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P00334 (ADH_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alcohol dehydrogenase

EC=1.1.1.1
Gene names
Name:Adh
ORF Names:CG3481
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Enzyme regulation

Inhibited by 2,2,2-trifluoroethanol and pyrazole.

Subunit structure

Homodimer.

Polymorphism

Virtually all natural populations of this species are polymorphic for 2 electrophoretically distinguishable alleles, Adh-S and Adh-F. The sequence of the Adh-S allele is shown. Other naturally occurring alleles include Adh-JA-F, Adh-AF-S, Adh-F-CHD, Adh-71K, Adh-UF and Adh-F'. Artificially induced mutations include Adh-NB, Adh-NLA248, Adh-N4 and Adh-N11.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.19 Ref.20
Chain2 – 256255Alcohol dehydrogenase
PRO_0000054474

Regions

Nucleotide binding12 – 4130NAD

Sites

Active site1531Proton acceptor
Binding site651NAD
Binding site1401Substrate
Binding site1571NAD

Amino acid modifications

Modified residue21N-acetylserine Ref.20

Natural variations

Natural variant91N → V in allele Adh-UF.
Natural variant461A → D in allele Adh-UF.
Natural variant461A → V in strain: NC16.
Natural variant521A → E in allele Adh-F'.
Natural variant711A → S in strain: NC16.
Natural variant1931K → T in allele Adh-F, allele Adh-F-CHD, allele Adh-71K, allele Adh-JA-F and in strain Berkeley.
Natural variant2151P → S in allele Adh-F-CHD and allele Adh-71K.

Experimental info

Mutagenesis151G → A: 31% decrease in activity.
Mutagenesis151G → D in Adh-N11; loss of activity.
Mutagenesis151G → V: Complete loss of activity.
Mutagenesis1301G → C: Complete loss of activity. Ref.28
Mutagenesis1331G → I: Complete loss of activity. Ref.28
Mutagenesis1361C → A: No decrease in activity.
Mutagenesis1531Y → C: Retains only 0.25% activity. Ref.26 Ref.27 Ref.28
Mutagenesis1531Y → F, H, E or Q: Complete loss of activity. Ref.26 Ref.27 Ref.28
Mutagenesis1571K → I: Complete loss of activity. Ref.27 Ref.28
Mutagenesis1571K → R: Retains only 2.2% activity. Ref.27 Ref.28
Mutagenesis1841G → L: Complete loss of activity. Ref.28
Mutagenesis2191C → A: No decrease in activity.

Secondary structure

.......................................... 256
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00334 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: EB4DF91029007284

FASTA25627,761
        10         20         30         40         50         60 
MSFTLTNKNV IFVAGLGGIG LDTSKELLKR DLKNLVILDR IENPAAIAEL KAINPKVTVT 

        70         80         90        100        110        120 
FYPYDVTVPI AETTKLLKTI FAQLKTVDVL INGAGILDDH QIERTIAVNY TGLVNTTTAI 

       130        140        150        160        170        180 
LDFWDKRKGG PGGIICNIGS VTGFNAIYQV PVYSGTKAAV VNFTSSLAKL APITGVTAYT 

       190        200        210        220        230        240 
VNPGITRTTL VHKFNSWLDV EPQVAEKLLA HPTQPSLACA ENFVKAIELN QNGAIWKLDL 

       250 
GTLEAIQWTK HWDSGI 

« Hide

References

« Hide 'large scale' references
[1]"Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein."
Benyajati C., Place A.R., Powers D.A., Sofer W.
Proc. Natl. Acad. Sci. U.S.A. 78:2717-2721(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-S).
[2]"In vitro suppression of a nonsense mutant of Drosophila melanogaster."
Kubli E., Schmidt T., Martin P.F., Sofer W.
Nucleic Acids Res. 10:7145-7152(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-NB).
[3]"Nucleotide polymorphism at the alcohol dehydrogenase locus of Drosophila melanogaster."
Kreitman M.
Nature 304:412-417(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES ADH-S AND ADH-F).
[4]"UGA nonsense mutation in the alcohol dehydrogenase gene of Drosophila melanogaster."
Martin P.F., Place A.R., Pentz E., Sofer W.
J. Mol. Biol. 184:221-229(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-NB).
[5]"Excess polymorphism at the Adh locus in Drosophila melanogaster."
Kreitman M.E., Aguade M.
Genetics 114:93-110(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES ADH-JA-F AND ADH-AF-S).
[6]"Adhn4 of Drosophila melanogaster is a nonsense mutation."
Chia W., Savakis C., Karp R., Ashburner M.
Nucleic Acids Res. 15:3931-3931(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-N4).
[7]"Recent origin for a thermostable alcohol dehydrogenase allele of Drosophila melanogaster."
Collet C.
J. Mol. Evol. 27:142-146(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-F-CHD).
Tissue: Embryo.
[8]"Analysis of the gene encoding the multifunctional alcohol dehydrogenase allozyme ADH-71k of Drosophila melanogaster."
Eisses K.T., Andriesse A.J., de Boer A.D., Thorig G.E.W., Weisbeek P.J.
Mol. Biol. Evol. 7:459-469(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-71K).
[9]"Inferring the evolutionary histories of the Adh and Adh-dup loci in Drosophila melanogaster from patterns of polymorphism and divergence."
Kreitman M., Hudson R.R.
Genetics 127:565-582(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-S).
[10]"Associations between DNA sequence variation and variation in expression of the Adh gene in natural populations of Drosophila melanogaster."
Laurie C.C., Bridgham J.T., Choudhary M.
Genetics 129:489-499(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ADH-F).
Strain: KA12, NC-016 and RI32.
[11]"Effects of a transposable element insertion on alcohol dehydrogenase expression in Drosophila melanogaster."
Dunn R.C., Laurie C.C.
Genetics 140:667-677(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[12]Brogna S., Ashburner M.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE ADH-S).
Strain: Canton-S.
[13]"Is the fast/slow allozyme variation at the Adh locus of Drosophila melanogaster an ancient balanced polymorphism?"
Begun D., Betancourt A., Langley C., Stephan W.
Mol. Biol. Evol. 16:1816-1819(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES ADH-H3; ADH-H12; ADH-H13; ADH-H18; ADH-H21; ADH-K15; ADH-K30; ADH-K35; ADH-K37 AND ADH-K82).
Strain: Zimbabwe.
[14]"An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region."
Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R. expand/collapse author list , Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.
Genetics 153:179-219(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[15]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[16]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[17]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE ADH-S).
Strain: Berkeley.
Tissue: Head.
[18]Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE ADH-S).
Strain: Berkeley.
Tissue: Head.
[19]"Chemical basis of the electrophoretic variation observed at the alcohol dehydrogenase locus of Drosophila melanogaster."
Retzios A.D., Thatcher D.R.
Biochimie 61:701-704(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-256 (ALLELE ADH-F').
[20]"The complete amino acid sequence of three alcohol dehydrogenase alleloenzymes (AdhN-11, AdhS and AdhUF) from the fruitfly Drosophila melanogaster."
Thatcher D.R.
Biochem. J. 187:875-883(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-256 (ALLELES ADH-F; ADH-S; ADH-UF AND ADH-N11), ACETYLATION AT SER-2.
[21]Erratum
Thatcher D.R.
Biochem. J. 191:895-895(1980)
[22]"Mutation of the Adh gene of Drosophila melanogaster containing an internal tandem duplication."
Chia W., Savakis C., Karp R., Pelham H., Ashburner M.
J. Mol. Biol. 186:679-688(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-256 (ALLELE ADH-NLA248).
[23]"Alcohol dehydrogenase in Drosophila: isolation and characterization of messenger RNA and cDNA clone."
Benyajati C., Wang N., Reddy A., Weinberg E., Sofer W.
Nucleic Acids Res. 8:5649-5667(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 141-256 (ALLELE ADH-F).
[24]"Structural analysis of an electrophoretically cryptic alcohol dehydrogenase variant from an Australian population of Drosophila melanogaster."
Chambers G.K., Laver W.G., Campbell S., Gibson J.B.
Proc. Natl. Acad. Sci. U.S.A. 78:3103-3107(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 208-225 (ALLELE ADH-F-CHD).
[25]"Site-directed mutagenesis of glycine-14 and two 'critical' cysteinyl residues in Drosophila alcohol dehydrogenase."
Chen Z., Lu L., Shirley M., Lee W.R., Chang S.H.
Biochemistry 29:1112-1118(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[26]"Protein engineering of Drosophila alcohol dehydrogenase. The hydroxyl group of Tyr152 is involved in the active site of the enzyme."
Albalat R., Gonzalez-Duarte R., Atrian S.
FEBS Lett. 308:235-239(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-153.
[27]"Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for involvement of tyrosine-152 and lysine-156 in catalysis."
Chen Z., Jiang J.C., Lin Z.-G., Lee W.R., Baker M.E., Chang S.H.
Biochemistry 32:3342-3346(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-153 AND LYS-157.
[28]"Effect of site-directed mutagenesis on conserved positions of Drosophila alcohol dehydrogenase."
Cols N., Marfany G., Atrian S., Gonzalez-Duarte R.
FEBS Lett. 319:90-94(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-130; GLY-133; TYR-153; LYS-157 AND GLY-184.
[29]"Drosophila alcohol dehydrogenase: acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis."
Benach J., Winberg J.-O., Svendsen J.-S., Atrian S., Gonzalez-Duarte R., Ladenstein R.
J. Mol. Biol. 345:579-598(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17827 Genomic DNA. Translation: AAA28341.1.
M17828 Genomic DNA. Translation: AAA28342.1.
M19547 Genomic DNA. Translation: AAA70210.1.
M17830 Genomic DNA. Translation: AAA28343.1.
M17831 Genomic DNA. Translation: AAA28344.1.
M17832 Genomic DNA. Translation: AAA28345.1.
M17833 Genomic DNA. Translation: AAA28346.1.
M17834 Genomic DNA. Translation: AAA28347.1.
M17835 Genomic DNA. Translation: AAA28348.1.
M17836 Genomic DNA. Translation: AAA28349.1.
M17837 Genomic DNA. Translation: AAA70212.1.
Z00030 Genomic DNA. Translation: CAA77330.1.
M22210 Genomic DNA. Translation: AAA28338.1.
M57239 Genomic DNA. Translation: AAA28330.1.
X78384 Genomic DNA. Translation: CAA55151.1.
M36580 Genomic DNA. Translation: AAA28331.1.
X60791 Genomic DNA. Translation: CAA43204.1.
X60792 Genomic DNA. Translation: CAA43205.1.
X60793 Genomic DNA. Translation: CAA43206.1.
U20765 Genomic DNA. Translation: AAA88817.1.
X98338 mRNA. Translation: CAA66981.1.
AF175211 Genomic DNA. Translation: AAF00229.1.
AF175212 Genomic DNA. Translation: AAF00230.1.
AF175213 Genomic DNA. Translation: AAF00231.1.
AF175214 Genomic DNA. Translation: AAF00232.1.
AF175215 Genomic DNA. Translation: AAF00233.1.
AF175216 Genomic DNA. Translation: AAF00234.1.
AF175217 Genomic DNA. Translation: AAF00235.1.
AF175218 Genomic DNA. Translation: AAF00236.1.
AF175219 Genomic DNA. Translation: AAF00237.1.
AF175220 Genomic DNA. Translation: AAF00238.1.
AE014134 Genomic DNA. Translation: AAO41197.1.
AE014134 Genomic DNA. Translation: AAO41199.1.
AE014134 Genomic DNA. Translation: AAO41200.1.
AE014134 Genomic DNA. Translation: AAO41201.1.
AY060227 mRNA. Translation: AAL25266.1.
BT012435 mRNA. Translation: AAS93706.1.
M17845 Genomic DNA. Translation: AAA28363.1.
PIRDEFFA. A93309.
RefSeqNP_001027266.1. NM_001032095.1.
NP_001027267.1. NM_001032096.1.
NP_001027268.1. NM_001032097.1.
NP_001027269.1. NM_001032098.1.
NP_001027270.1. NM_001032099.1.
UniGeneDm.6818.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MG5X-ray1.63A/B2-256[»]
ProteinModelPortalP00334.
SMRP00334. Positions 2-256.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid533474. 58 interactions.
IntActP00334. 1 interaction.
MINTMINT-877153.

Proteomic databases

PaxDbP00334.
PRIDEP00334.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3771877.
KEGGdme:Dmel_CG3481.

Organism-specific databases

CTD3771877.
FlyBaseFBgn0000055. Adh.

Phylogenomic databases

eggNOGCOG1028.
InParanoidP00334.
KOK00001.
OrthoDBEOG7966HT.
PhylomeDBP00334.

Enzyme and pathway databases

SABIO-RKP00334.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002425. ADH_Drosophila-type.
IPR002424. ADH_insect.
IPR002198. DH_sc/Rdtase_SDR.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR01168. ALCDHDRGNASE.
PR01167. INSADHFAMILY.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00334.
GenomeRNAi3771877.
NextBio851589.

Entry information

Entry nameADH_DROME
AccessionPrimary (citable) accession number: P00334
Secondary accession number(s): A4V0Q1 expand/collapse secondary AC list , Q27332, Q27579, Q27596, Q2MGK2, Q53XD5, Q95TC8, Q9NKC0, Q9VJS3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase