Alcohol dehydrogenase 1C - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase 1C
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase subunit gamma

Gene names

Name:	ADH1C
Synonyms:	ADH3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Polymorphism	Two main alleles are known, ADH31 or gamma-1 has Arg-272/Ile-350 while ADH32 or gamma-2 has Gln-272/Val-350. ADH31 is associated with a fast rate of ethanol oxidation and ADH32 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.

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Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular alcohol metabolic process Non-traceable author statement. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Non-traceable author statement. Source: UniProtKB
Molecular function	alcohol dehydrogenase activity, zinc-dependent Ref.2 Ref.6 Non-traceable author statement. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed

Chain

2 – 375

374

Alcohol dehydrogenase 1C

PRO_0000160664

Sites

Metal binding

47

1

Zinc 1; catalytic

Metal binding

68

1

Zinc 1; catalytic

Metal binding

98

1

Zinc 2

Metal binding

101

1

Zinc 2

Metal binding

104

1

Zinc 2

Metal binding

112

1

Zinc 2

Metal binding

175

1

Zinc 1; catalytic

Amino acid modifications

Modified residue

2

1

N-acetylserine

Natural variations

Natural variant

48

1

R → H

VAR_023992

Natural variant

166

1

P → S

VAR_023993

Natural variant

272

1

R → Q in allele ADH3*2/gamma-2. dbSNP rs1693482.

VAR_000428

Natural variant

350

1

I → V in allele ADH3*2/gamma-2. dbSNP rs698.

VAR_000429

Natural variant

352

1

P → T

VAR_023994

Experimental info

Sequence conflict

130

1

Missing AA sequence Ref.6

Sequence conflict

171

1

C → R in AAH67421. Ref.5

Secondary structure

1

.

375

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P00326-1 [UniParc].

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

375

39,868

        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

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References

	« Hide 'large scale' referencesShow '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: 3758060] [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: 2935875] [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: 1524834] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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., Shaffer T., Bertucci C., Baier C.N., Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A. 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]	"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], VARIANTS GAMMA-2 GLN-272 AND VAL-350. Tissue: Brain and Femoral artery.
[6]	"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: 6391921] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-375. Tissue: Liver.
+	Additional computationally mapped references.