ABD12_XENTR
ID ABD12_XENTR Reviewed; 386 AA.
AC B4F753;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Lysophosphatidylserine lipase ABHD12 {ECO:0000305};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q8N2K0};
DE AltName: Full=2-arachidonoylglycerol hydrolase ABHD12 {ECO:0000305};
DE AltName: Full=Abhydrolase domain-containing protein 12 {ECO:0000305};
DE AltName: Full=Monoacylglycerol lipase ABHD12 {ECO:0000305};
DE EC=3.1.1.23 {ECO:0000250|UniProtKB:Q8N2K0};
DE AltName: Full=Oxidized phosphatidylserine lipase ABHD12 {ECO:0000305};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q8N2K0};
GN Name=abhd12 {ECO:0000250|UniProtKB:Q8N2K0};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lysophosphatidylserine (LPS) lipase that mediates the
CC hydrolysis of lysophosphatidylserine, a class of signaling lipids that
CC regulates immunological and neurological processes (By similarity).
CC Represents a major lysophosphatidylserine lipase in the brain, thereby
CC playing a key role in the central nervous system (By similarity). Also
CC able to hydrolyze oxidized phosphatidylserine; oxidized
CC phosphatidylserine is produced in response to severe inflammatory
CC stress and constitutes a proapoptotic 'eat me' signal. Also has
CC monoacylglycerol (MAG) lipase activity: hydrolyzes 2-
CC arachidonoylglycerol (2-AG), thereby acting as a regulator of
CC endocannabinoid signaling pathways. Has a strong preference for very-
CC long-chain lipid substrates; substrate specificity is likely due to
CC improved catalysis and not improved substrate binding (By similarity).
CC {ECO:0000250|UniProtKB:Q8N2K0, ECO:0000250|UniProtKB:Q99LR1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine;
CC Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-(1'-sn-
CC glycerol); Xref=Rhea:RHEA:44584, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64717,
CC ChEBI:CHEBI:72828; Evidence={ECO:0000250|UniProtKB:Q99LR1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) +
CC H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-1D-myo-
CC inositol; Xref=Rhea:RHEA:44588, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:58444, ChEBI:CHEBI:78762;
CC Evidence={ECO:0000250|UniProtKB:Q99LR1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:40895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74971, ChEBI:CHEBI:143890;
CC Evidence={ECO:0000250|UniProtKB:Q99LR1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z-
CC octadecenoyl)-sn-glycerol + H(+) + phosphocholine;
CC Xref=Rhea:RHEA:41091, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:75757, ChEBI:CHEBI:295975;
CC Evidence={ECO:0000250|UniProtKB:Q99LR1};
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:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phospho-L-serine + H2O = H(+) +
CC hexadecanoate + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:44552,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64765, ChEBI:CHEBI:75020;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
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:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC EC=3.1.1.23; Evidence={ECO:0000250|UniProtKB:Q8N2K0};
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:Q8N2K0};
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:Q8N2K0};
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:Q8N2K0};
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:Q8N2K0};
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:Q8N2K0};
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:Q8N2K0};
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:Q8N2K0};
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:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:39959, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:69081; Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoylglycerol + H2O = glycerol + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:38363, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:75555; Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9,10-epoxyoctadecanoyl)-sn-glycero-3-
CC phospho-L-serine + H2O = 1-octadecanoyl-sn-glycero-3-phosphoserine +
CC 9,10-epoxyoctadecanoate + H(+); Xref=Rhea:RHEA:59364,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:84467,
CC ChEBI:CHEBI:85195, ChEBI:CHEBI:143087;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(10-hydroxyoctadecanoyl)-sn-glycero-3-
CC phospho-L-serine + H2O = 1-octadecanoyl-sn-glycero-3-phosphoserine +
CC 10-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:59368,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:84467,
CC ChEBI:CHEBI:143088, ChEBI:CHEBI:143089;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(10-hydroxyoctadecanoyl)-sn-glycero-3-
CC phospho-L-serine + H2O = 1-hexadecanoyl-sn-glycero-3-phospho-L-serine
CC + 10-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:59372,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75020,
CC ChEBI:CHEBI:143089, ChEBI:CHEBI:143094;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8N2K0}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the serine esterase family. {ECO:0000305}.
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DR EMBL; BC168136; AAI68136.1; -; mRNA.
DR RefSeq; NP_001135601.1; NM_001142129.1.
DR AlphaFoldDB; B4F753; -.
DR SMR; B4F753; -.
DR STRING; 8364.ENSXETP00000027942; -.
DR ESTHER; xentr-abd12; ABHD12-PHARC.
DR MEROPS; S09.939; -.
DR PaxDb; B4F753; -.
DR PRIDE; B4F753; -.
DR GeneID; 100216158; -.
DR KEGG; xtr:100216158; -.
DR CTD; 26090; -.
DR Xenbase; XB-GENE-990130; abhd12.
DR eggNOG; KOG1552; Eukaryota.
DR HOGENOM; CLU_029375_1_0_1; -.
DR InParanoid; B4F753; -.
DR OMA; YELHNCL; -.
DR OrthoDB; 691954at2759; -.
DR PhylomeDB; B4F753; -.
DR TreeFam; TF315122; -.
DR Reactome; R-XTR-426048; Arachidonate production from DAG.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000012789; Expressed in brain and 13 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0047372; F:acylglycerol lipase activity; ISS:UniProtKB.
DR GO; GO:0004622; F:lysophospholipase activity; ISS:UniProtKB.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IBA:GO_Central.
DR GO; GO:0004620; F:phospholipase activity; ISS:UniProtKB.
DR GO; GO:0046464; P:acylglycerol catabolic process; ISS:UniProtKB.
DR GO; GO:0052651; P:monoacylglycerol catabolic process; ISS:UniProtKB.
DR GO; GO:0006660; P:phosphatidylserine catabolic process; ISS:UniProtKB.
DR GO; GO:0009395; P:phospholipid catabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR026605; ABHD12.
DR InterPro; IPR022742; Hydrolase_4.
DR PANTHER; PTHR12277:SF61; PTHR12277:SF61; 1.
DR Pfam; PF12146; Hydrolase_4; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Lipid metabolism; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..386
FT /note="Lysophosphatidylserine lipase ABHD12"
FT /id="PRO_0000375812"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q99LR1"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q99LR1"
FT TOPO_DOM 88..386
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q99LR1"
FT ACT_SITE 237
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT ACT_SITE 324
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT ACT_SITE 363
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 386 AA; 44608 MW; 796029F875C4969D CRC64;
MRKRAEPVPP EHESFGRAPL DRECSIKQKL RIPGTKGHYP HDSDCDSKGM KRFGRRYGLW
SRLRMFLIFL LGLYIAIPFL VKICPAIQTQ LVFLNLVRFP YFIDLKRPED QGLNHTCNFY
LQPEEDVSIG VWHTVPAVLW KDAQGKDLEW YEEVLSTSYP VILYLHGNAG TRGGDHRVQL
YKVLSSMGYH VISFDYRGWG DSVGSPSESG MTYDALHVFD WIKARSGDNP VYIWGHSLGT
GVATNLVRRL CERETPPDSL ILESPFTNIR EEAKSHPFSV IYRYFPGFDW FFLDPITASG
IKFANDDNVK YISCPLLILH AEDDPVIPFH LGKKLYNIAA PARSLRDYKV QFVPFHKDLG
YRHKYIYRSP ELRQILRDFL GNTEQQ
