[1]	NUCLEOTIDE SEQUENCE, AND PARTIAL PROTEIN SEQUENCE. STRAIN=Sprague-Dawley; TISSUE=Lens; DOI=10.1016/0014-5793(87)80905-5; PubMed=3111886 [NCBI, ExPASy, EBI, Israel, Japan] Carper D., Nishimura C., Shinohara T., Dietzchold B., Wistow G., Craft C., Kador P., Kinoshita J.H.; "Aldose reductase and p-crystallin belong to the same protein superfamily as aldehyde reductase."; FEBS Lett. 220:209-213(1987).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0378-1119(91)90326-7; PubMed=1748296 [NCBI, ExPASy, EBI, Israel, Japan] Graham C.E., Szpirer C., Levan G., Carper D.; "Characterization of the aldose reductase-encoding gene family in rat."; Gene 107:259-267(1991).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Prostate; 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).
[4]	PROTEIN SEQUENCE OF 42-53; 156-169; 178-195; 276-294 AND 307-316, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Spinal cord; Lubec G., Afjehi-Sadat L.; Submitted (NOV-2006) to UniProtKB.
[5]	PROTEIN SEQUENCE OF 156-169 AND 205-210. TISSUE=Astrocyte; PubMed=7498172 [NCBI, ExPASy, EBI, Israel, Japan] Laeng P., Bouillon P., Taupenot L., Labourdette G.; "Long-term induction of an aldose reductase protein by basic fibroblast growth factor in rat astrocytes in vitro."; Electrophoresis 16:1240-1250(1995).

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

X05884; CAA29308.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M60322; AAA40721.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC062034; AAH62034.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A60603; A60603.

NP_036630.1; -.

3D structure databases

HSSP

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

SMR

P07943; 1-315.

ModBase

P07943.

Organism-specific databases

RGD

2092; Akr1b1.

Gene expression databases

ArrayExpress

P07943; -.

GermOnline

ENSRNOG00000009513; Rattus norvegicus.

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

P07943.

Genome annotation databases

Ensembl

ENSRNOG00000009513; Rattus norvegicus. [Contig view]

GeneID

24192; -.

KEGG

rno:24192; -.

Phylogenomic databases

HOVERGEN

P07943; -.

Other

ProtoNet

P07943.

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_0000124627`
`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: 35797 Da [This is the MW of the unprocessed precursor]

CRC64: D6D07843B6850002 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASHLELNNG TKMPTLGLGT WKSPPGQVTE AVKVAIDMGY RHIDCAQVYQ NEKEVGVALQ 

        70         80         90        100        110        120 
EKLKEQVVKR QDLFIVSKLW CTFHDQSMVK GACQKTLSDL QLDYLDLYLI HWPTGFKPGP 

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

       190        200        210        220        230        240 
AVNQIECHPY LTQEKLIEYC HCKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKEIAAK 

       250        260        270        280        290        300 
YNKTTAQVLI RFPIQRNLVV IPKSVTPARI AENFKVFDFE LSNEDMATLL SYNRNWRVCA 

       310 
LMSCAKHKDY PFHAEV

P07943 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