ABH2B_DANRE
ID ABH2B_DANRE Reviewed; 422 AA.
AC Q05AK6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Monoacylglycerol lipase ABHD2 {ECO:0000250|UniProtKB:P08910};
DE EC=3.1.1.23 {ECO:0000250|UniProtKB:P08910};
DE AltName: Full=2-arachidonoylglycerol hydrolase {ECO:0000305};
DE AltName: Full=Abhydrolase domain-containing protein 2-B {ECO:0000305};
DE AltName: Full=Acetylesterase;
DE EC=3.1.1.6;
DE AltName: Full=Triacylglycerol lipase;
DE EC=3.1.1.79;
GN Name=abhd2b; ORFNames=zgc:153750;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Progesterone-dependent acylglycerol lipase that catalyzes
CC hydrolysis of endocannabinoid arachidonoylglycerol (AG) from cell
CC membrane. Acts as a progesterone receptor: progesterone-binding
CC activates the acylglycerol lipase activity, mediating degradation of 1-
CC arachidonoylglycerol (1AG) and 2-arachidonoylglycerol (2AG) to glycerol
CC and arachidonic acid (AA). Also displays an ester hydrolase activity
CC against acetyl ester, butanoate ester and hexadecanoate ester. Plays a
CC key role in sperm capacitation in response to progesterone by mediating
CC degradation of 2AG, an inhibitor of the sperm calcium channel CatSper,
CC leading to calcium influx via CatSper and sperm activation (By
CC similarity). May also play a role in smooth muscle cells migration (By
CC similarity). {ECO:0000250|UniProtKB:P08910,
CC ECO:0000250|UniProtKB:Q9QXM0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC EC=3.1.1.23; Evidence={ECO:0000250|UniProtKB:P08910};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+);
CC Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; EC=3.1.1.6;
CC Evidence={ECO:0000250|UniProtKB:P08910};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12958;
CC Evidence={ECO:0000250|UniProtKB:P08910};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.79;
CC Evidence={ECO:0000250|UniProtKB:P08910};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000250|UniProtKB:P08910};
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:P08910};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133;
CC Evidence={ECO:0000250|UniProtKB:P08910};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate +
CC H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477;
CC Evidence={ECO:0000250|UniProtKB:P08910};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349;
CC Evidence={ECO:0000250|UniProtKB:P08910};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoate ester = an aliphatic alcohol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:47392, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25835; Evidence={ECO:0000250|UniProtKB:P08910};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47393;
CC Evidence={ECO:0000250|UniProtKB:P08910};
CC -!- ACTIVITY REGULATION: Acylglycerol lipase activity is activated upon
CC binding to progesterone. {ECO:0000250|UniProtKB:P08910}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08910};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:P08910}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 4
CC family. {ECO:0000305}.
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DR EMBL; BC124444; AAI24445.1; -; mRNA.
DR RefSeq; NP_001073145.1; NM_001079677.1.
DR AlphaFoldDB; Q05AK6; -.
DR STRING; 7955.ENSDARP00000067326; -.
DR ESTHER; danre-abh2b; abh_upf0017.
DR PaxDb; Q05AK6; -.
DR GeneID; 559290; -.
DR KEGG; dre:559290; -.
DR CTD; 559290; -.
DR ZFIN; ZDB-GENE-061027-74; abhd2b.
DR eggNOG; KOG1838; Eukaryota.
DR InParanoid; Q05AK6; -.
DR OrthoDB; 1033151at2759; -.
DR PhylomeDB; Q05AK6; -.
DR PRO; PR:Q05AK6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0036126; C:sperm flagellum; IBA:GO_Central.
DR GO; GO:0097524; C:sperm plasma membrane; IBA:GO_Central.
DR GO; GO:0008126; F:acetylesterase activity; ISS:UniProtKB.
DR GO; GO:0047372; F:acylglycerol lipase activity; ISS:UniProtKB.
DR GO; GO:0042562; F:hormone binding; ISS:UniProtKB.
DR GO; GO:0033878; F:hormone-sensitive lipase activity; ISS:UniProtKB.
DR GO; GO:0003707; F:nuclear steroid receptor activity; ISS:UniProtKB.
DR GO; GO:0034338; F:short-chain carboxylesterase activity; IBA:GO_Central.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:RHEA.
DR GO; GO:0046464; P:acylglycerol catabolic process; ISS:UniProtKB.
DR GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
DR GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0051793; P:medium-chain fatty acid catabolic process; IBA:GO_Central.
DR GO; GO:0032570; P:response to progesterone; ISS:UniProtKB.
DR GO; GO:0048240; P:sperm capacitation; IBA:GO_Central.
DR GO; GO:0043401; P:steroid hormone mediated signaling pathway; ISS:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR012020; ABHD4.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF005211; Ab_hydro_YheT; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Reference proteome; Serine esterase;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..422
FT /note="Monoacylglycerol lipase ABHD2"
FT /id="PRO_0000280784"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..422
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 134..385
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 213
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q86WA6"
FT ACT_SITE 348
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q86WA6"
FT ACT_SITE 379
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q86WA6"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 422 AA; 47472 MW; 3A0AAFF58FC22250 CRC64;
MSAQLEADVR TMSPEMPAMF DGMKLAAVAA VLYVIVRSLN LKCPTAAADI TCQDTLLNHY
LLKSCPVLTK EYIPPLLWGK SGHLQTALYG KIGRVKSPKP CGLRKFLPMQ DGATATFDLF
EPQGVHSTGD DITMVICPGI GNHSEKHYIR TFVDYSQKQG YRCAVLNHLG ALPNIELTSP
RMFTYGCTWE FSAMVGFIKR TFPQTQLIVV GFSLGGNIAC KYLGENPANQ ERVLCCVSVC
QGYSALRAQE TFLQWDQCRR LYNFLMADNM KKIILSHRGS LFGMNSSRME FADLSRLYTA
TSLMQIDDNI MRKFHGHNSL KEYYEKESCV HYIHNISVPL LLVNSSDDPL VHQSLLTIPR
TLAEKKQNVI FALTLHGGHL GFFEGAVLFP QPLSWMDKVI VSYANAVCQW EKHKPQCHQQ
KE
