P40394 (ADH7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alcohol dehydrogenase class 4 mu/sigma chain
EC=1.1.1.1

Alternative name(s):
Alcohol dehydrogenase class IV mu/sigma chain
Gastric alcohol dehydrogenase
Retinol dehydrogenase

Gene names

Name:

ADH7

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	386 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Could function in retinol oxidation for the synthesis of retinoic acid, a hormone important for cellular differentiation. Medium-chain (octanol) and aromatic (m-nitrobenzaldehyde) compounds are the best substrates. Ethanol is not a good substrate but at the high ethanol concentrations reached in the digestive tract, it plays a role in the ethanol oxidation and contributes to the first pass ethanol metabolism.
Catalytic activity	An alcohol + NAD+ = an aldehyde or ketone + NADH.
Cofactor	Binds 2 zinc ions per subunit.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Tissue specificity	Preferentially expressed in stomach.
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. Class-IV subfamily.
Caution	It is uncertain whether Met-1 or Met-13 is the initiator.
Sequence caution	The sequence AAA19002.1 differs from that shown. Reason: Erroneous initiation. The sequence AAC51351.1 differs from that shown. Reason: Erroneous initiation. The sequence BAG35707.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA53960.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA53961.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ethanol catabolic process Inferred from electronic annotation. Source: Compara ethanol oxidation Inferred from direct assay PubMed 10969996Ref.9. Source: UniProtKB fatty acid omega-oxidation Inferred from direct assay PubMed 9600267. Source: UniProtKB response to bacterium Inferred from direct assay PubMed 11410738. Source: UniProtKB response to ethanol Inferred from direct assay PubMed 9600267. Source: UniProtKB retinoic acid metabolic process Inferred from electronic annotation. Source: Compara retinoid metabolic process Inferred from direct assay PubMed 9600267. Source: UniProtKB retinol metabolic process Inferred from electronic annotation. Source: Compara xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome extracellular region Inferred from direct assay PubMed 9600267. Source: GOC nucleolus Inferred from direct assay. Source: HPA
Molecular_function	alcohol dehydrogenase activity, zinc-dependent Inferred from direct assay Ref.9. Source: UniProtKB aldehyde oxidase activity Inferred from direct assay PubMed 9600267. Source: UniProtKB ethanol binding Inferred from direct assay Ref.13. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro receptor antagonist activity Inferred from direct assay PubMed 9600267. Source: UniProtKB retinol binding Inferred from direct assay Ref.13. Source: UniProtKB retinol dehydrogenase activity Inferred from direct assay PubMed 11997393Ref.9. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P40394-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P40394-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MFAEIQIQDKDRMGTAGK → MKCLVSRHTVRETLDMVFQRMSVEAG

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 386

386

Alcohol dehydrogenase class 4 mu/sigma chain

PRO_0000160691

Regions

Nucleotide binding

211 – 216

6

NAD

Nucleotide binding

304 – 306

3

NAD

Sites

Metal binding

59

1

Zinc 1; catalytic

Metal binding

80

1

Zinc 1; catalytic

Metal binding

110

1

Zinc 2

Metal binding

113

1

Zinc 2

Metal binding

116

1

Zinc 2

Metal binding

124

1

Zinc 2

Metal binding

186

1

Zinc 1; catalytic

Binding site

235

1

NAD

Binding site

240

1

NAD

Binding site

381

1

NAD

Natural variations

Alternative sequence

1 – 18

18

MFAEI…GTAGK → MKCLVSRHTVRETLDMVFQR MSVEAG in isoform 2.

VSP_043093

Natural variant

92

1

G → A.
Corresponds to variant rs1573496 [ dbSNP | Ensembl ].

VAR_024364

Experimental info

Sequence conflict

9

1

D → E in AAA19002. Ref.2

Sequence conflict

32

1

Q → R AA sequence Ref.11

Sequence conflict

83

1

T → R AA sequence Ref.11

Sequence conflict

110

1

C → V in AAB38424. Ref.10

Sequence conflict

150 – 151

2

HH → GR AA sequence Ref.11

Sequence conflict

160 – 161

2

EY → VI in AAB38424. Ref.10

Sequence conflict

169

1

V → E in AAB38424. Ref.10

Sequence conflict

175

1

A → T in BAG35707. Ref.4

Sequence conflict

217

1

L → V in AAB38424. Ref.10

Secondary structure

1

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386

Helix Strand Turn

Details...

Beta strand

20 – 29

10

Beta strand

35 – 41

7

Beta strand

48 – 57

10

Helix

60 – 67

8

Beta strand

68 – 70

3

Beta strand

74 – 76

3

Beta strand

81 – 89

9

Beta strand

101 – 104

4

Beta strand

111 – 113

3

Helix

114 – 117

4

Beta strand

142 – 150

9

Turn

153 – 155

3

Beta strand

158 – 165

8

Helix

166 – 168

3

Beta strand

169 – 171

3

Helix

178 – 181

4

Helix

182 – 185

4

Helix

187 – 196

10

Beta strand

206 – 210

5

Helix

214 – 225

12

Beta strand

229 – 234

6

Helix

238 – 240

3

Helix

241 – 247

7

Beta strand

250 – 253

4

Helix

255 – 257

3

Helix

262 – 270

9

Beta strand

276 – 279

4

Helix

284 – 291

8

Turn

296 – 298

3

Beta strand

300 – 303

4

Beta strand

313 – 315

3

Helix

318 – 321

4

Beta strand

325 – 328

4

Helix

331 – 333

3

Helix

336 – 347

12

Turn

348 – 350

3

Helix

355 – 357

3

Beta strand

358 – 363

6

Helix

364 – 366

3

Helix

367 – 375

9

Beta strand

380 – 385

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 23, 2010. Version 2. Checksum: E34C959778ED6817	FASTA	386	41,481
	10 20 30 40 50 60 MFAEIQIQDK DRMGTAGKVI KCKAAVLWEQ KQPFSIEEIE VAPPKTKEVR IKILATGICR 70 80 90 100 110 120 TDDHVIKGTM VSKFPVIVGH EATGIVESIG EGVTTVKPGD KVIPLFLPQC RECNACRNPD 130 140 150 160 170 180 GNLCIRSDIT GRGVLADGTT RFTCKGKPVH HFMNTSTFTE YTVVDESSVA KIDDAAPPEK 190 200 210 220 230 240 VCLIGCGFST GYGAAVKTGK VKPGSTCVVF GLGGVGLSVI MGCKSAGASR IIGIDLNKDK 250 260 270 280 290 300 FEKAMAVGAT ECISPKDSTK PISEVLSEMT GNNVGYTFEV IGHLETMIDA LASCHMNYGT 310 320 330 340 350 360 SVVVGVPPSA KMLTYDPMLL FTGRTWKGCV FGGLKSRDDV PKLVTEFLAK KFDLDQLITH 370 380 VLPFKKISEG FELLNSGQSI RTVLTF
	Isoform 2 [UniParc]. Checksum: 2EBC96FC412B6729	FASTA	394	42,467
	10 20 30 40 50 60 MKCLVSRHTV RETLDMVFQR MSVEAGVIKC KAAVLWEQKQ PFSIEEIEVA PPKTKEVRIK 70 80 90 100 110 120 ILATGICRTD DHVIKGTMVS KFPVIVGHEA TGIVESIGEG VTTVKPGDKV IPLFLPQCRE 130 140 150 160 170 180 CNACRNPDGN LCIRSDITGR GVLADGTTRF TCKGKPVHHF MNTSTFTEYT VVDESSVAKI 190 200 210 220 230 240 DDAAPPEKVC LIGCGFSTGY GAAVKTGKVK PGSTCVVFGL GGVGLSVIMG CKSAGASRII 250 260 270 280 290 300 GIDLNKDKFE KAMAVGATEC ISPKDSTKPI SEVLSEMTGN NVGYTFEVIG HLETMIDALA 310 320 330 340 350 360 SCHMNYGTSV VVGVPPSAKM LTYDPMLLFT GRTWKGCVFG GLKSRDDVPK LVTEFLAKKF 370 380 390 DLDQLITHVL PFKKISEGFE LLNSGQSIRT VLTF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Alcohol dehydrogenase of class IV (sigma sigma-ADH) from human stomach. cDNA sequence and structure/function relationships." Farres J., Moreno A., Crosas B., Peralba J.M., Allali-Hassani A., Hjelmqvist L., Joernvall H., Pares X. Eur. J. Biochem. 224:549-557(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Stomach.
[2]	"The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene." Satre M.A., Zgombic-Knight M., Duester G. J. Biol. Chem. 269:15606-15612(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Stomach.
[3]	"Genomic structure and expression of the ADH7 gene encoding human class IV alcohol dehydrogenase, the form most efficient for retinol metabolism in vitro." Zgombic-Knight M., Foglio M.H., Duester G. J. Biol. Chem. 270:4305-4311(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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] (ISOFORMS 1 AND 2). Tissue: Esophagus and Trachea.
[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. , 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]	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].
[7]	"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] (ISOFORM 1).
[8]	"Molecular characterization of a class IV human alcohol dehydrogenase gene (ADH7)." Yokoyama S., Matsuo Y., Ramsbotham R., Yokoyama R. FEBS Lett. 351:411-415(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-386 (ISOFORM 1), ZINC-BINDING SITES. Tissue: Stomach.
[9]	"Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase. Active-site amino acid sequence explains substrate specificity compared with liver isozymes." Kedishvili N.Y., Bosron W.F., Stone C.L., Hurley T.D., Peggs C.F., Thomasson H.R., Popov K.M., Carr L.G., Edenberg H.J., Li T.K. J. Biol. Chem. 270:3625-3630(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-386 (ISOFORM 1). Tissue: Stomach.
[10]	"Molecular cloning and chromosomal localization of the ADH7 gene encoding human class IV (sigma) ADH." Yokoyama H., Baraona E., Lieber C.S. Genomics 31:243-245(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-386. Tissue: Foreskin.
[11]	"Class IV alcohol dehydrogenase (the gastric enzyme). Structural analysis of human sigma sigma-ADH reveals class IV to be variable and confirms the presence of a fifth mammalian alcohol dehydrogenase class." Pares X., Cederlund E., Moreno A., Saubi N., Hoeoeg J.-O., Joernvall H. FEBS Lett. 303:69-72(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-33; 53-58; 74-92; 97-123; 147-154 AND 181-186.
[12]	"Human stomach class IV alcohol dehydrogenase: molecular genetic analysis." Cheung B., Anderson J.K., Holmes R.S., Beacham I.R. Alcohol. Clin. Exp. Res. 19:185-186(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 239-311 (ISOFORM 1). Tissue: Stomach.
[13]	"X-ray structure of human class IV sigmasigma alcohol dehydrogenase. Structural basis for substrate specificity." Xie P., Parsons S.H., Speckhard D.C., Bosron W.F., Hurley T.D. J. Biol. Chem. 272:18558-18563(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 14-386.
[14]	"Methionine-141 directly influences the binding of 4-methylpyrazole in human sigma sigma alcohol dehydrogenase." Xie P.T., Hurley T.D. Protein Sci. 8:2639-2644(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 14-386 IN COMPLEX WITH NAD AND ZINC IONS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X76342 mRNA. Translation: CAA53961.1. Different initiation.
X76342 mRNA. Translation: CAA53960.1. Different initiation.
U07821 mRNA. Translation: AAA19002.1. Different initiation.
U16293 , U16286, U16287, U16288, U16289, U16290, U16291, U16292 Genomic DNA. Translation: AAC51351.1. Different initiation.
AK301696 mRNA. Translation: BAG63168.1.
AK312854 mRNA. Translation: BAG35707.1. Different initiation.
AP001960 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX06101.1.
BC131512 mRNA. Translation: AAI31513.1.
L33179 mRNA. Translation: AAA59211.1.
U09623 mRNA. Translation: AAA82165.1.
L47166 Genomic DNA. Translation: AAB38424.1.
S77168 mRNA. Translation: AAB34478.1.

IPI

IPI00872487.
IPI00908386.

PIR

DEHUAS. A55878.

RefSeq

NP_000664.2. NM_000673.4.
NP_001159976.1. NM_001166504.1.

UniGene

Hs.389.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AGN	X-ray	3.00	A/B/C/D	14-386	[»]
1D1S	X-ray	2.50	A/B/C/D	14-386	[»]
1D1T	X-ray	2.40	A/B/C/D	14-386	[»]

ProteinModelPortal

P40394.

SMR

P40394. Positions 14-386.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000209665.

PTM databases

PhosphoSite

P40394.

Polymorphism databases

DMDM

292495000.

Proteomic databases

PaxDb

P40394.

PRIDE

P40394.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000209665; ENSP00000209665; ENSG00000196344.
ENST00000437033; ENSP00000414254; ENSG00000196344.
ENST00000476959; ENSP00000420269; ENSG00000196344.

GeneID

131.

KEGG

hsa:131.

UCSC

uc003huv.2. human.

Organism-specific databases

CTD

131.

GeneCards

GC04M100333.

HGNC

HGNC:256. ADH7.

HPA

HPA039695.

MIM

600086. gene.

neXtProt

NX_P40394.

PharmGKB

PA24577.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1062.

HOGENOM

HOG000294674.

HOVERGEN

HBG000195.

KO

K13951.

OMA

QEGFELL.

OrthoDB

EOG4BRWM5.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P40394.

Bgee

P40394.

CleanEx

HS_ADH7.

Genevestigator

P40394.

GermOnline

ENSG00000196344. 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

P40394.

ChEMBL

CHEMBL3867.

DrugBank

DB00157. NADH.

EvolutionaryTrace

P40394.

GenomeRNAi

131.

NextBio

523.

SOURCE

Search...

Entry information

Entry name

ADH7_HUMAN

Accession

Primary (citable) accession number: P40394
Secondary accession number(s): A2RRB6 , A8MVN9, B2R760, B4DWV6, Q13713

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	March 23, 2010
Last modified:	April 3, 2013
This is version 129 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.