ID M7US60_BOTF1 Unreviewed; 820 AA.
AC M7US60;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Patatin-like phospholipase domain-containing protein {ECO:0000256|RuleBase:RU362055};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU362055};
GN ORFNames=BcDW1_1542 {ECO:0000313|EMBL:EMR89833.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR89833.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
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}.
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DR EMBL; KB707721; EMR89833.1; -; Genomic_DNA.
DR AlphaFoldDB; M7US60; -.
DR STRING; 1290391.M7US60; -.
DR HOGENOM; CLU_009031_1_2_1; -.
DR Proteomes; UP000012045; 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}.
FT DOMAIN 232..429
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 591..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 91721 MW; 27F0623860241B13 CRC64;
MVLFGYLQTP QFCVVNNNNT TATSAKPSNA NEYGHDREKV SEPSVGLFGP ATRILRTGAD
ILNNKLLQVR DGLTEEERSA LRKKEERIQI LNLRMKNAET MEVWRSAAKE LDLLEDNEAW
KLDSLSTDFD AALIEARTKQ MDTARIDCDI KKMLTLVRTT LSRDLGGMGN IRLYKHSHVG
TKVVIERYIE STLDTVRALV ENSKYTLPVG LETKDILEQV VYARQAFGRS ALLLSGGATF
GMNHVGVLKA LFEARLLPRI ISGASAGSIV CAVLCARTDE EIPDVLKEFP HGDLAVFEEN
GNEDGVLDRI RRLLTEGAWI DIKHLTRVMR ELLGDMTFQE AYNRSRRILN ICVSSASVYE
LPRLLNYVTA PNVMIWSAVA ASCSVPLLFS AAELLMKNPL TGETSSWNPT PQRWIDGSVD
NDLPMTRLAE MFNVNHFIVS QVNPHVIPFI AKDEEAIKDT VMKDGSGGPG WVYNLTHLAK
AEALHRMQVL AELGVFPNLV TKCKSILSQK YSGDITILPE INFKDFPRIL KNPTTEFMEQ
ACLSGERATW PKLSRVWNHC AVELELDAAV QKLRARVVFS PSEVNLRRLR AGEGSRQSSG
MGRQRFDNGN LLLMSRDEDG EFSKQDGKRE NSSRPSLRAT ASVLDITKHK ERSHYTVHHS
AQTTPRRTPR LGLENEMFSF PIPSKDMLYI KNQIRDLSSA GETTLSPSSS DADKGSQTDG
STTELEAEEA IYGIASSTSD RQLDLFSRNQ PITAGTDRVL ATSPSIVRNG TEFIYSPTAM
SPAEMRPREE RKSLTEPSSP DWSYKKMFHQ WKEDDMRDAA
//