NTE1_CANAL
ID NTE1_CANAL Reviewed; 1386 AA.
AC Q5A368; A0A1D8PTQ9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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; OrderedLocusNames=CAALFM_CR08300CA;
GN ORFNames=CaO19.13754, CaO19.6396;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017630; AOW31511.1; -; Genomic_DNA.
DR RefSeq; XP_716236.1; XM_711143.2.
DR AlphaFoldDB; Q5A368; -.
DR SMR; Q5A368; -.
DR BioGRID; 1225170; 1.
DR STRING; 237561.Q5A368; -.
DR PRIDE; Q5A368; -.
DR GeneID; 3642076; -.
DR KEGG; cal:CAALFM_CR08300CA; -.
DR CGD; CAL0000194621; orf19.13754.
DR VEuPathDB; FungiDB:CR_08300C_A; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_1_1; -.
DR InParanoid; Q5A368; -.
DR OMA; FTMNFTT; -.
DR OrthoDB; 253518at2759; -.
DR PRO; PR:Q5A368; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProt.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 2.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
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; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS51635; PNPLA; 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..1386
FT /note="Lysophospholipase NTE1"
FT /id="PRO_0000295314"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..65
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..1386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 1081..1245
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 394..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1085..1090
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1112..1116
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1232..1234
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1114
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1232
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 577..701
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT BINDING 697..821
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
SQ SEQUENCE 1386 AA; 155704 MW; 30459D16F3477170 CRC64;
MGPEFEDSIP LVHSDNRTTT IYSVYIIISD IFSFVQWLLF KVLNLIIIDS PAFVLRLLSK
NFEINLHLSS ILATLIGVSV VTYLVIRYKF LTGYSHSNDQ KEGAGKKGIH PASSKVFVGK
SKQDKKPSNY LDEFLLAIKV FGYLDKAVFH ELTKSMTTQK LSHEEILCLD ESLGFSIVVE
GVAQVYTKKS KENSSKYKQR YFEEIEEERD EFLILGDKQY QLLNEVKSGA PLSSLFSTLD
LFRPRNKNEE MALTPNDEDG NSVVALNMDY LSKSEPATDS KLSNSDDDEN GQDYPEIIVR
PKKSHNNGTI TIAIIPHTAF ERVQSKYPKA TSHIVTMVLT RLYKVTMSTV QNYLGLTSEI
LKSEIKLNEE NATSLPRYFV DGLLERLNKK EEAEAEAENL PKKLKHHHRN QLQRTTSRYV
SLDSKVKSNH PGDLLSSVPI SRSEFQKKVL PKSSTTSLSD GDNKRMNFTD EMEETEENSL
RVAIIENIFK MVGIEETNGI VERTGYFQSL SSSTSSSIVG LDSLNQSIMS GATTPTTKRS
HPVFNNQGSL MNTINLAELR KPSTAENSTL PKLSGKKRLL SDMNIKDAFA KSLEIKYIGP
DSTIVSQNSA ITGLYYVIDG SLEIYNRSAD VSAPNRYIYT VESGGIAGYL TSVVGFRSMV
TIKTPKKTGA VVAYIPKNDY NKLLDKYYFL QLPVALKLKN LLSKQILTID YALEWCHIPA
GEVLCSQGDL ANGFHVVLSG RFRVVRSTNK NTEKEDVEVL GEYGHGESIG EVEVLTASRR
SNTLIAVRDS ETARIPRSLF EMLSNENPSI MVSVSRLVAS KVLASQYQPR ERNFITSTTS
QESFTSANYK TITILPTVSG LPVRQFAEKL VQALRQIGRN VIALDQASIL THLGRHAFDE
SLARLKLSGY FAYLEEEYET IVYICDTPVQ SNWTSTCISQ GDCILLLADA EDDSTTIGEY
EQLLVKLKTT ARTDLCLLHQ DKVVRAGSTS PWLKNRIWVQ GHHHIQMKFE QGANVLPHKK
SFISDLAAKL SQNKAIKSTF EATKQHIKWY VKENDQSKVL KIYKDDFMRL ARILSNEAVG
LVLGGGGSRG ISHVGVVTSL ERHGIPVDII GGTSIGSFVG GLYAKEYNIV SIYAMAKKFS
KRISSVWRML FDLTYPVTSY ITGYEFNRGI WKVFGFAEIE DFWIKYFCNS ANITNSTMDI
HEKGYAWRFI RASMSLAGLL PPIAFNGCML LDGGYLDNLP VNEMKKRGVK HIIAVDVGSV
DDRTPMNYGD TLSGFWVLLN RWNPFSSHPN IPTMMDIQMR LTYVSSVNAL EEAKRTPGVY
YLRPPIDPYA TLDFGKFDEI YKVGLKYADD LFADWKSKGK FPRIAGLVEK KKDGEEKKIL
YRRNSI