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Protein

Lysophospholipase NTE1

Gene

NTE1

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

Functioni

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.3 Publications

Catalytic activityi

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

Enzyme regulationi

Positively regulated by SEC14. Inhibited by organophosphorus esters in the order phenyl saligenin phosphate (PSP) > phenyldipentyl phosphinate (PDPP) = diisopropyl fluorophosphate (DFP) > and paraoxon (PXN).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1406NucleophilePROSITE-ProRule annotation1
Active sitei1524Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi803 – 947cNMP 1Add BLAST145
Nucleotide bindingi943 – 1074cNMP 2Add BLAST132

GO - Molecular functioni

  • lysophospholipase activity Source: SGD

GO - Biological processi

  • phosphatidylcholine catabolic process Source: SGD
  • regulation of phospholipid biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:G3O-32654-MONOMER.
YEAST:G3O-32654-MONOMER.
ReactomeiR-SCE-6814848. Glycerophospholipid catabolism.

Chemistry databases

SwissLipidsiSLP:000000073.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysophospholipase NTE1 (EC:3.1.1.5)
Alternative name(s):
Intracellular phospholipase B
Neuropathy target esterase homolog
Gene namesi
Name:NTE1
Ordered Locus Names:YML059C
ORF Names:YM9958.03C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YML059C.
SGDiS000004524. NTE1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 49CytoplasmicSequence analysisAdd BLAST49
Transmembranei50 – 70HelicalSequence analysisAdd BLAST21
Topological domaini71 – 103LumenalSequence analysisAdd BLAST33
Transmembranei104 – 124HelicalSequence analysisAdd BLAST21
Topological domaini125 – 1679CytoplasmicSequence analysisAdd BLAST1555

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1406S → A: Loss of esterase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001725281 – 1679Lysophospholipase NTE1Add BLAST1679

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei300PhosphoserineCombined sources1
Modified residuei312PhosphoserineCombined sources1
Modified residuei632PhosphoserineCombined sources1
Modified residuei634PhosphoserineCombined sources1
Modified residuei653PhosphoserineCombined sources1
Modified residuei661PhosphoserineCombined sources1
Modified residuei670PhosphoserineCombined sources1
Modified residuei680PhosphoserineCombined sources1
Modified residuei739PhosphoserineCombined sources1
Modified residuei803PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ04958.
PRIDEiQ04958.
TopDownProteomicsiQ04958.

PTM databases

iPTMnetiQ04958.

Interactioni

Protein-protein interaction databases

BioGridi35107. 25 interactors.
DIPiDIP-5949N.
IntActiQ04958. 16 interactors.
MINTiMINT-653305.

Structurei

3D structure databases

ProteinModelPortaliQ04958.
SMRiQ04958.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1373 – 1537PNPLAPROSITE-ProRule annotationAdd BLAST165

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1377 – 1382GXGXXGPROSITE-ProRule annotation6
Motifi1404 – 1408GXSXGPROSITE-ProRule annotation5
Motifi1524 – 1526DGA/GPROSITE-ProRule annotation3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi259 – 297Asp-richAdd BLAST39
Compositional biasi713 – 718Poly-Ser6

Sequence similaritiesi

Belongs to the NTE family.Curated
Contains 2 cyclic nucleotide-binding domains.PROSITE-ProRule annotation
Contains 1 PNPLA (patatin-like phospholipase) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000002533.
HOGENOMiHOG000048680.
InParanoidiQ04958.
KOiK14676.
OMAiSPWTQTC.
OrthoDBiEOG092C0BAH.

Family and domain databases

Gene3Di2.60.120.10. 5 hits.
InterProiIPR016035. 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]
PfamiPF00027. cNMP_binding. 1 hit.
PF01734. Patatin. 1 hit.
[Graphical view]
SMARTiSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 4 hits.
SSF52151. SSF52151. 1 hit.
PROSITEiPS50042. CNMP_BINDING_3. 2 hits.
PS51635. PNPLA. 1 hit.
PS01237. UPF0028. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04958-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSMNCTTNN TNNTGQNTKN SLGSSFNSSN YTSYRFQTCL TDQIISEAQT
60 70 80 90 100
WSLSSLFNFS WVVSYFVMGA SRMIFRYGWY LATLSLLRIP KWIFFKLHHV
110 120 130 140 150
QFTLSFWLIL FALAVIVFVT YTIMKERILS QYKRLTPEFL PLENTGKSGS
160 170 180 190 200
SANINAASTQ SANAPPAIGS STTGASSIID SKKHSLKDGN ENETFLSSYL
210 220 230 240 250
DQFLSAIKIF GYLEKPVFHD LTKNMKTQKM DEGEILLLDS TIGFAIVVEG
260 270 280 290 300
TLQLYHEVDH SDKDHGDETD HSDTDGLDDQ DRDEEDEEED DDIDNYDTKS
310 320 330 340 350
CSSNLIDEED ESVGYIHLKN GLGNFQLLNT VKPGNPLTSL VSILNLFTHS
360 370 380 390 400
MSSYGNSNFP SELSSPIDTT VSVNNMFCSS EQNFSNTDSM TNSTNSFPTF
410 420 430 440 450
PSSMPKLVAR AATDCTIGII PPQSFAKLTA KYPRSASHII QMVLTKLYHV
460 470 480 490 500
TFQTAHDYLG LTKEIMDIEV LLNKSIVYEL PYYLKEAVIR KFKTVDKSSG
510 520 530 540 550
SADLEPKPKN SNASSKLKKP PKAKPSDGII QSLKIANANA NTSSNSLSLK
560 570 580 590 600
PEFTHHPSSR HVVLGSRDQF NPGDLLSNVP LSRTMDILSP NPIHNNNRNK
610 620 630 640 650
SNGINTSTSN QHKRSSRSSS NNASVHSKKF SSLSPELRNA QLSTSPLSLD
660 670 680 690 700
NTSVHDHIHP SPVHLKGRVS PRPNLLPTTS FSAAQEETED SALRMALVEA
710 720 730 740 750
MLTYLGVNKS NMSVSSSSIA NMSSLNSPQL NEMYSRRPSN ASFLMSPHCT
760 770 780 790 800
PSDISVASSF ASPQTQPTML RILPKEYTIS NKRHNKSKSQ DKKKPRAYKE
810 820 830 840 850
ELTPNLDFED VKKDFAQGIQ LKFFKKGTTI VEQNARGKGL FYIISGKVNV
860 870 880 890 900
TTNSSSSVVS SMSKPEQVSA QSSHKGENPH HTQHLLYSVG SGGIVGYLSS
910 920 930 940 950
LIGYKSFVNI VAKSDVYVGF LSSATLERLF DKYFLIYLRI SDSLTKLLSS
960 970 980 990 1000
RLLKLDHALE WVHLRASETL FSQGDSANGI YVVLNGRLRQ LQQQSLSNSN
1010 1020 1030 1040 1050
TSSEEVETQN IILGELAQGE SFGEVEVLTA MNRYSTIVAV RDSELARIPR
1060 1070 1080 1090 1100
TLFELLALEH PSIMIRVSRL VAKKIVGDRT VPALTGDPLS IKENDFTSLI
1110 1120 1130 1140 1150
PPTKASYSSS LSHKPQNITS GTITFRTITI LPITSGLPVE AFAMKLVQAF
1160 1170 1180 1190 1200
KQVGRTTIGL NQRTTLTHLG RHAFDRLSKL KQSGYFAELE EMYQTVVYIS
1210 1220 1230 1240 1250
DTPVKSNWTR TCIAQGDCIL LLADARSPSA EIGEYEKLLL NSKTTARTEL
1260 1270 1280 1290 1300
ILLHPERYVE PGLTHKWLRY RPWVHSHHHI QFSLTGTTLM NEGKMHVLNN
1310 1320 1330 1340 1350
GALALMDKLI QTEFSRKTQQ NISKLLPDSI KNTVENFSSR FMKSKRQYYT
1360 1370 1380 1390 1400
PVHRHKNDFL RLARILSGQA IGLVLGGGGA RGISHLGVIQ AIEEQGIPVD
1410 1420 1430 1440 1450
VIGGTSIGSF VGGLYAKDYD LVPIYGRVKK FAGRISSIWR MLTDLTWPVT
1460 1470 1480 1490 1500
SYTTGHEFNR GIWKTFGDTR IEDFWIQYYC NSTNITDSVQ EIHSFGYAWR
1510 1520 1530 1540 1550
YIRASMSLAG LLPPLEENGS MLLDGGYVDN LPVTEMRARG CQTIFAVDVG
1560 1570 1580 1590 1600
SADDRTPMEY GDSLNGFWII FNRWNPFSSH PNIPNMAEIQ VRLGYVASVN
1610 1620 1630 1640 1650
ALEKAKNTPG VVYVRPPIEE YATLDFSKFE EIYHVGVDYG RIFLQGLIDD
1660 1670
DKMPYIPGSQ ETTLNSQVPE FLLHRRNSI
Length:1,679
Mass (Da):187,133
Last modified:November 1, 1997 - v1
Checksum:i550FFCD4ACAF8E25
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46729 Genomic DNA. Translation: CAA86716.1.
BK006946 Genomic DNA. Translation: DAA09838.1.
PIRiS49802.
RefSeqiNP_013652.1. NM_001182418.1.

Genome annotation databases

EnsemblFungiiYML059C; YML059C; YML059C.
GeneIDi854943.
KEGGisce:YML059C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46729 Genomic DNA. Translation: CAA86716.1.
BK006946 Genomic DNA. Translation: DAA09838.1.
PIRiS49802.
RefSeqiNP_013652.1. NM_001182418.1.

3D structure databases

ProteinModelPortaliQ04958.
SMRiQ04958.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35107. 25 interactors.
DIPiDIP-5949N.
IntActiQ04958. 16 interactors.
MINTiMINT-653305.

Chemistry databases

SwissLipidsiSLP:000000073.

PTM databases

iPTMnetiQ04958.

Proteomic databases

MaxQBiQ04958.
PRIDEiQ04958.
TopDownProteomicsiQ04958.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYML059C; YML059C; YML059C.
GeneIDi854943.
KEGGisce:YML059C.

Organism-specific databases

EuPathDBiFungiDB:YML059C.
SGDiS000004524. NTE1.

Phylogenomic databases

GeneTreeiENSGT00390000002533.
HOGENOMiHOG000048680.
InParanoidiQ04958.
KOiK14676.
OMAiSPWTQTC.
OrthoDBiEOG092C0BAH.

Enzyme and pathway databases

BioCyciMetaCyc:G3O-32654-MONOMER.
YEAST:G3O-32654-MONOMER.
ReactomeiR-SCE-6814848. Glycerophospholipid catabolism.

Miscellaneous databases

PROiQ04958.

Family and domain databases

Gene3Di2.60.120.10. 5 hits.
InterProiIPR016035. 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]
PfamiPF00027. cNMP_binding. 1 hit.
PF01734. Patatin. 1 hit.
[Graphical view]
SMARTiSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 4 hits.
SSF52151. SSF52151. 1 hit.
PROSITEiPS50042. CNMP_BINDING_3. 2 hits.
PS51635. PNPLA. 1 hit.
PS01237. UPF0028. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNTE1_YEAST
AccessioniPrimary (citable) accession number: Q04958
Secondary accession number(s): D6VZB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 139 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 521 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. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: 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.