ID A0A090L6Z8_STRRB Unreviewed; 653 AA.
AC A0A090L6Z8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN ORFNames=SRAE_1000215400 {ECO:0000313|EMBL:CEF63898.1,
GN ECO:0000313|WBParaSite:SRAE_1000215400.1,
GN ECO:0000313|WormBase:SRAE_1000215400};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF63898.1};
RN [1] {ECO:0000313|EMBL:CEF63898.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_1000215400.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF63898.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_1000215400.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) 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; LN609528; CEF63898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090L6Z8; -.
DR EnsemblMetazoa; SRAE_1000215400.1; SRAE_1000215400.1; WBGene00258768.
DR WBParaSite; SRAE_1000215400.1; SRAE_1000215400.1; WBGene00258768.
DR WormBase; SRAE_1000215400; SRP12371; WBGene00258768; -.
DR OMA; KVWECRL; -.
DR OrthoDB; 373802at2759; -.
DR Proteomes; UP000035682; Chromosome X.
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; IPR018247; EF_Hand_1_Ca_BS.
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.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000035682};
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..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 348..489
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
SQ SEQUENCE 653 AA; 75143 MW; DECE9274A65C513D CRC64;
MPALIAFGRR WNIASDDFVF PGFLESFIRF FWFLIMLILQ SLYNFKLCEG ERYFKAFAFL
LILNFFTILV CILLVIEAGK GTILEVEKRK NVSKLLYIKM VLFISEGICT GVASVFLFID
RRNGSCNAKI IILVALILEA ILLFVFAVGV LLVFSKHGNK NLDYYATENK KTLRQILKYL
RLASDHEINN ALDEVADILT AFFLDNDFVI SDILAGLVLF LNNSDTKESS YEIIENNEVP
EWMEIIHINR TNRFTKFALA VYGWTTFIAL NSNKKLIWQF IKKVNCCPKK ENDFENEEEE
ENKSLLNVKA FMTLTGIRRE DLLFVSFENM VFQIPFIVCL DHQTNSIVIA IRGSASIHDF
VTDLSLHEDV IMLDVDSDKT IEGDEMKVKA HKGMLLVAKN ILTKLDNSQI LDKTFFDYPS
YDLVITGHSL GGGVGALLTL LLKQKYSRNI KCYSISPPGC VLDNEGRKYL KDSVLSIIVG
EDIVPRMSYH SLFKLKCAIE EELYRTRMKK YEILTKGIFK LFVKKERIDI NGLNYERRNN
IPFYNDNIEE GSIPSDDFIE EPITETRINM RHTTYQADRT KLLPPGQLFH IQFDKETAHW
RWITPECLSE IHLNARVALD HFPYAVVNAL QQIMEQSQSS TFPSESSTSQ NLI
//
