NTE1_EMENI
ID NTE1_EMENI Reviewed; 1527 AA.
AC Q5BAE9; C8VPA5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
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=AN2481;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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=CBF86943.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA63799.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AACD01000041; EAA63799.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001307; CBF86943.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_660085.1; XM_654993.1.
DR AlphaFoldDB; Q5BAE9; -.
DR SMR; Q5BAE9; -.
DR STRING; 162425.CADANIAP00009202; -.
DR EnsemblFungi; EAA63799; EAA63799; AN2481.2.
DR GeneID; 2875190; -.
DR KEGG; ani:AN2481.2; -.
DR VEuPathDB; FungiDB:AN2481; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_1_1; -.
DR InParanoid; Q5BAE9; -.
DR OrthoDB; 253518at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
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; 2.
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..1527
FT /note="Lysophospholipase nte1"
FT /id="PRO_0000295320"
FT TOPO_DOM 1..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..116
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..1527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 1224..1388
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 299..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1504..1527
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..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..596
FT /note="Basic and acidic 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 682..809
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; 168413 MW; 27E5289D1C9A881A CRC64;
MADSGASVPS PDLPDLDSLH ASLSLPDIPS VAATSLSTSL PAISAKVSGF PSFSSHLPPP
PLLSPPTPTT MVGWIGWVFS LVFQTIPSVL YWVITFSTIT LPTWLFTLFS MSLTFTMNFT
TLLLIVLGLV STVSWFIRYR FLNMYSRLPP EPQRKEPQLD LFPDVQEGDS KPGLANYLDE
FLSAIKVFGY LERPVFHELT RTMQTRKLIA GETLQLEEEK GFCLVVDGLV QIFVKSMRSG
KHGLNGEVIE GSSDEDDQAR DGKQGYQLLT EVKNGASMSS LFSILSLFTE DIRLRASEGS
SSSMSSVQPS PARTTPAPFL DSPGEMLNGS PMVLPRDSEV DSSAINGEAE PLPPVPPLHL
GESRASSYHP NGQSTASERV RGNRRKSVHP DIVARAMVDT TIAIIPASAF RRLTRLYPRA
TAHIVQVILT RLQRVTFATA HSYLGLTNEV LGIEKQMTKF TTYDLPNDIR GAALDRLKDK
FLKEKDRLGS EEVTRGIALH NPYAGRRRRS MSFVRKEAAL KAKMPLPKRP NSLINPERPF
HGYDTAGVSP GDLLSTIQLS RFGPRHDQFA TTPRLHSPLT EKERSPLRRS SLQRKDSVDE
DALFRESILD CIMKGIGLTP SSHNALRKGS HSGELSPKLV SYDSRRQKAV FSNNAFGFID
AYEGSGDGDT ESMMSMSVTS AGGTSPIVYL REDLLNDIEI VYFPKGAVLV EQGERHPGLY
YVIDGFLDVG VQVNEKGDDL VGASRPGHAQ PDEELFPTLK RTQTATSRGA TAAAPINESK
RKKPSRKSLY MIKPGGMQGY VGAMASYRSY TDVVAKTDVY VGFLPRASLE RLAERYPIAL
LTLAKRLTGL LPRLLLHIDF ALEWVQVNAG QVIYHQGDES DAIYITLNGR LRSVHEGKGG
KMTVVGEHGQ GESVGELEVM TESTRPATLH AIRDTELAKF PRSLFNSLAQ EHTGITIQVS
KLIAQRMRDL VENPMTEQGE PGNTGSVKTA TSTLNLRTVG ILPITTGVPV VEFGNRLLSA
LQQIGVTDGV TSLNQAAILN HLGRHAFSRM GKLKLSQYLA DLEEKYGMVL YIADTNVNSP
WTQTCISQAD CILLVGLAES SPNVGEYERF LLGMKTTARK ELVLLHADRY CPPGLTRKWL
KNRVWINGGH HHIQMAFRLT AEPSHPQTKR LGTVLKQRVQ ILQAEIQKYT SRRIRQTPIY
SAQTPFKGDF HRLARRLCGR AVGLVLGGGG ARGIAHVGVI KALEEAGIPV DIVGGTSIGA
FIGGLYARDA DVVPMYGRAK KFAGRMGSIW RFALDLTYPS VSYTTGHEFN RGIFKTFGDS
QIEDFWLEFY CNTTNISRSR AEYHSSGYVW RYVRASMSLA GLLPPICDEG SMLLDGGYID
NLTVAHMKTL GADVIFAIDV GSIDDNTPQG YGDSLSGMWS VINRWNPFSS IPNPPTLSEI
QARLAYVSSI DNLERAKNIP GCLYMRPPID RYGTLEFGNF DEIYQVGYAY GKEYLQKLKS
QGSLPLPEEN EEKKKLQRTL APRRASI
