ESTD_MOUSE
ID ESTD_MOUSE Reviewed; 282 AA.
AC Q9R0P3; Q80ZX4; Q9CWI4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=S-formylglutathione hydrolase;
DE Short=FGH;
DE EC=3.1.2.12;
DE AltName: Full=Esterase 10;
DE AltName: Full=Esterase D;
DE AltName: Full=Sid 478;
GN Name=Esd; Synonyms=Es10, Sid478;
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 [MRNA].
RA Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
RT "Mouse homologue of human esterase D sid478.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-200, SUCCINYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-4, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Serine hydrolase involved in the detoxification of
CC formaldehyde. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-formylglutathione = formate + glutathione + H(+);
CC Xref=Rhea:RHEA:14961, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:57688, ChEBI:CHEBI:57925; EC=3.1.2.12;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB27115.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB025408; BAA84693.1; -; mRNA.
DR EMBL; AK007527; BAB25090.1; -; mRNA.
DR EMBL; AK010683; BAB27115.1; ALT_INIT; mRNA.
DR EMBL; AK021209; BAB32330.1; -; mRNA.
DR EMBL; AK079131; BAC37555.1; -; mRNA.
DR EMBL; AK088115; BAC40154.1; -; mRNA.
DR EMBL; BC046766; AAH46766.2; -; mRNA.
DR CCDS; CCDS36975.1; -.
DR RefSeq; NP_058599.1; NM_016903.5.
DR AlphaFoldDB; Q9R0P3; -.
DR SMR; Q9R0P3; -.
DR BioGRID; 199507; 2.
DR IntAct; Q9R0P3; 1.
DR MINT; Q9R0P3; -.
DR STRING; 10090.ENSMUSP00000022573; -.
DR ChEMBL; CHEMBL3259483; -.
DR ESTHER; mouse-ES10; A85-EsteraseD-FGH.
DR iPTMnet; Q9R0P3; -.
DR PhosphoSitePlus; Q9R0P3; -.
DR SwissPalm; Q9R0P3; -.
DR EPD; Q9R0P3; -.
DR jPOST; Q9R0P3; -.
DR MaxQB; Q9R0P3; -.
DR PaxDb; Q9R0P3; -.
DR PRIDE; Q9R0P3; -.
DR ProteomicsDB; 275652; -.
DR Antibodypedia; 23747; 225 antibodies from 29 providers.
DR DNASU; 13885; -.
DR Ensembl; ENSMUST00000022573; ENSMUSP00000022573; ENSMUSG00000021996.
DR GeneID; 13885; -.
DR KEGG; mmu:13885; -.
DR UCSC; uc007uqd.2; mouse.
DR CTD; 2098; -.
DR MGI; MGI:95421; Esd.
DR VEuPathDB; HostDB:ENSMUSG00000021996; -.
DR eggNOG; KOG3101; Eukaryota.
DR GeneTree; ENSGT00390000011864; -.
DR HOGENOM; CLU_056472_0_0_1; -.
DR InParanoid; Q9R0P3; -.
DR OMA; TFMEDHL; -.
DR PhylomeDB; Q9R0P3; -.
DR TreeFam; TF300793; -.
DR Reactome; R-MMU-156590; Glutathione conjugation.
DR BioGRID-ORCS; 13885; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Esd; mouse.
DR PRO; PR:Q9R0P3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9R0P3; protein.
DR Bgee; ENSMUSG00000021996; Expressed in right kidney and 227 other tissues.
DR ExpressionAtlas; Q9R0P3; baseline and differential.
DR Genevisible; Q9R0P3; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0018738; F:S-formylglutathione hydrolase activity; IBA:GO_Central.
DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR014186; S-formylglutathione_hydrol.
DR PANTHER; PTHR10061; PTHR10061; 1.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR02821; fghA_ester_D; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoplasmic vesicle; Hydrolase; Reference proteome;
KW Serine esterase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CHAIN 2..282
FT /note="S-formylglutathione hydrolase"
FT /id="PRO_0000210340"
FT ACT_SITE 149
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 4
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 200
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 1
FT /note="M -> V (in Ref. 2; BAB27115)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 282 AA; 31320 MW; 9151D328FBB460A6 CRC64;
MALKQISSNR CFGGLQKVFE HSSVELKCKM RFAVYLPPQA ESGKCPALYW LSGLTCTEQN
FISKSGYQQA ASEHGLVVIA PDTSPRGCNI KGEDDSWDFG TGAGFYVNAT EDPWKANYRM
YSYVTEELPQ LINANFPVDP QRMSIFGHSM GGHGALICAL KNPGKYRSVS AFAPICNPVL
CSWGKKAFSG YLGPDESKWK AYDATCLVKA YSGSQIDILI DQGKDDEFLS NGQLLPDNFI
AACTEKKIPV VFRLQEGYDH SYYFIATFIA DHIRHHAKYL NA
