ID   PLPL_YARLI              Reviewed;         818 AA.
AC   Q6C8W4;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Patatin-like phospholipase domain-containing protein YALI0D16379g;
DE            EC=3.1.1.-;
GN   OrderedLocusNames=YALI0D16379g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382130; CAG81089.1; -; Genomic_DNA.
DR   RefSeq; XP_502898.1; XM_502898.1.
DR   AlphaFoldDB; Q6C8W4; -.
DR   STRING; 4952.CAG81089; -.
DR   EnsemblFungi; CAG81089; CAG81089; YALI0_D16379g.
DR   GeneID; 2911293; -.
DR   KEGG; yli:YALI0D16379g; -.
DR   VEuPathDB; FungiDB:YALI0_D16379g; -.
DR   HOGENOM; CLU_009031_2_2_1; -.
DR   InParanoid; Q6C8W4; -.
DR   OMA; DMNKWLR; -.
DR   Proteomes; UP000001300; Chromosome D.
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..818
FT                   /note="Patatin-like phospholipase domain-containing protein
FT                   YALI0D16379g"
FT                   /id="PRO_0000295566"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          398..589
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           429..433
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        431
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        576
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   818 AA;  93855 MW;  027699976823B11D CRC64;
     MLKLKFRWNK PDDGPRVKRQ KSQQLTLDSP EGSETSSRPG GGYDNDRDVN GTFKRPWDIT
     KIPGYNQTYV NEASLDKFAA YLKEEEVPVE SSTPVSSEEM LPLEPVQKEY ITSKHDWTPV
     FSVLKNNNSV NKRKMSHTAL KSDFKHYLDM YDKEEKRRRG KSKKDKEGSE GDKTKTKEPK
     ELVRKSVFSS ILGVFSIFSK TKDGRKLKRD EIGEGIGFWL MRWPALFFIG MWLLFLTTIY
     ASVRVLVAGY ENILTWRGKR AKLRKVLRGA RTYEQWVQAA QDLDVELGNA EWRENPKFGY
     YDHVTISKLT KMVRKLRLQD QAEDLSNILQ GCIKNNFAGT ESSTLYSQTY YGTKKVVEQW
     NEELGKAVTY VLESPKIDDE EKRDLFRLYS KNFGKSALCL SGGGCFAYLH FGIVKAMLDQ
     DLLPQIISGT SGGALIAALA CTRTDEELRQ ILVPELAYKI TACWEPFPKW VFRWWRTGAR
     FDSVDWARRS CWFTLGDMTF KEAYQRTGRI LNVSTVPADP HSPVILCNYI TSPDCLIWSA
     LLASAAVPGI LNPVMLMNKT KSGDIVPFSF GSKWKDGSLR TDIPVDALNT YFNVNCSIVS
     QVNPHIALFF YAPRGTVGRP VSHRKGKGWR GGFLGAALES MIKLEIRKWL KFIKAVELLP
     RFVDQDWTNV WLQRFSGSVT LWPKIHLADF WHILGDPWPE KMEDLLYRGQ QCAFPKLLFL
     KHRMNIEKRI RNGRQATRHR KRKLEETDVC DLVRKTFSES DPDSDVKHSF VFPALMAPRS
     AGTDISSSNS DYDHEPQWEM DEGDSFLTAD EEYPTTIL