ID L1JBD4_GUITC Unreviewed; 809 AA.
AC L1JBD4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN ORFNames=GUITHDRAFT_108508 {ECO:0000313|EMBL:EKX45632.1};
OS Guillardia theta (strain CCMP2712) (Cryptophyte).
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX NCBI_TaxID=905079 {ECO:0000313|EMBL:EKX45632.1};
RN [1] {ECO:0000313|EMBL:EKX45632.1, ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|EMBL:EKX45632.1,
RC ECO:0000313|Proteomes:UP000011087};
RX PubMed=23201678; DOI=10.1038/nature11681;
RG DOE Joint Genome Institute;
RA Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., Maruyama S.,
RA Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F., Kuo A.,
RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA Durnford D.G., Fast N.M., Green B.R., Grisdale C.J., Hempel F.,
RA Henrissat B., Hoppner M.P., Ishida K., Kim E., Koreny L., Kroth P.G.,
RA Liu Y., Malik S.B., Maier U.G., McRose D., Mock T., Neilson J.A.,
RA Onodera N.T., Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W.,
RA Sarai C., Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RT "Algal genomes reveal evolutionary mosaicism and the fate of
RT nucleomorphs.";
RL Nature 492:59-65(2012).
RN [2] {ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|Proteomes:UP000011087};
RA Kuo A., Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M.,
RA Maruyama S., Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F.,
RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA Durnford D.G., Fast N.M., Green B.R., Grisdale C., Hempe F., Henrissat B.,
RA Hoppner M.P., Ishida K.-I., Kim E., Koreny L., Kroth P.G., Liu Y.,
RA Malik S.-B., Maier U.G., McRose D., Mock T., Neilson J.A., Onodera N.T.,
RA Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W., Sarai C.,
RA Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblProtists:EKX45632}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (MAR-2016) to UniProtKB.
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; JH992998; EKX45632.1; -; Genomic_DNA.
DR RefSeq; XP_005832612.1; XM_005832555.1.
DR AlphaFoldDB; L1JBD4; -.
DR PaxDb; 55529-EKX45632; -.
DR EnsemblProtists; EKX45632; EKX45632; GUITHDRAFT_108508.
DR GeneID; 17302374; -.
DR KEGG; gtt:GUITHDRAFT_108508; -.
DR eggNOG; KOG2088; Eukaryota.
DR HOGENOM; CLU_008300_2_1_1; -.
DR OMA; KVWECRL; -.
DR OrthoDB; 373802at2759; -.
DR Proteomes; UP000011087; 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 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:UP000011087};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 65..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 515..674
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 261..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 809 AA; 88648 MW; 004F274859526604 CRC64;
MPALRLLGRA WLVGSDDLVL PAAIGSFLRA CLLGTLIAFH YTLSGDISCS SDWCPAVFVE
RCIDLYVYGI ILLMGATCFL EALIAISSSK GRIMEERSRR PVSTLVLVHV LVSLLEAAWT
AWAAIVFLSP SLECKGDSPE HEREGEAFLR MIVWISIATI GWMCAGVLFA FDLSGHVDVA
DIDKLHRHWE RRCNFLCCLM PREDDREIAL RSLVKSLSSW FAGLDLVPSD IFAALLLLNL
WSTVSDTSCL DDIYGQFERT ESSAHKDENN KHVGPATLLD HHEDVDNRSK IEEGVSEDSF
SSQAGAETEG ITGGDSVDGE VEEHHSANAG DISLHSFDSP GFLSALMTAT VSSIALGSNS
SAGDSQSQGS NEPSATVSAP DMSRSPAELP EAIQPSSREP PSRQSEDVDA GRHETAIEIL
RRAELYIPYA IACYGMMLQV WRCCSNCCDG FCWILQNILC CTCLSRSSGD GWVDKKALER
EAQERDYHII LEAPADAFSP AFFLVADLTL KSVVLAIRGT FSISDTLTDG TAHCCLLPAR
VREFVQGVLR LGAEHRGGEE LADEQVEFES NGPYGHAGMV QAAERLRNLL HDSNFLPLLL
SEDHVSHELV KSGIEIPSCR GFRLVVVGHS LGAGVASILS LMLRSEELPV YQDMECFALS
CPPVLSRSAA ESCEPFITTV APPFAPSLAL SATKIAVGED MISRMSLRSL QLLRTRALEL
LILCRRPKWQ VTDLKDLCAS LPDSQPREGH DALKSKHEIF ACGPIQPALR LPGRAFLFET
DKSHSMPMLR RMHHTEMEAE TSWTCGHQD
//
