ID D5GMX7_TUBMM Unreviewed; 1422 AA.
AC D5GMX7;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Lysophospholipase NTE1 {ECO:0000256|ARBA:ARBA00018317, ECO:0000256|RuleBase:RU362043};
DE EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362043};
DE AltName: Full=Intracellular phospholipase B {ECO:0000256|RuleBase:RU362043};
GN ORFNames=GSTUM_00010985001 {ECO:0000313|EMBL:CAZ85870.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ85870.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ85870.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ85870.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(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.
CC {ECO:0000256|ARBA:ARBA00024965}.
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 Evidence={ECO:0000256|ARBA:ARBA00000960,
CC ECO:0000256|RuleBase:RU362043};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000256|ARBA:ARBA00006636,
CC ECO:0000256|RuleBase:RU362043}.
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DR EMBL; FN430360; CAZ85870.1; -; Genomic_DNA.
DR RefSeq; XP_002841679.1; XM_002841633.1.
DR STRING; 656061.D5GMX7; -.
DR EnsemblFungi; CAZ85870; CAZ85870; GSTUM_00010985001.
DR GeneID; 9183438; -.
DR KEGG; tml:GSTUM_00010985001; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_1_1; -.
DR InParanoid; D5GMX7; -.
DR OMA; SSGYVWR; -.
DR OrthoDB; 5303733at2759; -.
DR Proteomes; UP000006911; 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:0034638; P:phosphatidylcholine catabolic process; IEA:EnsemblFungi.
DR GO; GO:0071071; P:regulation of phospholipid biosynthetic process; IEA:EnsemblFungi.
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; 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; 2.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 2.
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.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU362043};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362043};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU362043};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU362043};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362043};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362043};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362043}.
FT TRANSMEM 81..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362043"
FT DOMAIN 654..749
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 762..864
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 1117..1281
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 278..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1422 AA; 156850 MW; 2B07A620538061D7 CRC64;
MASPSFNSAV FESAVSPVSS EPSGALPTIS SQDTQSIFWL SASLAYSIVY LLQRIFFWVI
SFSTYTLPTW LFTLFSTSLT FTMNFTTLLI IFLIFGSIVS WAVRYRLLYN YNRLPHEPQR
KEPQIDLFPD SQEGDSKPGF SSYLDEFLSA IKVFGYLERP VFHELTRSMQ TRKLIAGETL
LLEEEKGFCI VVDGLVQVFV KASRDVGNMA AAASGPGYQL LTEVKNGAPM SSLFTILSLF
TEDVKLRHED EDESGPVSTS SSMVNLHAAG DLAHFEAERN PAGLPPGRSA DSGRFHLPPV
PPLSLSGDFT RSSSRPVTPH DQQPPRPQRP RIKKSKSVHP DIVARATVDT TIAVIPASAF
RRLTRIYPKA TAHIVQVILT RFQRVTFLTG YRYLGLTAEV LRTEKFMNRY TMYELPNHLR
GEPLERLKEK FEKEQERAEP EDSMKGIVLH NPDVSSGKRR RSSSSLRKEA VIHARLAAAR
GQPSPALDTA PSPFRDNRGK FKGQFEQNHP TGQLAPFSQG WTMSASSMGL DTPMPMTEKA
FNPFAQRAAQ KFKADGPSEN EDSAFREAVL ECMFKAIGLT GSAVNVRSGT ESGEQSPRLV
SYDAKRQKAV FSNAFGYIDP IEGDGETESA ASTSGSGAST GGFVNVGISG VHAELKGEVE
IVFFPKGSVL VEQGERNPGL YYVIDGFLDA SIPVDEKTEN SRKSLFMVKP GGIAGYIGSV
SSYRSFIDVT AKTDVYVGFL PRAALERIVE RHPVVLLTMA KRLTSLLPRL ILHIDFALEW
LQVNAGQVIY HQEDESDAIY IVLNGRLRAV QEDEKGGMRV VGEFGQGESV GELEVMTETT
RPATLHAIRD TEVARFPKSL FNSLALEHPG ITIQISKIIA SRMRALIDDP LSEQRRGADR
SRNAPARKIS STMNLRTVCV LPVTSGVPVS EFAHRLSTAL QQISTPNGVT VLNQAAILNH
LGRHAFSRMG KLKLQGYLAD LEEKYGMVIY VADTSVNAPW TQTCISQADS ILLVGLAEGS
PAIGEYERFL VGMKTTARKE LVLLHSERYC PSGLTRQWLK NRMWVNGGHH HIQMSFRTTP
EPVNTQMRSA PIYSAGTPVK SDFHRLARRL CGKSIGLVLG GGGARGISQV GVIRALEEAG
IPIDIVGGTS IGAFVGALYS RDADIVPVLG RAKKFAGRMA SLWRFVLDLT YPSVSYTTGH
EFNRGIFKTF GNSQIEDFWL EFYCNTTSIS KSRMEIHTSG YAWRYIRASM SLAGLLPPLC
DEGEMLLDGG YVDNLTVAHM KSLGADVIFA VDVGSIDDNT PQEFGDSLSG FWAFWNRWNP
FSPHPNPPTL AEIQARLAYV SSVDALERAK LIPGCIYMRP PIDPYGTLDF AKFNEIYNVG
YEYGKKFLEE MKGKGVLPPV APGVADGKRG FRRTMAPRRA SI
//
