ID   NTE1_COCIM              Reviewed;        1569 AA.
AC   Q1DLC7;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   16-JUN-2009, entry version 21.
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=CIMG_08886;
OS   Coccidioides immitis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; mitosporic Onygenales; Coccidioides.
OX   NCBI_TaxID=5501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RA   Birren B.W., Lander E.S., Galagan J.E., Devon K., Nusbaum C., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Kodira C.D.,
RA   Zeng Q., Yandava C., Alvarado L., Oleary S., Orbach M.J., Galgiani J.,
RA   Mandel M.A., Kellner E.M.;
RT   "Annotation of the Coccidioides immitis RS genome.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SEQUENCE CAUTION:
CC       Sequence=EAS30140.1; Type=Erroneous gene model prediction;
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DR   EMBL; CH476729; EAS30140.1; ALT_SEQ; Genomic_DNA.
DR   BRENDA; 3.1.1.5; 97654.
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   1569       Lysophospholipase NTE1.
FT                                /FTId=PRO_0000295317.
FT   TOPO_DOM      1     93       Cytoplasmic (By similarity).
FT   TRANSMEM     94    114       Potential.
FT   TOPO_DOM    115    145       Lumenal (By similarity).
FT   TRANSMEM    146    166       Potential.
FT   TOPO_DOM    167   1569       Cytoplasmic (By similarity).
FT   DOMAIN     1266   1430       Patatin.
FT   NP_BIND     731    850       cNMP 1.
FT   NP_BIND     888   1008       cNMP 2.
FT   MOTIF      1297   1301       GXSXG.
FT   COMPBIAS     41     88       Pro-rich.
FT   ACT_SITE   1299   1299       By similarity.
SQ   SEQUENCE   1569 AA;  172722 MW;  026AEFA28D8B2B2B CRC64;
     MPAAVAPDPP AQLAVSSRSL SDSSDAAGAS RTSSSCRASS PSHCPTHAWN PDPPPSSLQP
     VFSFSPSLPP PCPSPAISSC PPNTLSPPNL LQGIVSQLAM ASYIGRLLLY LFQVVPSLLY
     WAITFTTITV PTALFTLFSM SLTFTMNFTT LLIIVLLLVS TVSWFIRYRF LNIYSRLPPE
     PQRKEPEIDL FPDSQDGDSK PGLSNYLDEF LSAIKVFGYL ERPVFHELTR TMQTRKLIAG
     ETLLLEEEKG FCLVVDGLVQ IFVKSIQERD DDRDGWQLDE AVEDSVDEDD EIRRRGHQGY
     QLLTEVKNGA SMSSLFSILS LFSEDIKLRH NEDMESSSSS FNNVPAPDSN PMSPALLLES
     PTRVSFPDQR DIPTQPSADT LPKVSPLALE GSPGPFEHDP KPRGHRRKRP SRPKRAKSVH
     PDILARAMVD TTIAIIPASA FRRLTRVYPK ATAHIIQVIL TRLQRVTFAT AHSYLGLTTE
     VLSIEQQMTK YTSFDLPNHL RGAALDKLKS KFTKEKERLG PEDGTKGIAL HNPALNRRRR
     SSSSLRKDAA LHAKLTAVRG KGSASNPIRY GDHESTGVSP GDLLSTIQLS RFGPRYGSER
     LNGRSVFYDA ASGMKTPAGG PPSPLATPGQ PLFRFPAQNV TFQRQDSLDQ DAIFRESILD
     CMMKALGLTG STQDALRKTH NSGDASPHLV SYDSRRQKAV FNNAFGFIDP YDGFGDGDSE
     SLMSMSVTSA GGTSPVHNLR TELQDEIEIV YFPKGSVLIE QGEHNPGLYY VIDGFLDVGI
     PVNEKGEDLI GSSRRPTAED ILLPITGNAS RVSSTLGTAH NQRKKASRRS LYMVKPGGVE
     GYIGSITSYR SFTDVTAKTD VYVGFLPRAV LERIADRYPL VMLTMAKRLT TVLPRLILHI
     DFALEWVQVN AGQVIHHQGD ESDAIYIVLN GRLRAVLDKG DGKVSVLGEY GQGDSVGELE
     VMTESTRPGT LHAIRDTELA KFPRTLFNSL AQEHPGITIQ ISKLIAQRMR HIIDNPLEKG
     SDKGSPDSAK PTTSTLNLRT VAVLPVTAGI PVVEFGNRLL NAFNQVGVTN GVTSLHQADI
     LNHLGRHAFS KMGKLKLAQY LADLEERYGM VLYVGDTSVN APWTQTCIAQ ADCILLVALA
     EGSPAIGEYE RFLLGMKTTA RKELVLLHAE RYSQPGLTRQ WLKNRMWING GHHHIQMAFR
     LTAEPVHPET KRLGAVLKQR VQVIQAEIQK YTSRRIRQTP VYSTSTPVKG DFHRLARRLC
     GKSVGLVLGG GGARGIAHIG VIKALEEAGI PIDIIGGTSI GSFIGALYAR DADVVPAYGR
     AKKFSGRMAS MWRFALDLTY PSASYTTGHE FNRGIFKAFG NSHIEDFWLE FYCNTTNISK
     SRLEFHSSGY AWRYVRASMS LAGLIPPLCD EGNMLLDGGY VDNLTVARMK SLGADVIFAV
     DVGAIDDNTP QGYGDSLSGF WALVNRWNPF SSLPNPPTLS EIQARLAYVS SVDALERAKS
     TPGCLYMRPP IDAFGTLDFA KFDEIYQVGY KFGKEFLDRL KNEGGLPIQE ETEEKKKLRR
     TMAPRRASI
//