ID A0A3D8QZU0_9EURO Unreviewed; 1391 AA.
AC A0A3D8QZU0;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Lysophospholipase NTE1 {ECO:0000256|ARBA:ARBA00018317, ECO:0000256|RuleBase:RU362043};
DE EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362043};
DE AltName: Full=Intracellular phospholipase B {ECO:0000256|RuleBase:RU362043};
GN ORFNames=DSM5745_09175 {ECO:0000313|EMBL:RDW67309.1};
OS Aspergillus mulundensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW67309.1, ECO:0000313|Proteomes:UP000256690};
RN [1] {ECO:0000313|EMBL:RDW67309.1, ECO:0000313|Proteomes:UP000256690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW67309.1,
RC ECO:0000313|Proteomes:UP000256690};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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.
CC {ECO:0000256|ARBA:ARBA00024965}.
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 Evidence={ECO:0000256|ARBA:ARBA00000960,
CC ECO:0000256|RuleBase:RU362043};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000256|ARBA:ARBA00006636,
CC ECO:0000256|RuleBase:RU362043}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDW67309.1}.
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DR EMBL; PVWQ01000012; RDW67309.1; -; Genomic_DNA.
DR STRING; 1810919.A0A3D8QZU0; -.
DR OrthoDB; 5303733at2759; -.
DR Proteomes; UP000256690; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 2.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR Gene3D; 2.60.120.10; Jelly Rolls; 3.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR001423; LysoPLipase_patatin_CS.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR14226:SF29; NEUROPATHY TARGET ESTERASE SWS; 1.
DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 2.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 3.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 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 {ECO:0000256|RuleBase:RU362043};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362043};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU362043};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU362043}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000256690};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 555..638
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 710..812
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 1088..1252
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 165..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1369..1391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1391 AA; 154562 MW; 3C69862BC09B59E8 CRC64;
MAVHTLFYEL DVYDEFHYIT IDRAGPSLDH HRLPPEPQRK EPQIDLFPDV QEGDSKPGLA
NYLDEFLSAI KVFGYLERPV FHELTRTMQT KKLIAGETLQ LEEEKGFCLV VDGEVFEVSS
DEEDQARDGR QGYQLLTEVK NGASMSSLFS ILSLFTEDIR LRASEDSQSS MSSVQPSPAR
VPVPFMDSPG GKLNGSPMGV SKHQEDDSST INGDGESLPP VPPLNLGESR TSFYRHNGRS
TSERVHGNRR KSVHPDIVAR AMVDTTIAII PASAFRRLTR LYPRATAHIV QVILTRLQRV
TFATAHSYLG LTDEVLGIEK QMTRFTTYDL PNDIRGSALD RLKDKFLKEK DRLGSEEVTR
GIALHNPYAG RRRRSSSFMR KEAALKAKLP TARRPISFVN SERSPSERDT AGVSPGDLLS
TIQLSRFGPR HEQFTTTPRL HSPLTEKEHS PLRRSSLQRK DSVDEDTLFR ESILDCIMNG
IGLTPRSHDA LRKGSHSGES PKLVSYDSRR QKAVFSNNAF GFMDAYEGSG DAETESMMSM
SVTSAGGTSP IVNLREELLN DIEIVYFPRG SVLVEQGERH PGLYYVIDGF LDVGVQVNDT
GEDLVGTSRP GHAQPEEEPF PTLKRTQTAT SRVATTAAPA NEYKRKRPSR KSLYMIKPGG
MQGYVGAMAS YRSYTDVVAK TDVYVGFLPR ASLERLAERY PIALLTLAKR LTGLLPRLLL
HIDFALEWVQ VNAGQVIYHQ GDESDAIYIT LNGRLRSIHE GKAGKMTVVG EHGQGESVGE
LEVMTESTRP ATLHAIRDTE LAKFPRSLFN SLAQEHTGIT IQVSKLIAQR MRDLVENPMT
EQGEPGNTGS VKTATSTLNL RTVGILPITT GVPVVEFGNR LLNALQQIGV TDGVTSLNQA
AILNHLGRHA FSRMGKLKLS QYLADLEEKY GMVLYIADTN VNSPWTQTCI SQADCILLVG
LAESSPNVGE YERFLLGMKT TARKELVLLH ADRYCPPGVT RKWLKNRVWI NGGHHHIQMA
FRLTAEPSHP QTKRLGTVLK QRVQILQAEI QKYTSRRIRQ TPLYSAQTPF KGDFHRLARR
LCGRAVGLVL GGGGARGIAH VGVIKALEEA GIPVDIVGGT SIGAFIGGLY ARDADVVPMY
GRAKKFAGRM GSMWRFALDL TYPSVSYTTG HEFNRGIFKT FGDSQIEDFW LEFYCNTTNI
SRSRAEYHSS GYVWRYVRAS MSLAGLLPPI CDEGSMLLDG GYIDNLTVAH MKTLGADVIF
AIDVGSIDDN TPQGYGDSLS GMWSVVNRWN PFSSVPNPPT LSEIQARLAY VSSIDNLERA
KNIPGCLYMR PPIDRYGTLE FGNFDEIYQV GYVYGKEFLQ KLKSQGSLPL PEETEEKKKL
QRTLAPRRAS I
//
