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P45376 (ALDR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 122. 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

Short name=AR
EC=1.1.1.21
Alternative name(s):
Aldehyde reductase
Gene names
Name:Akr1b1
Synonyms:Akr1b3, Aldor1, Aldr1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

Tissue specificity

Abundant in the testis, skeletal muscle and kidney.

Sequence similarities

Belongs to the aldo/keto reductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 316315Aldose reductase
PRO_0000124624

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

Experimental info

Sequence conflict461A → S in BAA06980. Ref.1
Sequence conflict2211A → G in AAC13358. Ref.4
Sequence conflict2811V → L in AAH04725. Ref.7
Sequence conflict2811V → L in AAH21655. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P45376 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E18759AD160B4A0E

FASTA31635,732
        10         20         30         40         50         60 
MASHLELNNG TKMPTLGLGT WKSPPGQVTE AVKVAIDLGY RHIDCAQVYQ NEKEVGVALQ 

        70         80         90        100        110        120 
EKLKEQVVKR QDLFIVSKLW CTFHDKSMVK GAFQKTLSDL QLDYLDLYLI HWPTGFKPGP 

       130        140        150        160        170        180 
DYFPLDASGN VIPSDTDFVD TWTAMEQLVD EGLVKTIGVS NFNPLQIERI LNKPGLKYKP 

       190        200        210        220        230        240 
AVNQIECHPY LTQEKLIEYC HSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK 

       250        260        270        280        290        300 
YNKTTAQVLI RFPIQRNLVV IPKSVTPVRI AENLKVFDFE VSSEDMATLL SYNRNWRVCA 

       310 
LMSCAKHKDY PFHAEV 

« Hide

References

« Hide 'large scale' references
[1]"Presence of a closely related subgroup in the aldo-ketoreductase family of the mouse."
Gui T., Tanimoto T., Kokai Y., Nishimura C.
Eur. J. Biochem. 227:448-453(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Kidney.
[2]Iwata T., Carper D.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ICR X Swiss Webster.
Tissue: Liver.
[3]Daoudal S., Berger M., Pailhoux E., Tournaire C., Veyssiere G., Jean C.
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: CD-1.
Tissue: Kidney.
[4]"Characterization of the mouse aldose reductase gene and promoter in a lens epithelial cell line."
McGowan M.H., Iwata T., Carper D.A.
Mol. Vis. 4:2-2(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Ola.
[5]"Comparisons of genomic structures and chromosomal locations of the mouse aldose reductase and aldose reductase-like genes."
Ho H.T.B., Jenkins N.A., Copeland N.G., Gilbert D.J., Winkles J.A., Louie H.W.Y., Lee F.K., Chung S.S.M., Chung S.K.
Eur. J. Biochem. 259:726-730(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
[6]"Characterization of genomic regions directing the cell-specific expression of the mouse aldose reductase gene."
Li H., Nobukuni Y., Gui T., Yabe-Nishimura C.
Biochem. Biophys. Res. Commun. 255:759-764(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary tumor.
[8]Lubec G., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 156-169.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D32250 mRNA. Translation: BAA06980.1.
L39795 mRNA. Translation: AAA62176.1.
U29152 mRNA. Translation: AAA69958.1.
U89150 expand/collapse EMBL AC list , U89140, U89142, U89143, U89144, U89145, U89146, U89147, U89148, U89149 Genomic DNA. Translation: AAC13358.1.
U93231, U93230 Genomic DNA. Translation: AAD32300.1.
AB016665 Genomic DNA. Translation: BAA76413.1.
BC004725 mRNA. Translation: AAH04725.1.
BC021655 mRNA. Translation: AAH21655.1.
PIRI49484.
RefSeqNP_033788.3. NM_009658.3.
UniGeneMm.389126.
Mm.451.

3D structure databases

ProteinModelPortalP45376.
SMRP45376. Positions 2-315.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198069. 2 interactions.
IntActP45376. 6 interactions.
MINTMINT-1869603.

PTM databases

PhosphoSiteP45376.

2D gel databases

COMPLUYEAST-2DPAGEP45376.
REPRODUCTION-2DPAGEIPI00223757.
P45376.
SWISS-2DPAGEP45376.

Proteomic databases

PaxDbP45376.
PRIDEP45376.

Protocols and materials databases

DNASU11677.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102980; ENSMUSP00000100045; ENSMUSG00000001642.
GeneID11677.
KEGGmmu:11677.
UCSCuc009bgy.2. mouse.

Organism-specific databases

CTD11677.
MGIMGI:1353494. Akr1b3.

Phylogenomic databases

eggNOGCOG0656.
HOGENOMHOG000250272.
HOVERGENHBG000020.
InParanoidP45376.
KOK00011.
OMADFLDTWT.
OrthoDBEOG70KGQF.
TreeFamTF106492.

Gene expression databases

ArrayExpressP45376.
BgeeP45376.
GenevestigatorP45376.

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

NextBio279311.
PROP45376.
SOURCESearch...

Entry information

Entry nameALDR_MOUSE
AccessionPrimary (citable) accession number: P45376
Secondary accession number(s): O70130, Q99KC9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 122 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot