ID   NTE1_SCHPO              Reviewed;        1316 AA.
AC   Q9USJ4;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=SPCC4B3.04c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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; CU329672; CAB60678.1; -; Genomic_DNA.
DR   PIR; T50444; T50444.
DR   RefSeq; NP_588086.1; NM_001023078.2.
DR   AlphaFoldDB; Q9USJ4; -.
DR   SMR; Q9USJ4; -.
DR   BioGRID; 275976; 2.
DR   STRING; 4896.SPCC4B3.04c.1; -.
DR   iPTMnet; Q9USJ4; -.
DR   MaxQB; Q9USJ4; -.
DR   PaxDb; Q9USJ4; -.
DR   PRIDE; Q9USJ4; -.
DR   EnsemblFungi; SPCC4B3.04c.1; SPCC4B3.04c.1:pep; SPCC4B3.04c.
DR   GeneID; 2539411; -.
DR   KEGG; spo:SPCC4B3.04c; -.
DR   PomBase; SPCC4B3.04c; nte1.
DR   VEuPathDB; FungiDB:SPCC4B3.04c; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   InParanoid; Q9USJ4; -.
DR   OMA; FTMNFTT; -.
DR   PhylomeDB; Q9USJ4; -.
DR   Reactome; R-SPO-6814848; Glycerophospholipid catabolism.
DR   PRO; PR:Q9USJ4; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004622; F:lysophospholipase activity; ISO:PomBase.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0034638; P:phosphatidylcholine catabolic process; ISO:PomBase.
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; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00100; cNMP; 2.
DR   SUPFAM; SSF51206; SSF51206; 3.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 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..1316
FT                   /note="Lysophospholipase NTE1"
FT                   /id="PRO_0000295330"
FT   TOPO_DOM        1..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..61
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        83..1316
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          1011..1176
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          229..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1296..1316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1015..1020
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1042..1046
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1163..1165
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        229..255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1044
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         516..644
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         640..763
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
SQ   SEQUENCE   1316 AA;  147846 MW;  AF7FB587D61CC69D CRC64;
     MDITDRILQN RIVSKVIFFV LRSVTLSLVS VTRFSLFLLS FATITVPKWA YKIVTYSLTI
     QFNFKSLLFL FFVSICVVIL VVRYRYLNKY ARLPHEAPIK EAKLGPDTNI RPSEPRIGFQ
     NYLDEFLSAI SIFGYLEKPV FVELARHIRT QRVAEGNTIY LGEQSSFILV VDGCFQVFTA
     PEKDSAEVVE EAGQPEYRLL TEVSNGAPLS SFFTVLELFT ELIPEATSKE NPFKSTTSSL
     RPGSSTTTEA GANNASKPHM PQPKKARIIA KAKIDTTIAV IPANAFHHLV HKFPNSSAQI
     VQVILTRFQR VTFSTGYEYL GLSDAIFSIE KNFNSLTAYE LPNYIRSDII DDFKKEAMSE
     HLSQASNESF IVLRSKGAQS RLSNQYFSKA FDKEHGNFVS DIDRSTANAG DLLSSTNPHS
     TLLSTSVGPL RKFPLNRSYS REVGDYDISA SFRDGLLQCI FKSLGVFNYE LKEDNDDLCT
     ENDSSEGDSD SLKKVDFLGQ IAMMSATDRE EVKSSIVVST KKSTILEFAK EIEIIFYKKG
     TTIVRQGDHA DGLYYIIDGF LDATCPSKLT FSTSYDTDLG MHSFMIKPGG IVNYQACVSN
     YRSFINVTAR SDVLVGFLPR SCLERIIDQE PLISLTIAKR LISLVPSLLL KLDFAVGWIH
     LNPDQVVYEK NDPSDCVYVV LNGRLRSIED ERGSARTQVD YFNEYGKGDS VGELEMLLNN
     RRSSTLFAIR DSELAKIPET LFNALSLSHP AVGLQLSKII ANRMNLLLNN KSMDGMQHQP
     HEKHSIRTLA IVPSSSTGLL ILFSQKLTSV LSVMGKSVKV LRQSSVLEHL GKHAFSRMGR
     FKLSSYLSDL EDKYDILIYV ADSGVGSAWL QTCIRQADCI YILAEADQNP NIGEYEQHLI
     AMKSTARKEL VLLHPERFCP SGLTRLWLKE RPWVYAHHHV QLRIGLDNEI SQNNEAKVFL
     NIIRAKVQNL HYGFRKYIDW KHLHPVYQAN RAQDSDFARL ARRICGKAIA LVLGGGGARG
     ISQIGILYAL EEAGIPFDII GGTSIGAFNG GLYAWEADLV PMFGRAKKFC GRMANLWRFV
     LDVTYPQAAY TTGHEFNRGI WKTFGEIHIE DFWLPFYANT TNITHSRMDI HSSGYAWRYI
     RASMSLAGLV PPMLSDSGDM LLDGGYMDNL TVSHMQSLGA SSIFAIDVGS EDSREPMHYG
     DTVSGVWALI SRWIPFIPKT SFPSLAEIQS RLTYVTSVAT GEKVKSMPGC FYMRPPVKDF
     PTLEFGSFEK IYNVGYNYGK EYVEKLKTSH KLDDILSPRD TSKRHPKFLS SRRNSL