[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. TISSUE=Spleen; PubMed=7938022 [NCBI, ExPASy, EBI, Israel, Japan] Ferraris J.D., Williams C.K., Martin B.M., Burg M.B., Garcia-Perez A.; "Cloning, genomic organization, and osmotic response of the aldose reductase gene."; Proc. Natl. Acad. Sci. U.S.A. 91:10742-10746(1994).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 15-316. TISSUE=Kidney; PubMed=2506183 [NCBI, ExPASy, EBI, Israel, Japan] Garcia-Perez A., Martin B., Murphy H.R., Uchida S., Murer H., Cowley B.D. Jr., Handler J.S., Burg M.B.; "Molecular cloning of cDNA coding for kidney aldose reductase. Regulation of specific mRNA accumulation by NaCl-mediated osmotic stress."; J. Biol. Chem. 264:16815-16821(1989).

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.
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

U13694; AAB60687.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U13689; AAB60687.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U13690; AAB60687.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U13691; AAB60687.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U13692; AAB60687.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U13693; AAB60687.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32818; AAA31160.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U12316; AAA50833.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J05048; AAA31157.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A34406; A34406.

NP_001075756.1; -.

3D structure databases

HSSP

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

SMR

P15122; 1-316.

ModBase

P15122.

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

P15122.

Genome annotation databases

GeneID

100009122; -.

Phylogenomic databases

HOVERGEN

P15122; -.

Other

ProtoNet

P15122.

UniRef

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

Keywords

Acetylation; Cytoplasm; 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_0000124626`
`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).`

Sequence information

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

Molecular weight: 35763 Da [This is the MW of the unprocessed precursor]

CRC64: E52C078822BC2DFB [This is a checksum on the sequence]

        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

P15122 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