ABH2A_DANRE
ID ABH2A_DANRE Reviewed; 432 AA.
AC Q802V6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
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-A {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=abhd2a; Synonyms=abhd2; ORFNames=zgc:55722 {ECO:0000303|Ref.1};
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 STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2003) 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; BC047183; AAH47183.1; -; mRNA.
DR RefSeq; NP_957208.1; NM_200914.1.
DR AlphaFoldDB; Q802V6; -.
DR STRING; 7955.ENSDARP00000035450; -.
DR ESTHER; danre-Q802V6; abh_upf0017.
DR PaxDb; Q802V6; -.
DR Ensembl; ENSDART00000035067; ENSDARP00000035450; ENSDARG00000025797.
DR Ensembl; ENSDART00000191360; ENSDARP00000155700; ENSDARG00000025797.
DR GeneID; 393888; -.
DR KEGG; dre:393888; -.
DR CTD; 393888; -.
DR ZFIN; ZDB-GENE-040426-784; abhd2a.
DR eggNOG; KOG1838; Eukaryota.
DR GeneTree; ENSGT00950000182902; -.
DR HOGENOM; CLU_032487_5_0_1; -.
DR InParanoid; Q802V6; -.
DR OMA; DHCRRFY; -.
DR OrthoDB; 1033151at2759; -.
DR PhylomeDB; Q802V6; -.
DR TreeFam; TF313195; -.
DR PRO; PR:Q802V6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000025797; Expressed in caudal fin and 24 other tissues.
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..432
FT /note="Monoacylglycerol lipase ABHD2"
FT /id="PRO_0000280783"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..432
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 132..383
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 413..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 212
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q86WA6"
FT ACT_SITE 346
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q86WA6"
FT ACT_SITE 377
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q86WA6"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 432 AA; 48673 MW; 783E31FC76862DED CRC64;
MNTHESEVYT VAPEMPAMFD GMKLAAVATV LYVIVRCLNL KSPTAPPDLT FQDTTLNHFL
LKSCPILTKE YIPPLLWGKS GHLQTALYGK LGRVSSPHPF GLRKYLPMQD GATATFDLFE
PLADHQSGED VTMVICPGIG NHSEKHYIRT FVDHSQKQGY RCAVLNHLGA LPNIELTSPR
MFTYGCTWEF AAMVGFIKKT YPQSKLIVVG FSLGGNIVCK FLGENRTNQE RVLCCVSVCQ
GYSALRAQET FLQWDQCRRF YNFLMADNMK KIILSHRGVL FGVGSKMVDS ELSRLYTATS
LMQIDDNIMR KFHGHNSLKE YYEKESCVHY IHNINVPLLL VNSVDDPLVH NSLLTIPRTL
AEKKENVVFA LTLHGGHLGF FEGAVLFPQP LTWMDKVIVD YATAMCQWEK QKPPCQSKDA
QSNQTTCQEN TS
