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Database: UniProt
Entry: G7XPB9_ASPKW
LinkDB: G7XPB9_ASPKW
Original site: G7XPB9_ASPKW 
ID   G7XPB9_ASPKW            Unreviewed;       752 AA.
AC   G7XPB9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Patatin-like phospholipase domain-containing protein {ECO:0000256|RuleBase:RU362055};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU362055};
GN   ORFNames=AKAW_06779 {ECO:0000313|EMBL:GAA88665.1};
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA88665.1};
RN   [1] {ECO:0000313|EMBL:GAA88665.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA88665.1};
RX   PubMed=22045919; DOI=10.1128/EC.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
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. {ECO:0000256|ARBA:ARBA00006104,
CC       ECO:0000256|RuleBase:RU362055}.
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DR   EMBL; DF126464; GAA88665.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7XPB9; -.
DR   STRING; 1033177.G7XPB9; -.
DR   VEuPathDB; FungiDB:AKAW_06779; -.
DR   eggNOG; KOG2214; Eukaryota.
DR   InParanoid; G7XPB9; -.
DR   Proteomes; UP000006812; 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; cd07232; Pat_PLPL; 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:SF66; TRIACYLGLYCEROL LIPASE PTL2; 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   Coiled coil {ECO:0000256|SAM:Coils};
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}; Membrane {ECO:0000256|RuleBase:RU362055};
KW   Transmembrane {ECO:0000256|RuleBase:RU362055};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362055}.
FT   TRANSMEM        89..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362055"
FT   DOMAIN          277..468
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          170..197
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        628..649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..710
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   752 AA;  85578 MW;  D0F1465D42BEFEBF CRC64;
     MNGAEKSAAG DTYDPSTIPD YDREFINPDD LRQFELALTD QGASPLVALN DWRPIYQRVR
     RERGRRKEPR RTKDETREGV LYTVLKWPFL FTVFGWITAL AFAYTLTRVY IFLYEQWVTW
     RGRRQSLRRQ LRAQTNYPDW QKAARALDDH LGNQRWKEID EYAYYDHLTI SNLVKQLKKV
     RREVERERRE KRRGSGQSPA AEELCTLLEA CVKNNFAGVE NPRLYSEAYS GTKDLVQEYI
     DELHACIQLV ADSKGIGSEE KLQHFKHLDT NFGRTALCLS GGATFAYYHF GVVRALLDNG
     VLPEIITGTS GGALVAALVA TRTDEELKQL LVPALAHRIR ACQEGFPTWV WRWWRTGARF
     DTLEWARQCS WFCRGSTTFR EAYERTGRIL NVSCVPSDPH SPTILANYLT SPNCVIWSAV
     LASAAVPGIL NPVVLMTKKR DGTLAPYSFG HKWKDGSLRT DIPIKALNLH FNVNFTIVSQ
     VNPHINLFFF SSRGTVGRPV THRKGRGWRG GFLGSAIEQY IKLDMNKWLR VLRHLELLPR
     PMGQDWSEIW LQKFSGTVTI WPKTVPSDFF HILSDPNPER LARMLRVGQQ SAFPKLQFIK
     NRLKIEIAVV KSLQKFAHAG GRPISPAPSR WRQNNDPDNH YNPSPRTATD PLNERLDHNL
     PGRRGDNVNI TFGEGGGSGE DAHLLDGSLS ENSSNESAGR PTSSASSSRL LRVPEHRRGS
     TGSSIFEEMR RQSAVFFDDV DMYGDDEALR PG
//
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