ESTD_HUMAN
ID ESTD_HUMAN Reviewed; 282 AA.
AC P10768; Q5TBU8; Q5TBV0; Q5TBV2; Q9BVJ2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 203.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Donoso L.A.,
RA 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., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT 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 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., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., 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., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., 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., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 65-86 AND 254-274, AND IDENTIFICATION BY MASS
RP 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 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 linked to
RT 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 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 IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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., Buerckstuemmer T.,
RA 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
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 [17]
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 [18]
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, nine
RT 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. {ECO:0000269|PubMed:3770744, ECO:0000269|PubMed:4768551}.
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 Evidence={ECO:0000269|PubMed:4768551};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone +
CC acetate + H(+); Xref=Rhea:RHEA:12208, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17224, ChEBI:CHEBI:17763,
CC ChEBI:CHEBI:30089; EC=3.1.1.56;
CC Evidence={ECO:0000269|PubMed:4768551};
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P10768; P10768: ESD; NbExp=5; IntAct=EBI-1052334, EBI-1052334;
CC P10768; A1L4K1: FSD2; NbExp=7; IntAct=EBI-1052334, EBI-5661036;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle.
CC -!- POLYMORPHISM: There are two major electrophoretic isotypes. The
CC sequence of the ESD*1 variant is shown (PubMed:12721789,
CC PubMed:7907313). {ECO:0000269|PubMed:12721789,
CC ECO:0000269|PubMed:7907313}.
CC -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) 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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001169; AAH01169.1; -; mRNA.
DR EMBL; AF052509; AAC06298.1; -; Genomic_DNA.
DR CCDS; CCDS9404.1; -.
DR PIR; A23543; A23543.
DR RefSeq; NP_001975.1; NM_001984.1.
DR RefSeq; XP_005266335.1; XM_005266278.2.
DR RefSeq; XP_011533256.1; XM_011534954.1.
DR PDB; 3FCX; X-ray; 1.50 A; A/B=1-282.
DR PDBsum; 3FCX; -.
DR AlphaFoldDB; P10768; -.
DR SMR; P10768; -.
DR BioGRID; 108402; 41.
DR IntAct; P10768; 17.
DR STRING; 9606.ENSP00000367992; -.
DR BindingDB; P10768; -.
DR ChEMBL; CHEMBL2189130; -.
DR DrugBank; DB00143; Glutathione.
DR ESTHER; human-ESD; A85-EsteraseD-FGH.
DR MEROPS; S09.990; -.
DR GlyGen; P10768; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P10768; -.
DR MetOSite; P10768; -.
DR PhosphoSitePlus; P10768; -.
DR SwissPalm; P10768; -.
DR BioMuta; ESD; -.
DR DMDM; 544254; -.
DR DOSAC-COBS-2DPAGE; P10768; -.
DR OGP; P10768; -.
DR REPRODUCTION-2DPAGE; IPI00411706; -.
DR UCD-2DPAGE; P10768; -.
DR CPTAC; CPTAC-73; -.
DR CPTAC; CPTAC-74; -.
DR EPD; P10768; -.
DR jPOST; P10768; -.
DR MassIVE; P10768; -.
DR MaxQB; P10768; -.
DR PaxDb; P10768; -.
DR PeptideAtlas; P10768; -.
DR PRIDE; P10768; -.
DR ProteomicsDB; 52652; -.
DR TopDownProteomics; P10768; -.
DR Antibodypedia; 23747; 225 antibodies from 29 providers.
DR DNASU; 2098; -.
DR Ensembl; ENST00000378720.8; ENSP00000367992.3; ENSG00000139684.15.
DR GeneID; 2098; -.
DR KEGG; hsa:2098; -.
DR MANE-Select; ENST00000378720.8; ENSP00000367992.3; NM_001984.2; NP_001975.1.
DR UCSC; uc001vbn.3; human.
DR CTD; 2098; -.
DR DisGeNET; 2098; -.
DR GeneCards; ESD; -.
DR HGNC; HGNC:3465; ESD.
DR HPA; ENSG00000139684; Low tissue specificity.
DR MIM; 133280; gene.
DR neXtProt; NX_P10768; -.
DR OpenTargets; ENSG00000139684; -.
DR PharmGKB; PA27882; -.
DR VEuPathDB; HostDB:ENSG00000139684; -.
DR eggNOG; KOG3101; Eukaryota.
DR GeneTree; ENSGT00390000011864; -.
DR InParanoid; P10768; -.
DR OMA; TFMEDHL; -.
DR OrthoDB; 942551at2759; -.
DR PhylomeDB; P10768; -.
DR TreeFam; TF300793; -.
DR PathwayCommons; P10768; -.
DR Reactome; R-HSA-156590; Glutathione conjugation.
DR SignaLink; P10768; -.
DR BioGRID-ORCS; 2098; 14 hits in 1081 CRISPR screens.
DR ChiTaRS; ESD; human.
DR EvolutionaryTrace; P10768; -.
DR GeneWiki; ESD_(gene); -.
DR GenomeRNAi; 2098; -.
DR Pharos; P10768; Tchem.
DR PRO; PR:P10768; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P10768; protein.
DR Bgee; ENSG00000139684; Expressed in blood vessel layer and 212 other tissues.
DR ExpressionAtlas; P10768; baseline and differential.
DR Genevisible; P10768; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; NAS:UniProtKB.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0047374; F:methylumbelliferyl-acetate deacetylase activity; IEA:UniProtKB-EC.
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 3D-structure; Acetylation; Cytoplasm; Cytoplasmic vesicle;
KW Direct protein sequencing; Hydrolase; Reference proteome; Serine esterase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9R0P3"
FT CHAIN 2..282
FT /note="S-formylglutathione hydrolase"
FT /id="PRO_0000210339"
FT ACT_SITE 149
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:19126594"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:19126594"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:19126594"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0P3"
FT MOD_RES 4
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0P3"
FT MOD_RES 200
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 190
FT /note="G -> E (in allele ESD*2; dbSNP:rs9778)"
FT /evidence="ECO:0000269|PubMed:12721789,
FT ECO:0000269|PubMed:7907313"
FT /id="VAR_005202"
FT VARIANT 257
FT /note="G -> D (in dbSNP:rs15303)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_022275"
FT MUTAGEN 54
FT /note="L->A: 83% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:19126594"
FT MUTAGEN 149
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19126594"
FT MUTAGEN 149
FT /note="S->T: 1.3% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:19126594"
FT MUTAGEN 150
FT /note="M->A: 62% increase in activity."
FT /evidence="ECO:0000269|PubMed:19126594"
FT MUTAGEN 226
FT /note="D->A: 4.3% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:19126594"
FT MUTAGEN 226
FT /note="D->N: 9% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:19126594"
FT MUTAGEN 260
FT /note="H->A: 3% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:19126594"
FT MUTAGEN 260
FT /note="H->Q: 1.3% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:19126594"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:3FCX"
FT STRAND 14..23
FT /evidence="ECO:0007829|PDB:3FCX"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:3FCX"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:3FCX"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:3FCX"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:3FCX"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:3FCX"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:3FCX"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3FCX"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3FCX"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:3FCX"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:3FCX"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:3FCX"
FT STRAND 136..148
FT /evidence="ECO:0007829|PDB:3FCX"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:3FCX"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:3FCX"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:3FCX"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:3FCX"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:3FCX"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:3FCX"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:3FCX"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:3FCX"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:3FCX"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:3FCX"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:3FCX"
FT HELIX 262..279
FT /evidence="ECO:0007829|PDB:3FCX"
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
