ABHDA_RAT
ID ABHDA_RAT Reviewed; 297 AA.
AC Q5I0K5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
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 {ECO:0000312|RGD:1308084};
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 MRNA] OF 2-297.
RC TISSUE=Brain, and Liver;
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RC STRAIN=Holtzman; TISSUE=Sperm;
RX PubMed=20966424; DOI=10.2164/jandrol.110.010967;
RA Suryawanshi A.R., Khan S.A., Gajbhiye R.K., Gurav M.Y., Khole V.V.;
RT "Differential proteomics leads to identification of domain specific
RT epididymal sperm proteins.";
RL J. Androl. 32:240-259(2011).
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 -!- TISSUE SPECIFICITY: Expressed in epididymal sperm but not in testicular
CC sperm (at protein level). {ECO:0000269|PubMed:20966424}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; BC088235; AAH88235.1; -; mRNA.
DR RefSeq; NP_001116824.1; NM_001123352.1.
DR RefSeq; XP_008766895.2; XM_008768673.2.
DR AlphaFoldDB; Q5I0K5; -.
DR SMR; Q5I0K5; -.
DR STRING; 10116.ENSRNOP00000043990; -.
DR ESTHER; rat-abhda; ABHD10.
DR iPTMnet; Q5I0K5; -.
DR PhosphoSitePlus; Q5I0K5; -.
DR PaxDb; Q5I0K5; -.
DR GeneID; 303953; -.
DR KEGG; rno:303953; -.
DR UCSC; RGD:1308084; rat.
DR CTD; 55347; -.
DR RGD; 1308084; Abhd10.
DR VEuPathDB; HostDB:ENSRNOG00000054334; -.
DR eggNOG; ENOG502QT21; Eukaryota.
DR HOGENOM; CLU_066961_0_0_1; -.
DR InParanoid; Q5I0K5; -.
DR OMA; TISRWLE; -.
DR OrthoDB; 1106156at2759; -.
DR PhylomeDB; Q5I0K5; -.
DR TreeFam; TF329757; -.
DR Reactome; R-RNO-156588; Glucuronidation.
DR PRO; PR:Q5I0K5; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000043107; Expressed in heart and 18 other tissues.
DR ExpressionAtlas; Q5I0K5; baseline and differential.
DR Genevisible; Q5I0K5; RN.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; ISO:RGD.
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; ISO:RGD.
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 1: Evidence at protein level;
KW Hydrolase; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 44..297
FT /note="Palmitoyl-protein thioesterase ABHD10,
FT mitochondrial"
FT /id="PRO_0000280736"
FT DOMAIN 69..181
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 143
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9NUJ1"
FT ACT_SITE 240
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT ACT_SITE 270
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
SQ SEQUENCE 297 AA; 33153 MW; DEF615DED420BBF8 CRC64;
MAAWVPCRKW GWAAVSFGRH RGLIASLARK PPWAWWLSAC RQKTTLSFLK RPELPSLAYK
RLKGKNPGII FIPGYLSNMN GKKAVAIEEF CKSIGHAFIR FDYSGVGSSD GNLAECSVGK
WRKDVLSILD DIAEGPQILV GSSLGGWLML HAAIARPEKV IALIGIASAT DGVVTQFHSL
PVEMQKEIEM KGEWSLPSKY NKEGYYSIPY SFIKEAAHHC LLHSPIPVTC PVRLLHGMKD
EIVPWHRSLQ VADRVVSPDV DVILRKHSDH RMKETADIHL LICTIDDLID KLSTVTH
