ABHD2_BOVIN
ID ABHD2_BOVIN Reviewed; 425 AA.
AC Q5EA42; A6H753;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Monoacylglycerol lipase ABHD2 {ECO:0000305};
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 {ECO:0000305};
DE AltName: Full=Acetylesterase {ECO:0000250|UniProtKB:P08910};
DE EC=3.1.1.6 {ECO:0000250|UniProtKB:P08910};
DE AltName: Full=Triacylglycerol lipase {ECO:0000250|UniProtKB:P08910};
DE EC=3.1.1.79 {ECO:0000250|UniProtKB:P08910};
GN Name=ABHD2;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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; BT020727; AAX08744.1; -; mRNA.
DR EMBL; BC146116; AAI46117.1; -; mRNA.
DR RefSeq; NP_001015549.1; NM_001015549.1.
DR AlphaFoldDB; Q5EA42; -.
DR STRING; 9913.ENSBTAP00000026579; -.
DR ESTHER; bovin-abhd2; abh_upf0017.
DR PaxDb; Q5EA42; -.
DR PRIDE; Q5EA42; -.
DR Ensembl; ENSBTAT00000026579; ENSBTAP00000026579; ENSBTAG00000019954.
DR GeneID; 508717; -.
DR KEGG; bta:508717; -.
DR CTD; 11057; -.
DR VEuPathDB; HostDB:ENSBTAG00000019954; -.
DR VGNC; VGNC:25500; ABHD2.
DR eggNOG; KOG1838; Eukaryota.
DR GeneTree; ENSGT00950000182902; -.
DR HOGENOM; CLU_032487_5_0_1; -.
DR InParanoid; Q5EA42; -.
DR OMA; DHCRRFY; -.
DR OrthoDB; 1033151at2759; -.
DR TreeFam; TF313195; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000019954; Expressed in neutrophil and 107 other tissues.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
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:0007340; P:acrosome reaction; IEA:Ensembl.
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:0030336; P:negative regulation of cell migration; ISS:AgBase.
DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; ISS:UniProtKB.
DR GO; GO:0009611; P:response to wounding; ISS:AgBase.
DR GO; GO:0014909; P:smooth muscle cell migration; IEA:Ensembl.
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; IPR000952; AB_hydrolase_4_CS.
DR InterPro; IPR012020; ABHD4.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF005211; Ab_hydro_YheT; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01133; UPF0017; 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..425
FT /note="Monoacylglycerol lipase ABHD2"
FT /id="PRO_0000280780"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..425
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 128..382
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 207
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q86WA6"
FT ACT_SITE 345
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q86WA6"
FT ACT_SITE 376
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q86WA6"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 425 AA; 48252 MW; BF8ABE6F44A0225F CRC64;
MNAMMETSEL PAVFDGVKLA AVAAVLYVIV RCLNLKSPTA PPDLYFQDSG LSRFLLKSCP
LLTKEYIPPL IWGKSGHIQT ALYGKMGRVR SPHPYGHRKF ITMSDGATST FDLFEPLAEH
CVGDDITMVI CPGIANHSEK QYIRTFVDYA QKNGYRCAVL NHLGALPNIE LTSPRMFTYG
CTWEFGAMVN YIKKTYPLTQ LVVVGFSLGG NIVCKYLGET QANQEKVLCC VSVCQGYSAL
RAQETFMQWD QCRRFYNFLM ADNMKKIILS HRQALFGDHV KKPQSLEDTD LSRLYTATSL
MQIDDNVMRK FHGYNSLKEY YEEESCMRYL HRIYVPLMLV NAADDPLVHE SLLAIPKSLS
EKRENVMFVL PLHGGHLGFF EGSVLFPEPL TWMDKLVVEY ANAICQWERN KSQCSDTELV
EADLE
