NTE1_ASPOR
ID NTE1_ASPOR Reviewed; 1538 AA.
AC Q2UDH2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 87.
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=AO090012000173;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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=BAE60393.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP007161; BAE60393.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q2UDH2; -.
DR SMR; Q2UDH2; -.
DR STRING; 510516.Q2UDH2; -.
DR PRIDE; Q2UDH2; -.
DR VEuPathDB; FungiDB:AO090012000173; -.
DR Proteomes; UP000006564; Chromosome 4.
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..1538
FT /note="Lysophospholipase nte1"
FT /id="PRO_0000295312"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..117
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..1538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 1235..1399
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 242..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1517..1538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1239..1244
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1266..1270
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1386..1388
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 302..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1268
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1386
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 692..811
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT BINDING 856..976
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
SQ SEQUENCE 1538 AA; 169603 MW; F4CE23D63EA35DD7 CRC64;
MATDGGPLAA SSASLDSSLS PLHASPSPSS TYTASSLALS APAIAASFSV ASTFSNSLIP
PPPLPPPTPS TMAGWFGWVF SFFFQVIPSV LYWVITFATI TLPTWLFTLF SMSLTFTMNF
TTLLLIALAI VSTISWFIRY RFLNMYSRLP SEPQRKEPHL DLFPDVQEGD SKPGLANYLD
EFLSAIKVFG YLERPVFHEL TRTMQTRKLI AGETLMLEEE KGFCLVVDGL VQIFVKSMRD
GKPNVDEGSN HMGAESSDED DHRVDGKQGY QLLTEVKNGA SMSSLFSILS LFTEDIQLRA
SEGSSSSASS VGPSTNARVS DSFPASPHGL EDSPRSNFVR DHGDSVAHIS NSNGELLPSV
PPLNLGESHA MPIQEPYPKP RSQPGKRRRK SVHPDIVARA MVDTTIAIIP ASAFRRLTRV
YPRATAHIVQ VILTRLQRVT FATAHSYLGL NNDVLGIEKQ MTKFTTQDLP NEMRGAALDR
LKDKFIKERD RLGPEEIIKG IALHNPFAGR RRRSSSFLRK EAVLHAKMAA QSKRPVSMAS
PEDISGDRES AGPSPGDLLS TIQLSRFGPR YEHLAPKLLS PLTDKENPPF MAPVMHSSPF
HRKKDAVDED ALFRESILDC IMNGIGLTSS TRDVLRKSSH TSGDISPKLL SYDSRRQKAV
FTNNAFGFID PYDSSADGET ESMMSMSMTS AGGTSPIVNL REELRNDIEI VYFPQGSVLV
EQGERHPGLY YVIDGFLDVG IPVSDKGEDL VGGSRPVYGQ PPEEFFPTLK RTTTSSSRVS
GVTSATNDTK RKRQSRKSLY LIKPGGIQGY VGSVASYRSY TDVVAKTDVY VGFLPRSSLE
RIAERYPIAL LTLAKRLTSL LPRLLLHIDF ALEWVQVSAG QVIYHQGDES DAIYLVLNGR
LRSVLEGTDG KITVVGEYGQ GESVGELEVM TESTRPATLH AIRDTELAKF PRSLFNSLAQ
EHPGITIQVS KLIAQRMRDL VELPMPEKGG EHANVGSVKT AASVVNLRTV GILPVTAGVP
VVEFGHRLQN ALHQIGVTNG VTSLNQAAIL NHLGRHAFSK MGKLKLSQYL ADLEEKYGMV
LYIADTNVNS PWTQTCITQA DCILLVGLAE SSPSIGEYER FLLGMKTTAR KELVLLHSER
YCPPGLTRQW LKNRMWINGG HHHIQMGFRL TPEPSHPQAK RLGAVLKQRV QVIQAEIQKY
TSRRIRQTPL YSAQTPFKGD FHRLARRLCG RSVGLVLGGG GARGIAQVGV IKALEEAGIP
IDIIGGTSIG SFIGALYARD ADVVPMYGRA KKFAGRMASM WRFMLDLTYP TTSYTTGHEF
NRGIFKTFGD SQIEDFWLEY YCNTTNISKS RPEFHSSGYT WRYVRASMSL AGLIPPICDE
GSMLLDGGYI DNLTVTHMKG LGADVIFAVD VGSIDDNTPQ GYGDSLSGFW TVLNRWNPFS
ACPNPPTLSE IQARLAYVSS IDNLERAKNT PGCLYMRPPI DPYGTLEFGK FDEIYQVGYA
YGKQYLEKLR SEGSLPLPEE TEEKKKLQRT LAPRRASI
