ABHGA_BOVIN
ID ABHGA_BOVIN Reviewed; 558 AA.
AC Q1JPD2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 72.
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};
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).
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; BT025421; ABF57377.1; -; mRNA.
DR RefSeq; NP_001069073.1; NM_001075605.1.
DR AlphaFoldDB; Q1JPD2; -.
DR SMR; Q1JPD2; -.
DR STRING; 9913.ENSBTAP00000000755; -.
DR ESTHER; bovin-ABHD16A; ABHD16.
DR PaxDb; Q1JPD2; -.
DR PRIDE; Q1JPD2; -.
DR GeneID; 513252; -.
DR KEGG; bta:513252; -.
DR CTD; 7920; -.
DR eggNOG; KOG1553; Eukaryota.
DR InParanoid; Q1JPD2; -.
DR OrthoDB; 580247at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0047372; F:acylglycerol lipase 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: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_0000333741"
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 REGION 23..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 63304 MW; D3BA4EFB1DCCF00E CRC64;
MAKLLSCVLG PRLYKIYRER DSERAPSSVP GTPTSVTNPH SSSWDTYYQP RALEKHADSI
LALASVFWSI SYYSSPFAFF YLYRKGYLSL SKVVPFSHYA GTLLLLLAGV ACLRGIGRWT
NPQYRQFITI LEATHRNHSA ENKRQLANYN FDFRSWPVDF HWEEPSSRKE SRGGPSRRGV
ALLRPEPLHR GTADTFLNRV KKLPCQITSY LVAHTLGRRM LYPGSVYLLQ KALMPVLLQG
QARLVEECHG RRAKLLACDG NEIDTMFVDR RGTAEPQGQK LVICCEGNAG FYEVGCVSTP
LEAGYSVLGW NHPGFAGSTG VPFPQNEANA MDVVVQFAIH RLGFQPEDII LYAWSIGGFT
ATWAAMSYPD ISAVILDASF DDLVPLALKV MPDSWRGLVT RTVRQHLNLN NAEQLCRYQG
PVLLIRRTRD EIITTTVPED IMSNRGNDLL LKFLQHRYPR VMAEEGLRVV RQWLEASSQL
EEASIYSRWE VEEDWCLSVL RSYQAEHGPE FPWSVGEDMS ADGRRQLALF LAQKHLNNFE
ATHCTPLPAQ NFQMPWHL
