Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00326 (ADH1G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alcohol dehydrogenase 1C

EC=1.1.1.1
Alternative name(s):
Alcohol dehydrogenase subunit gamma
Gene names
Name:ADH1C
Synonyms:ADH3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

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.

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.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Caution

The reference genome assembly, GRCh37, describes a non-functional copy of that gene with a stop codon at position 78. However, this premature stop codon is not present in available mRNAs.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processethanol oxidation

Inferred from direct assay PubMed 6391957. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_functionalcohol dehydrogenase (NAD) activity

Inferred from direct assay PubMed 6391957. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 375374Alcohol dehydrogenase 1C
PRO_0000160664

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

Natural variations

Natural variant481R → H. Ref.4
Corresponds to variant rs35385902 [ dbSNP | Ensembl ].
VAR_023992
Natural variant1661P → S. Ref.4
VAR_023993
Natural variant2721R → Q in allele ADH3*2/gamma-2. Ref.1 Ref.4 Ref.6
Corresponds to variant rs1693482 [ dbSNP | Ensembl ].
VAR_000428
Natural variant3501I → V in allele ADH3*2/gamma-2. Ref.1 Ref.4 Ref.6
Corresponds to variant rs698 [ dbSNP | Ensembl ].
VAR_000429
Natural variant3521P → T. Ref.4
Corresponds to variant rs35719513 [ dbSNP | Ensembl ].
VAR_023994

Experimental info

Sequence conflict1301Missing AA sequence Ref.7
Sequence conflict1711C → R in AAH67421. Ref.6

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P00326 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 414D73CC4C104C84

FASTA37539,868
        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 

« Hide

References

« Hide 'large scale' references
[1]"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."
Hoeoeg J.-O., Heden L.-O., Larsson K., Joernvall H.
Eur. J. Biochem. 159:215-218(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GAMMA-2 GLN-272 AND VAL-350.
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Molecular structure of the human alcohol dehydrogenase 3 gene."
Yokoyama S., Matsuo Y., Rajasekharan S., Yokoyama R.
Jpn. J. Genet. 67:167-171(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]NIEHS SNPs program
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-48; SER-166; GLN-272; VAL-350 AND THR-352.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GAMMA-2 GLN-272 AND VAL-350.
Tissue: Brain and Femoral artery.
[7]"Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1 protein chain."
Buhler R., Hempel J., Kaiser R., de Zalenski C., von Wartburg J.-P., Joernvall H.
Eur. J. Biochem. 145:447-453(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-375.
Tissue: Liver.
[8]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC IONS.
[9]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC IONS.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04299 mRNA. Translation: CAA27842.1.
X04350 mRNA. Translation: CAA27876.1.
M12272 mRNA. Translation: AAC41757.1.
D11067 Genomic DNA. Translation: BAC06856.1.
DQ088981 Genomic DNA. Translation: AAY68222.1.
AC097530 Genomic DNA. No translation available.
BC062476 mRNA. Translation: AAH62476.1.
BC066227 mRNA. Translation: AAH66227.1.
BC066228 mRNA. Translation: AAH66228.1.
BC067419 mRNA. Translation: AAH67419.1.
BC067420 mRNA. Translation: AAH67420.1.
BC067421 mRNA. Translation: AAH67421.1.
BC067422 mRNA. Translation: AAH67422.1.
BC074771 mRNA. Translation: AAH74771.1.
BC074786 mRNA. Translation: AAH74786.1.
PIRDEHUAG. C25428.
RefSeqNP_000660.1. NM_000669.3.
UniGeneHs.654537.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DDAmodel-A/B1-375[»]
1HT0X-ray2.00A/B2-375[»]
1U3WX-ray1.45A/B2-375[»]
ProteinModelPortalP00326.
SMRP00326. Positions 2-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000209668.

Chemistry

BindingDBP00326.
ChEMBLCHEMBL3285.
DrugBankDB01213. Fomepizole.
DB00157. NADH.

PTM databases

PhosphoSiteP00326.

Polymorphism databases

DMDM113398.

Proteomic databases

PRIDEP00326.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID126.
KEGGhsa:126.
UCSCuc031sgp.1. human.

Organism-specific databases

CTD126.
GeneCardsGC04M100257.
HGNCHGNC:251. ADH1C.
MIM103730. gene.
neXtProtNX_P00326.
PharmGKBPA24572.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG000195.
InParanoidP00326.
KOK13951.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKP00326.

Gene expression databases

CleanExHS_ADH1C.
GenevestigatorP00326.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. SSF50129. 2 hits.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00326.
GeneWikiADH1C.
GenomeRNAi126.
NextBio503.
PROP00326.
SOURCESearch...

Entry information

Entry nameADH1G_HUMAN
AccessionPrimary (citable) accession number: P00326
Secondary accession number(s): Q4PJ18 expand/collapse secondary AC list , Q5WRV0, Q6LBW4, Q6NWV0, Q6NZA7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

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