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Reviewed, UniProtKB/Swiss-Prot P51635 (AK1A1_RAT)

Last modified January 19, 2010. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Alcohol dehydrogenase [NADP+]
    EC=1.1.1.2
Alternative name(s):
    Aldehyde reductase
    Aldo-keto reductase family 1 member A1
    3-DG-reducing enzyme
Gene names
Name: Akr1a1
Synonyms: Alr
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs By similarity. Catalyzes the NADPH-dependent reduction of 3-deoxyglucosone (3-DG).

Catalytic activity

An alcohol + NADP+ = an aldehyde + NADPH.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the aldo/keto reductase family.

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Ontologies

Keywords
   LigandNADP
   Molecular functionOxidoreductase
   PTMAcetylation
Glycation
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalcohol dehydrogenase (NADP+) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 325324Alcohol dehydrogenase [NADP+]
PRO_0000124620

Regions

Nucleotide binding11 – 2010NADP Potential
Nucleotide binding211 – 27363NADP By similarity

Sites

Active site501Proton donor By similarity
Binding site1131Substrate By similarity
Site131Not glycated
Site301Not glycated
Site341Not glycated
Site611Not glycated
Site801Lowers pKa of active site Tyr By similarity
Site801Not glycated
Site971Not glycated
Site1271Not glycated
Site1341Not glycated
Site1451Not glycated
Site1571Not glycated
Site2401Not glycated
Site2571Not glycated
Site2631Not glycated
Site2871Not glycated
Site2941Not glycated
Site3081Not glycated

Amino acid modifications

Modified residue21N-acetylthreonine Ref.5
Glycosylation231N-linked (Glc) (glycation) Ref.3
Glycosylation681N-linked (Glc) (glycation) Ref.3
Glycosylation851N-linked (Glc) (glycation) Ref.3
Glycosylation1411N-linked (Glc) (glycation) Ref.3
Glycosylation1531N-linked (Glc) (glycation) Ref.3

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Sequences

Sequence LengthMass (Da)Tools
P51635-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F95573B7411884DA

FASTA32536,506
        10         20         30         40         50         60 
MTASSVLLHT GQKMPLIGLG TWKSEPGQVK AAIKYALSVG YRHIDCASVY GNETEIGEAL 

        70         80         90        100        110        120 
KESVGAGKAV PREELFVTSK LWNTKHHPED VEPAVRKTLA DLQLEYLDLY LMHWPYAFER 

       130        140        150        160        170        180 
GDNPFPKNAD GTVKYDSTHY KETWKALEAL VAKGLVKALG LSNFSSRQID DVLSVASVRP 

       190        200        210        220        230        240 
AVLQVECHPY LAQNELIAHC QARGLEVTAY SPLGSSDRAW RHPDEPVLLE EPVVLALAEK 

       250        260        270        280        290        300 
HGRSPAQILL RWQVQRKVIC IPKSITPSRI LQNIQVFDFT FSPEEMKQLD ALNKNWRYIV 

       310        320 
PMITVDGKRV PRDAGHPLYP FNDPY

« Hide

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References

« Hide 'large scale' references
[1]"Identity of a major 3-deoxyglucosone-reducing enzyme with aldehyde reductase in rat liver established by amino acid sequencing and cDNA expression."
Takahashi M., Fujii J., Teshima T., Suzuki K., Shiba T., Taniguchi N.
Gene 127:249-253(1993) [PubMed: 8500767] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Kidney and Liver.
[2]"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: Pituitary.
[3]"In vivo glycation of aldehyde reductase, a major 3-deoxyglucosone reducing enzyme: identification of glycation sites."
Takahashi M., Lu Y.B., Myint T., Fujii J., Wada Y., Taniguchi N.
Biochemistry 34:1433-1438(1995) [PubMed: 7827091] [Abstract]
Cited for: PROTEIN SEQUENCE OF 14-30; 62-77; 81-97; 135-145 AND 146-157, GLYCATION AT LYS-23; LYS-68; LYS-85; LYS-141 AND LYS-153, ABSENCE OF GLYCATION AT LYS-13; LYS-30; LYS-34; LYS-61; LYS-80; LYS-97; LYS-127; LYS-134; LYS-145; LYS-157; LYS-240; LYS-257; LYS-263; LYS-287; LYS-294 AND LYS-308.
[4]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 204-218; 222-240; 270-287 AND 313-325, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
[5]Lubec G., Chen W.-Q.
Submitted (FEB-2007) to UniProtKB
Cited for: ACETYLATION AT THR-2, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D10854 mRNA. Translation: BAA01627.1.
BC059133 mRNA. Translation: AAH59133.1.
IPIIPI00230859.
PIRJN0629.
RefSeqNP_112262.1.
UniGeneRn.835

3D structure databases

SMRP51635. Positions 3-325.
ModBaseSearch...

Protein-protein interaction databases

STRINGP51635.

Proteomic databases

PRIDEP51635.

Genome annotation databases

EnsemblENSRNOT00000023072; ENSRNOP00000023072; ENSRNOG00000016727; Rattus norvegicus. [Genome view]
GeneID78959.
KEGGrno:78959.
UCSCNM_031000. rat.

Organism-specific databases

CTD78959.
RGD68346. Akr1a1.

Phylogenomic databases

eggNOGroNOG06774.
HOVERGENP51635.
InParanoidP51635.
OMAWRHPDEP.
OrthoDBEOG9JT2QW.
PhylomeDBP51635.

Enzyme and pathway databases

BRENDA1.1.1.2. 248.

Gene expression databases

ArrayExpressP51635.
GenevestigatorP51635.
GermOnlineENSRNOG00000016727. Rattus norvegicus.

Family and domain databases

InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_sg.
[Graphical view]
Gene3DG3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHERPTHR11732. Aldo/ket_red. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSPR00069. ALDKETRDTASE.
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio614380.

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Entry information

Entry nameAK1A1_RAT
AccessionPrimary (citable) accession number: P51635
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: January 19, 2010
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents