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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alcohol dehydrogenase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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 Ref.7

Chain

2 – 375

374

Alcohol dehydrogenase 1C

PRO_0000160664

Regions

Nucleotide binding

200 – 205

6

NAD

Nucleotide binding

293 – 295

3

NAD

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

Binding site

224

1

NAD

Binding site

229

1

NAD

Binding site

370

1

NAD

Amino acid modifications

Modified residue

2

1

N-acetylserine

Natural variations

Natural variant

48

1

R → H: dbSNP rs35385902. Ref.4

VAR_023992

Natural variant

166

1

P → S Ref.4

VAR_023993

Natural variant

272

1

R → Q in allele ADH3*2/gamma-2. dbSNP rs1693482. Ref.4 Ref.1 Ref.6

VAR_000428

Natural variant

350

1

I → V in allele ADH3*2/gamma-2. dbSNP rs698. Ref.4 Ref.1 Ref.6

VAR_000429

Natural variant

352

1

P → T: dbSNP rs35719513. Ref.4

VAR_023994

Experimental info

Sequence conflict

130

1

Missing AA sequence Ref.7

Sequence conflict

171

1

C → R in AAH67421. Ref.6

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 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. Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [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: 15489334] [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: 6391921] [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: 11274460] [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: 15449945] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.49 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

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.

IPI

IPI00465343.

PIR

DEHUAG. C25428.

RefSeq

NP_000660.1.

UniGene

Hs.654537

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DDA	model	-	A/B	1-375	[»]
1HT0	X-ray	2.00	A/B	2-375	[»]
1U3W	X-ray	1.45	A/B	2-375	[»]

ModBase

Search...

PTM databases

PhosphoSite

P00326.

Proteomic databases

PRIDE

P00326.

Genome annotation databases

Ensembl

ENSG00000196616. Homo sapiens. [Contig view]

GeneID

126.

KEGG

hsa:126.

Organism-specific databases

GeneCards

GC04M100457.

H-InvDB

HIX0031470.

HGNC

HGNC:251. ADH1C.

MIM

103730. gene.

PharmGKB

PA24572.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P00326.

Enzyme and pathway databases

BRENDA

1.1.1.1. 247.

Reactome

REACT_13433. Biological oxidations.

Gene expression databases

ArrayExpress

P00326.

Bgee

P00326.

CleanEx

HS_ADH1C.

GermOnline

ENSG00000196616. Homo sapiens.

Family and domain databases

InterPro

IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_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]

ProtoNet

Search...

Other Resources

DrugBank

DB01213. Fomepizole.
DB00157. NADH.

NextBio

503.

SOURCE

Search...

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Entry information

Entry name

ADH1G_HUMAN

Accession

Primary (citable) accession number: P00326
Secondary accession number(s): Q4PJ18

Q6NZA7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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