ABHGA_RAT
ID ABHGA_RAT Reviewed; 558 AA.
AC Q6MG55;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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:0000312|RGD:1303164};
GN Synonyms=Bat5 {ECO:0000250|UniProtKB:O95870};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BX883045; CAE83991.1; -; Genomic_DNA.
DR EMBL; BC091227; AAH91227.1; -; mRNA.
DR RefSeq; NP_997696.1; NM_212531.2.
DR AlphaFoldDB; Q6MG55; -.
DR SMR; Q6MG55; -.
DR STRING; 10116.ENSRNOP00000001121; -.
DR ChEMBL; CHEMBL4523343; -.
DR ESTHER; ratno-q6mg55; ABHD16.
DR iPTMnet; Q6MG55; -.
DR PhosphoSitePlus; Q6MG55; -.
DR SwissPalm; Q6MG55; -.
DR jPOST; Q6MG55; -.
DR PaxDb; Q6MG55; -.
DR PRIDE; Q6MG55; -.
DR GeneID; 361796; -.
DR KEGG; rno:361796; -.
DR UCSC; RGD:1303164; rat.
DR CTD; 7920; -.
DR RGD; 1303164; Abhd16a.
DR eggNOG; KOG1553; Eukaryota.
DR InParanoid; Q6MG55; -.
DR OrthoDB; 580247at2759; -.
DR PhylomeDB; Q6MG55; -.
DR TreeFam; TF314267; -.
DR PRO; PR:Q6MG55; -.
DR Proteomes; UP000002494; 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 GO; GO:1905344; P:prostaglandin catabolic process; ISO:RGD.
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_0000333744"
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; 63038 MW; 48DDFC0D95C2021F CRC64;
MAKLLSCVLG PRLYKIYRER DTDRAATSVP ETPTAVPAAS SSSWDSYYQP RALEKHADSI
LALASVFWSI SYYSSPFAFF YLYRKGYLSL SKVVPFSHYA GTLLVLLAGV ACLRGIGRWT
NPQYRQFITI LEATHRNQSA ENKRQLANYN FDFRSWPVDF HWEEPSSRKG SRGGPSRRGV
ALLRPEPLHR GTADTFLNRV KKLPCQITSY LVAHTLGRRM LYPGSVYLLQ KALMPVLLQG
QARLVEECNG RRAKLLACDG NEIDTMFVDR RGTAEPQGQK LVICCEGNAG FYEVGCVSTP
LEAGYSVLGW NHPGFAGSTG VPFPQNEANA MDVVVQFAIH RLGFQPQDIV IYAWSIGGFT
ATWAAMSYPD ISAVILDASF DDLVPLALKV MPDSWRALVT RTVRQHLNLN NAEQLCRFQG
PVLLVRRTKD EIITTTVPED IMSNRGNDLL LKLLQFRYPR VMTEEGLRAV RQWLEASSQL
EEASIYSRWE VDEDWCVSVL RSYQAEHGPD FPWSVGEDMS VDGRRQLALF LARKHLHNFE
ATHCTPLPAQ HFQMPWCL
