NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
DOI=10.1016/0014-5793(95)00554-M; PubMed=7541757 [NCBI, ExPASy, EBI, Israel, Japan]
Hjelmqvist L., Metsis M., Persson H., Hoeoeg J.-O., McLennan J., Joernvall H.;
"Alcohol dehydrogenase of class I: kiwi liver enzyme, parallel evolution in separate vertebrate lines, and correlation with 12S rRNA patterns.";
FEBS Lett. 367:306-310(1995).

[2]

PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT SER-2.
DOI=10.1016/0014-5793(95)00572-Q; PubMed=7607314 [NCBI, ExPASy, EBI, Israel, Japan]
Hjelmqvist L., Hackett M., Shafqat J., Danielsson O., Iida J., Hendrickson R.C., Michel H., Shabanowitz J., Hunt D.F., Jornvall H.;
"Multiplicity of N-terminal structures of medium-chain alcohol dehydrogenases. Mass-spectrometric analysis of plant, lower vertebrate and higher vertebrate class I, II, and III forms of the enzyme.";
FEBS Lett. 367:237-240(1995).

Comments

CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
SUBUNIT: Homodimer.
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

S78778; AAC60755.2; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S66272; S66272.

3D structure databases

HSSP

P00326; 1HT0. [HSSP ENTRY / PDB]

SMR

P49645; 2-375.

ModBase

P49645.

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:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
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

P49645.

Phylogenomic databases

HOVERGEN

P49645; -.

Other

UniRef

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

Keywords

Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 375`	`374`	`Alcohol dehydrogenase 1.`	`PRO_0000160671`
`METAL`	`47 47`		`Zinc 1; catalytic (By similarity).`
`METAL`	`68 68`		`Zinc 1; catalytic (By similarity).`
`METAL`	`98 98`		`Zinc 2 (By similarity).`
`METAL`	`101 101`		`Zinc 2 (By similarity).`
`METAL`	`104 104`		`Zinc 2 (By similarity).`
`METAL`	`112 112`		`Zinc 2 (By similarity).`
`METAL`	`175 175`		`Zinc 1; catalytic (By similarity).`
`MOD_RES`	`2 2`		`N-acetylserine.`

Sequence information

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

Molecular weight: 39631 Da [This is the MW of the unprocessed precursor]

CRC64: A6EBC1BEB0D66E02 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTAGKVIKC KAAVLWEPKK PFSIEEVEVA PPKAHEVRIK ILATGICRSD DHVITGALVR 

        70         80         90        100        110        120 
PFPIILGHEA AGVVESVGEG VTSVKPGDKV IPLFVPQCGE CSACLSTKGN LCSKNDIGSA 

       130        140        150        160        170        180 
SGLMPDGTTR FTCKGKAIHH FIGTSTFTEY TVVHETAVAK IAAAAPLEKV CLIGCGFSTG 

       190        200        210        220        230        240 
YGAAVQTAKV EPGSTCAVFG LGGVGLSVVM GCKAAGASRI IAIDINKDKF AKAKELGATD 

       250        260        270        280        290        300 
CVNPKDFTKP IHEVLMEMTG LGVDYSFEVI GHTETMAAAL ASCHFNYGVS VILGVPPAAE 

       310        320        330        340        350        360 
KISFDPMLLF SGRTWKGSVF GGWKSKDAVP KLVADYMEKK FVLEPLITHT LPFIKINEGF 

       370 
DLLRKGKSIR SVLVF

P49645 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