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P15122 (ALDR_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Short name=AR
EC=1.1.1.21
Alternative name(s):
Aldehyde reductase
Gene names
Name:AKR1B1
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.

Catalytic activity

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

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the aldo/keto reductase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
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

Initiator methionine11Removed By similarity
Chain2 – 316315Aldose reductase
PRO_0000124626

Regions

Nucleotide binding10 – 1910NADP Potential
Nucleotide binding211 – 27363NADP By similarity

Sites

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

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue951N6-acetyllysine By similarity
Modified residue2221N6-acetyllysine By similarity
Modified residue2631N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P15122 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E52C078822BC2DFB

FASTA31635,763
        10         20         30         40         50         60 
MATHLVLYNG AKMPILGLGT WKSPPGQVTE AVKTAIDLGY RHIDCAHVYQ NENEVGVALQ 

        70         80         90        100        110        120 
EKLKEQVVKR EELFIVSKLW CTSHDKSLVK GACQKTLNDL KLDYLDLYLI HWPTGFKHGS 

       130        140        150        160        170        180 
EYFPLDAAGN VIPSDTDFLD TWEAMEGLVD EGLVKSIGVS NFNHLQIERI LNKPGLKYKP 

       190        200        210        220        230        240 
AVNQIECHPY LTQEKLIQYC HSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIADK 

       250        260        270        280        290        300 
HKKTTAQVLI RFPMQRNLVV IPKSVTPARI AENFQVFDFE LSSEDMTTLL SYNRNWRVCA 

       310 
LVSCASHKDY PFHAEF 

« Hide

References

[1]"Cloning, genomic organization, and osmotic response of the aldose reductase gene."
Ferraris J.D., Williams C.K., Martin B.M., Burg M.B., Garcia-Perez A.
Proc. Natl. Acad. Sci. U.S.A. 91:10742-10746(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Spleen.
[2]"Molecular cloning of cDNA coding for kidney aldose reductase. Regulation of specific mRNA accumulation by NaCl-mediated osmotic stress."
Garcia-Perez A., Martin B., Murphy H.R., Uchida S., Murer H., Cowley B.D. Jr., Handler J.S., Burg M.B.
J. Biol. Chem. 264:16815-16821(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-316.
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U13694 expand/collapse EMBL AC list , U13689, U13690, U13691, U13692, U13693 Genomic DNA. Translation: AAB60687.1.
M32818 mRNA. Translation: AAA31160.1.
U12316 mRNA. Translation: AAA50833.1.
J05048 mRNA. Translation: AAA31157.1.
PIRA34406.
RefSeqNP_001075756.1. NM_001082287.1.
UniGeneOcu.1743.

3D structure databases

ProteinModelPortalP15122.
SMRP15122. Positions 1-316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000014272.

Chemistry

ChEMBLCHEMBL3567.

Proteomic databases

PRIDEP15122.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009122.

Organism-specific databases

CTD231.

Phylogenomic databases

eggNOGCOG0656.
HOGENOMHOG000250272.
HOVERGENHBG000020.

Enzyme and pathway databases

SABIO-RKP15122.

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...

Entry information

Entry nameALDR_RABIT
AccessionPrimary (citable) accession number: P15122
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: December 11, 2013
This is version 92 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