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Reviewed, UniProtKB/Swiss-Prot P07327 (ADH1A_HUMAN)

Last modified June 16, 2009. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Alcohol dehydrogenase 1A
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase subunit alpha
Gene names
Name: ADH1A
Synonyms: ADH1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

Dimer of identical or non-identical chains of three types; alpha, beta and gamma.

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.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcellular alcohol metabolic process Ref.7

Non-traceable author statement. Source: UniProtKB

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from Experiment. Source: Reactome

   Molecular functionalcohol dehydrogenase activity, zinc-dependent

Inferred from direct assay. Source: UniProtKB

protein binding

Inferred from physical interaction. Source: UniProtKB

transcription regulator activity

Inferred from direct assay. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 375374Alcohol dehydrogenase 1A
PRO_0000160658

Regions

Nucleotide binding200 – 2056NAD
Nucleotide binding293 – 2953NAD

Sites

Metal binding471Zinc 1; catalytic
Metal binding681Zinc 1; catalytic
Metal binding981Zinc 2
Metal binding1011Zinc 2
Metal binding1041Zinc 2
Metal binding1121Zinc 2
Metal binding1751Zinc 1; catalytic
Binding site2241NAD
Binding site2291NAD
Binding site3701NAD

Amino acid modifications

Modified residue21N-acetylserine

Secondary structure

1 ............................................................................. 375
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P07327-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B6DF4D57080D9BC1

FASTA37539,859
        10         20         30         40         50         60 
MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAVGICGTD DHVVSGTMVT 

        70         80         90        100        110        120 
PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLAIPQCGK CRICKNPESN YCLKNDVSNP 

       130        140        150        160        170        180 
QGTLQDGTSR FTCRRKPIHH FLGISTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG 

       190        200        210        220        230        240 
YGSAVNVAKV TPGSTCAVFG LGGVGLSAIM GCKAAGAARI IAVDINKDKF AKAKELGATE 

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

       310        320        330        340        350        360 
NLSMNPMLLL TGRTWKGAIL GGFKSKECVP KLVADFMAKK FSLDALITHV LPFEKINEGF 

       370 
DLLHSGKSIR TILMF

« Hide

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References

« Hide 'large scale' references
[1]"cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase."
von Bahr-Lindstroem H., Hoeoeg J.-O., Heden L.-O., Kaiser R., Fleetwood L., Larsson K., Lake M., Holmquist B., Holmgren A., Hempel J., Vallee B.L., Joernvall H.
Biochemistry 25:2465-2470(1986) [PubMed: 3013304] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-375.
Tissue: Liver.
[2]"Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence."
Ikuta T., Szeto S., Yoshida A.
Proc. Natl. Acad. Sci. U.S.A. 83:634-638(1986) [PubMed: 2935875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Molecular structure of the human alcohol dehydrogenase 1 gene."
Matsuo Y., Yokoyama S.
FEBS Lett. 243:57-60(1989) [PubMed: 2920825] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]NIEHS SNPs program
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"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: Brain.
[7]"The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome."
Yasunami M., Kikuchi I., Sarapata D., Yoshida A.
Genomics 7:152-158(1990) [PubMed: 2347582] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
[8]"Structure of three class I human alcohol dehydrogenases complexed with isoenzyme specific formamide inhibitors."
Gibbons B.J., Hurley T.D.
Biochemistry 43:12555-12562(2004) [PubMed: 15449945] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC IONS.
[9]"Three-dimensional structures of the three human class I alcohol dehydrogenases."
Niederhut M.S., Gibbons B.J., Perez-Miller S., Hurley T.D.
Protein Sci. 10:697-706(2001) [PubMed: 11274460] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC IONS.
+Additional computationally mapped references.

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Web resources

NIEHS-SNPs

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Cross-references

Sequence databases

M12963 mRNA. Translation: AAA51590.1.
M12271 mRNA. Translation: AAA68131.1.
BT019812 mRNA. Translation: AAV38615.1.
AY948115 Genomic DNA. Translation: AAX20115.1.
BC074738 mRNA. Translation: AAH74738.1.
BC117442 mRNA. Translation: AAI17443.1.
BC126306 mRNA. Translation: AAI26307.1.
M37066 Genomic DNA. Translation: AAA51591.1.
IPIIPI00218896.
PIRDEHUAA. S02265.
RefSeqNP_000658.1.
UniGeneHs.654433

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1HSOX-ray2.50A/B2-375[»]
1U3TX-ray2.49A/B2-375[»]
ModBaseSearch...

Proteomic databases

PRIDEP07327.

Genome annotation databases

EnsemblENSG00000187758. Homo sapiens. [Contig view]
GeneID124.
KEGGhsa:124.

Organism-specific databases

GeneCardsGC04M100450.
H-InvDBHIX0031477.
HGNCHGNC:249. ADH1A.
HPACAB009562.
MIM103700. gene.
PharmGKBPA24570.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP07327.
HOVERGENP07327.
OMAP07327. NPQGTLQ.

Enzyme and pathway databases

BRENDA1.1.1.1. 247.
ReactomeREACT_13433. Biological oxidations.

Gene expression databases

ArrayExpressP07327.
BgeeP07327.
CleanExHS_ADH1A.
GermOnlineENSG00000187758. Homo sapiens.

Family and domain databases

InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB01213. Fomepizole.
DB00157. NADH.
NextBio495.
SOURCESearch...

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Entry information

Entry nameADH1A_HUMAN
AccessionPrimary (citable) accession number: P07327
Secondary accession number(s): Q17R68
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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