Reviewed, UniProtKB/Swiss-Prot P28474 (ADHX_MOUSE)

Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase class-3
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase class-III
    Alcohol dehydrogenase 5
    Alcohol dehydrogenase 2
    Alcohol dehydrogenase B2
      Short name=ADH-B2
    S-(hydroxymethyl)glutathione dehydrogenase
    EC=1.1.1.284
    Glutathione-dependent formaldehyde dehydrogenase
      Short name=GSH-FDH
      Short name=FALDH
      Short name=FDH
    EC=1.1.1.-

Gene names

Name:	Adh5
Synonyms:	Adh-2, Adh2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	374 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)

Function	Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione.
Catalytic activity	An alcohol + NAD+ = an aldehyde or ketone + NADH. S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Tissue specificity	Ubiquitous. Ref.7
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	ethanol oxidation Inferred from electronic annotation. Source: InterPro formaldehyde catabolic process Inferred from mutant phenotype. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-cysteine S-nitrosylation Inferred from mutant phenotype. Source: MGI positive regulation of blood pressure Inferred from mutant phenotype. Source: MGI respiratory system process Inferred from mutant phenotype. Source: MGI response to lipopolysaccharide Inferred from mutant phenotype. Source: MGI response to nitrosative stress Inferred from mutant phenotype. Source: MGI retinoid metabolic process Inferred from mutant phenotype. Source: MGI
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	S-(hydroxymethyl)glutathione dehydrogenase activity Inferred from mutant phenotype. Source: MGI alcohol dehydrogenase activity Inferred from direct assay. Source: MGI protein homodimerization activity Inferred from physical interaction. Source: MGI zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 374

373

Alcohol dehydrogenase class-3

PRO_0000160760

Sites

Metal binding

45

1

Zinc 1; catalytic By similarity

Metal binding

67

1

Zinc 1; catalytic By similarity

Metal binding

97

1

Zinc 2 By similarity

Metal binding

100

1

Zinc 2 By similarity

Metal binding

103

1

Zinc 2 By similarity

Metal binding

111

1

Zinc 2 By similarity

Metal binding

174

1

Zinc 1; catalytic By similarity

Site

115

1

Important for FDH activity and activation by fatty acids By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Experimental info

Sequence conflict

55

1

A → R Ref.1

Sequence conflict

55

1

A → R Ref.2

Sequence conflict

55

1

A → R Ref.3

Sequence conflict

133

1

K → R in BAE35383. Ref.4

Sequence conflict

183

1

A → T in BAE35383. Ref.4

Sequence conflict

253

1

V → I in BAE35383. Ref.4

Secondary structure

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374

Helix Strand Turn

Details...

Beta strand

5 – 12

8

Beta strand

20 – 26

7

Beta strand

33 – 43

11

Helix

45 – 52

8

Beta strand

60 – 62

3

Beta strand

68 – 75

8

Beta strand

87 – 90

4

Beta strand

97 – 99

3

Helix

100 – 103

4

Helix

114 – 118

5

Beta strand

128 – 131

4

Turn

140 – 142

3

Beta strand

146 – 152

7

Helix

153 – 155

3

Beta strand

156 – 158

3

Helix

165 – 168

4

Helix

169 – 172

4

Helix

174 – 183

10

Beta strand

193 – 197

5

Helix

201 – 213

13

Beta strand

216 – 221

6

Helix

225 – 227

3

Helix

228 – 234

7

Beta strand

237 – 240

4

Helix

242 – 244

3

Helix

249 – 257

9

Beta strand

261 – 266

6

Helix

271 – 280

10

Turn

283 – 285

3

Beta strand

287 – 290

4

Helix

305 – 308

4

Beta strand

312 – 315

4

Helix

318 – 320

3

Helix

323 – 335

13

Helix

342 – 344

3

Beta strand

347 – 351

5

Helix

354 – 363

10

Beta strand

369 – 372

4

Sequences

	Sequence		Length	Mass (Da)
	P28474-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 32A3727B5DAB0919	FASTA	374	39,548
	10 20 30 40 50 60 MANQVIRCKA AVAWEAGKPL SIEEIEVAPP KAHEVRIKIL ATAVCHTDAY TLSGADPEGC 70 80 90 100 110 120 FPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC KFCLNPKTNL CQKIRVTQGK 130 140 150 160 170 180 GLMPDGTSRF TCKGKSVFHF MGTSTFSEYT VVADISVAKI DPSAPLDKVC LLGCGISTGY 190 200 210 220 230 240 GAAVNTAKVE PGSTCAVFGL GGVGLAVIMG CKVAGASRII GIDINKDKFA KAKEFGASEC 250 260 270 280 290 300 ISPQDFSKSI QEVLVEMTDG GVDYSFECIG NVKVMRSALE AAHKGWGVSV VVGVAASGEE 310 320 330 340 350 360 ISTRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTGNL SFDQINQAFD 370 LMHSGDSIRT VLKM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Alcohol dehydrogenase gene expression and cloning of the mouse chi-like ADH." Edenberg H.J., Brown C.J., Carr L.G., Ho W.H., Hur M.W. Adv. Exp. Med. Biol. 284:253-262(1991) [PubMed: 2053480] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning of mouse alcohol dehydrogenase-B2 cDNA: nucleotide sequences of the class III ADH genes evolve slowly even for silent substitutions." Hur M.W., Ho W.H., Brown C.J., Goldman D., Edenberg H.J. DNA Seq. 3:167-175(1992) [PubMed: 1472709] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Characterization of the functional gene encoding mouse class III alcohol dehydrogenase (glutathione-dependent formaldehyde dehydrogenase) and an unexpressed processed pseudogene with an intact open reading frame." Foglio M.H., Duester G. Eur. J. Biochem. 237:496-504(1996) [PubMed: 8647091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/SvJ.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Head and Kidney.
[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]. Tissue: Kidney.
[6]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 234-248, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[7]	"Cloning of the mouse class IV alcohol dehydrogenase (retinol dehydrogenase) cDNA and tissue-specific expression patterns of the murine ADH gene family." Zgombic-Knight M., Ang H.L., Foglio M.H., Duester G. J. Biol. Chem. 270:10868-10877(1995) [PubMed: 7738026] [Abstract] Cited for: TISSUE SPECIFICITY. Strain: FVB/N.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M84147 mRNA. Translation: AAA68896.1.
U48970 , U48964, U48965, U48966, U48968, U48969 Genomic DNA. Translation: AAC52763.1.
AK076507 mRNA. Translation: BAC36370.1.
AK146949 mRNA. Translation: BAE27558.1.
AK159803 mRNA. Translation: BAE35383.1.
BC090978 mRNA. Translation: AAH90978.1.

IPI

IPI00555004.

PIR

A56643.

RefSeq

NP_031436.2.

UniGene

Mm.3874

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OTQ	model	-	A	1-374	[»]

SMR

P28474. Positions 2-374.

ModBase

Search...

PTM databases

PhosphoSite

P28474.

2-D gel databases

REPRODUCTION-2DPAGE

P28474.

Proteomic databases

PRIDE

P28474.

Genome annotation databases

Ensembl

ENSMUSG00000028138. Mus musculus. [Contig view]

GeneID

11532.

KEGG

mmu:11532.

Organism-specific databases

MGI

MGI:87929. Adh5.

Phylogenomic databases

HOGENOM

P28474.

HOVERGEN

P28474.

OMA

P28474. VALYTPE.

Enzyme and pathway databases

BRENDA

1.1.1.1. 244.
1.1.1.284. 244.

Gene expression databases

ArrayExpress

P28474.

Bgee

P28474.

GermOnline

ENSMUSG00000028138. Mus musculus.

Family and domain databases

InterPro

IPR014183. ADH_3.
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]

TIGRFAMs

TIGR02818. adh_III_F_hyde. 1 hit.

PROSITE

PS00059. ADH_ZINC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

278968.

SOURCE

Search...

Entry information

Entry name

ADHX_MOUSE

Accession

Primary (citable) accession number: P28474
Secondary accession number(s): Q3TW83, Q8C662

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)