P07327 (ADH1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alcohol dehydrogenase 1A
EC=1.1.1.1

Alternative name(s):
Alcohol dehydrogenase subunit alpha

Gene names

Name:	ADH1A
Synonyms:	ADH1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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

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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	drug metabolic process Traceable author statement. Source: Reactome ethanol oxidation Traceable author statement. Source: Reactome xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	alcohol dehydrogenase activity, zinc-dependent Inferred from direct assay PubMed 9982. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 375

374

Alcohol dehydrogenase 1A

PRO_0000160658

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

Secondary structure

1

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375

Helix Strand Turn

Details...

Beta strand

8 – 15

8

Beta strand

23 – 29

7

Beta strand

36 – 45

10

Helix

48 – 54

7

Beta strand

62 – 65

4

Beta strand

69 – 77

9

Beta strand

89 – 92

4

Beta strand

99 – 101

3

Helix

102 – 105

4

Beta strand

116 – 119

4

Beta strand

131 – 133

3

Beta strand

136 – 139

4

Turn

142 – 144

3

Beta strand

147 – 154

8

Helix

155 – 157

3

Beta strand

158 – 160

3

Helix

167 – 170

4

Helix

171 – 174

4

Helix

176 – 185

10

Turn

186 – 188

3

Beta strand

195 – 199

5

Helix

203 – 214

12

Beta strand

218 – 223

6

Helix

227 – 229

3

Helix

230 – 235

6

Beta strand

239 – 242

4

Helix

244 – 246

3

Helix

251 – 258

8

Turn

259 – 261

3

Beta strand

263 – 268

6

Helix

273 – 282

10

Turn

285 – 287

3

Beta strand

289 – 292

4

Beta strand

302 – 304

3

Helix

307 – 310

4

Beta strand

314 – 317

4

Helix

320 – 322

3

Helix

325 – 337

13

Helix

344 – 346

3

Beta strand

347 – 352

6

Helix

353 – 355

3

Helix

356 – 364

9

Beta strand

369 – 374

6

Sequences

	Sequence		Length	Mass (Da)
	P07327 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: B6DF4D57080D9BC1	FASTA	375	39,859
	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

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.
[6]	NIEHS SNPs program Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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]. Tissue: Brain.
[9]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
[10]	"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.
[11]	"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.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M12963 mRNA. Translation: AAA51590.1.
M12271 mRNA. Translation: AAA68131.1.
BT019812 mRNA. Translation: AAV38615.1.
AY948115 Genomic DNA. Translation: AAX20115.1.
AK290558 mRNA. Translation: BAF83247.1.
CH471057 Genomic DNA. Translation: EAX06094.1.
BC074738 mRNA. Translation: AAH74738.1.
BC117442 mRNA. Translation: AAI17443.1.
BC126306 mRNA. Translation: AAI26307.1.
M37066 Genomic DNA. Translation: AAA51591.1.

IPI

IPI00218896.

PIR

DEHUAA. S02265.

RefSeq

NP_000658.1. NM_000667.3.

UniGene

Hs.654433.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HSO	X-ray	2.50	A/B	2-375	[»]
1U3T	X-ray	2.49	A/B	2-375	[»]

ProteinModelPortal

P07327.

ModBase

Search...

Protein-protein interaction databases

IntAct

P07327. 2 interactions.

PTM databases

PhosphoSite

P07327.

Polymorphism databases

DMDM

113390.

Proteomic databases

PaxDb

P07327.

PRIDE

P07327.

Protocols and materials databases

DNASU

124.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000209668; ENSP00000209668; ENSG00000187758.

GeneID

124.

KEGG

hsa:124.

UCSC

uc003hur.2. human.

Organism-specific databases

CTD

124.

GeneCards

GC04M100197.

HGNC

HGNC:249. ADH1A.

HPA

CAB009562.
HPA047814.

MIM

103700. gene.

neXtProt

NX_P07327.

PharmGKB

PA24570.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1062.

HOGENOM

HOG000294674.

HOVERGEN

HBG000195.

InParanoid

P07327.

KO

K13951.

OMA

VSNPQGT.

OrthoDB

EOG4BRWM5.

PhylomeDB

P07327.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P07327.

Gene expression databases

Bgee

P07327.

CleanEx

HS_ADH1A.

Genevestigator

P07327.

GermOnline

ENSG00000187758. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR013149. 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]

PANTHER

PTHR11695. PTHR11695. 1 hit.

Pfam

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

SUPFAM

SSF50129. GroES_like. 2 hits.

PROSITE

PS00059. ADH_ZINC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P07327.

ChEMBL

CHEMBL1970.

DrugBank

DB01213. Fomepizole.
DB00157. NADH.

EvolutionaryTrace

P07327.

GenomeRNAi

124.

NextBio

495.

SOURCE

Search...

Entry information

Entry name

ADH1A_HUMAN

Accession

Primary (citable) accession number: P07327
Secondary accession number(s): A8K3E3, Q17R68

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 147 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.