[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=C57BL/6; TISSUE=Kidney; PubMed=7851421 [NCBI, ExPASy, EBI, Israel, Japan] Gui T., Tanimoto T., Kokai Y., Nishimura C.; "Presence of a closely related subgroup in the aldo-ketoreductase family of the mouse."; Eur. J. Biochem. 227:448-453(1995).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=ICR X Swiss Webster; TISSUE=Liver; Iwata T., Carper D.; Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=CD-1; TISSUE=Kidney; Daoudal S., Berger M., Pailhoux E., Tournaire C., Veyssiere G., Jean C.; Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=129/Ola; PubMed=9485485 [NCBI, ExPASy, EBI, Israel, Japan] McGowan M.H., Iwata T., Carper D.A.; "Characterization of the mouse aldose reductase gene and promoter in a lens epithelial cell line."; Mol. Vis. 4:2-2(1998).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=129/SvJ; PubMed=10092857 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Comparisons of genomic structures and chromosomal locations of the mouse aldose reductase and aldose reductase-like genes."; Eur. J. Biochem. 259:726-730(1999).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=BALB/c; DOI=10.1006/bbrc.1999.0164; PubMed=10049784 [NCBI, ExPASy, EBI, Israel, Japan] Li H., Nobukuni Y., Gui T., Yabe-Nishimura C.; "Characterization of genomic regions directing the cell-specific expression of the mouse aldose reductase gene."; Biochem. Biophys. Res. Commun. 255:759-764(1999).
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Mammary tumor; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[8]	PROTEIN SEQUENCE OF 156-169. TISSUE=Brain; Lubec G., Yang J.W., Zigmond M.; Submitted (JUL-2007) to UniProtKB.

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: Monomer.
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Abundant in the testis, skeletal muscle and kidney.
SIMILARITY: Belongs to the aldo/keto reductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D32250; BAA06980.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L39795; AAA62176.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U29152; AAA69958.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U89150; AAC13358.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U89140; AAC13358.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U89142; AAC13358.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U89143; AAC13358.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U89144; AAC13358.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U89145; AAC13358.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U89146; AAC13358.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U89147; AAC13358.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U89148; AAC13358.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U89149; AAC13358.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U93231; AAD32300.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U93230; AAD32300.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB016665; BAA76413.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004725; AAH04725.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021655; AAH21655.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

I49484; I49484.

NP_033788.3; -.

3D structure databases

HSSP

P15121; 2ACQ. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

SMR

P45376; 1-315.

ModBase

P45376.

Protein-protein interaction databases

IntAct

P45376; -.

PTM databases

PhosphoSite

P45376; -.

2D gel databases

SWISS-2DPAGE

P45376; -.

PMMA-2DPAGE

P45376; -.

REPRODUCTION-2DPAGE

P45376; -.

Organism-specific databases

MGI

MGI:1353494; Akr1b3.

Gene expression databases

ArrayExpress

P45376; -.

GermOnline

ENSMUSG00000071414; Mus musculus.

Ontologies

GO:0004032;	Molecular function: aldehyde reductase activity (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR001395; Aldo/ket_red.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.100; Aldo/ket_red; 1.

PANTHER

PTHR11732; Aldo/ket_red; 1.

Pfam

PF00248; Aldo_ket_red; 1.
Pfam graphical view of domain structure.

PRINTS

PR00069; ALDKETRDTASE.

ProDom

PD000288; Aldo/ket_red; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00798; ALDOKETO_REDUCTASE_1; 1.
PS00062; ALDOKETO_REDUCTASE_2; 1.
PS00063; ALDOKETO_REDUCTASE_3; 1.

BLOCKS

P45376.

Genome annotation databases

Ensembl

ENSMUSG00000001642; Mus musculus. [Contig view]

GeneID

11677; -.

KEGG

mmu:11677; -.

Phylogenomic databases

HOGENOM

P45376; -.

HOVERGEN

P45376; -.

Other

SOURCE

Akr1b1; Mus musculus.

ProtoNet

P45376.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 316`	`315`	`Aldose reductase.`	`PRO_0000124624`
`NP_BIND`	`10 19`	`10`	`NADP (Potential).`
`NP_BIND`	`211 273`	`63`	`NADP (By similarity).`
`ACT_SITE`	`49 49`		`Proton donor (By similarity).`
`BINDING`	`111 111`		`Substrate (By similarity).`
`SITE`	`78 78`	`1`	`Lowers pKa of active site Tyr (By similarity).`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`
`MOD_RES`	`23 23`		`Phosphoserine (By similarity).`
`MOD_RES`	`40 40`		`Phosphotyrosine (By similarity).`
`CONFLICT`	`46 46`		`A -> S (in Ref. 1; BAA06980).`
`CONFLICT`	`221 221`		`A -> G (in Ref. 4; AAC13358).`
`CONFLICT`	`281 281`		`V -> L (in Ref. 7; AAH04725/AAH21655).`

Sequence information

Length: 316 AA [This is the length of the unprocessed precursor]

Molecular weight: 35732 Da [This is the MW of the unprocessed precursor]

CRC64: E18759AD160B4A0E [This is a checksum on the sequence]

        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

P45376 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools