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O08782 (ALD2_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 71. 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

Names and origin

Protein namesRecommended name:
Aldose reductase-related protein 2

Short name=AR
EC=1.1.1.21
Alternative name(s):
Aldehyde reductase
Aldo-keto reductase
Gene names
Name:AKR1B8
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reductase with a preference for aliphatic substrates. Can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. Ref.1

Catalytic activity

Alditol + NAD(P)+ = aldose + NAD(P)H.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Detected at very low levels in urinary bladder, testis and jejunum. Ref.1

Induction

By FGF-1 By similarity. Up-regulated by calpain inhibitor I (N-acetyl-leucyl-leucyl-norleucinal/ALLN). Ref.1

Sequence similarities

Belongs to the aldo/keto reductase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalditol:NADP+ 1-oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316Aldose reductase-related protein 2
PRO_0000124630

Regions

Nucleotide binding211 – 27363NADP

Sites

Active site491Proton donor By similarity
Binding site1111Substrate By similarity
Site781Lowers pKa of active site Tyr By similarity

Secondary structure

..................................................... 316
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O08782 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 80B4B8BF0F4FDDAE

FASTA31636,340
        10         20         30         40         50         60 
MSTFVELSTK AKMPIVGLGT WQSPPGQVKE AVKVAIDAGY RHIDCAYAYY NEHEVGEAIQ 

        70         80         90        100        110        120 
EKIKEKAVRR EDLFIVSKLW PTCFERKLLK EAFQKTLTDL KLDYLDLYLI HWPQGLQPGK 

       130        140        150        160        170        180 
ELFPKDDQGN VLTSKITFLD AWEVMEELVD EGLVKALGVS NFNHFQIERI LNKPGLKHKP 

       190        200        210        220        230        240 
VTNQVECHPY LTQEKLIEYC HSKGITVTAY SPLGSPNRPW AKPEDPSLLE DPKIKEIAAK 

       250        260        270        280        290        300 
HKKTSAQVLI RFHIQRNVVV IPKSVTPARI HENFQVFDFQ LSDQEMATIL GFNRNWRACL 

       310 
LPETVNMEEY PYDAEY 

« Hide

References

[1]"Cloning, sequencing, and enzymatic activity of an inducible aldo-keto reductase from Chinese hamster ovary cells."
Hyndman D.J., Takenoshita R., Vera N.L., Pang S.C., Flynn T.G.
J. Biol. Chem. 272:13286-13291(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, TISSUE SPECIFICITY.
Tissue: Ovary.
[2]"Crystal structure of CHO reductase, a member of the aldo-keto reductase superfamily."
Ye Q., Hyndman D.J., Li X., Flynn T.G., Jia Z.
Proteins 38:41-48(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NADPH.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U81045 mRNA. Translation: AAC53199.1.
RefSeqNP_001233680.1. NM_001246751.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C9WX-ray2.40A2-316[»]
ProteinModelPortalO08782.
SMRO08782. Positions 2-315.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100689318.
KEGGcge:100689318.

Organism-specific databases

CTD14187.

Phylogenomic databases

HOVERGENHBG000020.
KOK00011.

Family and domain databases

Gene3D3.20.20.100. 1 hit.
InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERPTHR11732. PTHR11732. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFPIRSF000097. AKR. 1 hit.
PRINTSPR00069. ALDKETRDTASE.
SUPFAMSSF51430. SSF51430. 1 hit.
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO08782.

Entry information

Entry nameALD2_CRIGR
AccessionPrimary (citable) accession number: O08782
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: December 11, 2013
This is version 71 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references