ID   C5LZE8_PERM5            Unreviewed;       532 AA.
AC   C5LZE8;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE            EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN   ORFNames=Pmar_PMAR025569 {ECO:0000313|EMBL:EEQ97942.1};
OS   Perkinsus marinus (strain ATCC 50983 / TXsc).
OC   Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC   Perkinsus.
OX   NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN   [1] {ECO:0000313|EMBL:EEQ97942.1, ECO:0000313|Proteomes:UP000007800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA   El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL   Submitted (JUL-2008) 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; GG686856; EEQ97942.1; -; Genomic_DNA.
DR   RefSeq; XP_002765225.1; XM_002765179.1.
DR   AlphaFoldDB; C5LZE8; -.
DR   EnsemblProtists; EEQ97942; EEQ97942; Pmar_PMAR025569.
DR   GeneID; 9037756; -.
DR   InParanoid; C5LZE8; -.
DR   Proteomes; UP000007800; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007800};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          289..433
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
SQ   SEQUENCE   532 AA;  57947 MW;  9A1A0DC7D30F17B3 CRC64;
     MADFTRLASA IASLSRVCKM RTFCDESGKE SSVDDNLKHI AAELQSESEW LSDKASELSR
     QAWEMSGGQA GGSFEDKRFD QALRAAESAR RAAEAARLAA GSVKAAARSQ WEGVGATARA
     VVESARHKAA RAKERQREAQ VNIDMVQRVW RRIADCGRLA ATSHGSDKPR PPQEVMADFL
     DMCRSRPLDM PNWDSNKFGR KVVDIDVAAA MSSLAYAEAA YDTINTGEMT RDEFEEEQLA
     ENERPPSSIF IMCPDLTKIF YMSPEGKFEV TDPLKPRFIV ALRNDGTVVL AIRGTATLAD
     AITDMLCDDV NVVHSNDHDT GSNSLRVHRG INAGAVWVVQ NAMPYIRKAL SSGASNGRLL
     ITGHSLGGGV ALVAGILIAP ELSPRVWVES IAFGPPPVLS DTLQSRGWRR SGSLPWNLSL
     KSYVNDGDVI SRTCMYSLEY LFGGWGESTS HLLADYEWST PLVIPGKVYV IGTDPSHPGK
     AILTNGMDPT LGESSLVDFF CEIARADRPM IPKAGYAHLI DSYKTALLGE VS
//