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P91615 (ADHR_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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-related 31 kDa protein
Gene names
Name:Adhr
Synonyms:Adh-dup
ORF Names:CG3484
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length272 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Sequence similarities

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

Ontologies

Keywords
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular functionalcohol dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: InterPro

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 272272Alcohol dehydrogenase-related 31 kDa protein
PRO_0000054509

Regions

Nucleotide binding11 – 3424NAD or NADP By similarity

Sites

Active site1521Proton acceptor By similarity
Binding site1391Substrate By similarity

Experimental info

Sequence conflict1271M → I in CAA55152. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P91615 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 6FD2B13EEE2FAEA6

FASTA27230,274
        10         20         30         40         50         60 
MFDLTGKHVC YVADCGGIAL ETSKVLMTKN IAKLAILQST ENPQAIAQLQ SIKPSTQIFF 

        70         80         90        100        110        120 
WTYDVTMARE DMKKYFDEVM VQMDYIDVLI NGATLCDENN IDATINTNLT GMMNTVATVL 

       130        140        150        160        170        180 
PYMDRKMGGT GGLIVNVTSV IGLDPSPVFC AYSASKFGVI GFTRSLADPL YYSQNGVAVM 

       190        200        210        220        230        240 
AVCCGPTRVF VDRELKAFLE YGQSFADRLR RAPCQSTSVC GQNIVNAIER SENGQIWIAD 

       250        260        270 
KGGLELVKLH WYWHMADQFV HYMQSNDEED QD

« Hide

References

« Hide 'large scale' references
[1]"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: 1673107] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The Adh-related gene of Drosophila melanogaster is expressed as a functional dicistronic messenger RNA: multigenic transcription in higher organisms."
Brogna S., Ashburner M.
EMBO J. 16:2023-2031(1997) [PubMed: 9155028] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Canton-S.
[3]"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: 10471707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[5]"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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[6]Haymerle H.
Thesis (1983), University of Cambridge, United Kingdom
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X78384 Genomic DNA. Translation: CAA55152.1.
X98338 mRNA. Translation: CAA66982.1.
AE014134 Genomic DNA. Translation: AAF53404.1.
AE014134 Genomic DNA. Translation: AAO41202.1.
Z00030 Genomic DNA. Translation: CAA77331.1.
RefSeqNP_001027272.1. NM_001032101.1.
NP_477495.1. NM_058147.3.
UniGeneDm.6818.

3D structure databases

ProteinModelPortalP91615.
SMRP91615. Positions 2-254.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-21911N.
MINTMINT-1329032.

Proteomic databases

PRIDEP91615.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0006151; FBpp0099544; FBgn0000056.
FBtr0100187; FBpp0099545; FBgn0000056.
GeneID3772432.
KEGGdme:Dmel_CG3484.
UCSCCG3484-RA. d. melanogaster.

Organism-specific databases

CTD3772432.
FlyBaseFBgn0000056. Adhr.

Phylogenomic databases

eggNOGinNOG11791.
GeneTreeEMGT00050000006799.
InParanoidP91615.
OMAVFCAYSA.
OrthoDBEOG44F4RW.
PhylomeDBP91615.

Gene expression databases

GermOnlineCG3484. Drosophila melanogaster.

Family and domain databases

InterProIPR002427. ADH-rel.
IPR002424. ADH_insect.
IPR002198. DH_sc/Rdtase_SDR.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR01170. ADHRELATED.
PR01167. INSADHFAMILY.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio853711.

Entry information

Entry nameADHR_DROME
AccessionPrimary (citable) accession number: P91615
Secondary accession number(s): A4V0Q4 expand/collapse secondary AC list , Q24230, Q6LAE8, Q9NKB9, Q9VJS2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents