ABHGA_MACFA
ID ABHGA_MACFA Reviewed; 558 AA.
AC Q4R8P0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Phosphatidylserine lipase ABHD16A {ECO:0000305};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q9Z1Q2};
DE AltName: Full=Alpha/beta hydrolase domain-containing protein 16A {ECO:0000305};
DE Short=Abhydrolase domain-containing protein 16A {ECO:0000305};
DE AltName: Full=HLA-B-associated transcript 5 homolog {ECO:0000250|UniProtKB:O95870};
DE AltName: Full=Monoacylglycerol lipase ABHD16A {ECO:0000305};
DE EC=3.1.1.23 {ECO:0000250|UniProtKB:O95870};
GN Name=ABHD16A {ECO:0000250|UniProtKB:O95870};
GN Synonyms=BAT5 {ECO:0000250|UniProtKB:O95870};
GN ORFNames=QtsA-11941 {ECO:0000303|Ref.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphatidylserine (PS) lipase that mediates the hydrolysis
CC of phosphatidylserine to generate lysophosphatidylserine (LPS). LPS
CC constitutes a class of signaling lipids that regulates immunological
CC and neurological processes (By similarity). Has no activity towards
CC diacylglycerol, triacylglycerol or lysophosphatidylserine lipase (By
CC similarity). Also has monoacylglycerol lipase activity, with preference
CC for 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) and 2-glyceryl-15-deoxy-
CC Delta(12,14)-prostaglandin J2 (15d-PGJ(2)-G) (By similarity).
CC {ECO:0000250|UniProtKB:O95870, ECO:0000250|UniProtKB:Q9Z1Q2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoserine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC heptadecanoyl-sn-glycero-3-phosphoserine + H(+);
CC Xref=Rhea:RHEA:44500, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:84461, ChEBI:CHEBI:84462;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phospho-L-serine + H(+); Xref=Rhea:RHEA:41752, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75020,
CC ChEBI:CHEBI:75029; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoserine + H2O = (9Z,12Z)-octadecadienoate + 1-octadecanoyl-sn-
CC glycero-3-phosphoserine + H(+); Xref=Rhea:RHEA:44516,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:84466, ChEBI:CHEBI:84467;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC heptadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:44520, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:74340, ChEBI:CHEBI:84470;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-
CC glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phospho-glycerol + H(+); Xref=Rhea:RHEA:44524, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:84472,
CC ChEBI:CHEBI:84475; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-
CC myo-inositol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC 3-phospho-(1D-myo-inositol) + H(+); Xref=Rhea:RHEA:44528,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:72833, ChEBI:CHEBI:72837;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC heptadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:44540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:84489, ChEBI:CHEBI:84490;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC 3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:72841, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC EC=3.1.1.23; Evidence={ECO:0000250|UniProtKB:O95870};
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:O95870};
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:O95870};
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:O95870};
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:O95870};
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:O95870};
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:O95870};
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:O95870};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + prostaglandin D2-1-glycerol ester = glycerol + H(+) +
CC prostaglandin D2; Xref=Rhea:RHEA:45412, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57406,
CC ChEBI:CHEBI:85232; Evidence={ECO:0000250|UniProtKB:O95870};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-oxo-5Z,9,12E,14E-prostatetraenoate + H2O = 15-deoxy-
CC Delta(12,14)-prostaglandin J2 + glycerol + H(+);
CC Xref=Rhea:RHEA:45416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:85236, ChEBI:CHEBI:85238;
CC Evidence={ECO:0000250|UniProtKB:Q9Z1Q2};
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:Q9Z1Q2};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Z1Q2}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD16 family.
CC {ECO:0000305}.
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DR EMBL; AB168411; BAE00532.1; -; mRNA.
DR RefSeq; NP_001271025.1; NM_001284096.1.
DR AlphaFoldDB; Q4R8P0; -.
DR SMR; Q4R8P0; -.
DR STRING; 9541.XP_005553548.1; -.
DR ESTHER; macfa-q4r8p0; ABHD16.
DR GeneID; 101866118; -.
DR CTD; 7920; -.
DR eggNOG; KOG1553; Eukaryota.
DR OrthoDB; 580247at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047372; F:acylglycerol lipase activity; ISS:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; ISS:UniProtKB.
DR GO; GO:0052651; P:monoacylglycerol catabolic process; ISS:UniProtKB.
DR GO; GO:0006660; P:phosphatidylserine catabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR026604; ABHD16A.
DR PANTHER; PTHR12277:SF54; PTHR12277:SF54; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Lipid metabolism; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..558
FT /note="Phosphatidylserine lipase ABHD16A"
FT /id="PRO_0000333742"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..558
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Q2"
FT DOMAIN 281..407
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 355
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT ACT_SITE 430
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT ACT_SITE 507
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
SQ SEQUENCE 558 AA; 63181 MW; E042303DCD19A62B CRC64;
MAKLLSCVLG PRLYKIYRER DSERAPASVP ETPTAVTAPH SSSWDTYYQP RALEKHADSI
LALASVFWSI SYYSSPFAFF YLYRKGYLSL SKVVPFSHYA GTLLLLLAGV ACLRGIGRWT
NPQYRQFITI LEATHRNQSS ENKRQLANYN FDFRSWPVDF HWEEPSSRKE SRGGPSRRGV
ALLRPEPLHR GTADTLLNRV KKLPCQITSY LVAHTLGRRM LYPGSVYLLQ KALMPVLLQG
QARLVEECNG RRAKLLACDG NEIDTMFVDR RGTAQPQGQK LVICCEGNAG FYEVGCISTP
LEAGYSVLGW NHPGFAGSTG VPFPQNEANA MDVVVQFAIH RLGFQPQDII IYAWSIGGFT
ATWAAMSYPD VSAVILDASF DDLVPLALKV MPDSWRGLVT RTVRQHLNLN NAEQLCRYLG
PVLLIRRTKD EIITTTVPED IMSNRGNDLL LKLLQHRYPR VMAEEGLQVV RQWLEASSQL
EEASIYSRWE VEEDWCLSVL RSYQAEHGPD FPWSVGEDMS ADGRRQLALF LARKHLHNFE
ATHCTPLPAQ NFQMPWHL
