ID H9GPJ7_ANOCA Unreviewed; 1031 AA.
AC H9GPJ7;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 62.
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:ENSACAP00000017433.4};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000017433.4, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000017433.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000017433.4};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000017433.4}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_003224182.1; XM_003224134.3.
DR RefSeq; XP_008114077.1; XM_008115870.2.
DR AlphaFoldDB; H9GPJ7; -.
DR STRING; 28377.ENSACAP00000017433; -.
DR Ensembl; ENSACAT00000017775.4; ENSACAP00000017433.4; ENSACAG00000017695.4.
DR GeneID; 103279659; -.
DR KEGG; acs:103279659; -.
DR CTD; 747; -.
DR eggNOG; KOG2088; Eukaryota.
DR GeneTree; ENSGT00940000161192; -.
DR HOGENOM; CLU_008300_1_0_1; -.
DR InParanoid; H9GPJ7; -.
DR OrthoDB; 373802at2759; -.
DR TreeFam; TF312928; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000017695; Expressed in testis and 9 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
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:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0043196; C:varicosity; IEA:Ensembl.
DR GO; GO:0047372; F:acylglycerol lipase activity; IEA:Ensembl.
DR GO; GO:0004465; F:lipoprotein lipase activity; IBA:GO_Central.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IBA:GO_Central.
DR GO; GO:1901696; P:cannabinoid biosynthetic process; IEA:Ensembl.
DR GO; GO:0046340; P:diacylglycerol catabolic process; IBA:GO_Central.
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; IBA:GO_Central.
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:UP000001646};
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 395..530
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 839..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1031 AA; 115006 MW; 74B1352B89C7F8F9 CRC64;
MPGIVVFRRR WSVGSDDLVL PAIFLFVLHT TWFIILSVVL FGLVYNPNET CSLNLVDHGR
GYLGILLSCM IAEVAIIWLS MRGSILYTEP RDSMQYVLYV RLAILVIEFI YAIVGIAWLT
QYYSSCNDVT AKSVTLGMVV CNWVVILSVC ITVLCVFDPT GRTFVKLRAT KRRQRNLRTY
NLRHRLEEGQ ASSWTRRLKV FLCCTRTKDS QSDAYSEIAY LFAEFFRDLD IVPSDIIAGL
VLLRQRQRAK RNAVLDEANN DILAFLSGMP VTRNTKYLDL KNSQEMLRYK EVCYYMLFAL
AAYGWPMYLM RKPACGLCRL ARSCSCCCLC PARPRYAPGV TIEEDNCCGC NAIAIRRHFL
DENMASVDIV YTSCHDAVYE TPFYVAVDHE KKKVVISIRG TLSPKDALTD LTGDAERLPV
EGHHGTWLGH KGMVLSAEYI KKKLEQEMVL SQAFGRDLGR GTKHYGLIVV GHSLGAGTAA
ILSFLLRPQY PTLKCYAYSP PGGLLSEDAM EYSKEFVTAV VLGKDLVPRI GLSQLEGFRR
QLLDVLQRST KPKWRIIVGA TKCIPKSELS EEPEANSVTS NRLWTHPSDL TIALSASTPL
YPPGRIIHVV HNHPAEQCCC CDQEDPTYFA IWGDNKAFNE VIISPAMLHE HLPYVVMEGL
NKVLENYNKG KTALLSAAKV MVSPTEVDLN PELIFQNQPL PSRPSVQIGI GEIAVDRRNS
SAKSKPQTEI NLEGFYETKL LSPVQKDPVE ILLLDTKERL SVELQDRRAP LATMESLSDN
ESIYSFDSRR SSGFRSIRGS PSLHAVMEKD ETHCFYIDPA IPEENPSLSS RTELLAADSL
SKHSQETQPP EAMPNSGGTT PQRQCSDEEA GSDTDHISFT PREELTLQNG RLSDDPSPQV
LEFAEFIDSL FNLDSKSSSF QDIYCMMVSD STSDFAEMPK SVSDQEILLR AQYEPNLVPK
PPRLFAGSTD PSSGISVSPS FPLSSSGELM DITPTGMSSQ ECLATDKIRT STPTGNMTSP
AKHEDLVISA L
//
