ABH6B_XENLA
ID ABH6B_XENLA Reviewed; 337 AA.
AC Q7SY73;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Monoacylglycerol lipase abhd6-B {ECO:0000305};
DE EC=3.1.1.23 {ECO:0000250|UniProtKB:Q9BV23};
DE AltName: Full=Abhydrolase domain-containing protein 6-B;
GN Name=abhd6-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Larva;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2003) 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}.
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DR EMBL; BC054984; AAH54984.1; -; mRNA.
DR RefSeq; NP_001080850.1; NM_001087381.2.
DR AlphaFoldDB; Q7SY73; -.
DR SMR; Q7SY73; -.
DR ESTHER; xenla-Q7SY73; ABHD6-Lip.
DR DNASU; 380544; -.
DR GeneID; 380544; -.
DR KEGG; xla:380544; -.
DR CTD; 380544; -.
DR Xenbase; XB-GENE-6256516; abhd6.L.
DR OrthoDB; 1285824at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 380544; Expressed in intestine and 19 other tissues.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
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:0047372; F:acylglycerol lipase activity; ISS:UniProtKB.
DR GO; GO:0046464; P:acylglycerol catabolic process; ISS:UniProtKB.
DR GO; GO:2001311; P:lysobisphosphatidic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0052651; P:monoacylglycerol catabolic process; ISS:UniProtKB.
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-B"
FT /id="PRO_0000281579"
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; 38087 MW; D000221283D321FF CRC64;
MDIDVLNMFL VAGGTLLVPL LAFMTSFLLW PAALIRIYYW YWRRALGMQV KYSSYGNYKF
CYTARGKPGN KPSVLMLHGF SAHKDMWLGM VKFLPKNLHL VCVDMPGHEG TSRSALDYYS
ICGQVKRIHQ FVESIGLNKK PFHLVGTSMG GNVAGVYAAQ HPTHISSLTL ICPAGLMYPI
ESKFLKQLKV LEKSGDNQRI PLIPSTAGEM EDMLRLCSFV RFKIPQQVLQ GLIDERIPHN
EFYRKLFLAL VDEKSRHSLH ENMNKIMAPT QIIWGKQDQV LDVSGAEVLA GSLRGCQVEI
LENCGHSVVM ERPRKSAKLM TDFLSSLQST DNHKKHD
