ID A0A0L0HFP6_SPIPD Unreviewed; 745 AA.
AC A0A0L0HFP6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN ORFNames=SPPG_05225 {ECO:0000313|EMBL:KNC99851.1};
OS Spizellomyces punctatus (strain DAOM BR117).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Spizellomycetales;
OC Spizellomycetaceae; Spizellomyces.
OX NCBI_TaxID=645134 {ECO:0000313|EMBL:KNC99851.1, ECO:0000313|Proteomes:UP000053201};
RN [1] {ECO:0000313|EMBL:KNC99851.1, ECO:0000313|Proteomes:UP000053201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM BR117 {ECO:0000313|EMBL:KNC99851.1,
RC ECO:0000313|Proteomes:UP000053201};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T.,
RA White J., Yandava C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Spizellomyces punctatus strain DAOM BR117.";
RL Submitted (AUG-2009) 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; KQ257457; KNC99851.1; -; Genomic_DNA.
DR RefSeq; XP_016607891.1; XM_016753448.1.
DR AlphaFoldDB; A0A0L0HFP6; -.
DR GeneID; 27688617; -.
DR VEuPathDB; FungiDB:SPPG_05225; -.
DR eggNOG; KOG2088; Eukaryota.
DR InParanoid; A0A0L0HFP6; -.
DR OMA; IYTWVLY; -.
DR OrthoDB; 373802at2759; -.
DR Proteomes; UP000053201; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053201};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 416..552
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 217..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 745 AA; 82790 MW; 9DA87E7F466D9537 CRC64;
MACFPYILPL PNTDNLHDRL IFVTIVIATH GEWIPIPYIP IFYCFVVACL LIEGIGMIIS
LRGTVADERP RRRMRNLVEI HSVMTLLELP LEIYTLYFTI HTLKTITHLA LLILLIISTL
LTALLTLLHL LAILALYIVS CPVVKDEQAA YESTQRLWQR RLRRLFSFGG KWVAGQDVME
EVARFFGEYF DGVDLAPSDV LVGLALLRKV QQESAKQHAR ERRQDAIPLV AQQNPQGEDA
APVSTGQGTD SAQLEDRELS SREDEREEEA EPVPLSPIHQ SGRANEAIVD KADLSNALHF
LNYAQAIYGL PLTFAENPFS TLKATCGSLC CACCVGCIPH PKPTPTKEVW QAVATEGGLF
PFLGTSTDSL ESGEVGEDIQ TVHKKLHSDL IYISHINSPF RSPFFVSLDH QSRSVVVAVR
GTFSTADVLV DLSLQVTDLE LCDGGKHWAH TGMLKTAKNL VKEMDKRGVL KRPELEADEN
GRSKYRVCVV GHSLGAGIAA LVCHILRRTS HAGAICYAYS PPGCLLSSDA SIHFQQFCTS
IILNDDLVPR LSRTSLERAK RDVAYLCGHS NVHKLHVLAA GFGLGWTKRW TRGEGVVECE
EDVLRVRENE EQKMAETTSS ECIVDLPRQE EVPADDNVQA EAASPTGGTT VEVRKSVQMY
VPGTIIHIVR LSPLGIPKAR SNKKYNRRHP PPRYTARWAD KADFTEILLS RSMLMDHFPY
NVRKGLNEAL ETFTAAEAIG HDVLE
//
