ABHD4_BOVIN
ID ABHD4_BOVIN Reviewed; 342 AA.
AC Q5EA59; Q24K17;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=(Lyso)-N-acylphosphatidylethanolamine lipase {ECO:0000305};
DE EC=3.1.1.-;
DE AltName: Full=Alpha/beta hydrolase domain-containing protein 4 {ECO:0000305};
DE Short=Abhydrolase domain-containing protein 4 {ECO:0000250|UniProtKB:Q8TB40};
DE AltName: Full=Alpha/beta-hydrolase 4;
DE AltName: Full=Protein ABHD4 {ECO:0000305};
DE EC=3.-.-.-;
GN Name=ABHD4 {ECO:0000250|UniProtKB:Q8TB40};
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lysophospholipase selective for N-acyl
CC phosphatidylethanolamine (NAPE). Contributes to the biosynthesis of N-
CC acyl ethanolamines, including the endocannabinoid anandamide by
CC hydrolyzing the sn-1 and sn-2 acyl chains from N-acyl
CC phosphatidylethanolamine (NAPE) generating glycerophospho-N-acyl
CC ethanolamine (GP-NAE), an intermediate for N-acyl ethanolamine
CC biosynthesis. Hydrolyzes substrates bearing saturated, monounsaturated,
CC polyunsaturated N-acyl chains. Shows no significant activity towards
CC other lysophospholipids, including lysophosphatidylcholine,
CC lysophosphatidylethanolamine and lysophosphatidylserine.
CC {ECO:0000250|UniProtKB:Q8VD66}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine = a
CC fatty acid + H(+) + N,1-diacyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:45460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:62537, ChEBI:CHEBI:85216;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45461;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-sn-
CC glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45384,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:85217, ChEBI:CHEBI:85226;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45385;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-octadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-octadecanoyl-sn-
CC glycero-3-phospho-ethanolamine; Xref=Rhea:RHEA:45388,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:85219, ChEBI:CHEBI:85227;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45389;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-eicosanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-eicosanoyl-sn-
CC glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45392,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:85221, ChEBI:CHEBI:85228;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45393;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45396,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:85222, ChEBI:CHEBI:85229;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45397;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1-(9Z-octadecenoyl)-
CC sn-glycero-3-phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:45400, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:85223, ChEBI:CHEBI:85230;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45401;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(N-
CC hexadecanoyl)-serine + H2O = (9Z)-octadecenoate + 1-octadecanoyl-2-
CC hydroxy-sn-glycero-3-phospho-(N-hexadecanoyl)-serine + H(+);
CC Xref=Rhea:RHEA:55236, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:138661, ChEBI:CHEBI:138662;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55237;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-
CC N-hexadecanoyl-ethanolamine + H2O = (9Z)-octadecenoate + 1-O-(1Z-
CC octadecenyl)-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + H(+);
CC Xref=Rhea:RHEA:55240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:137009, ChEBI:CHEBI:138663;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55241;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1-diacyl-sn-glycero-3-phosphoethanolamine = a fatty
CC acid + H(+) + N-acyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:45420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:85216, ChEBI:CHEBI:85225;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45421;
CC Evidence={ECO:0000250|UniProtKB:Q8VD66};
CC -!- SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Thr-291 is present instead of the conserved His which is
CC expected to be an active site residue. {ECO:0000305}.
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DR EMBL; BT020710; AAX08727.1; -; mRNA.
DR EMBL; BC114030; AAI14031.1; -; mRNA.
DR RefSeq; NP_001029540.1; NM_001034368.1.
DR AlphaFoldDB; Q5EA59; -.
DR SMR; Q5EA59; -.
DR STRING; 9913.ENSBTAP00000022154; -.
DR ESTHER; bovin-abhd4; CGI-58_ABHD5_ABHD4.
DR PaxDb; Q5EA59; -.
DR PRIDE; Q5EA59; -.
DR GeneID; 509896; -.
DR KEGG; bta:509896; -.
DR CTD; 63874; -.
DR eggNOG; KOG4409; Eukaryota.
DR HOGENOM; CLU_017361_0_1_1; -.
DR InParanoid; Q5EA59; -.
DR OrthoDB; 1555935at2759; -.
DR TreeFam; TF314196; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IBA:GO_Central.
DR GO; GO:0004622; F:lysophospholipase activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; ISS:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Lipid degradation; Lipid metabolism; Reference proteome.
FT CHAIN 1..342
FT /note="(Lyso)-N-acylphosphatidylethanolamine lipase"
FT /id="PRO_0000080863"
FT DOMAIN 70..324
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
SQ SEQUENCE 342 AA; 38797 MW; F0536EF0FA2757E0 CRC64;
MADDLEQQPQ GWLSSWLPTW RPTSMSQLKN VEARILQCLQ NKFLARYVSL PNQNKIWTVT
VSPELRDRTP LVMVHGFGGG VGLWILNMDS LSTRRTLHTF DLLGFGRSSR PTFPRDPEGA
EDEFVTSIET WRESMGIPSM ILLGHSLGGF LATSYSIKYP DRVKHLILVD PWGFPLRPAD
PSQVRAPPTW VKAVASVLGR SNPLAVLRVA GPWGPGLVQR FRPDFKRKFA DFFDDDTISE
YIYHCNAQNP SGETAFKAMM ESFGWARRPM LERIHLIRKD VPITMIYGAN TWIDTSTGKK
VKLQRPDSYV RDLEIEGASH HVYADQPHIF NAVVEEICDS VD
