ADH1G_HUMAN
ID ADH1G_HUMAN Reviewed; 375 AA.
AC P00326; Q4PJ18; Q5WRV0; Q6LBW4; Q6NWV0; Q6NZA7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Alcohol dehydrogenase 1C;
DE EC=1.1.1.1 {ECO:0000269|PubMed:6391957};
DE AltName: Full=Alcohol dehydrogenase subunit gamma;
GN Name=ADH1C; Synonyms=ADH3;
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 NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GAMMA-2 GLN-272 AND VAL-350, AND
RP POLYMORPHISM.
RC TISSUE=Liver;
RX PubMed=3758060; DOI=10.1111/j.1432-1033.1986.tb09855.x;
RA Hoeoeg J.-O., Heden L.-O., Larsson K., Joernvall H.;
RT "The gamma 1 and gamma 2 subunits of human liver alcohol dehydrogenase.
RT cDNA structures, two amino acid replacements, and compatibility with
RT changes in the enzymatic properties.";
RL Eur. J. Biochem. 159:215-218(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2935875; DOI=10.1073/pnas.83.3.634;
RA Ikuta T., Szeto S., Yoshida A.;
RT "Three human alcohol dehydrogenase subunits: cDNA structure and molecular
RT and evolutionary divergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:634-638(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1524834; DOI=10.1266/jjg.67.167;
RA Yokoyama S., Matsuo Y., Rajasekharan S., Yokoyama R.;
RT "Molecular structure of the human alcohol dehydrogenase 3 gene.";
RL Jpn. J. Genet. 67:167-171(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-48; SER-166; GLN-272;
RP VAL-350 AND THR-352.
RG NIEHS SNPs program;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GAMMA-2 GLN-272 AND
RP VAL-350.
RC TISSUE=Brain, and Femoral artery;
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 2-375, CLEAVAGE OF INITIATOR METHIONINE, AND
RP ACETYLATION AT SER-2.
RC TISSUE=Liver;
RX PubMed=6391921; DOI=10.1111/j.1432-1033.1984.tb08575.x;
RA Buhler R., Hempel J., Kaiser R., de Zalenski C., von Wartburg J.-P.,
RA Joernvall H.;
RT "Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1
RT protein chain.";
RL Eur. J. Biochem. 145:447-453(1984).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=6391957; DOI=10.1016/0014-5793(84)80610-9;
RA Buehler R., Von Wartburg J.P.;
RT "Differential susceptibility of human alcohol dehydrogenase isoenzymes to
RT anions.";
RL FEBS Lett. 178:249-252(1984).
RN [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC IONS.
RX PubMed=11274460; DOI=10.1110/ps.45001;
RA Niederhut M.S., Gibbons B.J., Perez-Miller S., Hurley T.D.;
RT "Three-dimensional structures of the three human class I alcohol
RT dehydrogenases.";
RL Protein Sci. 10:697-706(2001).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC IONS.
RX PubMed=15449945; DOI=10.1021/bi0489107;
RA Gibbons B.J., Hurley T.D.;
RT "Structure of three class I human alcohol dehydrogenases complexed with
RT isoenzyme specific formamide inhibitors.";
RL Biochemistry 43:12555-12562(2004).
CC -!- FUNCTION: Alcohol dehydrogenase. Exhibits high activity for ethanol
CC oxidation and plays a major role in ethanol catabolism.
CC {ECO:0000269|PubMed:6391957}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:6391957};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethanol + NAD(+) = acetaldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:25290, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16236, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:6391957};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25291;
CC Evidence={ECO:0000305|PubMed:6391957};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:11274460, ECO:0000269|PubMed:15449945};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:11274460,
CC ECO:0000269|PubMed:15449945};
CC -!- SUBUNIT: Dimer of identical or non-identical chains of class I alcohol
CC dehydrogenase: ADH1A, ADH1B, and ADH1C. {ECO:0000269|PubMed:11274460,
CC ECO:0000269|PubMed:15449945}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- POLYMORPHISM: Two main alleles are known, ADH3*1 or gamma-1 has Arg-
CC 272/Ile-350 while ADH3*2 or gamma-2 has Gln-272/Val-350. ADH3*1 is
CC associated with a fast rate of ethanol oxidation and ADH3*2 with a slow
CC rate. {ECO:0000269|PubMed:3758060}.
CC -!- MISCELLANEOUS: There are 7 different ADH's isozymes in human: three
CC belongs to class-I: ADH1A, ADH1B, and ADH1C, one to class-II: ADH4, one
CC to class-III: ADH5, one to class-IV: ADH7 and one to class-V: ADH6.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/adh1c/";
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DR EMBL; X04299; CAA27842.1; -; mRNA.
DR EMBL; X04350; CAA27876.1; -; mRNA.
DR EMBL; M12272; AAC41757.1; -; mRNA.
DR EMBL; D11067; BAC06856.1; -; Genomic_DNA.
DR EMBL; DQ088981; AAY68222.1; -; Genomic_DNA.
DR EMBL; AC133528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC062476; AAH62476.1; -; mRNA.
DR EMBL; BC066227; AAH66227.1; -; mRNA.
DR EMBL; BC066228; AAH66228.1; -; mRNA.
DR EMBL; BC067419; AAH67419.1; -; mRNA.
DR EMBL; BC067420; AAH67420.1; -; mRNA.
DR EMBL; BC067421; AAH67421.1; -; mRNA.
DR EMBL; BC067422; AAH67422.1; -; mRNA.
DR EMBL; BC074771; AAH74771.1; -; mRNA.
DR EMBL; BC074786; AAH74786.1; -; mRNA.
DR CCDS; CCDS54780.1; -.
DR PIR; C25428; DEHUAG.
DR RefSeq; NP_000660.1; NM_000669.4.
DR PDB; 1HT0; X-ray; 2.00 A; A/B=2-375.
DR PDB; 1U3W; X-ray; 1.45 A; A/B=2-375.
DR PDBsum; 1HT0; -.
DR PDBsum; 1U3W; -.
DR AlphaFoldDB; P00326; -.
DR SMR; P00326; -.
DR BioGRID; 106638; 20.
DR IntAct; P00326; 3.
DR STRING; 9606.ENSP00000426083; -.
DR BindingDB; P00326; -.
DR ChEMBL; CHEMBL3285; -.
DR DrugBank; DB03061; (R)-N-(1-Methyl-Hexyl)-Formamide.
DR DrugBank; DB01711; 2,3,4,5,6-Pentafluorobenzyl Alcohol.
DR DrugBank; DB04312; 2,3-Difluorobenzyl Alcohol.
DR DrugBank; DB04448; 2,4-Difluorobenzyl Alcohol 2,4-Difluoro-1-(Hydroxymethyl)Benzene.
DR DrugBank; DB02249; 2-Ethoxyethanol.
DR DrugBank; DB02871; 3-Butylthiolane 1-Oxide.
DR DrugBank; DB02721; 4-Iodopyrazole.
DR DrugBank; DB03020; 5-beta-D-ribofuranosylnicotinamide adenine dinucleotide.
DR DrugBank; DB02659; Cholic Acid.
DR DrugBank; DB04071; Cpad.
DR DrugBank; DB03559; Cyclohexylformamide.
DR DrugBank; DB00898; Ethanol.
DR DrugBank; DB01213; Fomepizole.
DR DrugBank; DB02131; N-1-methylheptylformamide.
DR DrugBank; DB04113; N-Formylpiperidine.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB02822; Para-Bromobenzyl Alcohol.
DR DrugBank; DB02757; Pyrazole.
DR DrugBank; DB03226; Trifluoroethanol.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR DrugCentral; P00326; -.
DR iPTMnet; P00326; -.
DR PhosphoSitePlus; P00326; -.
DR BioMuta; ADH1C; -.
DR DMDM; 113398; -.
DR jPOST; P00326; -.
DR MassIVE; P00326; -.
DR MaxQB; P00326; -.
DR PeptideAtlas; P00326; -.
DR PRIDE; P00326; -.
DR ProteomicsDB; 51229; -.
DR TopDownProteomics; P00326; -.
DR Antibodypedia; 73653; 149 antibodies from 23 providers.
DR DNASU; 126; -.
DR Ensembl; ENST00000515683.6; ENSP00000426083.1; ENSG00000248144.6.
DR GeneID; 126; -.
DR KEGG; hsa:126; -.
DR MANE-Select; ENST00000515683.6; ENSP00000426083.1; NM_000669.5; NP_000660.1.
DR UCSC; uc032trd.2; human.
DR CTD; 126; -.
DR DisGeNET; 126; -.
DR GeneCards; ADH1C; -.
DR HGNC; HGNC:251; ADH1C.
DR HPA; ENSG00000248144; Group enriched (intestine, liver, stomach).
DR MalaCards; ADH1C; -.
DR MIM; 103730; gene.
DR neXtProt; NX_P00326; -.
DR OpenTargets; ENSG00000248144; -.
DR PharmGKB; PA24572; -.
DR VEuPathDB; HostDB:ENSG00000248144; -.
DR eggNOG; KOG0022; Eukaryota.
DR GeneTree; ENSGT00940000155234; -.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; P00326; -.
DR OMA; RVKMIAT; -.
DR OrthoDB; 664798at2759; -.
DR BRENDA; 1.1.1.1; 2681.
DR PathwayCommons; P00326; -.
DR Reactome; R-HSA-5365859; RA biosynthesis pathway.
DR Reactome; R-HSA-71384; Ethanol oxidation.
DR SABIO-RK; P00326; -.
DR SignaLink; P00326; -.
DR BioGRID-ORCS; 126; 5 hits in 186 CRISPR screens.
DR ChiTaRS; ADH1C; human.
DR EvolutionaryTrace; P00326; -.
DR GeneWiki; ADH1C; -.
DR GenomeRNAi; 126; -.
DR Pharos; P00326; Tclin.
DR PRO; PR:P00326; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P00326; protein.
DR Bgee; ENSG00000248144; Expressed in mucosa of transverse colon and 128 other tissues.
DR ExpressionAtlas; P00326; baseline and differential.
DR Genevisible; P00326; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0006069; P:ethanol oxidation; IDA:UniProtKB.
DR GO; GO:0042573; P:retinoic acid metabolic process; IBA:GO_Central.
DR GO; GO:0042572; P:retinol metabolic process; IBA:GO_Central.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Metal-binding; NAD; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6391921"
FT CHAIN 2..375
FT /note="Alcohol dehydrogenase 1C"
FT /id="PRO_0000160664"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HT0,
FT ECO:0007744|PDB:1U3W"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HT0,
FT ECO:0007744|PDB:1U3W"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HT0,
FT ECO:0007744|PDB:1U3W"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HT0,
FT ECO:0007744|PDB:1U3W"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HT0,
FT ECO:0007744|PDB:1U3W"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HT0,
FT ECO:0007744|PDB:1U3W"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HT0,
FT ECO:0007744|PDB:1U3W"
FT BINDING 200..205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HT0,
FT ECO:0007744|PDB:1U3W"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HT0,
FT ECO:0007744|PDB:1U3W"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HT0,
FT ECO:0007744|PDB:1U3W"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:1HT0, ECO:0007744|PDB:1U3W"
FT BINDING 293..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HT0,
FT ECO:0007744|PDB:1U3W"
FT BINDING 318..320
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HT0,
FT ECO:0007744|PDB:1U3W"
FT BINDING 370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11274460,
FT ECO:0000269|PubMed:15449945, ECO:0007744|PDB:1HT0,
FT ECO:0007744|PDB:1U3W"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:6391921"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00325"
FT VARIANT 48
FT /note="R -> H (in dbSNP:rs35385902)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023992"
FT VARIANT 166
FT /note="P -> S (in dbSNP:rs34195308)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023993"
FT VARIANT 272
FT /note="R -> Q (in allele ADH3*2/gamma-2; dbSNP:rs1693482)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3758060, ECO:0000269|Ref.4"
FT /id="VAR_000428"
FT VARIANT 350
FT /note="I -> V (in allele ADH3*2/gamma-2; dbSNP:rs698)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3758060, ECO:0000269|Ref.4"
FT /id="VAR_000429"
FT VARIANT 352
FT /note="P -> T (in dbSNP:rs35719513)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023994"
FT CONFLICT 130
FT /note="Missing (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="C -> R (in Ref. 6; AAH67421)"
FT /evidence="ECO:0000305"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1U3W"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:1U3W"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 251..258
FT /evidence="ECO:0007829|PDB:1U3W"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:1U3W"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 325..337
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:1U3W"
FT HELIX 356..364
FT /evidence="ECO:0007829|PDB:1U3W"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:1U3W"
SQ SEQUENCE 375 AA; 39868 MW; 414D73CC4C104C84 CRC64;
MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAAGICRSD EHVVSGNLVT
PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK CRICKNPESN YCLKNDLGNP
RGTLQDGTRR FTCSGKPIHH FVGVSTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG
YGSAVKVAKV TPGSTCAVFG LGGVGLSVVM GCKAAGAARI IAVDINKDKF AKAKELGATE
CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ
NLSINPMLLL TGRTWKGAIF GGFKSKESVP KLVADFMAKK FSLDALITNI LPFEKINEGF
DLLRSGKSIR TVLTF
