ABHD6_RAT
ID ABHD6_RAT Reviewed; 337 AA.
AC Q5XI64;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
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:0000312|RGD:1359323};
GN Name=Abhd6 {ECO:0000312|RGD:1359323};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PROTEIN SEQUENCE OF 245-254, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
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}.
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DR EMBL; BC083826; AAH83826.1; -; mRNA.
DR RefSeq; NP_001007681.1; NM_001007680.1.
DR RefSeq; XP_006251828.1; XM_006251766.3.
DR RefSeq; XP_006251829.1; XM_006251767.3.
DR RefSeq; XP_006251830.1; XM_006251768.3.
DR AlphaFoldDB; Q5XI64; -.
DR SMR; Q5XI64; -.
DR CORUM; Q5XI64; -.
DR STRING; 10116.ENSRNOP00000012271; -.
DR ChEMBL; CHEMBL3708569; -.
DR GuidetoPHARMACOLOGY; 2919; -.
DR ESTHER; rat-abhd6; ABHD6-Lip.
DR PhosphoSitePlus; Q5XI64; -.
DR jPOST; Q5XI64; -.
DR PaxDb; Q5XI64; -.
DR PRIDE; Q5XI64; -.
DR Ensembl; ENSRNOT00000012271; ENSRNOP00000012271; ENSRNOG00000008167.
DR GeneID; 305795; -.
DR KEGG; rno:305795; -.
DR CTD; 57406; -.
DR RGD; 1359323; Abhd6.
DR eggNOG; KOG1454; Eukaryota.
DR GeneTree; ENSGT00510000047225; -.
DR InParanoid; Q5XI64; -.
DR OMA; VYILENC; -.
DR OrthoDB; 1285824at2759; -.
DR PhylomeDB; Q5XI64; -.
DR TreeFam; TF331946; -.
DR Reactome; R-RNO-426048; Arachidonate production from DAG.
DR PRO; PR:Q5XI64; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000008167; Expressed in jejunum and 20 other tissues.
DR Genevisible; Q5XI64; RN.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; ISO:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0047372; F:acylglycerol lipase activity; ISS:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; ISO:RGD.
DR GO; GO:0046464; P:acylglycerol catabolic process; ISS:UniProtKB.
DR GO; GO:0060292; P:long-term synaptic depression; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0009395; P:phospholipid catabolic process; ISO:RGD.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISO:RGD.
DR GO; GO:2000124; P:regulation of endocannabinoid signaling pathway; ISO:RGD.
DR GO; GO:0099178; P:regulation of retrograde trans-synaptic signaling by endocanabinoid; ISO:RGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endosome; Hydrolase; Lipid metabolism; Lysosome;
KW Membrane; Mitochondrion; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..337
FT /note="Monoacylglycerol lipase ABHD6"
FT /id="PRO_0000281577"
FT TOPO_DOM 1..8
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..337
FT /note="Cytoplasmic"
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; 38312 MW; BDE7B746E276023E CRC64;
MDLDVVNMFV IAGGTLAIPI LAFVASFLLW PSALIRIYYW YWRRTLGMQV RYVHHEDYQF
CYSFRGRPGH KPSVLMLHGF SAHKDMWLSV VKFLPKNLHL VCVDMPGHEG TTRSSLDDLS
IVGQVKRIHQ FVECLKLNKK PFHLIGTSMG GNVAGVYAAY YPSDVCSLSL VCPAGLQYST
DNRFVQRLKE LEDSAATQKI PLIPSTPEEM SEMLQLCSYV RFKVPQQILQ GLVDVRIPHN
SFYRKLFLEI VSEKSRYSLH ENMDKIKVPT QIIWGKQDQV LDVSGADILA KSITNSQVEV
LENCGHSVVM ERPRKTAKLV VDFLASVHNP DNNKKLN
