ID   ABHDA_PONAB             Reviewed;         306 AA.
AC   Q5REX5;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 65.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR857388; CAH89682.1; -; mRNA.
DR   RefSeq; NP_001124761.1; NM_001131289.1.
DR   AlphaFoldDB; Q5REX5; -.
DR   SMR; Q5REX5; -.
DR   STRING; 9601.ENSPPYP00000015158; -.
DR   ESTHER; ponab-abhda; ABHD10.
DR   MEROPS; S09.023; -.
DR   GeneID; 100171612; -.
DR   KEGG; pon:100171612; -.
DR   CTD; 55347; -.
DR   eggNOG; ENOG502QT21; Eukaryota.
DR   InParanoid; Q5REX5; -.
DR   OrthoDB; 1106156at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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: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_0000280735"
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;  33807 MW;  A72EC43DF60C7F31 CRC64;
     MAVARLAAVA AWVPCRSWGC AAVPFGPHRG LSALLARIPQ RAPRWLPACR QKTSLSFLNR
     PDLPNLAYKK LKGKSPGIIF IPGYLSYMNG TKALAIEEFC KSLGHACIRF DYSGVGSSDG
     NSEESTLGKW RKDVLSIIDD LADGPQILVG SSLGGWLMLH AAIARPEKVV ALLGVATAAD
     TLVTKFNQLP VELKKEVEMK GVWSMPSKYS EEGVYNIQYS FIKEAEHHCL LHSPIPVNCP
     IRLLHGMKDD IVPWHTSMQV ADRVLSTDVD VILRKHSDHR MKEKADIQLL VYTIDDLIDK
     LSTIVN