ABHDA_MOUSE
ID ABHDA_MOUSE Reviewed; 297 AA.
AC Q6PE15; Q3TMB4; Q8C3S8; Q8C724; Q8K188;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Palmitoyl-protein thioesterase ABHD10, mitochondrial {ECO:0000303|PubMed:31740833};
DE EC=3.1.2.22 {ECO:0000269|PubMed:31740833};
DE AltName: Full=Acyl-protein thioesterase ABHD10 {ECO:0000303|PubMed:31740833};
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;
DE EC=3.1.1.93 {ECO:0000250|UniProtKB:Q9NUJ1};
DE Flags: Precursor;
GN Name=Abhd10 {ECO:0000312|MGI:MGI:2442422};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Thymus;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4] {ECO:0007744|PDB:6NY9}
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 44-293, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=31740833; DOI=10.1038/s41589-019-0399-y;
RA Cao Y., Qiu T., Kathayat R.S., Azizi S.A., Thorne A.K., Ahn D., Fukata Y.,
RA Fukata M., Rice P.A., Dickinson B.C.;
RT "ABHD10 is an S-depalmitoylase affecting redox homeostasis through
RT peroxiredoxin-5.";
RL Nat. Chem. Biol. 15:1232-1240(2019).
CC -!- FUNCTION: Acts as an acyl-protein thioesterase that hydrolyzes fatty
CC acids from acylated residues in proteins (PubMed:31740833). Regulates
CC the mitochondrial S-depalmitoylation of the nucleophilic active site
CC residue of peroxiredoxin-5/PRDX5, a key antioxidant protein, therefore
CC modulating mitochondrial antioxidant ability (PubMed:31740833). Also
CC catalyzes the deglucuronidation of mycophenolic acid acyl-glucuronide,
CC an active metabolite of the immunosuppressant drug mycophenolate (By
CC similarity). {ECO:0000250|UniProtKB:Q9NUJ1,
CC ECO:0000269|PubMed:31740833}.
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:0000269|PubMed:31740833};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234;
CC Evidence={ECO:0000305|PubMed:31740833};
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PE15-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PE15-2; Sequence=VSP_023893, VSP_023894;
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; AK052670; BAC35091.1; -; mRNA.
DR EMBL; AK084998; BAC39335.1; -; mRNA.
DR EMBL; AK166025; BAE38528.1; -; mRNA.
DR EMBL; BC027656; AAH27656.1; -; mRNA.
DR EMBL; BC058347; AAH58347.1; -; mRNA.
DR CCDS; CCDS28201.1; -. [Q6PE15-1]
DR RefSeq; NP_001258999.1; NM_001272070.1. [Q6PE15-2]
DR RefSeq; NP_766099.3; NM_172511.4. [Q6PE15-1]
DR PDB; 6NY9; X-ray; 1.66 A; B=44-293.
DR PDBsum; 6NY9; -.
DR AlphaFoldDB; Q6PE15; -.
DR SMR; Q6PE15; -.
DR BioGRID; 229387; 9.
DR IntAct; Q6PE15; 1.
DR MINT; Q6PE15; -.
DR STRING; 10090.ENSMUSP00000065282; -.
DR ChEMBL; CHEMBL2146294; -.
DR ESTHER; mouse-abhda; ABHD10.
DR MEROPS; S09.023; -.
DR iPTMnet; Q6PE15; -.
DR PhosphoSitePlus; Q6PE15; -.
DR SwissPalm; Q6PE15; -.
DR EPD; Q6PE15; -.
DR MaxQB; Q6PE15; -.
DR PaxDb; Q6PE15; -.
DR PeptideAtlas; Q6PE15; -.
DR PRIDE; Q6PE15; -.
DR ProteomicsDB; 286055; -. [Q6PE15-1]
DR ProteomicsDB; 286056; -. [Q6PE15-2]
DR Antibodypedia; 32454; 76 antibodies from 21 providers.
DR DNASU; 213012; -.
DR Ensembl; ENSMUST00000066983; ENSMUSP00000065282; ENSMUSG00000033157. [Q6PE15-1]
DR GeneID; 213012; -.
DR KEGG; mmu:213012; -.
DR UCSC; uc007zix.3; mouse. [Q6PE15-2]
DR UCSC; uc007ziy.3; mouse. [Q6PE15-1]
DR CTD; 55347; -.
DR MGI; MGI:2442422; Abhd10.
DR VEuPathDB; HostDB:ENSMUSG00000033157; -.
DR eggNOG; ENOG502QT21; Eukaryota.
DR GeneTree; ENSGT00390000017765; -.
DR HOGENOM; CLU_066961_0_0_1; -.
DR InParanoid; Q6PE15; -.
DR OMA; TISRWLE; -.
DR OrthoDB; 1106156at2759; -.
DR PhylomeDB; Q6PE15; -.
DR TreeFam; TF329757; -.
DR Reactome; R-MMU-156588; Glucuronidation.
DR BioGRID-ORCS; 213012; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Abhd10; mouse.
DR PRO; PR:Q6PE15; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q6PE15; protein.
DR Bgee; ENSMUSG00000033157; Expressed in granulocyte and 229 other tissues.
DR ExpressionAtlas; Q6PE15; baseline and differential.
DR Genevisible; Q6PE15; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; ISO:MGI.
DR GO; GO:0102390; F:mycophenolic acid acyl-glucuronide esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IDA:UniProtKB.
DR GO; GO:0019391; P:glucuronoside catabolic process; ISO:MGI.
DR GO; GO:0002084; P:protein depalmitoylation; IDA: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 3D-structure; Alternative splicing; Hydrolase; Mitochondrion;
KW 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_0000280734"
FT DOMAIN 69..196
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"
FT VAR_SEQ 269
FT /note="D -> AQSVDICGAATPSEWSSKPLGTDS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023893"
FT VAR_SEQ 270..297
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023894"
FT CONFLICT 267
FT /note="Q -> R (in Ref. 1; BAC35091)"
FT /evidence="ECO:0000305"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:6NY9"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:6NY9"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:6NY9"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:6NY9"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:6NY9"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:6NY9"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:6NY9"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:6NY9"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:6NY9"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:6NY9"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:6NY9"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:6NY9"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:6NY9"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:6NY9"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:6NY9"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:6NY9"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:6NY9"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:6NY9"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:6NY9"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:6NY9"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:6NY9"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:6NY9"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:6NY9"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:6NY9"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:6NY9"
FT HELIX 275..292
FT /evidence="ECO:0007829|PDB:6NY9"
SQ SEQUENCE 297 AA; 33040 MW; 7AE4AEBD214ED6CE CRC64;
MAAWAPCRRW GWAAVSFGRH PGLSASLARK PPRAWWLSAC RQKASLSFLN RSELPNLAYK
RLKGKTPGII FIPGYLSNMN GIKAVAVEEF CKSLGHAFIR FDYSGIGSSD GNLAECTVGK
WRKDVLSILD DVAEGPQILV GSSLGGWLML HAAIARPEKV IALIGIATAA DGLVTQYHAL
PVETQKEIEM KGEWTLPSRY NKEGYFRIPY SFIKEAEHHC LLHSPIPVTC PVRLLHGMKD
EIVPWQRSLQ VADRIVSPDV DVILRKQGDH RMKEKADIHL LICTIDDLID KLSTVVP
