ABHDA_BOVIN
ID ABHDA_BOVIN Reviewed; 306 AA.
AC Q5E9H9;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Palmitoyl-protein thioesterase ABHD10, mitochondrial {ECO:0000250|UniProtKB:Q9NUJ1};
DE EC=3.1.2.22 {ECO:0000250|UniProtKB:Q9NUJ1};
DE AltName: Full=Acyl-protein thioesterase ABHD10 {ECO:0000250|UniProtKB:Q9NUJ1};
DE AltName: Full=Alpha/beta hydrolase domain-containing protein 10 {ECO:0000250|UniProtKB:Q9NUJ1};
DE Short=Abhydrolase domain-containing protein 10 {ECO:0000250|UniProtKB:Q9NUJ1};
DE AltName: Full=Mycophenolic acid acyl-glucuronide esterase, mitochondrial {ECO:0000250|UniProtKB:Q9NUJ1};
DE EC=3.1.1.93 {ECO:0000250|UniProtKB:Q9NUJ1};
DE Flags: Precursor;
GN Name=ABHD10;
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=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as an acyl-protein thioesterase that hydrolyzes fatty
CC acids from acylated residues in proteins. Regulates the mitochondrial
CC S-depalmitoylation of the nucleophilic active site residue of
CC peroxiredoxin-5/PRDX5, a key antioxidant protein, therefore modulating
CC mitochondrial antioxidant ability. Also catalyzes the deglucuronidation
CC of mycophenolic acid acyl-glucuronide, an active metabolite of the
CC immunosuppressant drug mycophenolate. {ECO:0000250|UniProtKB:Q9NUJ1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:74151; EC=3.1.2.22;
CC Evidence={ECO:0000250|UniProtKB:Q9NUJ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234;
CC Evidence={ECO:0000250|UniProtKB:Q9NUJ1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + mycophenolic acid O-acyl-beta-D-glucuronide = D-
CC glucuronate + H(+) + mycophenolate; Xref=Rhea:RHEA:34179,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58720,
CC ChEBI:CHEBI:62932, ChEBI:CHEBI:66982; EC=3.1.1.93;
CC Evidence={ECO:0000250|UniProtKB:Q9NUJ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34180;
CC Evidence={ECO:0000250|UniProtKB:Q9NUJ1};
CC -!- ACTIVITY REGULATION: Inhibited by palmostatin-B.
CC {ECO:0000250|UniProtKB:Q9NUJ1}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NUJ1}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; BT020941; AAX08958.1; -; mRNA.
DR EMBL; BC112739; AAI12740.1; -; mRNA.
DR RefSeq; NP_001015606.1; NM_001015606.2.
DR AlphaFoldDB; Q5E9H9; -.
DR SMR; Q5E9H9; -.
DR STRING; 9913.ENSBTAP00000006038; -.
DR ESTHER; bovin-ABHDA; ABHD10.
DR PaxDb; Q5E9H9; -.
DR PRIDE; Q5E9H9; -.
DR Ensembl; ENSBTAT00000006038; ENSBTAP00000006038; ENSBTAG00000004601.
DR GeneID; 515563; -.
DR KEGG; bta:515563; -.
DR CTD; 55347; -.
DR VEuPathDB; HostDB:ENSBTAG00000004601; -.
DR VGNC; VGNC:25488; ABHD10.
DR eggNOG; ENOG502QT21; Eukaryota.
DR GeneTree; ENSGT00390000017765; -.
DR HOGENOM; CLU_066961_0_0_1; -.
DR InParanoid; Q5E9H9; -.
DR OMA; TISRWLE; -.
DR OrthoDB; 1106156at2759; -.
DR TreeFam; TF329757; -.
DR Reactome; R-BTA-156588; Glucuronidation.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000004601; Expressed in oocyte and 105 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0102390; F:mycophenolic acid acyl-glucuronide esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; ISS:UniProtKB.
DR GO; GO:0019391; P:glucuronoside catabolic process; IEA:Ensembl.
DR GO; GO:0002084; P:protein depalmitoylation; ISS:UniProtKB.
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 SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..52
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 53..306
FT /note="Palmitoyl-protein thioesterase ABHD10,
FT mitochondrial"
FT /id="PRO_0000280732"
FT DOMAIN 78..177
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9NUJ1"
FT ACT_SITE 249
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT ACT_SITE 279
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
SQ SEQUENCE 306 AA; 33983 MW; 13EAC6357029E0C7 CRC64;
MAGVGLAAVP AWVPCRRWGL AAVTFGFHHG LSTLLARKTE RAPQWLRACR HKTSISFLSR
PDLPNLAYKR LKGKSPGIIF IPGYISNMNG TKALAIEEFC KSLGHAYIRF DYSGVGNSDG
NLEECTVGKW RKDVLSIIDD LAEGPQILVG SSLGGWLMFH AAIARPQKVV ALVGVATAVD
GLVTQFNQLP IETKKEIEMK GVWPMPSKYS EEGVYRIQYS VIKEAEHHCL LHSPIPVKCP
VRLLHGMKDD IVPWHTSVQV ADRVVSTDVD VILRKNSDHR MKEKADIQLL VYTIDDLIDK
LSTIVH
