ID   PLPL_LODEL              Reviewed;         815 AA.
AC   A5DUA8;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Patatin-like phospholipase domain-containing protein LELG_00944;
DE            EC=3.1.1.-;
GN   ORFNames=LELG_00944;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: Probable lipid hydrolase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PLPL family. {ECO:0000305}.
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DR   EMBL; CH981524; EDK42766.1; -; Genomic_DNA.
DR   RefSeq; XP_001528424.1; XM_001528374.1.
DR   AlphaFoldDB; A5DUA8; -.
DR   STRING; 379508.A5DUA8; -.
DR   PRIDE; A5DUA8; -.
DR   EnsemblFungi; EDK42766; EDK42766; LELG_00944.
DR   GeneID; 5235808; -.
DR   KEGG; lel:LELG_00944; -.
DR   VEuPathDB; FungiDB:LELG_00944; -.
DR   eggNOG; KOG2214; Eukaryota.
DR   HOGENOM; CLU_009031_2_2_1; -.
DR   InParanoid; A5DUA8; -.
DR   OMA; DMNKWLR; -.
DR   OrthoDB; 425613at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006641; P:triglyceride metabolic process; IEA:UniProt.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR021771; Triacylglycerol_lipase_N.
DR   Pfam; PF11815; DUF3336; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..815
FT                   /note="Patatin-like phospholipase domain-containing protein
FT                   LELG_00944"
FT                   /id="PRO_0000295560"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          360..552
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          41..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          753..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           391..395
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        72..95
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..796
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        797..815
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        393
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        539
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   815 AA;  92518 MW;  01D2109F3CE1FD7B CRC64;
     MMVGSSSEKK IPLYDEQNDY INEDHISEFA KALVWQDYDD VSTTAPTTPL NGPLDMGDLS
     LLGGELGNGS DDVVVGDDDD DDDDDDDDDD DDDDDKTKYS SPQLKAAQEI NDEATEIGAV
     PATTKPDLIS SKNDWFPINS ENLNPNSKRT KFAKSSKSSK SKSTSPIRAL QNEFRNSASF
     TLLRWPILTF VVIWVTILGF LYLAVRVYVA LLEYFFTWTG ERKRLRDKLR QSTTYKEWIE
     NAKELDKYLG LDKWATNPKF SYYDSQTVQL TINKLKKARL NNSMPELLIL LQGCLKRNFA
     GIENRQLYSH MYYGTKNLVQ DYYKEVVICI NKVIESNEIN SETKYKFFKT VLQNFGKSAL
     CLSGGACFAY THFGIAKALL DQDLLPNIIS GTSGGGLIAA LLCTRTNEEL KKLLVPQLAR
     KITACEDPWY VWIPRLLKTG ARFDSVAWAR KSNFFTKGST TFEEAMAMTG RKLNISTVPA
     DPHSPVILCN DITSPHCIIW STLLASSAVP GILNPVVLMM KNPVNGAVVP FSLGSKWRDG
     SLRTDIPIDA LNTYYHVNFT IVSQVNPHIS LFFFAPKGTV GRPVSMSKRK TAKEKFASFR
     GGFIATALEQ LFRLEIKKWL QIVKSLDLLP HVLQQDWSNV WLQNFTGTIT IWPRNRLIDF
     WYILSDPNEK QMEEIITKGE RSMYPKILFI KNRLSIEKAI EKGRKTSTAE LRETQMNVAL
     ASDDDEDYVP SDYSLAKFKD RIGVTSKDFD MLGSTLRDDD ADADVDEDDN EDEDEEDEDE
     NDYEEYDVED LDDPYESDAF DPHIVLTKER RHTVY