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Protein

Alcohol dehydrogenase class-3

Gene

Adh5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

An alcohol + NAD+ = an aldehyde or ketone + NADH.
S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Zinc 1; catalyticBy similarity
Metal bindingi67 – 671Zinc 1; catalyticBy similarity
Metal bindingi97 – 971Zinc 2By similarity
Metal bindingi100 – 1001Zinc 2By similarity
Metal bindingi103 – 1031Zinc 2By similarity
Metal bindingi111 – 1111Zinc 2By similarity
Sitei115 – 1151Important for FDH activity and activation by fatty acidsBy similarity
Metal bindingi174 – 1741Zinc 1; catalyticBy similarity

GO - Molecular functioni

  • alcohol dehydrogenase (NAD) activity Source: MGI
  • fatty acid binding Source: MGI
  • formaldehyde dehydrogenase activity Source: MGI
  • protein homodimerization activity Source: MGI
  • S-(hydroxymethyl)glutathione dehydrogenase activity Source: MGI
  • zinc ion binding Source: MGI

GO - Biological processi

  • ethanol oxidation Source: InterPro
  • formaldehyde catabolic process Source: MGI
  • peptidyl-cysteine S-nitrosylation Source: MGI
  • positive regulation of blood pressure Source: MGI
  • respiratory system process Source: MGI
  • response to lipopolysaccharide Source: MGI
  • response to nitrosative stress Source: MGI
  • response to redox state Source: MGI
  • retinoid metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-71384. Ethanol oxidation.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase class-3 (EC:1.1.1.1)
Alternative name(s):
Alcohol dehydrogenase 2
Alcohol dehydrogenase 5
Alcohol dehydrogenase B2
Short name:
ADH-B2
Alcohol dehydrogenase class-III
Glutathione-dependent formaldehyde dehydrogenase (EC:1.1.1.-)
Short name:
FALDH
Short name:
FDH
Short name:
GSH-FDH
S-(hydroxymethyl)glutathione dehydrogenase (EC:1.1.1.284)
Gene namesi
Name:Adh5
Synonyms:Adh-2, Adh2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:87929. Adh5.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 374373Alcohol dehydrogenase class-3PRO_0000160760Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei233 – 2331N6-succinyllysineCombined sources
Modified residuei247 – 2471PhosphoserineCombined sources
Modified residuei315 – 3151N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP28474.
PaxDbiP28474.
PRIDEiP28474.

2D gel databases

REPRODUCTION-2DPAGEP28474.

PTM databases

iPTMnetiP28474.
PhosphoSiteiP28474.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiP28474.
ExpressionAtlasiP28474. baseline and differential.
GenevisibleiP28474. MM.

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

IntActiP28474. 2 interactions.
MINTiMINT-1869168.
STRINGi10090.ENSMUSP00000005964.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OTQmodel-A1-374[»]
ProteinModelPortaliP28474.
SMRiP28474. Positions 2-374.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0022. Eukaryota.
COG1062. LUCA.
HOGENOMiHOG000294674.
HOVERGENiHBG000195.
InParanoidiP28474.
KOiK00121.
OMAiANHEEVC.
OrthoDBiEOG72NRQ6.
PhylomeDBiP28474.
TreeFamiTF300429.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR014183. ADH_3.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 2 hits.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P28474-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANQVIRCKA AVAWEAGKPL SIEEIEVAPP KAHEVRIKIL ATAVCHTDAY
60 70 80 90 100
TLSGADPEGC FPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC
110 120 130 140 150
KFCLNPKTNL CQKIRVTQGK GLMPDGTSRF TCKGKSVFHF MGTSTFSEYT
160 170 180 190 200
VVADISVAKI DPSAPLDKVC LLGCGISTGY GAAVNTAKVE PGSTCAVFGL
210 220 230 240 250
GGVGLAVIMG CKVAGASRII GIDINKDKFA KAKEFGASEC ISPQDFSKSI
260 270 280 290 300
QEVLVEMTDG GVDYSFECIG NVKVMRSALE AAHKGWGVSV VVGVAASGEE
310 320 330 340 350
ISTRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTGNL
360 370
SFDQINQAFD LMHSGDSIRT VLKM
Length:374
Mass (Da):39,548
Last modified:January 23, 2007 - v3
Checksum:i32A3727B5DAB0919
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551A → R no nucleotide entry (PubMed:2053480).Curated
Sequence conflicti55 – 551A → R in AAA68896 (PubMed:1472709).Curated
Sequence conflicti55 – 551A → R in AAC52763 (PubMed:8647091).Curated
Sequence conflicti133 – 1331K → R in BAE35383 (PubMed:16141072).Curated
Sequence conflicti183 – 1831A → T in BAE35383 (PubMed:16141072).Curated
Sequence conflicti253 – 2531V → I in BAE35383 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS17868.1.
PIRiA56643.
RefSeqiNP_001275507.1. NM_001288578.1.
NP_031436.2. NM_007410.3.
UniGeneiMm.3874.

Genome annotation databases

EnsembliENSMUST00000005964; ENSMUSP00000005964; ENSMUSG00000028138.
GeneIDi11532.
KEGGimmu:11532.
UCSCiuc008rnk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS17868.1.
PIRiA56643.
RefSeqiNP_001275507.1. NM_001288578.1.
NP_031436.2. NM_007410.3.
UniGeneiMm.3874.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OTQmodel-A1-374[»]
ProteinModelPortaliP28474.
SMRiP28474. Positions 2-374.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP28474. 2 interactions.
MINTiMINT-1869168.
STRINGi10090.ENSMUSP00000005964.

PTM databases

iPTMnetiP28474.
PhosphoSiteiP28474.

2D gel databases

REPRODUCTION-2DPAGEP28474.

Proteomic databases

EPDiP28474.
PaxDbiP28474.
PRIDEiP28474.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005964; ENSMUSP00000005964; ENSMUSG00000028138.
GeneIDi11532.
KEGGimmu:11532.
UCSCiuc008rnk.2. mouse.

Organism-specific databases

CTDi128.
MGIiMGI:87929. Adh5.

Phylogenomic databases

eggNOGiKOG0022. Eukaryota.
COG1062. LUCA.
HOGENOMiHOG000294674.
HOVERGENiHBG000195.
InParanoidiP28474.
KOiK00121.
OMAiANHEEVC.
OrthoDBiEOG72NRQ6.
PhylomeDBiP28474.
TreeFamiTF300429.

Enzyme and pathway databases

ReactomeiR-MMU-71384. Ethanol oxidation.

Miscellaneous databases

PROiP28474.
SOURCEiSearch...

Gene expression databases

BgeeiP28474.
ExpressionAtlasiP28474. baseline and differential.
GenevisibleiP28474. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR014183. ADH_3.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 2 hits.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
    Strain: FVB/N.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-233 AND LYS-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiADHX_MOUSE
AccessioniPrimary (citable) accession number: P28474
Secondary accession number(s): Q3TW83, Q8C662
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 154 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.