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Database: UniProt
Entry: A0A0F7RVK3_9BASI
LinkDB: A0A0F7RVK3_9BASI
Original site: A0A0F7RVK3_9BASI 
ID   A0A0F7RVK3_9BASI        Unreviewed;       485 AA.
AC   A0A0F7RVK3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE            EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN   Name=SSCI07090.1 {ECO:0000313|EMBL:CDR98807.1};
OS   Sporisorium scitamineum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=49012 {ECO:0000313|EMBL:CDR98807.1, ECO:0000313|Proteomes:UP000242770};
RN   [1] {ECO:0000313|Proteomes:UP000242770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Berkman P.J.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty
CC         acid + H(+); Xref=Rhea:RHEA:33275, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815,
CC         ChEBI:CHEBI:28868; EC=3.1.1.116;
CC         Evidence={ECO:0000256|ARBA:ARBA00024531};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33276;
CC         Evidence={ECO:0000256|ARBA:ARBA00024531};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CCFA01000363; CDR98807.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F7RVK3; -.
DR   OrthoDB; 1424726at2759; -.
DR   Proteomes; UP000242770; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd00519; Lipase_3; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002921; Fungal_lipase-like.
DR   PANTHER; PTHR45792; DIACYLGLYCEROL LIPASE HOMOLOG-RELATED; 1.
DR   PANTHER; PTHR45792:SF8; DIACYLGLYCEROL LIPASE-ALPHA; 1.
DR   Pfam; PF01764; Lipase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          130..290
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
FT   REGION          381..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   485 AA;  53528 MW;  796AA4DFA1323F1D CRC64;
     MDAMRPGQAN SGYFGRVYDF MTSPQVGASQ PGADNRDLRP FKETNRNLVR TIKWCGRLAI
     SAYGIHVHIV DLPPTFTPSG ERFSRQTFAY LSRLNADDVL HADIQTLDAD ADYSPTFYIV
     RDYVRKVVCV AVRGTQSFSD IIVDLELQTE EIELPQVQPT PGEEFRCHAG IWRAAKALVS
     PQSKLFATLR QALAENEGFG IVFCGHSLGG AIASAAALLL AEYFIPDGAE PDAGTWVTNM
     SSGLPARRPI RAVSFASPVI MTADLASRAA LGSVPLVTTV VLGSDVIPRV GHGQVRELRR
     VLGALSRVRR RHAMASTEGS DDARVHILRS YWDWRSICRA EDADDVMLHR KERIEAQLWS
     LRREVESDLY AAIKARLDAE STASTASTAS TRIPPSPWVG PQQRDQAPLH ALSARRQELD
     TATLRSEAAQ GGPLVPPGRC IWIHNKRIYH VESALAFFSL PELRSDMFAA HFPAAYEEAI
     LELRT
//
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