[1]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GAMMA-2 GLN-272 AND VAL-350. TISSUE=Liver; DOI=10.1111/j.1432-1033.1986.tb09855.x; PubMed=3758060 [NCBI, ExPASy, EBI, Israel, Japan] Hoeoeg J.-O., Heden L.-O., Larsson K., Joernvall H.; "The gamma 1 and gamma 2 subunits of human liver alcohol dehydrogenase. cDNA structures, two amino acid replacements, and compatibility with changes in the enzymatic properties."; Eur. J. Biochem. 159:215-218(1986).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; PubMed=2935875 [NCBI, ExPASy, EBI, Israel, Japan] Ikuta T., Szeto S., Yoshida A.; "Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence."; Proc. Natl. Acad. Sci. U.S.A. 83:634-638(1986).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1524834 [NCBI, ExPASy, EBI, Israel, Japan] Yokoyama S., Matsuo Y., Rajasekharan S., Yokoyama R.; "Molecular structure of the human alcohol dehydrogenase 3 gene."; Jpn. J. Genet. 67:167-171(1992).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-48; SER-166; GLN-272; VAL-350 AND THR-352. Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.; "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."; Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GAMMA-2 GLN-272 AND VAL-350. TISSUE=Brain, and Femoral artery; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[6]	PROTEIN SEQUENCE OF 2-375. TISSUE=Liver; DOI=10.1111/j.1432-1033.1984.tb08575.x; PubMed=6391921 [NCBI, ExPASy, EBI, Israel, Japan] Buhler R., Hempel J., Kaiser R., de Zalenski C., von Wartburg J.-P., Joernvall H.; "Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1 protein chain."; Eur. J. Biochem. 145:447-453(1984).

Comments

CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit.
SUBUNIT: Dimer of identical or non-identical chains of three types; alpha, beta and gamma.
SUBCELLULAR LOCATION: Cytoplasm.
POLYMORPHISM: Two main alleles are known, ADH3*1 or gamma-1 has Arg-272/Ile-350 while ADH3*2 or gamma-2 has Gln-272/Val-350. ADH3*1 is associated with a fast rate of ethanol oxidation and ADH3*2 with a slow rate.
MISCELLANEOUS: There are 7 different ADH's isozymes in human: three belongs to class-I: alpha, beta, and gamma, one to class-II: pi, one to class-III: chi, one to class-IV: ADH7 and one to class-V: ADH6.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X04299; CAA27842.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04350; CAA27876.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M12272; AAC41757.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D11067; BAC06856.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ088981; AAY68222.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC062476; AAH62476.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC066227; AAH66227.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC066228; AAH66228.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC067419; AAH67419.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC067420; AAH67420.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC067421; AAH67421.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC067422; AAH67422.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC074771; AAH74771.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC074786; AAH74786.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

C25428; DEHUAG.

NP_000660.1; -.

3D structure databases

PDB

1DDA; Model; -; A/B=1-375.	[ExPASy / RCSB / EBI]
1HT0; X-ray; 2.00 A; A/B=1-375.	[ExPASy / RCSB / EBI]
1U3W; X-ray; 1.45 A; A/B=1-375.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DDA; -.
1HT0; -.
1U3W; -.

ModBase

P00326.

PTM databases

PhosphoSite

P00326; -.

Enzyme and pathway databases

Reactome

REACT_2063; Metabolism of xenobiotics.

Polymorphism databases

NIEHS-SNPs

ADH1C.

Organism-specific databases

HIX0031470; -.

HGNC:251; ADH1C.

103730; gene. [NCBI / EBI]

PharmGKB

PA24572; -.

GeneCards

P00326.

Gene expression databases

ArrayExpress

P00326; -.

CleanEx

HS_ADH1C; -.

GermOnline

ENSG00000196616; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (non-traceable author statement from UniProtKB).
GO:0004024;	Molecular function: alcohol dehydrogenase activity, zinc-dependent (non-traceable author statement from UniProtKB).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006066;	Biological process: cellular alcohol metabolic process (non-traceable author statement from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.

PANTHER

PTHR11695; ADH_Sf_Zn; 1.

Pfam

PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00059; ADH_ZINC; 1.

ProtoNet

P00326.

Genome annotation databases

Ensembl

ENSG00000196616; Homo sapiens. [Contig view]

GeneID

126; -.

KEGG

hsa:126; -.

Phylogenomic databases

HOVERGEN

P00326; -.

Other

DrugBank

DB01213; Fomepizole.
DB00157; NADH.

NextBio

503; -.

SOURCE

ADH1C; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Polymorphism; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 375`	`374`	`Alcohol dehydrogenase 1C.`	`PRO_0000160664`
`METAL`	`47 47`		`Zinc 1; catalytic.`
`METAL`	`68 68`		`Zinc 1; catalytic.`
`METAL`	`98 98`		`Zinc 2.`
`METAL`	`101 101`		`Zinc 2.`
`METAL`	`104 104`		`Zinc 2.`
`METAL`	`112 112`		`Zinc 2.`
`METAL`	`175 175`		`Zinc 1; catalytic.`
`MOD_RES`	`2 2`		`N-acetylserine.`
`VARIANT`	`48 48`	`1`	`R -> H.`	`VAR_023992 [3D]`
`VARIANT`	`166 166`	`1`	`P -> S.`	`VAR_023993 [3D]`
`VARIANT`	`272 272`	`1`	`R -> Q (in allele ADH3*2/gamma-2; dbSNP:rs1693482 [NCBI]).`	`VAR_000428 [3D]`
`VARIANT`	`350 350`	`1`	`I -> V (in allele ADH3*2/gamma-2; dbSNP:rs698 [NCBI]).`	`VAR_000429 [3D]`
`VARIANT`	`352 352`	`1`	`P -> T.`	`VAR_023994 [3D]`
`CONFLICT`	`130 130`		`Missing (in Ref. 6; AA sequence).`
`CONFLICT`	`171 171`		`C -> R (in Ref. 5; AAH67421).`
`STRAND`	`8 15`	`8`
`STRAND`	`23 29`	`7`
`STRAND`	`36 45`	`10`
`HELIX`	`48 54`	`7`
`STRAND`	`62 65`	`4`
`STRAND`	`69 77`	`9`
`STRAND`	`89 92`	`4`
`STRAND`	`99 101`	`3`
`HELIX`	`102 105`	`4`
`STRAND`	`117 119`	`3`
`STRAND`	`131 133`	`3`
`STRAND`	`136 139`	`4`
`TURN`	`142 144`	`3`
`STRAND`	`147 154`	`8`
`HELIX`	`155 157`	`3`
`STRAND`	`158 160`	`3`
`HELIX`	`167 170`	`4`
`HELIX`	`171 174`	`4`
`HELIX`	`176 185`	`10`
`TURN`	`186 188`	`3`
`STRAND`	`195 199`	`5`
`HELIX`	`203 214`	`12`
`STRAND`	`218 223`	`6`
`HELIX`	`227 229`	`3`
`HELIX`	`230 235`	`6`
`STRAND`	`239 242`	`4`
`HELIX`	`244 246`	`3`
`HELIX`	`251 258`	`8`
`TURN`	`259 261`	`3`
`STRAND`	`262 268`	`7`
`HELIX`	`273 282`	`10`
`TURN`	`285 287`	`3`
`STRAND`	`289 292`	`4`
`STRAND`	`302 304`	`3`
`HELIX`	`307 310`	`4`
`STRAND`	`314 317`	`4`
`HELIX`	`320 322`	`3`
`HELIX`	`325 337`	`13`
`HELIX`	`344 346`	`3`
`STRAND`	`347 352`	`6`
`HELIX`	`353 355`	`3`
`HELIX`	`356 364`	`9`
`STRAND`	`369 374`	`6`

Sequence information

Length: 375 AA [This is the length of the unprocessed precursor]

Molecular weight: 39868 Da [This is the MW of the unprocessed precursor]

CRC64: 414D73CC4C104C84 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAAGICRSD EHVVSGNLVT 

        70         80         90        100        110        120 
PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK CRICKNPESN YCLKNDLGNP 

       130        140        150        160        170        180 
RGTLQDGTRR FTCSGKPIHH FVGVSTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG 

       190        200        210        220        230        240 
YGSAVKVAKV TPGSTCAVFG LGGVGLSVVM GCKAAGAARI IAVDINKDKF AKAKELGATE 

       250        260        270        280        290        300 
CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ 

       310        320        330        340        350        360 
NLSINPMLLL TGRTWKGAIF GGFKSKESVP KLVADFMAKK FSLDALITNI LPFEKINEGF 

       370 
DLLRSGKSIR TVLTF

P00326 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools