ID A0A0C7MTP0_9SACH Unreviewed; 849 AA.
AC A0A0C7MTP0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Patatin-like phospholipase domain-containing protein {ECO:0000256|RuleBase:RU362055};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU362055};
GN ORFNames=LALA0_S01e18140g {ECO:0000313|EMBL:CEP60752.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP60752.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP60752.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP60752.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lipid hydrolase. {ECO:0000256|RuleBase:RU362055}.
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; LN736360; CEP60752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7MTP0; -.
DR STRING; 1245769.A0A0C7MTP0; -.
DR HOGENOM; CLU_009031_4_0_1; -.
DR OrthoDB; 154387at2759; -.
DR Proteomes; UP000054304; 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; 1.
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:UP000054304}.
FT DOMAIN 224..424
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 645..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 94819 MW; 0734835C018147A1 CRC64;
MVKGEFSLNG EPVDITQRLI HRYYDALWAA KNDVDLNGSS SANENANNLS EGDDCYSDDA
SGGTFRKLAS IVKRMFSRDY ERNVLIEKVT QEKQHATSYE EWLAAALRLD ELTRTNEWKA
REESVLYDYK FIQTHTQNMR QARLDKDYAQ LLYLIRTTWI RNLGNMGNVN LYRHSHVGTK
YVIDDYMRES KLALQELVRH SDLDESYLLG MLVQTRKNIG RTALVLSGGG TFGLFHIGVL
STLLEQDLLP RVISGSSAGA IVASILCSCH RREIVGLVES VLEKELNIFQ DDSEKTQGEN
LLIKISRFFK SGTWFDNKNL VKTMIDFLGD LTFREAYNRT GKILNITVSP ASVFEQPGLL
NNLTAPNVLI WSAVCASCSL PGIFPSTPLY EKDAKTGETR EWNSGTVKFV DGSVDNDLPI
SRLSEMFNVD HIIACQVNLH VFPILKMSVS CVGGEIEDEF SARFRQNLSS VYNFVSNEII
HVLEIVTELG IATNVLTKFR SILSQQYSGD ITILPDIKML FRLNELLANP STDFLLRETV
NGARATWPKI SIIKNHCEQE FELDKAISYL KGKIISNPTF TTKNPFQFTD LSISLINTPE
MPSHDEQVPN DLDDTLLNHH ETDRMLVIND SSKRPHSYGK TSISIADAGR SLHHHRRKSD
SYAKGKSGAR YSISHPGTTT SHISTKLLPT LMGYSPRLDR KKSVGQLPSA SVASRPLDNN
FRLEPKRHSS SFTALHGPRN SNVYSSVRTN PPSPLSAPIN TNMEGTSRKG SFSSYESPLK
AYHKRGAKAH KGRAPAGNRS NSTGSAKLKS SGKVKTGGKP DLKTVSYVDD DPMDPVETGG
DEEINRESN
//