NTE1_ASPCL
ID NTE1_ASPCL Reviewed; 1528 AA.
AC A1C9L6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 82.
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=ACLA_055880;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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=EAW13540.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DS027048; EAW13540.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001274966.1; XM_001274965.1.
DR AlphaFoldDB; A1C9L6; -.
DR SMR; A1C9L6; -.
DR STRING; 5057.CADACLAP00005041; -.
DR EnsemblFungi; EAW13540; EAW13540; ACLA_055880.
DR GeneID; 4707103; -.
DR KEGG; act:ACLA_055880; -.
DR eggNOG; KOG2968; Eukaryota.
DR OrthoDB; 253518at2759; -.
DR Proteomes; UP000006701; 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..1528
FT /note="Lysophospholipase nte1"
FT /id="PRO_0000295309"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..115
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..1528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 1225..1389
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 238..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1507..1528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1229..1234
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1256..1260
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1376..1378
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 372..388
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1507..1521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1258
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1376
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 686..805
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 1528 AA; 168937 MW; D5982DE223A05DD9 CRC64;
MADGNLLGSS TSLTALLPTP SSASLSASLS SSSLPVSPFL APAPTTAITA SIASLSAQPP
PPLPATPATM AGWIGWVFSF FFQFIPSVLY SVITFTTITL PTWLFTLFSM SLTFTMNFTT
LLLILLAVVS TLGWFVRYRF LNMYSRLPPE PQRKEPQIDL FPDVQGGDSK PGLANYLDEF
LSAIKVFGYL ERPVFHELTR TMQTRKLIAG ETLMLEEEKG FCLVVDGLVQ IFVKSTRDGK
SGSDDELHHL GAESSDEEHH IDGKQGYQLL TEVKNGASMS SLFSILSLFT EDIQVWDSQS
STSSSSSIAM RAARVPDSTP NSPRGGMDSP TPIFRDVPDP VSLVNENGDL PLVPPLHLEE
SPIPPTNHAH DRRQHDHRKH HGRKHRKSVH PDIVARAMVD TTIAIIPASA FRRLTRVYPR
ATAHIVQVIL TRLQRVTFAT AHSYLGLSNE VLGIEKQMTK FTTYDLPNNM RGTALDRLKD
KFIKERDRLG TEEVTKGIAL HNPSAGRRRR SSSFMRKDAV LHAKMMSPKR AATVITSDNS
YDHDSAGVSP GDLLSTIQQS RFGPRYEQPT PRLRSPLAEK ENSHFRLPAM QARNAFHRKE
SLDEDALFRE CILDCIMKAI GLTSSTGEVL RKSSHSGEAS PKLLSYDSRR QKAVFSNNAF
GFIDPYEGSG DGETESMMSM SVTSAGGTSP VTSLREELRN DIEIVYFPQG SVLVEQGERH
PGLYYVIDGF LDVGMPVVDK GEDLVGVSKP ATAREPFPTL KRTTTASSIK PSATAANDPR
RRKQSRKSLY LIKPGGIQGY VGAVASYRSY TDVVAKTDVY VGFLPRASLE RIAERYPIAL
LTLAKRLTSL LPRLLLHIDF ALEWVQVNAG QVIYHQGDES DAIYLVLNGR LRSVLESADN
KLTVIGEYGQ GESVGELEVM TESTRPATLH AIRDTELAKF PRSLFNSLAQ EHPGITIQVS
KLIAQRMRDL VERPVTEKGA ERSSAGGVQT ATSTLNLRTV GILPVTAGVP VVEFGNRLLH
ALHQIGVVNG VTSLNQSAIL NHLGRHAFSK MGKLKLAQYL ADLEEKYGMV LYIADTNVNS
PWTQTCITQA DCILLVGLAE SSPSIGEYER FLLGMKTTAR KELVLLHSER YCPPGLTRRW
LKNRVWINGG HHHIQMAFRL TAEPSHPETK RFGTVLKQRV QVLQAEIQKY TSRRIRQTPL
YSAQTPFKGD FHRLARRLCG RAVGLVLGGG GARGIAHVGV IKALEEAGIP VDIIGGTSIG
SFIGALYARD ADVVPMYGRA KKFAGRMGSM WRFALDLTYP TISYTTGHEF NRGIFKTFGD
SQIEDFWLEF YCNTTNISKS RQEYHSSGYV WRYVRASMSL AGLIPPICDE GSMLLDGGYI
DNLTVDHMKG LGADVIFAVD VGSIDDNTPQ GYGDSLSGFW VAFNRWNPFS SCPNPPTLSE
IQARLAYVSS IDNLERAKIT PGCLYMRPPI DAYGTLEFGK FDEIYQVGYK FGKQFLEKLK
NEGSLPLPEE TEEEKKLLRT MAPRRASI
