK14676.
OMASPWTQTC.
OrthoDBEOG70W3NS.

Enzyme and pathway databases

BioCycMetaCyc:G3O-32654-MONOMER.
YEAST:G3O-32654-MONOMER.

Gene expression databases

GenevestigatorQ04958.

Family and domain databases

Gene3D2.60.120.10. 5 hits.
InterProIPR016035. Acyl_Trfase/lysoPLipase.
IPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR001423. LysoPLipase_patatin_CS.
IPR002641. Patatin/PLipase_A2-rel.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamPF00027. cNMP_binding. 2 hits.
PF01734. Patatin. 1 hit.
[Graphical view]
SMARTSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMSSF51206. SSF51206. 4 hits.
SSF52151. SSF52151. 1 hit.
PROSITEPS50042. CNMP_BINDING_3. 2 hits.
PS01237. UPF0028. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977998.
PROQ04958.

Entry information

Entry nameNTE1_YEAST
AccessionPrimary (citable) accession number: Q04958
Secondary accession number(s): D6VZB4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: March 19, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Uncharacterized protein families (UPF)

List of uncharacterized protein family (UPF) entries

SIMILARITY comments

Index of protein domains and families