ABHD3_BOVIN
ID ABHD3_BOVIN Reviewed; 411 AA.
AC Q0VC00;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Phospholipase ABHD3 {ECO:0000305};
DE EC=3.1.1.32 {ECO:0000250|UniProtKB:Q91ZH7};
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:Q91ZH7};
DE AltName: Full=Abhydrolase domain-containing protein 3 {ECO:0000250|UniProtKB:Q8WU67};
GN Name=ABHD3 {ECO:0000250|UniProtKB:Q8WU67};
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].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phospholipase that may play a role in phospholipids
CC remodeling. May selectively cleave myristate (C14)-containing
CC phosphatidylcholines through its predominant phospholipase 1 activity,
CC cleaving preferentially acyl groups in sn1 position. In parallel, may
CC have a minor phospholipase 2 activity acting on acyl groups in position
CC sn2. In addition to (C14)-containing phosphatidylcholines, may also act
CC on other medium-chain-containing and oxidatively truncated
CC phospholipids. {ECO:0000250|UniProtKB:Q91ZH7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H(+) + tetradecanoate; Xref=Rhea:RHEA:54388,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:76084, ChEBI:CHEBI:86094;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54389;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-tetradecanoyl-
CC sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:54392,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:64489, ChEBI:CHEBI:86094;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54393;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphocholine + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:54396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:76079, ChEBI:CHEBI:86102;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54397;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphocholine + H2O = 2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphocholine + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:54400, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:76085, ChEBI:CHEBI:86162;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54401;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 2-
CC tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:54404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:131738;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54405;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-
CC octadecanoyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:54408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:73858, ChEBI:CHEBI:75220;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54409;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:54456, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:64489;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54457;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-pentanoyl-sn-glycero-3-phosphocholine + H2O =
CC 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + pentanoate;
CC Xref=Rhea:RHEA:54460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31011, ChEBI:CHEBI:73858, ChEBI:CHEBI:138211;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54461;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-hexanoyl-sn-glycero-3-phosphocholine + H2O =
CC 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexanoate;
CC Xref=Rhea:RHEA:54464, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:73858, ChEBI:CHEBI:138212;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54465;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-octanoyl-sn-glycero-3-phosphocholine + H2O =
CC 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + octanoate;
CC Xref=Rhea:RHEA:54468, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25646, ChEBI:CHEBI:73858, ChEBI:CHEBI:138213;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54469;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-nonanoyl-sn-glycero-3-phosphocholine + H2O =
CC 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + nonanoate;
CC Xref=Rhea:RHEA:54472, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32361, ChEBI:CHEBI:73858, ChEBI:CHEBI:138214;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54473;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-nonadioyl-sn-glycero-3-phosphocholine + H2O =
CC 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + nonanedioate;
CC Xref=Rhea:RHEA:54552, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64496, ChEBI:CHEBI:78208, ChEBI:CHEBI:138269;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54553;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-nonadioyl-sn-glycero-3-phosphocholine + H2O =
CC 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + nonanedioate;
CC Xref=Rhea:RHEA:41388, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:78207, ChEBI:CHEBI:78208;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41389;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine +
CC H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + 9-oxononanoate +
CC H(+); Xref=Rhea:RHEA:41179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:61042, ChEBI:CHEBI:72998, ChEBI:CHEBI:77812;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41180;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine
CC + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + 5-oxopentanoate
CC + H(+); Xref=Rhea:RHEA:40483, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16120, ChEBI:CHEBI:72998, ChEBI:CHEBI:77890;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40484;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-glutaroyl-sn-glycero-3-phosphocholine + H2O =
CC 1-hexadecanoyl-sn-glycero-3-phosphocholine + glutarate + H(+);
CC Xref=Rhea:RHEA:41159, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30921, ChEBI:CHEBI:72998, ChEBI:CHEBI:77756;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41160;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-
CC O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC Evidence={ECO:0000250|UniProtKB:Q91ZH7};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 4
CC family. {ECO:0000305}.
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DR EMBL; BC120421; AAI20422.1; -; mRNA.
DR RefSeq; NP_001069655.1; NM_001076187.1.
DR AlphaFoldDB; Q0VC00; -.
DR STRING; 9913.ENSBTAP00000024863; -.
DR ESTHER; bovin-abhd3; abh_upf0017.
DR PRIDE; Q0VC00; -.
DR Ensembl; ENSBTAT00000024863; ENSBTAP00000024863; ENSBTAG00000005709.
DR GeneID; 539795; -.
DR KEGG; bta:539795; -.
DR CTD; 171586; -.
DR VEuPathDB; HostDB:ENSBTAG00000005709; -.
DR VGNC; VGNC:58350; ABHD3.
DR GeneTree; ENSGT00950000182902; -.
DR InParanoid; Q0VC00; -.
DR OMA; RNDPFVP; -.
DR OrthoDB; 1162019at2759; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000005709; Expressed in spermatocyte and 102 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008126; F:acetylesterase activity; IBA:GO_Central.
DR GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; ISS:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0034338; F:short-chain carboxylesterase activity; IBA:GO_Central.
DR GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
DR GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0051793; P:medium-chain fatty acid catabolic process; IBA:GO_Central.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000952; AB_hydrolase_4_CS.
DR InterPro; IPR012020; ABHD4.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF005211; Ab_hydro_YheT; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01133; UPF0017; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Lipid metabolism; Membrane; Phospholipid metabolism;
KW Reference proteome; Serine esterase; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..411
FT /note="Phospholipase ABHD3"
FT /id="PRO_0000280207"
FT TRANSMEM 25..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 140..247
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 220
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 346
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 375
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 411 AA; 46527 MW; 6F8F142688B46185 CRC64;
MQRLAMDLRM LSRELSHYLE HQVRVGFFGS GVGFSLILGF SVAYACYYLS SIAKKPQLVT
GGESFSRFLQ DHCPVVTETY YPTVWCWESR GQTLLRPFIT SKPLVQYRNE LIKTADGGQI
SLDWFDNDNS KHYMDASTRP TVLLLPGLTG TSKESYILHM IHLSEELGYR YVVFNNRGVA
GENLLTPRTY CCSNTEDLET VIHHVHSLYP SAPFLAAGVS MGGMLLLNYL GKIGPKTPLK
AAATFSVGWN TFACSESLEK PLNWLLFNYY LTTCLQSSVN KHRHMFVKQI DVDHVMKAKS
IREFDKRFTS VMFGYRTIDD YYTDASPNRR LKSVGIPVLC LNSVDDVFSP SHAIPIETAK
QNPNVALVLT SYGGHIGFLE GIWPRQSTYM DRVFKQFVQA MIEHGHELSS M
