ABHD6_BOVIN
ID ABHD6_BOVIN Reviewed; 337 AA.
AC Q1LZ86;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Monoacylglycerol lipase ABHD6 {ECO:0000305};
DE EC=3.1.1.23 {ECO:0000250|UniProtKB:Q9BV23};
DE AltName: Full=2-arachidonoylglycerol hydrolase {ECO:0000250|UniProtKB:Q8R2Y0};
DE AltName: Full=Abhydrolase domain-containing protein 6 {ECO:0000250|UniProtKB:Q9BV23};
GN Name=ABHD6 {ECO:0000250|UniProtKB:Q9BV23};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lipase that preferentially hydrolysis medium-chain saturated
CC monoacylglycerols including 2-arachidonoylglycerol (By similarity).
CC Through 2-arachidonoylglycerol degradation may regulate endocannabinoid
CC signaling pathways. Also has a lysophosphatidyl lipase activity with a
CC preference for lysophosphatidylglycerol among other lysophospholipids
CC (By similarity). Also able to degrade bis(monoacylglycero)phosphate
CC (BMP) and constitutes the major enzyme for BMP catabolism. BMP, also
CC known as lysobisphosphatidic acid, is enriched in late endosomes and
CC lysosomes and plays a key role in the formation of intraluminal
CC vesicles and in lipid sorting (By similarity).
CC {ECO:0000250|UniProtKB:Q8R2Y0, ECO:0000250|UniProtKB:Q9BV23}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC EC=3.1.1.23; Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octanoylglycerol + H2O = glycerol + H(+) + octanoate;
CC Xref=Rhea:RHEA:44328, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:25646, ChEBI:CHEBI:85241;
CC Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-decanoylglycerol + H2O = decanoate + glycerol + H(+);
CC Xref=Rhea:RHEA:44320, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:27689, ChEBI:CHEBI:75547;
CC Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-dodecanoylglycerol + H2O = dodecanoate + glycerol + H(+);
CC Xref=Rhea:RHEA:44316, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:18262, ChEBI:CHEBI:75539;
CC Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoylglycerol + H2O = glycerol + H(+) +
CC tetradecanoate; Xref=Rhea:RHEA:44312, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:75562; Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:39963, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:75455; Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-
CC octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:44732,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75457;
CC Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392;
CC Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC Xref=Rhea:RHEA:44728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:75612;
CC Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-
CC octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:48428,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75568;
CC Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S,S)-3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(3'-(9Z-
CC octadecenoyl)-1'-sn-glycerol) + H2O = (9Z)-octadecenoate + (S,S)-3-
CC (9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) + H(+);
CC Xref=Rhea:RHEA:55712, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:139150, ChEBI:CHEBI:139152;
CC Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S,S)-2-(9Z-octadecenoyl)-sn-glycero-1-phospho-(2'-(9Z-
CC octadecenoyl)-1'-sn-glycerol) + H2O = (9Z)-octadecenoate + (S,S)-2-
CC (9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) + H(+);
CC Xref=Rhea:RHEA:55716, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:139156, ChEBI:CHEBI:139157;
CC Evidence={ECO:0000250|UniProtKB:Q8R2Y0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R,R)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(2'-(9Z-
CC octadecenoyl)-3'-sn-glycerol) + H2O = (9Z)-octadecenoate + (R,R)-2-
CC (9Z-octadecenoyl)-sn-glycero-3-phospho-(3'-sn-glycerol) + H(+);
CC Xref=Rhea:RHEA:55804, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:139228, ChEBI:CHEBI:139230;
CC Evidence={ECO:0000250|UniProtKB:Q8R2Y0};
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:Q8R2Y0}; Single-pass type II membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q8R2Y0};
CC Single-pass type II membrane protein {ECO:0000255}. Mitochondrion
CC membrane {ECO:0000250|UniProtKB:Q8R2Y0}; Single-pass type II membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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 EMBL; BC116144; AAI16145.1; -; mRNA.
DR RefSeq; NP_001068664.1; NM_001075196.1.
DR RefSeq; XP_005222787.1; XM_005222730.3.
DR RefSeq; XP_005222789.1; XM_005222732.3.
DR AlphaFoldDB; Q1LZ86; -.
DR SMR; Q1LZ86; -.
DR STRING; 9913.ENSBTAP00000022100; -.
DR ESTHER; bovin-q1lz86; ABHD6-Lip.
DR PaxDb; Q1LZ86; -.
DR PRIDE; Q1LZ86; -.
DR Ensembl; ENSBTAT00000022100; ENSBTAP00000022100; ENSBTAG00000016615.
DR GeneID; 505283; -.
DR KEGG; bta:505283; -.
DR CTD; 57406; -.
DR VEuPathDB; HostDB:ENSBTAG00000016615; -.
DR VGNC; VGNC:25503; ABHD6.
DR eggNOG; KOG1454; Eukaryota.
DR GeneTree; ENSGT00510000047225; -.
DR HOGENOM; CLU_020336_13_9_1; -.
DR InParanoid; Q1LZ86; -.
DR OMA; VYILENC; -.
DR OrthoDB; 1285824at2759; -.
DR TreeFam; TF331946; -.
DR Reactome; R-BTA-426048; Arachidonate production from DAG.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000016615; Expressed in diaphragm and 104 other tissues.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IEA:Ensembl.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0047372; F:acylglycerol lipase activity; ISS:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; IEA:Ensembl.
DR GO; GO:0046464; P:acylglycerol catabolic process; ISS:UniProtKB.
DR GO; GO:0060292; P:long-term synaptic depression; IEA:Ensembl.
DR GO; GO:2001311; P:lysobisphosphatidic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0052651; P:monoacylglycerol catabolic process; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:Ensembl.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IEA:Ensembl.
DR GO; GO:2000124; P:regulation of endocannabinoid signaling pathway; IEA:Ensembl.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Endosome; Hydrolase; Lipid metabolism; Lysosome; Membrane; Mitochondrion;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..337
FT /note="Monoacylglycerol lipase ABHD6"
FT /id="PRO_0000281574"
FT TOPO_DOM 1..19
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 72..313
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 148
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q99685"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q99685"
FT ACT_SITE 306
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q99685"
SQ SEQUENCE 337 AA; 38353 MW; BB43E3D8743F9A5E CRC64;
MDLDVVNMFV IAGGTLALPI LAFVASFLLW PSALIRIYYW YWRRTLGMQV RYVRHEDYQF
CYSFRGRPGH KPSILMLHGF SAHKDMWLSM VKFLPKNLHL VCVDMPGHEG TTRSSLDDLS
IDGQVKRIHQ FVECLKLNKK PFHLVGTSMG GHVAGVYAAH YPSDVCSLSL VCPAGLQYST
DNKFVQRLKE LQESAAVEKI PLIPTTPKEM SEMLQLCSYV RFKVPQQILQ GLVDVRIPHN
TFYRKLFLEI VSEKSRYSLH QNMDKIKVPT QIIWGKQDQV LDVSGADMLA KSIANSQVEL
LENCGHSVVM ERPRKTAKLL VDFLASVHST DNSKKLD
