[1]	PROTEIN SEQUENCE. TISSUE=Lens; PubMed=2105951 [NCBI, ExPASy, EBI, Israel, Japan] Schade S.Z., Early S.L., Williams T.R., Kezdy F.J., Heinrikson R.L., Grimshaw C.E., Doughty C.C.; "Sequence analysis of bovine lens aldose reductase."; J. Biol. Chem. 265:3628-3635(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 9-315. TISSUE=Testis; DOI=10.1021/bi00057a003; PubMed=8431420 [NCBI, ExPASy, EBI, Israel, Japan] Warren J.C., Murdock G.L., Ma Y., Goodman S.R., Zimmer W.E.; "Molecular cloning of testicular 20 alpha-hydroxysteroid dehydrogenase: identity with aldose reductase."; Biochemistry 32:1401-1406(1993).
[3]	PROTEIN SEQUENCE OF 20-315. TISSUE=Lens; PubMed=2515032 [NCBI, ExPASy, EBI, Israel, Japan] Petrash J.M., Favello A.D.; "Isolation and characterization of cDNA clones encoding aldose reductase."; Curr. Eye Res. 8:1021-1027(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.
CATALYTIC ACTIVITY: 17-alpha,20-alpha-dihydroxypregn-4-en-3-one + NAD(P)⁺ = 17-alpha-hydroxyprogesterone + 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

M31463; AAA30370.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S54973; AAB25333.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A35452; A35452.

UniGene

Bt.63116

3D structure databases

PDB

2GO6; Model; -; A=1-315.

[ExPASy / RCSB / EBI]

2GO6; -.

P16116; 1-315.

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

P16116.

Genome annotation databases

Ensembl

ENSBTAG00000009902; Bos taurus. [Contig view]

Phylogenomic databases

HOVERGEN

P16116; -.

Other

ProtoNet

P16116.

UniRef

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

Keywords

3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 315`	`315`	`Aldose reductase.`	`PRO_0000124622`
`NP_BIND`	`9 18`	`10`	`NADP (Potential).`
`NP_BIND`	`210 272`	`63`	`NADP (By similarity).`
`ACT_SITE`	`48 48`		`Proton donor (By similarity).`
`BINDING`	`110 110`		`Substrate (By similarity).`
`SITE`	`77 77`	`1`	`Lowers pKa of active site Tyr (By similarity).`
`MOD_RES`	`1 1`		`N-acetylalanine.`
`MOD_RES`	`22 22`		`Phosphoserine (By similarity).`
`MOD_RES`	`39 39`		`Phosphotyrosine (By similarity).`
`VARIANT`	`4 4`	`1`	`I -> L.`
`VARIANT`	`6 6`	`1`	`L -> I.`
`CONFLICT`	`65 65`		`Q -> K (in Ref. 2; AAA30370/AAB25333).`

Sequence information

Length: 315 AA [This is the length of the unprocessed precursor]

Molecular weight: 35919 Da [This is the MW of the unprocessed precursor]

CRC64: 18597E7332A3F9C2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
AHNIVLYTGA KMPILGLGTW KSPPGKVTEA VKVAIDLGYR HIDCAHVYQN ENEVGLALQA 

        70         80         90        100        110        120 
KLQEQVVKRE DLFIVSKLWC TYHDKDLVKG ACQKTLSDLK LDYLDLYLIH WPTGFKPGKD 

       130        140        150        160        170        180 
FFPLDEDGNV IPSEKDFVDT WTAMEELVDE GLVKAIGVSN FNHLQVEKIL NKPGLKYKPA 

       190        200        210        220        230        240 
VNQIECHPYL TQEKLIQYCN SKGIVVTAYS PLGSPDRPWA KPEDPSILED PRIKAIADKY 

       250        260        270        280        290        300 
NKTTAQVLIR FPIQRNLIVI PKSVTPERIA ENFQVFDFEL DKEDMNTLLS YNRDWRACAL 

       310 
VSCASHRDYP FHEEF

P16116 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