ID   A0A074XN84_AURPU        Unreviewed;       788 AA.
AC   A0A074XN84;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Patatin-like phospholipase domain-containing protein {ECO:0000256|RuleBase:RU362055};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU362055};
GN   ORFNames=M438DRAFT_313803 {ECO:0000313|EMBL:KEQ86988.1};
OS   Aureobasidium pullulans EXF-150.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ86988.1, ECO:0000313|Proteomes:UP000030706};
RN   [1] {ECO:0000313|EMBL:KEQ86988.1, ECO:0000313|Proteomes:UP000030706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ86988.1,
RC   ECO:0000313|Proteomes:UP000030706};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
CC   -!- FUNCTION: Lipid hydrolase. {ECO:0000256|RuleBase:RU362055}.
CC   -!- FUNCTION: Probable lipid hydrolase. {ECO:0000256|ARBA:ARBA00002682}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362055}; Single-
CC       pass membrane protein {ECO:0000256|RuleBase:RU362055}.
CC   -!- SIMILARITY: Belongs to the PLPL family.
CC       {ECO:0000256|RuleBase:RU362055}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KL584977; KEQ86988.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074XN84; -.
DR   STRING; 1043002.A0A074XN84; -.
DR   HOGENOM; CLU_009031_1_2_1; -.
DR   OrthoDB; 154387at2759; -.
DR   Proteomes; UP000030706; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006641; P:triglyceride metabolic process; IEA:UniProt.
DR   CDD; cd07230; Pat_TGL4-5_like; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR021771; Triacylglycerol_lipase_N.
DR   PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR   PANTHER; PTHR14226:SF10; TRIACYLGLYCEROL LIPASE 4-RELATED; 1.
DR   Pfam; PF11815; DUF3336; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362055};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|RuleBase:RU362055};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU362055};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030706}.
FT   DOMAIN          231..428
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REGION          15..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          633..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   788 AA;  87243 MW;  6382C58A615F5E99 CRC64;
     MDFFHDSLVL PGSSSARLAP NNATANNSSS ASRATRSNGG STRISPSLIR ALRDPYYLVG
     ARPVESGSHR QRAEGPQLDD SEWRRQVLNL KVSQAKCYTD WFSAASELDT LEGRDAWKEE
     EECDEYDTAL LKARLQELED ARISCDAKRM LFLARTSLTR DLGNMGDLRL YKHCRVGTKA
     LIERYISAAL EMLETIVDMC SPANKKDTYV DVREVYEQLL SARQAFGRSA LLLSGGGTLG
     MNHIGVLKTL FEAHLLPRII SGASAGSIVA AVLCTKTDDE IPQVLRDFCY GDLDVFEKEG
     EPENVLKKVF RFCTKGALFD ISNLVRVMKD LLGDMTFQEA YNRTRRILNI GVSTASLYEL
     PRLLNYITAP NVMIWSAVAT SCSVPFIFSP AQLLAKDPRT GLEVPWDQSP QRWIDGSVDN
     DLPMTRLAEM FNVNHFIVSQ VNPHVVPFLE RDDEIANFGS QTSRFSLAAG PGWLRSVANL
     AKGEALHRMH VLAELGVLPT TMSKVRSVLS QRYSGDITIL PEVSYTQFPR VLMNPTPDFM
     SRAMLSGETA TWPKLSQVRN HCAIELALDV AVQKVRYGLV FSPSQIDLRL NAFAFTAAAN
     ESQIRHARRA SHGSPPESER PHLLAVPPTY SLRKPSAAHT SHASSIFHAP KHSGHDDFAS
     GQETAVDSED ADWSDSSLEP HSPRQTPKLW PPVFLSRSQP VTPNLHSKMY NTSSPALVLT
     RLNKDGYGGD EDSGALVASP MEYKSVFQNA RPSYAGEEGY DVSGTRGMVR RKRSLTTGFR
     GLWPPGRS
//