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Q0CNC7 (NTE1_ASPTN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
ORF Names:ATEG_04807
OrganismAspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome]
Taxonomic identifier341663 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length1527 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Catalytic activity

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

Enzyme regulation

Inhibited by organophosphorus esters By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the NTE family.

Contains 2 cyclic nucleotide-binding domains.

Contains 1 patatin domain.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
   DomainRepeat
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionlysophospholipase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15271527Lysophospholipase nte1
PRO_0000295313

Regions

Topological domain1 – 6969Cytoplasmic By similarity
Transmembrane70 – 9021Helical; Potential
Topological domain91 – 11222Lumenal By similarity
Transmembrane113 – 13321Helical; Potential
Topological domain134 – 15271394Cytoplasmic By similarity
Domain1224 – 1388165Patatin
Nucleotide binding685 – 804120cNMP 1
Nucleotide binding846 – 966121cNMP 2
Motif1255 – 12595GXSXG
Compositional bias11 – 5242Ser-rich
Compositional bias55 – 6410Poly-Pro

Sites

Active site12571 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0CNC7 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: BD39EDE81FBB46C5

FASTA1,527168,858
        10         20         30         40         50         60 
MADDGGPFPL SSSLLHASSS TTILESSSSS LLATSSPAIA ATFSSFSGRP SSYLPPPPLP 

        70         80         90        100        110        120 
PPAPSTMVGW IGWVFSFVFQ VIPSILYWAI TFCTITLPTW LFTLFSMSLT FTMNFTTLLL 

       130        140        150        160        170        180 
IALAIVSTVS WFIRYRFLNM YSRLPPEPQR KEPQLDLFPD VQEGDSKPGL ANYLDEFLSA 

       190        200        210        220        230        240 
IKVFGYLERP VFHELTRTMQ TRKLIAGETL LLEEEKGFCL VVDGLVQIFV KSIRDGKSPA 

       250        260        270        280        290        300 
DHELNLAGDD STDEEGQNVD GRQGYQLLTE VKNGASMSSL FSILSLFTED IQLRTSESLS 

       310        320        330        340        350        360 
SSVSSVGPNL ARVPDSSPSS PRGLVHSPVP VREPSESGHN LPTNGEFLPT VPPLHLEESR 

       370        380        390        400        410        420 
GTPDHDHQPE SRTRPGKKRR KSVHPDIVAR AMVDTTIAII PASAFRRLTR VYPRATAHIV 

       430        440        450        460        470        480 
QVILTRLQRV TFATAHSYLG LTNEVLGIEK QMTKFTTYDL PNDMRGAALD RLKDKFIKER 

       490        500        510        520        530        540 
DRLGHEEVTK GIALHNPSAG RRRRSSSFLR KEAALQARMA TTPRRPTATG SQENMSFHDR 

       550        560        570        580        590        600 
DAAGVSPGDL LSTIQLSRFG PRYEHLAPKI YSPLAEKEQS PFRPPTMRGP ASPFHRKESL 

       610        620        630        640        650        660 
DEDALFRESI LDCIMKALGL TSSTRDILRK SSHNSGDASP KLLSYDSRRQ KAVFSNNAFG 

       670        680        690        700        710        720 
FIDPYEGSVD GETESMMSMS VTSAGGTSPI VNLREELRND IEIVYFPQGS VLVEQGERHP 

       730        740        750        760        770        780 
GLYYVIDGFL DVGMPACDKG DDLVGATRPA HGEEAFPTLK RTTTASSRTS SVAPGGSDSK 

       790        800        810        820        830        840 
RRRQSRKSLY LIKPGGIQGY VGSVASYRSY TDVLAKTDVY VGFLPRASLE RIAERYPIAL 

       850        860        870        880        890        900 
LTLAKRLTSL LPRLLLHIDF ALEWVQVNAG QVIYHQGDES DAIYLVLNGR LRSVLEGTDG 

       910        920        930        940        950        960 
KMNVVGEYGQ GESVGELEVM TESTRPATLH AIRDTELAKF PRSLFNSLAQ EHPGITIQVS 

       970        980        990       1000       1010       1020 
KLIAQRMRDL VERPMTEKGA EHGAGSIKTA TSTVNLRTVS ILPVTAGVPV VEFGHRLLNA 

      1030       1040       1050       1060       1070       1080 
LHQIGVTNGV TSLNQAAILN HLGRHAFTKM GKLKLSQYLA DLEEKYGMVL YIADTNVNSP 

      1090       1100       1110       1120       1130       1140 
WTQTCITQAD CILLVGLAES TPSIGEYERF LLGMKTTSRK ELVLLHADRY CPPGLTRRWL 

      1150       1160       1170       1180       1190       1200 
KNRVWINGGH HHIQMGFRLT AEPSHPQTKR FGTVLKERVQ VIQAEIQKYT SRRIHQTALY 

      1210       1220       1230       1240       1250       1260 
SAQTPFKGDF HRLARRLCGR SVGLVLGGGG ARGIAQVGVI KALEEAGIPI DIIGGTSIGA 

      1270       1280       1290       1300       1310       1320 
FNGALYARDA DVVPMYGRAK KFAGRMGSMW RFALDLTYPT VSYTTGHEFN RGIFKTFGDS 

      1330       1340       1350       1360       1370       1380 
QIEDFWLEFY CNTTNISKSR PEYHSSGYVW RYVRASMTLA GLIPPICDEG SMLLDGGYID 

      1390       1400       1410       1420       1430       1440 
NLTVPHMKGL GADVIFAVDV GSIDDNTPQG YGDSLSGFWA TINRWNPFSS VPNPPTLSEI 

      1450       1460       1470       1480       1490       1500 
QARLAYVSSF ENLEQAKTTP GCLYMRPPID PYGTLDFGKF DEIYQVGYKY GKEYLEKLKN 

      1510       1520 
EGTLPLREET EEKKKLQRTL APRRASI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476599 Genomic DNA. Translation: EAU35254.1.
RefSeqXP_001213985.1. XM_001213985.1.

3D structure databases

ProteinModelPortalQ0CNC7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33178.CADATEAP00008780.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADATEAT00008780; CADATEAP00008780; CADATEAG00008780.
GeneID4320057.

Phylogenomic databases

eggNOGCOG0664.
HOGENOMHOG000048680.
OMASPWTQTC.
OrthoDBEOG70W3NS.

Family and domain databases

Gene3D2.60.120.10. 5 hits.
InterProIPR016035. Acyl_Trfase/lysoPLipase.
IPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
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. 5 hits.
SSF52151. SSF52151. 1 hit.
PROSITEPS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNTE1_ASPTN
AccessionPrimary (citable) accession number: Q0CNC7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: October 17, 2006
Last modified: February 19, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families