NTE1_COCIM
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-AUG-2022, entry version 88.
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}.
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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 PRIDE; Q1DLC7; -.
DR EnsemblFungi; EAS30140; EAS30140; CIMG_08886.
DR GeneID; 4560690; -.
DR KEGG; cim:CIMG_08886; -.
DR VEuPathDB; FungiDB:CIMG_08886; -.
DR InParanoid; Q1DLC7; -.
DR OMA; FTMNFTT; -.
DR OrthoDB; 253518at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
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: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; 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; IPR001423; LysoPLipase_patatin_CS.
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.
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
