Lysophospholipase NTE1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Sequence or UniProt identifier

>sp|Q04958|NTE1_YEAST Lysophospholipase NTE1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=NTE1 PE=1 SV=1 MRSMNCTTNNTNNTGQNTKNSLGSSFNSSNYTSYRFQTCLTDQIISEAQTWSLSSLFNFS WVVSYFVMGASRMIFRYGWYLATLSLLRIPKWIFFKLHHVQFTLSFWLILFALAVIVFVT YTIMKERILSQYKRLTPEFLPLENTGKSGSSANINAASTQSANAPPAIGSSTTGASSIID SKKHSLKDGNENETFLSSYLDQFLSAIKIFGYLEKPVFHDLTKNMKTQKMDEGEILLLDS TIGFAIVVEGTLQLYHEVDHSDKDHGDETDHSDTDGLDDQDRDEEDEEEDDDIDNYDTKS CSSNLIDEEDESVGYIHLKNGLGNFQLLNTVKPGNPLTSLVSILNLFTHSMSSYGNSNFP SELSSPIDTTVSVNNMFCSSEQNFSNTDSMTNSTNSFPTFPSSMPKLVARAATDCTIGII PPQSFAKLTAKYPRSASHIIQMVLTKLYHVTFQTAHDYLGLTKEIMDIEVLLNKSIVYEL PYYLKEAVIRKFKTVDKSSGSADLEPKPKNSNASSKLKKPPKAKPSDGIIQSLKIANANA NTSSNSLSLKPEFTHHPSSRHVVLGSRDQFNPGDLLSNVPLSRTMDILSPNPIHNNNRNK SNGINTSTSNQHKRSSRSSSNNASVHSKKFSSLSPELRNAQLSTSPLSLDNTSVHDHIHP SPVHLKGRVSPRPNLLPTTSFSAAQEETEDSALRMALVEAMLTYLGVNKSNMSVSSSSIA NMSSLNSPQLNEMYSRRPSNASFLMSPHCTPSDISVASSFASPQTQPTMLRILPKEYTIS NKRHNKSKSQDKKKPRAYKEELTPNLDFEDVKKDFAQGIQLKFFKKGTTIVEQNARGKGL FYIISGKVNVTTNSSSSVVSSMSKPEQVSAQSSHKGENPHHTQHLLYSVGSGGIVGYLSS LIGYKSFVNIVAKSDVYVGFLSSATLERLFDKYFLIYLRISDSLTKLLSSRLLKLDHALE WVHLRASETLFSQGDSANGIYVVLNGRLRQLQQQSLSNSNTSSEEVETQNIILGELAQGE SFGEVEVLTAMNRYSTIVAVRDSELARIPRTLFELLALEHPSIMIRVSRLVAKKIVGDRT VPALTGDPLSIKENDFTSLIPPTKASYSSSLSHKPQNITSGTITFRTITILPITSGLPVE AFAMKLVQAFKQVGRTTIGLNQRTTLTHLGRHAFDRLSKLKQSGYFAELEEMYQTVVYIS DTPVKSNWTRTCIAQGDCILLLADARSPSAEIGEYEKLLLNSKTTARTELILLHPERYVE PGLTHKWLRYRPWVHSHHHIQFSLTGTTLMNEGKMHVLNNGALALMDKLIQTEFSRKTQQ NISKLLPDSIKNTVENFSSRFMKSKRQYYTPVHRHKNDFLRLARILSGQAIGLVLGGGGA RGISHLGVIQAIEEQGIPVDVIGGTSIGSFVGGLYAKDYDLVPIYGRVKKFAGRISSIWR MLTDLTWPVTSYTTGHEFNRGIWKTFGDTRIEDFWIQYYCNSTNITDSVQEIHSFGYAWR YIRASMSLAGLLPPLEENGSMLLDGGYVDNLPVTEMRARGCQTIFAVDVGSADDRTPMEY GDSLNGFWIIFNRWNPFSSHPNIPNMAEIQVRLGYVASVNALEKAKNTPGVVYVRPPIEE YATLDFSKFEEIYHVGVDYGRIFLQGLIDDDKMPYIPGSQETTLNSQVPEFLLHRRNSI

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Q04958 (NTE1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	1679 AA.
Sequence status	Complete.
Protein existence	Evidence 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.8
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.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane
Domain	Repeat Transmembrane Transmembrane helix
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	phosphatidylcholine catabolic process Inferred from mutant phenotype Ref.5. Source: SGD regulation of phospholipid biosynthetic process Inferred from mutant phenotype PubMed 19841481. Source: SGD
Cellular_component	endoplasmic reticulum Inferred from direct assay Ref.3 Ref.5. Source: SGD endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD
Molecular_function	carboxylesterase activity Inferred from direct assay Ref.5. Source: SGD lysophospholipase activity Inferred from direct assay Ref.5. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1679

1679

Lysophospholipase NTE1

PRO_0000172528

Regions

Topological domain

1 – 49

Cytoplasmic Potential

Transmembrane

50 – 70

Helical; Potential

Topological domain

71 – 103

Lumenal Potential

Transmembrane

104 – 124

Helical; Potential

Topological domain

125 – 1679

1555

Cytoplasmic Potential

Domain

1373 – 1537

165

Patatin

Nucleotide binding

803 – 947

145

cNMP 1

Nucleotide binding

943 – 1074

132

cNMP 2

Motif

1404 – 1408

GXSXG

Compositional bias

259 – 297

Asp-rich

Compositional bias

713 – 718

Poly-Ser

Sites

Active site

1406

Amino acid modifications

Modified residue

303

Phosphoserine Ref.12

Modified residue

634

Phosphoserine Ref.7 Ref.10 Ref.11 Ref.12

Modified residue

670

Phosphoserine Ref.11 Ref.12

Modified residue

679

Phosphothreonine Ref.12

Modified residue

680

Phosphoserine Ref.11 Ref.12

Modified residue

682

Phosphoserine Ref.12

Modified residue

803

Phosphothreonine Ref.12

Experimental info

Mutagenesis

1406

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

Sequences

Sequence

Length

Mass (Da)

Tools

Q04958 [UniParc].

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

FASTA

1,679

187,133

        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' referencesShow '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. Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[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]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, MASS SPECTROMETRY. Strain: YAL6B.
[8]	"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.
[9]	"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.
[10]	"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, MASS SPECTROMETRY. Strain: ADR376.
[11]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634; SER-670 AND SER-680, MASS SPECTROMETRY.
[12]	"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-303; SER-634; SER-670; THR-679; SER-680; SER-682 AND THR-803, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z46729 Genomic DNA. Translation: CAA86716.1. BK006946 Genomic DNA. Translation: DAA09838.1.
PIR	S49802.
RefSeq	NP_013652.1. NM_001182418.1.
3D structure databases
ProteinModelPortal	Q04958.
SMR	Q04958. Positions 824-1054.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5949N.
IntAct	Q04958. 15 interactions.
MINT	MINT-653305.
STRING	4932.YML059C.
Proteomic databases
PaxDb	Q04958.
PeptideAtlas	Q04958.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YML059C; YML059C; YML059C.
GeneID	854943.
KEGG	sce:YML059C.
Organism-specific databases
CYGD	YML059c.
SGD	S000004524. NTE1.
Phylogenomic databases
eggNOG	COG0664.
GeneTree	ENSGT00390000002533.
HOGENOM	HOG000048680.
KO	K14676.
OMA	ERPVFHE.
OrthoDB	EOG4QNR48.
Gene expression databases
Genevestigator	Q04958.
GermOnline	YML059C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	2.60.120.10. 5 hits.
InterPro	IPR016035. 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]
Pfam	PF00027. cNMP_binding. 2 hits. PF01734. Patatin. 1 hit. [Graphical view]
SMART	SM00100. cNMP. 1 hit. [Graphical view]
SUPFAM	SSF52151. Acyl_Trfase/lysoPlipase. 1 hit. SSF51206. cNMP_binding. 3 hits.
PROSITE	PS00888. CNMP_BINDING_1. False negative. PS00889. CNMP_BINDING_2. False negative. PS50042. CNMP_BINDING_3. 2 hits. PS01237. UPF0028. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977998.

Entry information

Entry name

NTE1_YEAST

Accession

Primary (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:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIII

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

Uncharacterized protein families (UPF)

List of uncharacterized protein family (UPF) entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents