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UniProtKB/Swiss-Prot entry P28474


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ADHX_MOUSE
Primary accession number P28474
Secondary accession numbers Q3TW83 Q8C662
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 83)
Name and origin of the protein
Protein name Alcohol dehydrogenase class-3
Synonyms EC 1.1.1.1
Alcohol dehydrogenase class-III
Alcohol dehydrogenase 5
Alcohol dehydrogenase 2
Alcohol dehydrogenase B2
ADH-B2
S-(hydroxymethyl)glutathione dehydrogenase
EC 1.1.1.284
Glutathione-dependent formaldehyde dehydrogenase
GSH-FDH
FALDH
FDH
EC 1.1.1.-
Gene name
Name: Adh5
Synonyms: Adh-2, Adh2
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2053480 [NCBI, ExPASy, EBI, Israel, Japan]
Edenberg H.J., Brown C.J., Carr L.G., Ho W.H., Hur M.W.;
"Alcohol dehydrogenase gene expression and cloning of the mouse chi-like ADH.";
Adv. Exp. Med. Biol. 284:253-262(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1472709 [NCBI, ExPASy, EBI, Israel, Japan]
Hur M.W., Ho W.H., Brown C.J., Goldman D., Edenberg H.J.;
"Molecular cloning of mouse alcohol dehydrogenase-B2 cDNA: nucleotide sequences of the class III ADH genes evolve slowly even for silent substitutions.";
DNA Seq. 3:167-175(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ;
DOI=10.1111/j.1432-1033.1996.0496k.x; PubMed=8647091 [NCBI, ExPASy, EBI, Israel, Japan]
Foglio M.H., Duester G.;
"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.";
Eur. J. Biochem. 237:496-504(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Head, and Kidney;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
TISSUE SPECIFICITY.
STRAIN=FVB/N;
DOI=10.1074/jbc.270.18.10868; PubMed=7738026 [NCBI, ExPASy, EBI, Israel, Japan]
Zgombic-Knight M., Ang H.L., Foglio M.H., Duester G.;
"Cloning of the mouse class IV alcohol dehydrogenase (retinol dehydrogenase) cDNA and tissue-specific expression patterns of the murine ADH gene family.";
J. Biol. Chem. 270:10868-10877(1995).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M84147; AAA68896.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U48970; AAC52763.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U48964; AAC52763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U48965; AAC52763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U48966; AAC52763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U48968; AAC52763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U48969; AAC52763.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK076507; BAC36370.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK146949; BAE27558.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK159803; BAE35383.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC090978; AAH90978.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A56643; A56643.
RefSeq NP_031436.2; -.
UniGene Mm.3874
3D structure databases
PDB
1OTQ; Model; -; A=1-374.[ExPASy / RCSB / EBI]
PDBsum 1OTQ; -.
SMR P28474; 2-374.
ModBase P28474.
PTM databases
PhosphoSite P28474; -.
2D gel databases
REPRODUCTION-2DPAGE P28474; -.
Organism-specific databases
MGI MGI:87929; Adh5.
Gene expression databases
ArrayExpress P28474; -.
GermOnline ENSMUSG00000028138; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from MGI).
GO:0004022; Molecular function: alcohol dehydrogenase activity (inferred from direct assay from MGI).
GO:0042803; Molecular function: protein homodimerization activity (inferred from physical interaction from MGI).
GO:0051903; Molecular function: S-(hydroxymethyl)glutathione dehydrogenase activity (inferred from mutant phenotype from MGI).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0046294; Biological process: formaldehyde catabolic process (inferred from mutant phenotype from MGI).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
GO:0018119; Biological process: peptidyl-cysteine S-nitrosylation (inferred from mutant phenotype from MGI).
GO:0045777; Biological process: positive regulation of blood pressure (inferred from mutant phenotype from MGI).
GO:0003016; Biological process: respiratory system process (inferred from mutant phenotype from MGI).
GO:0032496; Biological process: response to lipopolysaccharide (inferred from mutant phenotype from MGI).
GO:0051409; Biological process: response to nitrosative stress (inferred from mutant phenotype from MGI).
GO:0001523; Biological process: retinoid metabolic process (inferred from mutant phenotype from MGI).
QuickGo view.
Family and domain databases
InterPro IPR014183; AlcDHase_3.
IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR02818; adh_III_F_hyde; 1.
PROSITE PS00059; ADH_ZINC; 1.
BLOCKS P28474.
ProtoNet P28474.
Genome annotation databases
Ensembl ENSMUSG00000028138; Mus musculus. [Contig view]
GeneID 11532; -.
KEGG mmu:11532; -.
Phylogenomic databases
HOGENOM P28474; -.
HOVERGEN P28474; -.
Other
NextBio 278968; -.
SOURCE Adh5; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   374  373     Alcohol dehydrogenase class-3. PRO_0000160760
METAL   45    45        Zinc 1; catalytic (By similarity). 
METAL   67    67        Zinc 1; catalytic (By similarity). 
METAL   97    97        Zinc 2 (By similarity). 
METAL   100   100        Zinc 2 (By similarity). 
METAL   103   103        Zinc 2 (By similarity). 
METAL   111   111        Zinc 2 (By similarity). 
METAL   174   174        Zinc 1; catalytic (By similarity). 
SITE   115   115  1     Important for FDH activity and activation by fatty acids (By similarity). 
MOD_RES   2     2        N-acetylalanine (By similarity). 
CONFLICT   55    55        A -> R (in Ref. 1, 2 and 3). 
CONFLICT   133   133        K -> R (in Ref. 4; BAE35383). 
CONFLICT   183   183        A -> T (in Ref. 4; BAE35383). 
CONFLICT   253   253        V -> I (in Ref. 4; BAE35383). 
STRAND   5    12  8      
STRAND   20    26  7      
STRAND   33    43  11      
HELIX   45    52  8      
STRAND   60    62  3      
STRAND   68    75  8      
STRAND   87    90  4      
STRAND   97    99  3      
HELIX   100   103  4      
HELIX   114   118  5      
STRAND   128   131  4      
TURN   140   142  3      
STRAND   146   152  7      
HELIX   153   155  3      
STRAND   156   158  3      
HELIX   165   168  4      
HELIX   169   172  4      
HELIX   174   183  10      
STRAND   193   197  5      
HELIX   201   213  13      
STRAND   216   221  6      
HELIX   225   227  3      
HELIX   228   234  7      
STRAND   237   240  4      
HELIX   242   244  3      
HELIX   249   257  9      
STRAND   261   266  6      
HELIX   271   280  10      
TURN   283   285  3      
STRAND   287   290  4      
HELIX   305   308  4      
STRAND   312   315  4      
HELIX   318   320  3      
HELIX   323   335  13      
HELIX   342   344  3      
STRAND   347   351  5      
HELIX   354   363  10      
STRAND   369   372  4      
Sequence information
Length: 374 AA [This is the length of the unprocessed precursor] Molecular weight: 39548 Da [This is the MW of the unprocessed precursor] CRC64: 32A3727B5DAB0919 [This is a checksum on the sequence]
        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 

P28474 in FASTA format

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