Full text data of ESD
ESD
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
S-formylglutathione hydrolase; FGH; 3.1.2.12 (Esterase D; Methylumbelliferyl-acetate deacetylase; 3.1.1.56)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
S-formylglutathione hydrolase; FGH; 3.1.2.12 (Esterase D; Methylumbelliferyl-acetate deacetylase; 3.1.1.56)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00411706
IPI00411706 Esterase D serine esterase activity, A carboxylic ester + H2O = an alcohol + a carboxylate soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic vescicles n/a found at its expected molecular weight found at molecular weight
IPI00411706 Esterase D serine esterase activity, A carboxylic ester + H2O = an alcohol + a carboxylate soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic vescicles n/a found at its expected molecular weight found at molecular weight
UniProt
P10768
ID ESTD_HUMAN Reviewed; 282 AA.
AC P10768; Q5TBU8; Q5TBV0; Q5TBV2; Q9BVJ2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1994, sequence version 2.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=S-formylglutathione hydrolase;
DE Short=FGH;
DE EC=3.1.2.12;
DE AltName: Full=Esterase D;
DE AltName: Full=Methylumbelliferyl-acetate deacetylase;
DE EC=3.1.1.56;
GN Name=ESD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3462698; DOI=10.1073/pnas.83.17.6337;
RA Lee E.Y.-H.P., Lee W.-H.;
RT "Molecular cloning of the human esterase D gene, a genetic marker of
RT retinoblastoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6337-6341(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3164702; DOI=10.1007/BF00280552;
RA Young L.-J.S., Lee E.Y.-H.P., To H., Bookstein R., Shew J.-Y.,
RA Donoso L.A., Sery T., Giblin M., Shields J.A., Lee W.-H.;
RT "Human esterase D gene: complete cDNA sequence, genomic structure, and
RT application in the genetic diagnosis of human retinoblastoma.";
RL Hum. Genet. 79:137-141(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-257.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-257.
RC TISSUE=Muscle;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 65-86 AND 254-274, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 150-186, AND PROTEIN SEQUENCE OF
RP 150-175.
RX PubMed=3462714; DOI=10.1073/pnas.83.17.6573;
RA Squire J., Dryja T.P., Dunn J., Goddard A., Hofmann T., Musarella M.,
RA Willard H.F., Becker A.J., Gallie B.L., Phillips R.A.;
RT "Cloning of the esterase D gene: a polymorphic gene probe closely
RT linked to the retinoblastoma locus on chromosome 13.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6573-6577(1986).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 168-200.
RA Tuchhida S., Ikemoto S., Kajii E.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP FUNCTION AS METHYLUMBELLIFERYL-ACETATE DEACETYLASE, AND CATALYTIC
RP ACTIVITY.
RX PubMed=4768551; DOI=10.1111/j.1469-1809.1973.tb01820.x;
RA Hopkinson D.A., Mestriner M.A., Cortner J., Harris H.;
RT "Esterase D: a new human polymorphism.";
RL Ann. Hum. Genet. 37:119-137(1973).
RN [11]
RP FUNCTION.
RX PubMed=3770744; DOI=10.1007/BF00282085;
RA Eiberg H., Mohr J.;
RT "Identity of the polymorphisms for esterase D and S-formylglutathione
RT hydrolase in red blood cells.";
RL Hum. Genet. 74:174-175(1986).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-200, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), MUTAGENESIS OF LEU-54; SER-149;
RP MET-150; ASP-226 AND HIS-260, AND ACTIVE SITE.
RX PubMed=19126594; DOI=10.1096/fj.08-125286;
RA Wu D., Li Y., Song G., Zhang D., Shaw N., Liu Z.-J.;
RT "Crystal structure of human esterase D: a potential genetic marker of
RT retinoblastoma.";
RL FASEB J. 23:1441-1446(2009).
RN [15]
RP VARIANT GLU-190.
RX PubMed=7907313; DOI=10.1007/BF00212018;
RA Tsuchida S., Fukui E., Ikemoto S.;
RT "Molecular analysis of esterase D polymorphism.";
RL Hum. Genet. 93:255-258(1994).
RN [16]
RP VARIANT GLU-190.
RX PubMed=12721789; DOI=10.1007/s10038-003-0021-7;
RA Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C.,
RA Nakamura Y.;
RT "Catalog of 680 variations among eight cytochrome p450 (CYP) genes,
RT nine esterase genes, and two other genes in the Japanese population.";
RL J. Hum. Genet. 48:249-270(2003).
CC -!- FUNCTION: Serine hydrolase involved in the detoxification of
CC formaldehyde.
CC -!- CATALYTIC ACTIVITY: S-formylglutathione + H(2)O = glutathione +
CC formate.
CC -!- CATALYTIC ACTIVITY: 4-methylumbelliferyl acetate + H(2)O = 4-
CC methylumbelliferone + acetate.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle.
CC -!- POLYMORPHISM: There are two major electrophoretic isotypes. The
CC sequence of the ESD*1 variant is shown.
CC -!- SIMILARITY: Belongs to the esterase D family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI12225.1; Type=Erroneous gene model prediction;
CC Sequence=CAI12226.1; Type=Erroneous gene model prediction;
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DR EMBL; M13450; AAA52408.1; ALT_SEQ; mRNA.
DR EMBL; AF112219; AAC99788.1; -; mRNA.
DR EMBL; BT007059; AAP35708.1; -; mRNA.
DR EMBL; AL136958; CAI12225.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL136958; CAI12226.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL136958; CAI12228.1; -; Genomic_DNA.
DR EMBL; BC001169; AAH01169.1; -; mRNA.
DR EMBL; AF052509; AAC06298.1; -; Genomic_DNA.
DR PIR; A23543; A23543.
DR RefSeq; NP_001975.1; NM_001984.1.
DR RefSeq; XP_005266335.1; XM_005266278.1.
DR UniGene; Hs.432491; -.
DR PDB; 3FCX; X-ray; 1.50 A; A/B=1-282.
DR PDBsum; 3FCX; -.
DR ProteinModelPortal; P10768; -.
DR SMR; P10768; 3-281.
DR IntAct; P10768; 4.
DR MINT; MINT-5002423; -.
DR STRING; 9606.ENSP00000367992; -.
DR ChEMBL; CHEMBL2189130; -.
DR DrugBank; DB00143; Glutathione.
DR MEROPS; S09.990; -.
DR PhosphoSite; P10768; -.
DR DMDM; 544254; -.
DR DOSAC-COBS-2DPAGE; P10768; -.
DR OGP; P10768; -.
DR REPRODUCTION-2DPAGE; IPI00411706; -.
DR UCD-2DPAGE; P10768; -.
DR PaxDb; P10768; -.
DR PeptideAtlas; P10768; -.
DR PRIDE; P10768; -.
DR DNASU; 2098; -.
DR Ensembl; ENST00000378720; ENSP00000367992; ENSG00000139684.
DR GeneID; 2098; -.
DR KEGG; hsa:2098; -.
DR UCSC; uc001vbn.3; human.
DR CTD; 2098; -.
DR GeneCards; GC13M047345; -.
DR HGNC; HGNC:3465; ESD.
DR HPA; HPA039700; -.
DR MIM; 133280; gene.
DR neXtProt; NX_P10768; -.
DR PharmGKB; PA27882; -.
DR eggNOG; COG0627; -.
DR HOGENOM; HOG000263929; -.
DR HOVERGEN; HBG001326; -.
DR InParanoid; P10768; -.
DR KO; K01070; -.
DR OMA; SVELKCK; -.
DR OrthoDB; EOG7TF79G; -.
DR PhylomeDB; P10768; -.
DR ChiTaRS; ESD; human.
DR EvolutionaryTrace; P10768; -.
DR GeneWiki; ESD_(gene); -.
DR GenomeRNAi; 2098; -.
DR NextBio; 8487; -.
DR PRO; PR:P10768; -.
DR Bgee; P10768; -.
DR CleanEx; HS_ESD; -.
DR Genevestigator; P10768; -.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; NAS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; NAS:UniProtKB.
DR GO; GO:0047374; F:methylumbelliferyl-acetate deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0018738; F:S-formylglutathione hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:InterPro.
DR InterPro; IPR000801; Esterase_put.
DR InterPro; IPR014186; S-formylglutathione_hydrol.
DR PANTHER; PTHR10061; PTHR10061; 1.
DR Pfam; PF00756; Esterase; 1.
DR TIGRFAMs; TIGR02821; fghA_ester_D; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Cytoplasmic vesicle; Direct protein sequencing; Hydrolase;
KW Polymorphism; Reference proteome; Serine esterase.
FT CHAIN 1 282 S-formylglutathione hydrolase.
FT /FTId=PRO_0000210339.
FT ACT_SITE 149 149 Charge relay system.
FT ACT_SITE 226 226 Charge relay system.
FT ACT_SITE 260 260 Charge relay system.
FT MOD_RES 200 200 N6-acetyllysine.
FT VARIANT 190 190 G -> E (in allele ESD*2; dbSNP:rs9778).
FT /FTId=VAR_005202.
FT VARIANT 257 257 G -> D (in dbSNP:rs15303).
FT /FTId=VAR_022275.
FT MUTAGEN 54 54 L->A: 83% of wild-type activity.
FT MUTAGEN 149 149 S->A: Loss of activity.
FT MUTAGEN 149 149 S->T: 1.3% of wild-type activity.
FT MUTAGEN 150 150 M->A: 62% increase in activity.
FT MUTAGEN 226 226 D->A: 4.3% of wild-type activity.
FT MUTAGEN 226 226 D->N: 9% of wild-type activity.
FT MUTAGEN 260 260 H->A: 3% of wild-type activity.
FT MUTAGEN 260 260 H->Q: 1.3% of wild-type activity.
FT STRAND 4 11
FT STRAND 14 23
FT TURN 24 27
FT STRAND 28 36
FT HELIX 38 41
FT STRAND 45 51
FT HELIX 59 64
FT HELIX 68 74
FT STRAND 77 81
FT HELIX 114 117
FT HELIX 120 125
FT HELIX 127 135
FT STRAND 136 148
FT HELIX 150 160
FT TURN 163 165
FT STRAND 169 173
FT HELIX 178 180
FT HELIX 182 192
FT HELIX 199 202
FT HELIX 204 208
FT STRAND 218 223
FT HELIX 227 230
FT HELIX 236 245
FT STRAND 250 255
FT HELIX 262 279
SQ SEQUENCE 282 AA; 31463 MW; BFC20D5FA2BB0DCE CRC64;
MALKQISSNK CFGGLQKVFE HDSVELNCKM KFAVYLPPKA ETGKCPALYW LSGLTCTEQN
FISKSGYHQS ASEHGLVVIA PDTSPRGCNI KGEDESWDFG TGAGFYVDAT EDPWKTNYRM
YSYVTEELPQ LINANFPVDP QRMSIFGHSM GGHGALICAL KNPGKYKSVS AFAPICNPVL
CPWGKKAFSG YLGTDQSKWK AYDATHLVKS YPGSQLDILI DQGKDDQFLL DGQLLPDNFI
AACTEKKIPV VFRLQEGYDH SYYFIATFIT DHIRHHAKYL NA
//
ID ESTD_HUMAN Reviewed; 282 AA.
AC P10768; Q5TBU8; Q5TBV0; Q5TBV2; Q9BVJ2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1994, sequence version 2.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=S-formylglutathione hydrolase;
DE Short=FGH;
DE EC=3.1.2.12;
DE AltName: Full=Esterase D;
DE AltName: Full=Methylumbelliferyl-acetate deacetylase;
DE EC=3.1.1.56;
GN Name=ESD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3462698; DOI=10.1073/pnas.83.17.6337;
RA Lee E.Y.-H.P., Lee W.-H.;
RT "Molecular cloning of the human esterase D gene, a genetic marker of
RT retinoblastoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6337-6341(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3164702; DOI=10.1007/BF00280552;
RA Young L.-J.S., Lee E.Y.-H.P., To H., Bookstein R., Shew J.-Y.,
RA Donoso L.A., Sery T., Giblin M., Shields J.A., Lee W.-H.;
RT "Human esterase D gene: complete cDNA sequence, genomic structure, and
RT application in the genetic diagnosis of human retinoblastoma.";
RL Hum. Genet. 79:137-141(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-257.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-257.
RC TISSUE=Muscle;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 65-86 AND 254-274, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 150-186, AND PROTEIN SEQUENCE OF
RP 150-175.
RX PubMed=3462714; DOI=10.1073/pnas.83.17.6573;
RA Squire J., Dryja T.P., Dunn J., Goddard A., Hofmann T., Musarella M.,
RA Willard H.F., Becker A.J., Gallie B.L., Phillips R.A.;
RT "Cloning of the esterase D gene: a polymorphic gene probe closely
RT linked to the retinoblastoma locus on chromosome 13.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6573-6577(1986).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 168-200.
RA Tuchhida S., Ikemoto S., Kajii E.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP FUNCTION AS METHYLUMBELLIFERYL-ACETATE DEACETYLASE, AND CATALYTIC
RP ACTIVITY.
RX PubMed=4768551; DOI=10.1111/j.1469-1809.1973.tb01820.x;
RA Hopkinson D.A., Mestriner M.A., Cortner J., Harris H.;
RT "Esterase D: a new human polymorphism.";
RL Ann. Hum. Genet. 37:119-137(1973).
RN [11]
RP FUNCTION.
RX PubMed=3770744; DOI=10.1007/BF00282085;
RA Eiberg H., Mohr J.;
RT "Identity of the polymorphisms for esterase D and S-formylglutathione
RT hydrolase in red blood cells.";
RL Hum. Genet. 74:174-175(1986).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-200, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), MUTAGENESIS OF LEU-54; SER-149;
RP MET-150; ASP-226 AND HIS-260, AND ACTIVE SITE.
RX PubMed=19126594; DOI=10.1096/fj.08-125286;
RA Wu D., Li Y., Song G., Zhang D., Shaw N., Liu Z.-J.;
RT "Crystal structure of human esterase D: a potential genetic marker of
RT retinoblastoma.";
RL FASEB J. 23:1441-1446(2009).
RN [15]
RP VARIANT GLU-190.
RX PubMed=7907313; DOI=10.1007/BF00212018;
RA Tsuchida S., Fukui E., Ikemoto S.;
RT "Molecular analysis of esterase D polymorphism.";
RL Hum. Genet. 93:255-258(1994).
RN [16]
RP VARIANT GLU-190.
RX PubMed=12721789; DOI=10.1007/s10038-003-0021-7;
RA Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C.,
RA Nakamura Y.;
RT "Catalog of 680 variations among eight cytochrome p450 (CYP) genes,
RT nine esterase genes, and two other genes in the Japanese population.";
RL J. Hum. Genet. 48:249-270(2003).
CC -!- FUNCTION: Serine hydrolase involved in the detoxification of
CC formaldehyde.
CC -!- CATALYTIC ACTIVITY: S-formylglutathione + H(2)O = glutathione +
CC formate.
CC -!- CATALYTIC ACTIVITY: 4-methylumbelliferyl acetate + H(2)O = 4-
CC methylumbelliferone + acetate.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle.
CC -!- POLYMORPHISM: There are two major electrophoretic isotypes. The
CC sequence of the ESD*1 variant is shown.
CC -!- SIMILARITY: Belongs to the esterase D family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI12225.1; Type=Erroneous gene model prediction;
CC Sequence=CAI12226.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M13450; AAA52408.1; ALT_SEQ; mRNA.
DR EMBL; AF112219; AAC99788.1; -; mRNA.
DR EMBL; BT007059; AAP35708.1; -; mRNA.
DR EMBL; AL136958; CAI12225.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL136958; CAI12226.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL136958; CAI12228.1; -; Genomic_DNA.
DR EMBL; BC001169; AAH01169.1; -; mRNA.
DR EMBL; AF052509; AAC06298.1; -; Genomic_DNA.
DR PIR; A23543; A23543.
DR RefSeq; NP_001975.1; NM_001984.1.
DR RefSeq; XP_005266335.1; XM_005266278.1.
DR UniGene; Hs.432491; -.
DR PDB; 3FCX; X-ray; 1.50 A; A/B=1-282.
DR PDBsum; 3FCX; -.
DR ProteinModelPortal; P10768; -.
DR SMR; P10768; 3-281.
DR IntAct; P10768; 4.
DR MINT; MINT-5002423; -.
DR STRING; 9606.ENSP00000367992; -.
DR ChEMBL; CHEMBL2189130; -.
DR DrugBank; DB00143; Glutathione.
DR MEROPS; S09.990; -.
DR PhosphoSite; P10768; -.
DR DMDM; 544254; -.
DR DOSAC-COBS-2DPAGE; P10768; -.
DR OGP; P10768; -.
DR REPRODUCTION-2DPAGE; IPI00411706; -.
DR UCD-2DPAGE; P10768; -.
DR PaxDb; P10768; -.
DR PeptideAtlas; P10768; -.
DR PRIDE; P10768; -.
DR DNASU; 2098; -.
DR Ensembl; ENST00000378720; ENSP00000367992; ENSG00000139684.
DR GeneID; 2098; -.
DR KEGG; hsa:2098; -.
DR UCSC; uc001vbn.3; human.
DR CTD; 2098; -.
DR GeneCards; GC13M047345; -.
DR HGNC; HGNC:3465; ESD.
DR HPA; HPA039700; -.
DR MIM; 133280; gene.
DR neXtProt; NX_P10768; -.
DR PharmGKB; PA27882; -.
DR eggNOG; COG0627; -.
DR HOGENOM; HOG000263929; -.
DR HOVERGEN; HBG001326; -.
DR InParanoid; P10768; -.
DR KO; K01070; -.
DR OMA; SVELKCK; -.
DR OrthoDB; EOG7TF79G; -.
DR PhylomeDB; P10768; -.
DR ChiTaRS; ESD; human.
DR EvolutionaryTrace; P10768; -.
DR GeneWiki; ESD_(gene); -.
DR GenomeRNAi; 2098; -.
DR NextBio; 8487; -.
DR PRO; PR:P10768; -.
DR Bgee; P10768; -.
DR CleanEx; HS_ESD; -.
DR Genevestigator; P10768; -.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; NAS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; NAS:UniProtKB.
DR GO; GO:0047374; F:methylumbelliferyl-acetate deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0018738; F:S-formylglutathione hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046294; P:formaldehyde catabolic process; IEA:InterPro.
DR InterPro; IPR000801; Esterase_put.
DR InterPro; IPR014186; S-formylglutathione_hydrol.
DR PANTHER; PTHR10061; PTHR10061; 1.
DR Pfam; PF00756; Esterase; 1.
DR TIGRFAMs; TIGR02821; fghA_ester_D; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Cytoplasmic vesicle; Direct protein sequencing; Hydrolase;
KW Polymorphism; Reference proteome; Serine esterase.
FT CHAIN 1 282 S-formylglutathione hydrolase.
FT /FTId=PRO_0000210339.
FT ACT_SITE 149 149 Charge relay system.
FT ACT_SITE 226 226 Charge relay system.
FT ACT_SITE 260 260 Charge relay system.
FT MOD_RES 200 200 N6-acetyllysine.
FT VARIANT 190 190 G -> E (in allele ESD*2; dbSNP:rs9778).
FT /FTId=VAR_005202.
FT VARIANT 257 257 G -> D (in dbSNP:rs15303).
FT /FTId=VAR_022275.
FT MUTAGEN 54 54 L->A: 83% of wild-type activity.
FT MUTAGEN 149 149 S->A: Loss of activity.
FT MUTAGEN 149 149 S->T: 1.3% of wild-type activity.
FT MUTAGEN 150 150 M->A: 62% increase in activity.
FT MUTAGEN 226 226 D->A: 4.3% of wild-type activity.
FT MUTAGEN 226 226 D->N: 9% of wild-type activity.
FT MUTAGEN 260 260 H->A: 3% of wild-type activity.
FT MUTAGEN 260 260 H->Q: 1.3% of wild-type activity.
FT STRAND 4 11
FT STRAND 14 23
FT TURN 24 27
FT STRAND 28 36
FT HELIX 38 41
FT STRAND 45 51
FT HELIX 59 64
FT HELIX 68 74
FT STRAND 77 81
FT HELIX 114 117
FT HELIX 120 125
FT HELIX 127 135
FT STRAND 136 148
FT HELIX 150 160
FT TURN 163 165
FT STRAND 169 173
FT HELIX 178 180
FT HELIX 182 192
FT HELIX 199 202
FT HELIX 204 208
FT STRAND 218 223
FT HELIX 227 230
FT HELIX 236 245
FT STRAND 250 255
FT HELIX 262 279
SQ SEQUENCE 282 AA; 31463 MW; BFC20D5FA2BB0DCE CRC64;
MALKQISSNK CFGGLQKVFE HDSVELNCKM KFAVYLPPKA ETGKCPALYW LSGLTCTEQN
FISKSGYHQS ASEHGLVVIA PDTSPRGCNI KGEDESWDFG TGAGFYVDAT EDPWKTNYRM
YSYVTEELPQ LINANFPVDP QRMSIFGHSM GGHGALICAL KNPGKYKSVS AFAPICNPVL
CPWGKKAFSG YLGTDQSKWK AYDATHLVKS YPGSQLDILI DQGKDDQFLL DGQLLPDNFI
AACTEKKIPV VFRLQEGYDH SYYFIATFIT DHIRHHAKYL NA
//
MIM
133280
*RECORD*
*FIELD* NO
133280
*FIELD* TI
*133280 ESTERASE D; ESD
S-FORMYLGLUTATHIONE HYDROLASE, INCLUDED; FGH, INCLUDED
*FIELD* TX
read moreHopkinson et al. (1973) described a red cell esterase that they called
esterase D (EC 3.1.1.1). Although studied in red cell hemolysates,
esterase D was found in many different tissues including cultured
fibroblasts and lymphocytoid cells. Genetic polymorphism was discovered
in European, black, and Indian populations. Cowell et al. (1986) showed
that there is a consistently lower level of esterase D enzyme activity
in persons with the 2-2 phenotype when activity is measured in certain
ways. They emphasized the importance of checking the electrophoretic
phenotype before concluding that chromosome 13 deletion is present in a
family being studied in connection with retinoblastoma (see later).
Munier et al. (1988) reviewed 16 rare alleles at the ESD locus and
reported a previously undescribed variant in a Portuguese family. Data
on gene frequencies of allelic variants were tabulated by Roychoudhury
and Nei (1988).
From study of somatic cell hybrids, Van Heyningen et al. (1975)
concluded that the esterase D locus may be on chromosome 13. By the same
method, Chen et al. (1975) also assigned this locus to chromosome 13.
Namboodiri et al. (1977) concluded that Lp (152200) and esterase D are
closely linked; the lod score was 2.32 at a recombination fraction of
0.0. However, Greger et al. (1988) excluded the linkage of LPA not only
with ESD but also with RB1 (614041). (Subsequently, the LPA locus was
mapped to 6q27.) Sparkes et al. (1980) found that quantitative and
qualitative expression of esterase D in 5 persons with partial deletions
or duplications of chromosome 13 supported localization of the gene to
13q14. The same band had been found deleted in cases of retinoblastoma.
They suggested that linkage of familial retinoblastoma and esterase D
should be sought, to check on whether familial retinoblastoma represents
mutation at the same locus as that deleted in the 'chromosomal' form of
the disorder, and, if linkage were found, to provide a means of genetic
counseling and early diagnosis, including prenatal diagnosis. Rivera et
al. (1981) concluded that the retinoblastoma and esterase D loci are in
the proximal half of the 13q14 band. Mohandas et al. (1982) found that
mouse-human cell hybrid clones retaining a human X/13 translocation did
not express esterase D. They suggested that this may reflect spreading
of inactivation into the autosomal part of the translocation chromosome.
The breakpoint in chromosome 13 was 13q12. The X/13 translocation was
derived from a patient who had bilateral retinoblastoma and failure to
thrive, identified by Cross et al. (1977) and studied further by Nichols
et al. (1980), who proposed that since the translocation chromosome was
late-labeling, the patient was effectively monosomic for 13q14 in a
majority of her cells. (Couturier et al. (1979) gave a comparable
explanation for the low superoxide dismutase found in a case of X/21
translocation.) In a patient with retinoblastoma and deletion of
13q14.1-q22.3, Sparkes et al. (1984) found that the esterase D locus was
apparently intact--levels of enzyme activity were normal in red blood
cells and in fibroblasts. This indicated that the order of genes is
centromere--ESD--RB1. Frydman et al. (1985) investigated linkage of
Wilson disease (277900) with 27 autosomal markers. A lod score of 3.21
was found at theta = 0.06 for linkage of WD and esterase D on chromosome
13. In a note added in proof, they indicated that they had typed a
second unrelated 10-member sibship with WD; the maximum lod score was
1.48 at theta = 0, giving a combined maximum lod score of 4.55 at theta
= 0.04. Bonne-Tamir et al. (1985) corroborated the linkage of WD with
esterase D by studies of another inbred group, 2 unrelated Druze
kindreds. The combined lod score was 5.49 at theta = 0.03. By in situ
hybridization, Duncan et al. (1987) assigned the ESD locus to
13q14.2-q14.3. Restudy of the patient whose chromosomes formed the basis
of the study by Sparkes et al. (1984) suggested that the ESD locus may
lie distal rather than proximal to the retinoblastoma locus. The
contrary conclusion of Sparkes et al. (1984) was based on the fact that
the level of enzymatic activity of esterase D was normal in
retinoblastoma tissue. Quantitative in situ hybridization suggested to
Duncan et al. (1987) that in fact that locus was deleted from one
chromosome 13 and was duplicated on the other chromosome 13. They were
unable to offer a simple explanation for the inconsistency of their
results with the deletion described by Ward et al. (1984) that mapped
the ESD locus to 13q14.11. Through studies of a relatively large
deletion, 13q14-q31, in a case of retinoblastoma, Mitchell and Cowell
(1988) confirmed that ESD lies proximal to RB1; esterase D levels were
normal. Lee and Lee (1986) cloned ESD cDNA by screening an expression
library with an anti-ESD antibody. Squire et al. (1986) cloned the ESD
gene by means of oligonucleotides specific for a partial amino acid
sequence of the purified enzyme. A RFLP useful in identifying carriers
of retinoblastoma was found in the cloned gene. These 2 clones should be
helpful in 'walking' to the retinoblastoma and Wilson disease loci.
Eiberg and Mohr (1986) concluded that S-formylglutathione hydrolase (EC
3.1.2.12) is the same as esterase D. They studied the FGH polymorphism
of human red cells in unrelated persons both by isoelectric focusing and
starch-gel electrophoresis and with the substrates S-acetylglutathione
and 4-methylumbelliferyl-acetate (the standard substrate for ESD). With
both separation techniques, the 2 substrates consistently gave similar
and identically located zymograms. From analyses of data on families,
populations, and the somatic cell hybrids, Apeshiotis and Bender (1986)
likewise suggested that the FGH and ESD polymorphisms are identical.
Akiyama and Abe (1986) reported gene frequencies for the FGH
polymorphism in Japanese and also concluded that FGH and esterase D are
identical. Uotila (1984) demonstrated polymorphism of red cell FGH in
Finns. Like S-hydroxyacyl-glutathione hydrolase (glyoxalase II; 138760),
S-formylglutathione hydrolase is an enzyme capable of hydrolyzing thiol
esters of glutathione. FGH appears to be involved in the removal of
formaldehyde which is first converted to S-formylglutathione by reaction
with glutathione and NAD (catalyzed by formaldehyde dehydrogenase). FGH
catalyzes the hydrolysis of S-formylglutathione to reduced glutathione
and formate. Red cell hemolysates were fractionated by isoelectric
focusing on polyacrylamide gel and FGH located by activity staining.
Samples from all but 6 of 242 Finns studied showed a single band,
whereas in the 6 persons 3 enzyme bands were found. The enzyme is a
dimer and the polymorphism observed appeared to result from 2 alleles,
FGH(1) and FGH(2). The frequency of the more common allele was estimated
to be 0.988. No person homozygous for the rare allele was found. Family
studies were not reported. Board and Coggan (1986) found electrophoretic
variation in FGH in red cells and concluded that the polymorphism is the
product of 2 alleles at a single autosomal locus. Many other tissues
appeared to show the same gene expression.
*FIELD* SA
Gray et al. (1978); Hoo et al. (1982); Kondo et al. (1984); Kozio
and Stepien (1980); Mestriner et al. (1976); Nishigaki and Itoh (1984);
Olaisen et al. (1981); Omoto et al. (1975); Rittner and Muller (1975);
Sorensen and Fenger (1976); Telfer et al. (1980)
*FIELD* RF
1. Akiyama, K.; Abe, K.: Gene frequencies of S-formylglutathione
hydrolase isozyme in a Japanese population. Jpn. J. Hum. Genet. 31:
353-355, 1986.
2. Apeshiotis, F.; Bender, K.: Evidence that S-formylglutathione
hydrolase and esterase D polymorphisms are identical. Hum. Genet. 74:
176-177, 1986.
3. Board, P. G.; Coggan, M.: Genetic heterogeneity of S-formylglutathione
hydrolase. Ann. Hum. Genet. 50: 35-39, 1986.
4. Bonne-Tamir, B.; Farrer, L. A.; Frydman, M.; Kanani, C.: The locus
for Wilson disease linked to esterase D in two Druze kindreds. (Abstract) Am.
J. Hum. Genet. 37: A47 only, 1985.
5. Chen, S.-H.; Creagan, R. P.; Nichols, E. A.; Ruddle, F. H.: Assignment
of human esterase-D gene to chromosome 13. Birth Defects Orig. Art.
Ser. XI(3): 99-102, 1975. Note: Alternate: Cytogenet. Cell Genet.
14: 269-272, 1975.
6. Couturier, J.; Dutrillaux, B.; Garber, P.; Raoul, O.; Croquette,
M. F.; Fourlinnie, J. C.; Maillard, E.: Evidence for a correlation
between late replication and autosomal gene inactivation in a familial
translocation t(X;21). Hum. Genet. 49: 319-326, 1979.
7. Cowell, J. K.; Rutland, P.; Jay, M.; Hungerford, J.: Effect of
the esterase-D phenotype on its in vitro enzyme activity. Hum. Genet. 74:
298-301, 1986.
8. Cross, H. E.; Hansen, R. C.; Morrow, G.; Davis, J. R.: Retinoblastoma
in a patient with a 13qXp translocation. Am. J. Ophthal. 84: 548-554,
1977.
9. Duncan, A. M. V.; Morgan, C.; Gallie, B. L.; Phillips, R. A.; Squire,
J.: Re-evaluation of the sublocalization of esterase D and its relation
to the retinoblastoma locus by in situ hybridization. Cytogenet.
Cell Genet. 44: 153-157, 1987.
10. Eiberg, H.; Mohr, J.: Identity of the polymorphisms for esterase
D and S-formylglutathione hydrolase in red blood cells. Hum. Genet. 74:
174-175, 1986.
11. Frydman, M.; Bonne-Tamir, B.; Farrer, L. A.; Conneally, P. M.;
Magazanik, A.; Ashbel, S.; Goldwitch, Z.: Assignment of the gene
for Wilson disease to chromosome 13: linkage to the esterase D locus. Proc.
Nat. Acad. Sci. 82: 1819-1821, 1985.
12. Gray, J. E.; Bobrow, M.; Cook, P. J. L.; Robson, E. B.: Further
family data on ESD and chromosome 13. Cytogenet. Cell Genet. 22:
487-489, 1978.
13. Greger, V.; Gersdorf, E.; Utermann, G.; Horsthemke, B.: No evidence
for linkage between lipoprotein(a) (LPA) and esterase D (ESD). Cytogenet.
Cell Genet. 48: 248-249, 1988.
14. Hoo, J. J.; Koch, M.; Ziemsen, B.; Foerster, W.; Nishigaki, I.
: Confirmation of regional assignment of gene for human esterase-D
to chromosome band 13q14. Hum. Genet. 60: 276-277, 1982.
15. Hopkinson, D. A.; Mestriner, M. A.; Cortner, J. A.; Harris, H.
: Esterase D: a new human polymorphism. Ann. Hum. Genet. 37: 119-137,
1973.
16. Kondo, I.; Yamamoto, T.; Yamakawa, K.; Harada, S.; Oishi, H.;
Nishigaki, I.; Hamaguchi, H.: Genetic analysis of human lymphocyte
proteins by two-dimensional gel electrophoresis: VI. Identification
of esterase D in the two-dimensional gel electrophoresis pattern of
cellular proteins. Hum. Genet. 66: 248-251, 1984.
17. Kozio, P.; Stepien, J.: Atypical segregation of esterase D: evidence
of a rare 'silent' allele EsD(zero). Hum. Genet. 53: 223-225, 1980.
18. Lee, E. Y.-H. P.; Lee, W.-H.: Molecular cloning of the human
esterase D gene, a genetic marker of retinoblastoma. Proc. Nat. Acad.
Sci. 83: 6337-6341, 1986.
19. Mestriner, M. A.; Salzano, F. M.; Neel, J. V.; Ayres, M.: Esterase
D in South American Indians. Am. J. Hum. Genet. 28: 257-261, 1976.
20. Mitchell, C. D.; Cowell, J. K.: Molecular evidence that the esterase-D
gene lies proximal to the retinoblastoma susceptibility locus in chromosome
region 13q14. Hum. Genet. 81: 57-60, 1988.
21. Mohandas, T.; Sparkes, R. S.; Shapiro, L. J.: Genetic evidence
for the inactivation of a human autosomal locus attached to an inactive
X chromosome. Am. J. Hum. Genet. 34: 811-817, 1982.
22. Munier, F.; Pescia, G.; Balmer, A.; Bar, W.; Roth, M.; Dimo-Simonin,
N.; Weidinger, S.: A 'new' allele of esterase D in a retinoblastoma
family. Hum. Genet. 78: 289-290, 1988.
23. Namboodiri, K. K.; Elston, R. C.; Go, R. C. P.; Berg, K.; Hames,
C.: Linkage relationships of Lp and Ag serum lipoproteins with 25
polymorphic markers. Hum. Genet. 37: 291-297, 1977.
24. Nichols, W. W.; Miller, R. C.; Sobel, M.; Hoffman, E.; Sparkes,
R. S.; Mohandas, T.; Veomett, I.; Davis, J. R.: Further observations
on a 13qXp translocation associated with retinoblastoma. Am. J. Ophthal. 89:
621-627, 1980.
25. Nishigaki, I.; Itoh, T.: Isoelectric focusing studies of human
red cell esterase D: evidence for polymorphic occurrence of a new
allele EsD-7 in Japanese. Hum. Genet. 66: 92-95, 1984.
26. Olaisen, B.; Siverts, A.; Jonassen, R.; Mevag, B.; Gedde-Dahl,
T.: The ESD polymorphism: further studies of the ESD2 and ESD5 allele
products. Hum. Genet. 57: 351-353, 1981.
27. Omoto, K.; Aoki, K.; Harada, S.: Polymorphism of esterase D in
some population groups in Japan. Hum. Hered. 25: 378-381, 1975.
28. Rittner, C.; Muller, G.: Esterase D: some population and formal
genetical data. Hum. Hered. 25: 152-155, 1975.
29. Rivera, H.; Turleau, C.; de Grouchy, J.; Junien, C.; Despoisse,
S.; Zucker, J.-M.: Retinoblastoma-del(13q14): report of two patients,
one with a trisomic sib due to maternal insertion; gene-dosage effect
for esterase D. Hum. Genet. 59: 211-214, 1981.
30. Roychoudhury, A. K.; Nei, M.: Human Polymorphic Genes: World
Distribution. New York: Oxford Univ. Press (pub.) 1988.
31. Sorensen, S. A.; Fenger, K.: Gene frequencies and linkage data
on EsD in man. Hum. Hered. 26: 90-94, 1976.
32. Sparkes, R. S.; Sparkes, M. C.; Kalina, R. E.; Pagon, R. A.; Salk,
D. J.; Disteche, C. M.: Separation of retinoblastoma and esterase
D loci in a patient with sporadic retinoblastoma and del(13)(q14.1q22.3). Hum.
Genet. 68: 258-259, 1984.
33. Sparkes, R. S.; Sparkes, M. C.; Wilson, M. G.; Towner, J. W.;
Benedict, W.; Murphree, A. L.; Yunis, J. J.: Regional assignment
of genes for human esterase D and retinoblastoma to chromosome band
13q14. Science 208: 1042-1044, 1980.
34. Squire, J.; Dryja, T. P.; Dunn, J.; Goddard, A.; Hofmann, T.;
Musarella, M.; Willard, H. F.; Becker, A. J.; Gallie, B. L.; Phillips,
R. A.: Cloning of the esterase D gene: a polymorphic gene probe closely
linked to the retinoblastoma locus on chromosome 13. Proc. Nat. Acad.
Sci. 83: 6573-6577, 1986.
35. Telfer, M. A.; Clark, C. E.; Casey, P. A.; Cowell, H. R.; Stroud,
H. H.: Long arm deletion of chromosome 13 with exclusion of esterase
D from 13q32--13qter. Clin. Genet. 17: 428-432, 1980.
36. Uotila, L.: Polymorphism of red cell S-formylglutathione hydrolase
in a Finnish population. Hum. Hered. 34: 273-277, 1984.
37. Van Heyningen, V.; Bobrow, M.; Bodmer, W.; Gardiner, S. E.; Povey,
S.; Hopkinson, D. A.: Chromosome assignment of some human enzyme
loci: mitochondrial malate dehydrogenase to 7, mannosephosphate isomerase
and pyruvate kinase to 15 and probably, esterase D to 13. Ann. Hum.
Genet. 38: 295-303, 1975.
38. Ward, P.; Packman, S.; Loughman, W.; Sparkes, M.; Sparkes, R.;
McMahon, A.; Gregory, T.; Ablin, A.: Location of the retinoblastoma
susceptibility gene(s) and the human esterase D locus. J. Med. Genet. 21:
92-95, 1984.
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 06/17/2011
carol: 11/30/2004
terry: 7/31/1998
terry: 6/5/1998
pfoster: 4/4/1994
warfield: 3/28/1994
supermim: 3/16/1992
carol: 2/12/1991
carol: 2/4/1991
supermim: 3/20/1990
*RECORD*
*FIELD* NO
133280
*FIELD* TI
*133280 ESTERASE D; ESD
S-FORMYLGLUTATHIONE HYDROLASE, INCLUDED; FGH, INCLUDED
*FIELD* TX
read moreHopkinson et al. (1973) described a red cell esterase that they called
esterase D (EC 3.1.1.1). Although studied in red cell hemolysates,
esterase D was found in many different tissues including cultured
fibroblasts and lymphocytoid cells. Genetic polymorphism was discovered
in European, black, and Indian populations. Cowell et al. (1986) showed
that there is a consistently lower level of esterase D enzyme activity
in persons with the 2-2 phenotype when activity is measured in certain
ways. They emphasized the importance of checking the electrophoretic
phenotype before concluding that chromosome 13 deletion is present in a
family being studied in connection with retinoblastoma (see later).
Munier et al. (1988) reviewed 16 rare alleles at the ESD locus and
reported a previously undescribed variant in a Portuguese family. Data
on gene frequencies of allelic variants were tabulated by Roychoudhury
and Nei (1988).
From study of somatic cell hybrids, Van Heyningen et al. (1975)
concluded that the esterase D locus may be on chromosome 13. By the same
method, Chen et al. (1975) also assigned this locus to chromosome 13.
Namboodiri et al. (1977) concluded that Lp (152200) and esterase D are
closely linked; the lod score was 2.32 at a recombination fraction of
0.0. However, Greger et al. (1988) excluded the linkage of LPA not only
with ESD but also with RB1 (614041). (Subsequently, the LPA locus was
mapped to 6q27.) Sparkes et al. (1980) found that quantitative and
qualitative expression of esterase D in 5 persons with partial deletions
or duplications of chromosome 13 supported localization of the gene to
13q14. The same band had been found deleted in cases of retinoblastoma.
They suggested that linkage of familial retinoblastoma and esterase D
should be sought, to check on whether familial retinoblastoma represents
mutation at the same locus as that deleted in the 'chromosomal' form of
the disorder, and, if linkage were found, to provide a means of genetic
counseling and early diagnosis, including prenatal diagnosis. Rivera et
al. (1981) concluded that the retinoblastoma and esterase D loci are in
the proximal half of the 13q14 band. Mohandas et al. (1982) found that
mouse-human cell hybrid clones retaining a human X/13 translocation did
not express esterase D. They suggested that this may reflect spreading
of inactivation into the autosomal part of the translocation chromosome.
The breakpoint in chromosome 13 was 13q12. The X/13 translocation was
derived from a patient who had bilateral retinoblastoma and failure to
thrive, identified by Cross et al. (1977) and studied further by Nichols
et al. (1980), who proposed that since the translocation chromosome was
late-labeling, the patient was effectively monosomic for 13q14 in a
majority of her cells. (Couturier et al. (1979) gave a comparable
explanation for the low superoxide dismutase found in a case of X/21
translocation.) In a patient with retinoblastoma and deletion of
13q14.1-q22.3, Sparkes et al. (1984) found that the esterase D locus was
apparently intact--levels of enzyme activity were normal in red blood
cells and in fibroblasts. This indicated that the order of genes is
centromere--ESD--RB1. Frydman et al. (1985) investigated linkage of
Wilson disease (277900) with 27 autosomal markers. A lod score of 3.21
was found at theta = 0.06 for linkage of WD and esterase D on chromosome
13. In a note added in proof, they indicated that they had typed a
second unrelated 10-member sibship with WD; the maximum lod score was
1.48 at theta = 0, giving a combined maximum lod score of 4.55 at theta
= 0.04. Bonne-Tamir et al. (1985) corroborated the linkage of WD with
esterase D by studies of another inbred group, 2 unrelated Druze
kindreds. The combined lod score was 5.49 at theta = 0.03. By in situ
hybridization, Duncan et al. (1987) assigned the ESD locus to
13q14.2-q14.3. Restudy of the patient whose chromosomes formed the basis
of the study by Sparkes et al. (1984) suggested that the ESD locus may
lie distal rather than proximal to the retinoblastoma locus. The
contrary conclusion of Sparkes et al. (1984) was based on the fact that
the level of enzymatic activity of esterase D was normal in
retinoblastoma tissue. Quantitative in situ hybridization suggested to
Duncan et al. (1987) that in fact that locus was deleted from one
chromosome 13 and was duplicated on the other chromosome 13. They were
unable to offer a simple explanation for the inconsistency of their
results with the deletion described by Ward et al. (1984) that mapped
the ESD locus to 13q14.11. Through studies of a relatively large
deletion, 13q14-q31, in a case of retinoblastoma, Mitchell and Cowell
(1988) confirmed that ESD lies proximal to RB1; esterase D levels were
normal. Lee and Lee (1986) cloned ESD cDNA by screening an expression
library with an anti-ESD antibody. Squire et al. (1986) cloned the ESD
gene by means of oligonucleotides specific for a partial amino acid
sequence of the purified enzyme. A RFLP useful in identifying carriers
of retinoblastoma was found in the cloned gene. These 2 clones should be
helpful in 'walking' to the retinoblastoma and Wilson disease loci.
Eiberg and Mohr (1986) concluded that S-formylglutathione hydrolase (EC
3.1.2.12) is the same as esterase D. They studied the FGH polymorphism
of human red cells in unrelated persons both by isoelectric focusing and
starch-gel electrophoresis and with the substrates S-acetylglutathione
and 4-methylumbelliferyl-acetate (the standard substrate for ESD). With
both separation techniques, the 2 substrates consistently gave similar
and identically located zymograms. From analyses of data on families,
populations, and the somatic cell hybrids, Apeshiotis and Bender (1986)
likewise suggested that the FGH and ESD polymorphisms are identical.
Akiyama and Abe (1986) reported gene frequencies for the FGH
polymorphism in Japanese and also concluded that FGH and esterase D are
identical. Uotila (1984) demonstrated polymorphism of red cell FGH in
Finns. Like S-hydroxyacyl-glutathione hydrolase (glyoxalase II; 138760),
S-formylglutathione hydrolase is an enzyme capable of hydrolyzing thiol
esters of glutathione. FGH appears to be involved in the removal of
formaldehyde which is first converted to S-formylglutathione by reaction
with glutathione and NAD (catalyzed by formaldehyde dehydrogenase). FGH
catalyzes the hydrolysis of S-formylglutathione to reduced glutathione
and formate. Red cell hemolysates were fractionated by isoelectric
focusing on polyacrylamide gel and FGH located by activity staining.
Samples from all but 6 of 242 Finns studied showed a single band,
whereas in the 6 persons 3 enzyme bands were found. The enzyme is a
dimer and the polymorphism observed appeared to result from 2 alleles,
FGH(1) and FGH(2). The frequency of the more common allele was estimated
to be 0.988. No person homozygous for the rare allele was found. Family
studies were not reported. Board and Coggan (1986) found electrophoretic
variation in FGH in red cells and concluded that the polymorphism is the
product of 2 alleles at a single autosomal locus. Many other tissues
appeared to show the same gene expression.
*FIELD* SA
Gray et al. (1978); Hoo et al. (1982); Kondo et al. (1984); Kozio
and Stepien (1980); Mestriner et al. (1976); Nishigaki and Itoh (1984);
Olaisen et al. (1981); Omoto et al. (1975); Rittner and Muller (1975);
Sorensen and Fenger (1976); Telfer et al. (1980)
*FIELD* RF
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hydrolase and esterase D polymorphisms are identical. Hum. Genet. 74:
176-177, 1986.
3. Board, P. G.; Coggan, M.: Genetic heterogeneity of S-formylglutathione
hydrolase. Ann. Hum. Genet. 50: 35-39, 1986.
4. Bonne-Tamir, B.; Farrer, L. A.; Frydman, M.; Kanani, C.: The locus
for Wilson disease linked to esterase D in two Druze kindreds. (Abstract) Am.
J. Hum. Genet. 37: A47 only, 1985.
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Ser. XI(3): 99-102, 1975. Note: Alternate: Cytogenet. Cell Genet.
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6. Couturier, J.; Dutrillaux, B.; Garber, P.; Raoul, O.; Croquette,
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the esterase-D phenotype on its in vitro enzyme activity. Hum. Genet. 74:
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J.: Re-evaluation of the sublocalization of esterase D and its relation
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for Wilson disease to chromosome 13: linkage to the esterase D locus. Proc.
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487-489, 1978.
13. Greger, V.; Gersdorf, E.; Utermann, G.; Horsthemke, B.: No evidence
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Cell Genet. 48: 248-249, 1988.
14. Hoo, J. J.; Koch, M.; Ziemsen, B.; Foerster, W.; Nishigaki, I.
: Confirmation of regional assignment of gene for human esterase-D
to chromosome band 13q14. Hum. Genet. 60: 276-277, 1982.
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16. Kondo, I.; Yamamoto, T.; Yamakawa, K.; Harada, S.; Oishi, H.;
Nishigaki, I.; Hamaguchi, H.: Genetic analysis of human lymphocyte
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17. Kozio, P.; Stepien, J.: Atypical segregation of esterase D: evidence
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18. Lee, E. Y.-H. P.; Lee, W.-H.: Molecular cloning of the human
esterase D gene, a genetic marker of retinoblastoma. Proc. Nat. Acad.
Sci. 83: 6337-6341, 1986.
19. Mestriner, M. A.; Salzano, F. M.; Neel, J. V.; Ayres, M.: Esterase
D in South American Indians. Am. J. Hum. Genet. 28: 257-261, 1976.
20. Mitchell, C. D.; Cowell, J. K.: Molecular evidence that the esterase-D
gene lies proximal to the retinoblastoma susceptibility locus in chromosome
region 13q14. Hum. Genet. 81: 57-60, 1988.
21. Mohandas, T.; Sparkes, R. S.; Shapiro, L. J.: Genetic evidence
for the inactivation of a human autosomal locus attached to an inactive
X chromosome. Am. J. Hum. Genet. 34: 811-817, 1982.
22. Munier, F.; Pescia, G.; Balmer, A.; Bar, W.; Roth, M.; Dimo-Simonin,
N.; Weidinger, S.: A 'new' allele of esterase D in a retinoblastoma
family. Hum. Genet. 78: 289-290, 1988.
23. Namboodiri, K. K.; Elston, R. C.; Go, R. C. P.; Berg, K.; Hames,
C.: Linkage relationships of Lp and Ag serum lipoproteins with 25
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24. Nichols, W. W.; Miller, R. C.; Sobel, M.; Hoffman, E.; Sparkes,
R. S.; Mohandas, T.; Veomett, I.; Davis, J. R.: Further observations
on a 13qXp translocation associated with retinoblastoma. Am. J. Ophthal. 89:
621-627, 1980.
25. Nishigaki, I.; Itoh, T.: Isoelectric focusing studies of human
red cell esterase D: evidence for polymorphic occurrence of a new
allele EsD-7 in Japanese. Hum. Genet. 66: 92-95, 1984.
26. Olaisen, B.; Siverts, A.; Jonassen, R.; Mevag, B.; Gedde-Dahl,
T.: The ESD polymorphism: further studies of the ESD2 and ESD5 allele
products. Hum. Genet. 57: 351-353, 1981.
27. Omoto, K.; Aoki, K.; Harada, S.: Polymorphism of esterase D in
some population groups in Japan. Hum. Hered. 25: 378-381, 1975.
28. Rittner, C.; Muller, G.: Esterase D: some population and formal
genetical data. Hum. Hered. 25: 152-155, 1975.
29. Rivera, H.; Turleau, C.; de Grouchy, J.; Junien, C.; Despoisse,
S.; Zucker, J.-M.: Retinoblastoma-del(13q14): report of two patients,
one with a trisomic sib due to maternal insertion; gene-dosage effect
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30. Roychoudhury, A. K.; Nei, M.: Human Polymorphic Genes: World
Distribution. New York: Oxford Univ. Press (pub.) 1988.
31. Sorensen, S. A.; Fenger, K.: Gene frequencies and linkage data
on EsD in man. Hum. Hered. 26: 90-94, 1976.
32. Sparkes, R. S.; Sparkes, M. C.; Kalina, R. E.; Pagon, R. A.; Salk,
D. J.; Disteche, C. M.: Separation of retinoblastoma and esterase
D loci in a patient with sporadic retinoblastoma and del(13)(q14.1q22.3). Hum.
Genet. 68: 258-259, 1984.
33. Sparkes, R. S.; Sparkes, M. C.; Wilson, M. G.; Towner, J. W.;
Benedict, W.; Murphree, A. L.; Yunis, J. J.: Regional assignment
of genes for human esterase D and retinoblastoma to chromosome band
13q14. Science 208: 1042-1044, 1980.
34. Squire, J.; Dryja, T. P.; Dunn, J.; Goddard, A.; Hofmann, T.;
Musarella, M.; Willard, H. F.; Becker, A. J.; Gallie, B. L.; Phillips,
R. A.: Cloning of the esterase D gene: a polymorphic gene probe closely
linked to the retinoblastoma locus on chromosome 13. Proc. Nat. Acad.
Sci. 83: 6573-6577, 1986.
35. Telfer, M. A.; Clark, C. E.; Casey, P. A.; Cowell, H. R.; Stroud,
H. H.: Long arm deletion of chromosome 13 with exclusion of esterase
D from 13q32--13qter. Clin. Genet. 17: 428-432, 1980.
36. Uotila, L.: Polymorphism of red cell S-formylglutathione hydrolase
in a Finnish population. Hum. Hered. 34: 273-277, 1984.
37. Van Heyningen, V.; Bobrow, M.; Bodmer, W.; Gardiner, S. E.; Povey,
S.; Hopkinson, D. A.: Chromosome assignment of some human enzyme
loci: mitochondrial malate dehydrogenase to 7, mannosephosphate isomerase
and pyruvate kinase to 15 and probably, esterase D to 13. Ann. Hum.
Genet. 38: 295-303, 1975.
38. Ward, P.; Packman, S.; Loughman, W.; Sparkes, M.; Sparkes, R.;
McMahon, A.; Gregory, T.; Ablin, A.: Location of the retinoblastoma
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*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 06/17/2011
carol: 11/30/2004
terry: 7/31/1998
terry: 6/5/1998
pfoster: 4/4/1994
warfield: 3/28/1994
supermim: 3/16/1992
carol: 2/12/1991
carol: 2/4/1991
supermim: 3/20/1990