[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1016/0378-1119(86)90087-9; PubMed=2881847 [NCBI, ExPASy, EBI, Israel, Japan] Crabb D.W., Edenberg H.J.; "Complete amino acid sequence of rat liver alcohol dehydrogenase deduced from the cDNA sequence."; Gene 48:287-291(1986).
[2]	NUCLEOTIDE SEQUENCE. DOI=10.1016/0888-7543(89)90133-X; PubMed=2591969 [NCBI, ExPASy, EBI, Israel, Japan] Crabb D.W., Stein P.M., Dipple K.M., Hittle J.B., Sidhu R., Qulali M., Zhang K., Edenberg H.J.; "Structure and expression of the rat class I alcohol dehydrogenase gene."; Genomics 5:906-914(1989).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Prostate; 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).
[4]	ACETYLATION AT SER-2. DOI=10.1111/j.1432-1033.1972.tb01971.x; PubMed=4673366 [NCBI, ExPASy, EBI, Israel, Japan] Jornvall H., Markovic O.; "Structural studies of alcohol dehydrogenase from rat liver."; Eur. J. Biochem. 29:167-174(1972).

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 (A, B, C), which are coded by 3 separate genes at different loci.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Class-I subfamily.

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

M29523; AAA85462.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M29516; AAA85462.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M29517; AAA85462.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M29518; AAA85462.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M29519; AAA85462.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M29520; AAA85462.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M29521; AAA85462.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M29522; AAA85462.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M15327; AAA40681.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC062403; AAH62403.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A26468; A26468.

NP_062159.3; -.

3D structure databases

HSSP

P00326; 1HT0. [HSSP ENTRY / PDB]

SMR

P06757; 2-376.

ModBase

P06757.

Organism-specific databases

RGD

2044; Adh1.

Gene expression databases

ArrayExpress

P06757; -.

GermOnline

ENSRNOG00000012464; Rattus norvegicus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004022;	Molecular function: alcohol dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

Genome annotation databases

Ensembl

ENSRNOG00000012464; Rattus norvegicus. [Contig view]

GeneID

24172; -.

KEGG

rno:24172; -.

Phylogenomic databases

HOVERGEN

P06757; -.

Other

NextBio

602493; -.

UniRef

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

Keywords

Acetylation; Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 376`	`375`	`Alcohol dehydrogenase 1.`	`PRO_0000160669`
`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`	`176 176`		`Zinc 1; catalytic.`
`MOD_RES`	`2 2`		`N-acetylserine.`
`CONFLICT`	`143 143`		`I -> L (in Ref. 1; AAA40681).`

Sequence information

Length: 376 AA [This is the length of the unprocessed precursor]

Molecular weight: 39645 Da [This is the MW of the unprocessed precursor]

CRC64: 3C7026C6D7C0ED76 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTAGKVIKC KAAVLWEPHK PFTIEDIEVA PPKAHEVRIK MVATGVCRSD DHAVSGSLFT 

        70         80         90        100        110        120 
PLPAVLGHEG AGIVESIGEG VTCVKPGDKV IPLFSPQCGK CRICKHPESN LCCQTKNLTQ 

       130        140        150        160        170        180 
PKGALLDGTS RFSCRGKPIH HFISTSTFSQ YTVVDDIAVA KIDAAAPLDK VCLIGCGFST 

       190        200        210        220        230        240 
GYGSAVQVAK VTPGSTCAVF GLGGVGLSVV IGCKTAGAAK IIAVDINKDK FAKAKELGAT 

       250        260        270        280        290        300 
DCINPQDYTK PIQEVLQEMT DGGVDFSFEV IGRLDTMTSA LLSCHSACGV SVIVGVPPSA 

       310        320        330        340        350        360 
QSLSVNPMSL LLGRTWKGAI FGGFKSKDAV PKLVADFMAK KFPLEPLITH VLPFEKINEA 

       370 
FDLLRAGKSI RTVLTF

P06757 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