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 16-JUN-2009, entry version 17. 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=ACLA_055880; OS Aspergillus clavatus. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; OC mitosporic Trichocomaceae; Aspergillus. OX NCBI_TaxID=5057; 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., 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DS027048; EAW13540.1; ALT_INIT; Genomic_DNA. DR BRENDA; 3.1.1.5; 18580. 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 1528 Lysophospholipase nte1. FT /FTId=PRO_0000295309. FT TOPO_DOM 1 72 Cytoplasmic (By similarity). FT TRANSMEM 73 93 Potential. FT TOPO_DOM 94 115 Lumenal (By similarity). FT TRANSMEM 116 136 Potential. FT TOPO_DOM 137 1528 Cytoplasmic (By similarity). FT DOMAIN 1225 1389 Patatin. FT NP_BIND 686 805 cNMP 1. FT NP_BIND 846 966 cNMP 2. FT MOTIF 1256 1260 GXSXG. FT COMPBIAS 21 33 Poly-Ser. FT COMPBIAS 59 64 Poly-Pro. FT COMPBIAS 298 307 Poly-Ser. FT ACT_SITE 1258 1258 By similarity. 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 //