ID A0A0D9R294_CHLSB Unreviewed; 1043 AA.
AC A0A0D9R294;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=sn-1-specific diacylglycerol lipase {ECO:0000256|ARBA:ARBA00026104};
DE EC=3.1.1.116 {ECO:0000256|ARBA:ARBA00026104};
GN Name=DAGLA {ECO:0000313|Ensembl:ENSCSAP00000002733.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000002733.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000002733.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000002733.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701}.
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DR EMBL; AQIB01079254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007994159.1; XM_007995968.1.
DR RefSeq; XP_007994164.1; XM_007995973.1.
DR RefSeq; XP_007994170.1; XM_007995979.1.
DR RefSeq; XP_007994181.1; XM_007995990.1.
DR AlphaFoldDB; A0A0D9R294; -.
DR STRING; 60711.ENSCSAP00000002733; -.
DR ESTHER; chlsb-a0a0d9r294; Lipase_3.
DR Ensembl; ENSCSAT00000004483.1; ENSCSAP00000002733.1; ENSCSAG00000006443.1.
DR GeneID; 103234256; -.
DR KEGG; csab:103234256; -.
DR CTD; 747; -.
DR eggNOG; KOG2088; Eukaryota.
DR GeneTree; ENSGT00940000161192; -.
DR OMA; YCMVAPE; -.
DR OrthoDB; 373802at2759; -.
DR BioGRID-ORCS; 103234256; 0 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 1.
DR Bgee; ENSCSAG00000006443; Expressed in prefrontal cortex and 6 other cell types or tissues.
DR GO; GO:0032591; C:dendritic spine membrane; IEA:Ensembl.
DR GO; GO:0031901; C:early endosome membrane; IEA:Ensembl.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0043196; C:varicosity; IEA:Ensembl.
DR GO; GO:0047372; F:acylglycerol lipase activity; IEA:Ensembl.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IEA:Ensembl.
DR GO; GO:1901696; P:cannabinoid biosynthetic process; IEA:Ensembl.
DR GO; GO:0046340; P:diacylglycerol catabolic process; IEA:Ensembl.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006640; P:monoacylglycerol biosynthetic process; IEA:Ensembl.
DR GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR GO; GO:0150077; P:regulation of neuroinflammatory response; IEA:Ensembl.
DR GO; GO:0098921; P:retrograde trans-synaptic signaling by endocannabinoid; IEA:Ensembl.
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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 394..529
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 847..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 115025 MW; CD29CA875A9712AD CRC64;
MPGIVVFRRR WSVGSDDLVL PAIFLFLLHT TWFVILSVVL FGLVYNPHEA CSLNLVDHGR
GYLGILLSCM IAEMAIIWLS MRGGILYTEP RDSMQYVLYV RLAILVIEFI YAIVGIVWLT
QYYTSCNDLT AKNVTLGMVV CNWVVILSVC ITVLCVFDPT GRTFVKLRAT KRRQRNLRTY
NLRHRLEEGQ ATSWSRRLKV FLCCTRTKDS QSDAYSEIAY LFAEFFRDLD IVPSDIIAGL
VLLRQRQRAK RNAVLDEANN DILAFLSGMP VTRNTKYLDL KNSQEMLRYK EVCYYMLFAL
AAYGWPMYLM RKPACGLCQL ARSCSCCLCP ARPRFAPGVT IEEDNCCGCN AIAIRRHFLD
ENMTAVDIVY TSCHDAVYET PFYVAVDHDK KKVVISIRGT LSPKDALTDL TGDAERLPVE
GHHGTWLGHK GMVLSAEYIK KKLEQEMVLS QAFGRDLGRG TKHYGLIVVG HSLGAGTAAI
LSFLLRPQYP TLKCFAYSPP GGLLSEDAME YSKEFVTAVV LGKDLVPRIG LSQLEGFRRQ
LLDVLQRSTK PKWRIIVGAT KCIPKSELPE EVEVTTLAST RLWTHPSDLT IALSASTPLY
PPGRIIHVVH NHPAEQCCCC EQEEPTYFAI WGDNKAFNEV IISPAMLHEH LPYVVMEGLN
KVLENYNKGK TALLSAAKVM VSPTEVDLTP ELIFQQQPLP TGPPMPAGLA LELPTADHRN
SSVRSKSQSE MSLEGFSEGR LLSPVVAAAA ARQDPVELLL LSTQERLAAE LQARRAPLAT
MESLSDTESL YSFDSRRSSG FRSIRGSPSL HAVLERDEGH LFYIDPAIPE ENPSLSSRTE
LLAADSLSKH SQDTQPLEAA LGSGGVTPER PPSASANDEE EEVGGGGGGL ASRGELALHN
GRLGDSPSPQ VLEFAEFIDS LFNLDSKSSS FQDLYCMVVP ESPTSDYAEG PKSPSQQEIL
LRAQFEPNLV PKPPRLFAGS ADPSSGISLS PSFPLSSSGE LMDLTPTGLS SQECLAADKI
RTSTPTGHGA SPAKQDELVI SAR
//
