ID A0A0K0E1S5_STRER Unreviewed; 652 AA.
AC A0A0K0E1S5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000344300.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000344300.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) 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 AlphaFoldDB; A0A0K0E1S5; -.
DR STRING; 6248.A0A0K0E1S5; -.
DR WBParaSite; SSTP_0000344300.1; SSTP_0000344300.1; SSTP_0000344300.
DR Proteomes; UP000035681; 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:SF2; DIACYLGLYCEROL LIPASE-BETA; 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:UP000035681};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 347..488
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
SQ SEQUENCE 652 AA; 75049 MW; 864A9A67ECA2B29D CRC64;
MPALIAFGRR WNIASDDLVF PGFLESFIRF FWFLIMLVLQ SLYNFKLCEE ARYFKVFVFL
LILNFGTIII CILLTIEAGK GTILEVEKRK NVSKLLYIKM FLFIIEGICT AVASTFLFID
RNDSCDAKII ILVALILEVI LLFVFAVGVL LVFSKHGHKN LDYYATENKK TLRQILKYLR
LASDHEINNA LDEVADILTA FFLDNDFVIS DILAGLVLYL NNNDRKESSY DIIQNNSVPE
WMEISQINRT NRFTKLALAV YGWTSFIALN SNRKLIWQFI KNINCCRRKE EDFENEEEER
NKMQLNVKAF MTLTEISRED LLFVSFENMI FQIPFIVCLD HQTNSIVIAI RGSASIHDFV
TDLSVHEDVI SLDVDPDKTI EGDEVKVRAH KGMLLVAKNI LTKLDNSQIL TKSFSDYPSY
DLVITGHSLG GGVGALLTLL LKQKYTKNIK CYCISPPGCV LDNEGNKYLK DSVLSIIIGE
DIVPRMSYHS LFKLKCVIEE ELYRTRMKKY EILTKGIFKL FVKRERIHLS SNNFNTTNEN
SFLEDNIEDA SIPSDDFIEE PITETRINMR HTTYQADRIK LLPPGQLLHI QVDKEIAHWR
WITPECLSEI HLNARVALDH FPYAVMNALK QIMEQSHSSS FPGEVLTSQN LL
//
