Alcohol dehydrogenase 4 - Homo sapiens (Human)

Contribute

Send feedback

Reviewed, UniProtKB/Swiss-Prot P08319 (ADH4_HUMAN)

Last modified September 2, 2008. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (7) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase 4
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase class II pi chain

Gene names

Name:

ADH4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity	An alcohol + NAD(+) = an aldehyde or ketone + NADH.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
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.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Class-II subfamily.

Hide | Top

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	alcohol catabolic process Inferred from sequence or structural similarity. Source: UniProtKB cellular aldehyde metabolic process Inferred from direct assay. Source: UniProtKB ethanol oxidation Inferred from direct assay. Source: UniProtKB quinone cofactor metabolic process Inferred from sequence or structural similarity. Source: UniProtKB retinol metabolic process Inferred from direct assay. Source: UniProtKB
Molecular function	NAD binding Inferred from direct assay. Source: UniProtKB NADPH:quinone reductase activity Inferred from sequence or structural similarity. Source: UniProtKB alcohol dehydrogenase activity, zinc-dependent Inferred from direct assay. Source: UniProtKB all-trans retinal binding Inferred from direct assay. Source: UniProtKB benzaldehyde dehydrogenase activity Inferred from direct assay. Source: UniProtKB retinol binding Inferred from direct assay. Source: UniProtKB retinol dehydrogenase activity Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Initiator methionine

Removed

Chain

2 – 380

379

Alcohol dehydrogenase 4

Sites

Metal binding

Zinc 1; catalytic

Metal binding

Zinc 1; catalytic

Metal binding

Zinc 2

Metal binding

102

Zinc 2

Metal binding

105

Zinc 2

Metal binding

113

Zinc 2

Metal binding

180

Zinc 1; catalytic

Natural variations

Natural variant

Natural variant

Natural variant

Experimental info

Sequence conflict

T → S Ref.1 Ref.2

Sequence conflict

380

F → FGRCQEQFRILSD in AAA51595. Ref.1

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P08319-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 9ED102B3BA763B73
Show »

FASTA

380

40,222

        10         20         30         40         50         60 
MGTKGKVIKC KAAIAWEAGK PLCIEEVEVA PPKAHEVRIQ IIATSLCHTD ATVIDSKFEG 

        70         80         90        100        110        120 
LAFPVIVGHE AAGIVESIGP GVTNVKPGDK VIPLYAPLCR KCKFCLSPLT NLCGKISNLK 

       130        140        150        160        170        180 
SPASDQQLME DKTSRFTCKG KPVYHFFGTS TFSQYTVVSD INLAKIDDDA NLERVCLLGC 

       190        200        210        220        230        240 
GFSTGYGAAI NNAKVTPGST CAVFGLGGVG LSAVMGCKAA GASRIIGIDI NSEKFVKAKA 

       250        260        270        280        290        300 
LGATDCLNPR DLHKPIQEVI IELTKGGVDF ALDCAGGSET MKAALDCTTA GWGSCTFIGV 

       310        320        330        340        350        360 
AAGSKGLTVF PEELIIGRTI NGTFFGGWKS VDSIPKLVTD YKNKKFNLDA LVTHTLPFDK 

       370        380 
ISEAFDLMNQ GKSIRTILIF

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the class II enzyme of human liver alcohol dehydrogenase: combined cDNA and protein sequence determination of the pi subunit." Hoeoeg J.-O., von Bahr-Lindstroem H., Heden L.-O., Holmquist B., Larsson K., Hempel J., Vallee B.L., Joernvall H. Biochemistry 26:1926-1932(1987) [PubMed: 3036213] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANTS ILE-309 AND VAL-374.
[2]	"Cloning and characterization of the human ADH4 gene." von Bahr-Lindstroem H., Joernvall H., Hoeoeg J.-O. Gene 103:269-274(1991) [PubMed: 1889753] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-309 AND VAL-374. Tissue: Fetal liver.
[3]	"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)." Livingston R.J., Rieder M.J., Rajkumar N., Downing T.K., Olson A.N., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-309; HIS-318 AND VAL-374.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

M15943 mRNA. Translation: AAA51595.1.
X56411

X56419 Genomic DNA. Translation: CAA39813.1.
AY974245 Genomic DNA. Translation: AAX59034.1.
BC022319 mRNA. Translation: AAH22319.1.

PIR

DEHUAP. A27109.

RefSeq

NP_000661.2.

UniGene

Hs.1219

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3COS	X-ray	2.10	A/B/C/D	1-380	[»]

ModBase

Search...

Polymorphism databases

NIEHS-SNPs

Search...

Genome annotation databases

Ensembl

ENSG00000198099. Homo sapiens. [Contig view]

GeneID

127.

KEGG

hsa:127.

Organism-specific databases

HGNC

HGNC:252. ADH4.

MIM

103740. gene.

PharmGKB

PA24573.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P08319.

HOVERGEN

P08319.

Enzyme and pathway databases

Reactome

REACT_2063. Metabolism of xenobiotics.

Gene expression databases

ArrayExpress

P08319.

CleanEx

HS_ADH4.

GermOnline

ENSG00000198099. Homo sapiens.

Family and domain databases

InterPro

IPR013154. AlcDHase_GroES-like.
IPR002085. AlcDHase_SF_Zn.
IPR013149. AlcDHase_Zn-bd.
IPR002328. AlcDHase_Zn_CS.
[Graphical view]

PANTHER

PTHR11695. ADH_Sf_Zn. 1 hit.

Pfam

PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]

PROSITE

PS00059. ADH_ZINC. 1 hit.
[Graphical view]

ProDom

P08319.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

DrugBank

DB00157. NADH.

SOURCE

Search...

ProtoNet

Search...

Hide | Top

Entry information

Entry name

ADH4_HUMAN

Accession

Primary (citable) accession number: P08319
Secondary accession number(s): Q8TCD7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	September 2, 2008
This is version 91 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top