ID   NTE1_COCIM              Reviewed;        1575 AA.
AC   Q1DLC7; J3K1S9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 3.
DT   03-MAY-2023, entry version 92.
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=CIMG_08886;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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   ---------------------------------------------------------------------------
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; GG704913; EAS30140.3; -; Genomic_DNA.
DR   RefSeq; XP_001241723.2; XM_001241722.2.
DR   AlphaFoldDB; Q1DLC7; -.
DR   SMR; Q1DLC7; -.
DR   STRING; 246410.Q1DLC7; -.
DR   GeneID; 4560690; -.
DR   KEGG; cim:CIMG_08886; -.
DR   VEuPathDB; FungiDB:CIMG_08886; -.
DR   InParanoid; Q1DLC7; -.
DR   OMA; SSGYVWR; -.
DR   OrthoDB; 5303733at2759; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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: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; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 3.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR001423; LysoPLipase_patatin_CS.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR14226:SF29; NEUROPATHY TARGET ESTERASE SWS; 1.
DR   PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 3.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 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..1575
FT                   /note="Lysophospholipase NTE1"
FT                   /id="PRO_0000295317"
FT   TOPO_DOM        1..99
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..151
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        173..1575
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1272..1436
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          568..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1276..1281
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1303..1307
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1423..1425
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        20..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1305
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1423
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         737..856
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         894..1014
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1575 AA;  173384 MW;  1E6B773A6278AC61 CRC64;
     MNLTTTMPAA VAPDPPAQLA VSSRSLSDSS DAAGASRTSS SCRASSPSHC PTHAWNPDPP
     PSSLQPVFSF SPSLPPPCPS PAISSCPPNT LSPPNLLQGI VSQLAMASYI GRLLLYLFQV
     VPSLLYWAIT FTTITVPTAL FTLFSMSLTF TMNFTTLLII VLLLVSTVSW FIRYRFLNIY
     SRLPPEPQRK EPEIDLFPDS QDGDSKPGLS NYLDEFLSAI KVFGYLERPV FHELTRTMQT
     RKLIAGETLL LEEEKGFCLV VDGLVQIFVK SIQERDDDRD GWQLDEAVED SVDEDDEIRR
     RGHQGYQLLT EVKNGASMSS LFSILSLFSE DIKLRHNEDM ESSSSSFNNV PAPDSNPMSP
     ALLLESPTRV SFPDQRDIPT QPSADTLPKV SPLALEGSPG PFEHDPKPRG HRRKRPSRPK
     RAKSVHPDIL ARAMVDTTIA IIPASAFRRL TRVYPKATAH IIQVILTRLQ RVTFATAHSY
     LGLTTEVLSI EQQMTKYTSF DLPNHLRGAA LDKLKSKFTK EKERLGPEDG TKGIALHNPA
     LNRRRRSSSS LRKDAALHAK LTAVRGKGSA SNPIRYGDHE STGVSPGDLL STIQLSRFGP
     RYGSERLNGR SVFYDAASGM KTPAGGPPSP LATPGQPLFR FPAQNVTFQR QDSLDQDAIF
     RESILDCMMK ALGLTGSTQD ALRKTHNSGD ASPHLVSYDS RRQKAVFNNA FGFIDPYDGF
     GDGDSESLMS MSVTSAGGTS PVHNLRTELQ DEIEIVYFPK GSVLIEQGEH NPGLYYVIDG
     FLDVGIPVNE KGEDLIGSSR RPTAEDILLP ITGNASRVSS TLGTAHNQRK KASRRSLYMV
     KPGGVEGYIG SITSYRSFTD VTAKTDVYVG FLPRAVLERI ADRYPLVMLT MAKRLTTVLP
     RLILHIDFAL EWVQVNAGQV IHHQGDESDA IYIVLNGRLR AVLDKGDGKV SVLGEYGQGD
     SVGELEVMTE STRPGTLHAI RDTELAKFPR TLFNSLAQEH PGITIQISKL IAQRMRHIID
     NPLEKGSDKG SPDSAKPTTS TLNLRTVAVL PVTAGIPVVE FGNRLLNAFN QVGVTNGVTS
     LHQADILNHL GRHAFSKMGK LKLAQYLADL EERYGMVLYV GDTSVNAPWT QTCIAQADCI
     LLVALAEGSP AIGEYERFLL GMKTTARKEL VLLHAERYSQ PGLTRQWLKN RMWINGGHHH
     IQMAFRLTAE PVHPETKRLG AVLKQRVQVI QAEIQKYTSR RIRQTPVYST STPVKGDFHR
     LARRLCGKSV GLVLGGGGAR GIAHIGVIKA LEEAGIPIDI IGGTSIGSFI GALYARDADV
     VPAYGRAKKF SGRMASMWRF ALDLTYPSAS YTTGHEFNRG IFKAFGNSHI EDFWLEFYCN
     TTNISKSRLE FHSSGYAWRY VRASMSLAGL IPPLCDEGNM LLDGGYVDNL TVARMKSLGA
     DVIFAVDVGA IDDNTPQGYG DSLSGFWALV NRWNPFSSLP NPPTLSEIQA RLAYVSSVDA
     LERAKSTPGC LYMRPPIDAF GTLDFAKFDE IYQVGYKFGK EFLDRLKNEG GLPIQEETEE
     KKKLRRTMAP RRASI
//