NTE1_ASPTN
ID NTE1_ASPTN Reviewed; 1527 AA.
AC Q0CNC7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Lysophospholipase nte1;
DE EC=3.1.1.5;
DE AltName: Full=Intracellular phospholipase B;
DE AltName: Full=Neuropathy target esterase homolog;
GN Name=nte1; ORFNames=ATEG_04807;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Intracellular phospholipase B that catalyzes the double
CC deacylation of phosphatidylcholine (PC) to glycerophosphocholine
CC (GroPCho). Plays an important role in membrane lipid homeostasis.
CC Responsible for the rapid PC turnover in response to inositol, elevated
CC temperatures, or when choline is present in the growth medium (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC -!- ACTIVITY REGULATION: Inhibited by organophosphorus esters.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
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DR EMBL; CH476599; EAU35254.1; -; Genomic_DNA.
DR RefSeq; XP_001213985.1; XM_001213985.1.
DR AlphaFoldDB; Q0CNC7; -.
DR SMR; Q0CNC7; -.
DR STRING; 341663.Q0CNC7; -.
DR EnsemblFungi; EAU35254; EAU35254; ATEG_04807.
DR GeneID; 4320057; -.
DR VEuPathDB; FungiDB:ATEG_04807; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_1_1; -.
DR OMA; FTMNFTT; -.
DR OrthoDB; 253518at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IEA:EnsemblFungi.
DR GO; GO:0071071; P:regulation of phospholipid biosynthetic process; IEA:EnsemblFungi.
DR CDD; cd00038; CAP_ED; 2.
DR Gene3D; 2.60.120.10; -; 3.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 3.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS51635; PNPLA; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1527
FT /note="Lysophospholipase nte1"
FT /id="PRO_0000295313"
FT TOPO_DOM 1..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..112
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..1527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 1224..1388
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 240..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1228..1233
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1255..1259
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1375..1377
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 299..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1257
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1375
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 685..804
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT BINDING 846..966
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
SQ SEQUENCE 1527 AA; 168858 MW; BD39EDE81FBB46C5 CRC64;
MADDGGPFPL SSSLLHASSS TTILESSSSS LLATSSPAIA ATFSSFSGRP SSYLPPPPLP
PPAPSTMVGW IGWVFSFVFQ VIPSILYWAI TFCTITLPTW LFTLFSMSLT FTMNFTTLLL
IALAIVSTVS WFIRYRFLNM YSRLPPEPQR KEPQLDLFPD VQEGDSKPGL ANYLDEFLSA
IKVFGYLERP VFHELTRTMQ TRKLIAGETL LLEEEKGFCL VVDGLVQIFV KSIRDGKSPA
DHELNLAGDD STDEEGQNVD GRQGYQLLTE VKNGASMSSL FSILSLFTED IQLRTSESLS
SSVSSVGPNL ARVPDSSPSS PRGLVHSPVP VREPSESGHN LPTNGEFLPT VPPLHLEESR
GTPDHDHQPE SRTRPGKKRR KSVHPDIVAR AMVDTTIAII PASAFRRLTR VYPRATAHIV
QVILTRLQRV TFATAHSYLG LTNEVLGIEK QMTKFTTYDL PNDMRGAALD RLKDKFIKER
DRLGHEEVTK GIALHNPSAG RRRRSSSFLR KEAALQARMA TTPRRPTATG SQENMSFHDR
DAAGVSPGDL LSTIQLSRFG PRYEHLAPKI YSPLAEKEQS PFRPPTMRGP ASPFHRKESL
DEDALFRESI LDCIMKALGL TSSTRDILRK SSHNSGDASP KLLSYDSRRQ KAVFSNNAFG
FIDPYEGSVD GETESMMSMS VTSAGGTSPI VNLREELRND IEIVYFPQGS VLVEQGERHP
GLYYVIDGFL DVGMPACDKG DDLVGATRPA HGEEAFPTLK RTTTASSRTS SVAPGGSDSK
RRRQSRKSLY LIKPGGIQGY VGSVASYRSY TDVLAKTDVY VGFLPRASLE RIAERYPIAL
LTLAKRLTSL LPRLLLHIDF ALEWVQVNAG QVIYHQGDES DAIYLVLNGR LRSVLEGTDG
KMNVVGEYGQ GESVGELEVM TESTRPATLH AIRDTELAKF PRSLFNSLAQ EHPGITIQVS
KLIAQRMRDL VERPMTEKGA EHGAGSIKTA TSTVNLRTVS ILPVTAGVPV VEFGHRLLNA
LHQIGVTNGV TSLNQAAILN HLGRHAFTKM GKLKLSQYLA DLEEKYGMVL YIADTNVNSP
WTQTCITQAD CILLVGLAES TPSIGEYERF LLGMKTTSRK ELVLLHADRY CPPGLTRRWL
KNRVWINGGH HHIQMGFRLT AEPSHPQTKR FGTVLKERVQ VIQAEIQKYT SRRIHQTALY
SAQTPFKGDF HRLARRLCGR SVGLVLGGGG ARGIAQVGVI KALEEAGIPI DIIGGTSIGA
FNGALYARDA DVVPMYGRAK KFAGRMGSMW RFALDLTYPT VSYTTGHEFN RGIFKTFGDS
QIEDFWLEFY CNTTNISKSR PEYHSSGYVW RYVRASMTLA GLIPPICDEG SMLLDGGYID
NLTVPHMKGL GADVIFAVDV GSIDDNTPQG YGDSLSGFWA TINRWNPFSS VPNPPTLSEI
QARLAYVSSF ENLEQAKTTP GCLYMRPPID PYGTLDFGKF DEIYQVGYKY GKEYLEKLKN
EGTLPLREET EEKKKLQRTL APRRASI
