ABD12_CHICK
ID ABD12_CHICK Reviewed; 381 AA.
AC Q5ZIN0;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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};
GN ORFNames=RCJMB04_24m17 {ECO:0000303|PubMed:15642098};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720754; CAG32413.1; -; mRNA.
DR RefSeq; NP_001012889.1; NM_001012871.1.
DR AlphaFoldDB; Q5ZIN0; -.
DR SMR; Q5ZIN0; -.
DR STRING; 9031.ENSGALP00000013877; -.
DR ESTHER; chick-q5zin0; ABHD12-PHARC.
DR MEROPS; S09.939; -.
DR PaxDb; Q5ZIN0; -.
DR Ensembl; ENSGALT00000013893; ENSGALP00000013877; ENSGALG00000008525.
DR GeneID; 421249; -.
DR KEGG; gga:421249; -.
DR CTD; 26090; -.
DR VEuPathDB; HostDB:geneid_421249; -.
DR eggNOG; KOG1552; Eukaryota.
DR GeneTree; ENSGT00940000160517; -.
DR HOGENOM; CLU_029375_1_0_1; -.
DR InParanoid; Q5ZIN0; -.
DR OMA; YELHNCL; -.
DR OrthoDB; 691954at2759; -.
DR PhylomeDB; Q5ZIN0; -.
DR Reactome; R-GGA-426048; Arachidonate production from DAG.
DR PRO; PR:Q5ZIN0; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000008525; Expressed in cerebellum 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..381
FT /note="Lysophosphatidylserine lipase ABHD12"
FT /id="PRO_0000375810"
FT TOPO_DOM 1..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q99LR1"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q99LR1"
FT TOPO_DOM 80..381
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q99LR1"
FT ACT_SITE 229
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT ACT_SITE 316
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT ACT_SITE 355
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 381 AA; 43855 MW; 99BEB9EC3023A6AF CRC64;
MRKRNESVTV EHERAAAAPA PLDKGCSLRH SLRLPAADTG MKRPLGRRHG LWFRLRRLII
WLLGVYIAIP FLVKLCPAIQ AKLVFLNFVR VPYFIDLKRP QDQGLNHTCN YYLQPEEDVT
IGVWHTVPAA LWKNARGKDQ LWFEDALGSS HPVILYLHGN AGTRGGDHRV ELYKVLSSLG
YHVVTFDYRG WGDSVGSPSE RGMTYDALHV FDWIKARSGD NPVYIWGHSL GTGVATNLVR
RLCERETPPE ALILESPFTN IREEARSHPF SVIYRYFPGF DWFFLDPITT SGIKFANDEN
VKYISCSLLI LHAEDDPVVP FHLGKKLYNI AATSRSFRDY KVQFVPFHTD LGYRHKYIYR
SPELPRILRE FLGIPEHEHH H
