NTE1_NEOFI
ID NTE1_NEOFI Reviewed; 1523 AA.
AC A1D9Y2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 85.
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=NFIA_030460;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW20613.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DS027693; EAW20613.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001262510.1; XM_001262509.1.
DR AlphaFoldDB; A1D9Y2; -.
DR SMR; A1D9Y2; -.
DR STRING; 36630.CADNFIAP00002640; -.
DR EnsemblFungi; EAW20613; EAW20613; NFIA_030460.
DR GeneID; 4588979; -.
DR KEGG; nfi:NFIA_030460; -.
DR eggNOG; KOG2968; Eukaryota.
DR OrthoDB; 253518at2759; -.
DR Proteomes; UP000006702; 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; IPR001423; LysoPLipase_patatin_CS.
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.
DR PROSITE; PS01237; UPF0028; 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..1523
FT /note="Lysophospholipase nte1"
FT /id="PRO_0000295325"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..109
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..1523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 1220..1384
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 309..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1502..1523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1224..1229
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1251..1255
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1371..1373
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 328..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..384
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1253
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1371
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 681..800
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT BINDING 841..961
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
SQ SEQUENCE 1523 AA; 168447 MW; 95665818D567EF4B CRC64;
MADGVTLVDS TGLHSFSSSP SLSTSSSSLT AVALSLATSA SAVTASYSIS HLPPPPLPPV
PTTMAGWIGW VFSFFFQVIP SVLYWVITFS TITLPTWLFT LFSMSLTFTM NFTTLLLIVL
AMVSTISWFI RYRFLNMYSR LPPEPQRKEP QVDLFPDVQE GDSKPGLANY LDEFLSAIKV
FGYLERPVFH ELTRTMQTRK LIAGETLMLE EEKGFCLVVD GLVQIFVKSM RDGKSDTDEE
LHHLGAESSD EEHHIDGKQG YQLLTEVKNG ASMSSLFSIL SLFTEDIQLR ENESSGSSSS
SIALRAARVP NSIPTSPRGV MDSPSLGFQD HSDDTSNMIT NGDLPSVPPL HLGESHTPPS
GDQHHQQHHE SRKHSSRKRR KSVHPDIVAR AMVDTTIAII PASAFRRLTR VYPRATAHIV
QVILTRLQRV TFATAHSYLG LSNEVLGIEK QMTKFTTYDL PNNMRGAALD RLKDKFIKER
DRLGSEEVTK GIALHNPSAG RRRRSSSFLR KDAALQVKMM TPRRAATVVT PESAPAEHDT
YGVSPGDLLS TIQSSRFGPR YEQPPAKLQS PLAEKENTHF RLPAMQARHT FRRQDTMDED
ALFRECILDC IMKGIGLTSS TRDALRKSSH SGDASPKLLS YDSRRQKAIF TNNAFGFIDP
YEGSGDGETE SLMSMSVTSA GGTSPVINLR EELRNDIEIV YFPKGSVLVE QGERHPGLYY
VIDGFLDVGV PIVEKGEDLV GVSKPAASKE SFPTLKRTTT ANSIGAGGTA ANDSRRRKQS
RKSLYLIKPG GIQGYVGAVA SYRSYTDVVA KTDVYVGFLP RASLERIAER YPIALLTLAK
RLTSILPRLL LHIDFALEWL QVNAGQVIYH QGDESDAIYL VLNGRLRSVL ESPGNKLAVI
GEYGQGESVG ELEVMTESTR PATLHAIRDT ELAKFPRSLF NSLAQEHPGI TIQVSKLIAQ
RMRDLVERPV TEKGVERSNA GGVQTATSTV NLRTVGILPV TAGVPVVEFG NRLLHALHQV
GVTNGVTSLN QAAILNHLGR HAFSKMGKLK LSQYLADLEE KYGMVLYIAD TNVSSPWTQT
CITQADCILL VGLAESSPSI GEYERFLLGM KTTARKELVL LHSERYCPPG LTRRWLKNRV
WINGGHHHIQ MAFRLTAEPS HPETKRFGTV LKQRVQVLQA EIQKYTSRRI RQTPLYSAQS
PFKGDFHRLA RRLCGRAVGL VLGGGGARGI AHVGVIKALE EAGIPVDIIG GTSIGSFIGA
LYARDADVVP MYGRAKKFAG RMGSMWRFAL DLTYPTVSYT TGHEFNRGIF KTFGDSQIED
FWLEFYCNTT NISKSRPEYH SSGYVWRYVR ASMSLAGLIP PICDEGSMLL DGGYIDNLTV
DHMKGLGADV IFAVDVGSID DNTPQVYGDS LSGFWSVFNR WNPFSSCPNP PTLSEIQARL
AYVSSIDNLE RAKNIPGCLY MRPPIDGYGT LEFGKFDEIY QVGYAFGKQF LEKLKTEGSL
PLPEETEEKK KLQRTMAPRR ASI
