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   16-JUN-2009, entry version 18.
DE   RecName: Full=Lysophospholipase nte1;
DE            EC=3.1.1.5;
DE   AltName: Full=Neuropathy target esterase homolog;
DE   AltName: Full=Intracellular phospholipase B;
GN   Name=nte1; ORFNames=NFIA_030460;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL
OS   181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Neosartorya.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   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,
CC       elevated temperatures, or when choline is present in the growth
CC       medium (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2-lysophosphatidylcholine + H(2)O =
CC       glycerophosphocholine + a carboxylate.
CC   -!- ENZYME REGULATION: Inhibited by organophosphorus esters (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the NTE family.
CC   -!- SIMILARITY: Contains 2 cyclic nucleotide-binding domains.
CC   -!- SIMILARITY: Contains 1 patatin domain.
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DR   EMBL; DS027693; EAW20613.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001262510.1; -.
DR   GeneID; 4588979; -.
DR   KEGG; nfi:NFIA_030460; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR   InterPro; IPR000595; cNMP_bd.
DR   InterPro; IPR018488; cNMP_bd_CS.
DR   InterPro; IPR001423; Lysophospholipase_patatin_CS.
DR   InterPro; IPR002641; Patatin.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00100; cNMP; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; FALSE_NEG.
DR   PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS01237; UPF0028; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Endoplasmic reticulum; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Membrane; Repeat; Transmembrane.
FT   CHAIN         1   1523       Lysophospholipase nte1.
FT                                /FTId=PRO_0000295325.
FT   TOPO_DOM      1     66       Cytoplasmic (By similarity).
FT   TRANSMEM     67     87       Potential.
FT   TOPO_DOM     88    109       Lumenal (By similarity).
FT   TRANSMEM    110    130       Potential.
FT   TOPO_DOM    131   1523       Cytoplasmic (By similarity).
FT   DOMAIN     1220   1384       Patatin.
FT   NP_BIND     681    800       cNMP 1.
FT   NP_BIND     841    961       cNMP 2.
FT   MOTIF      1251   1255       GXSXG.
FT   COMPBIAS     15     50       Ser-rich.
FT   COMPBIAS     53     61       Poly-Pro.
FT   COMPBIAS    294    301       Poly-Ser.
FT   ACT_SITE   1253   1253       By similarity.
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
//