[1]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY. TISSUE=Ovary; DOI=10.1074/jbc.272.20.13286; PubMed=9148949 [NCBI, ExPASy, EBI, Israel, Japan] Hyndman D.J., Takenoshita R., Vera N.L., Pang S.C., Flynn T.G.; "Cloning, sequencing, and enzymatic activity of an inducible aldo-keto reductase from Chinese hamster ovary cells."; J. Biol. Chem. 272:13286-13291(1997).
[2]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NADPH. DOI=10.1002/(SICI)1097-0134(20000101)38:1<41::AID-PROT5>3.0.CO;2-M; PubMed=10651037 [NCBI, ExPASy, EBI, Israel, Japan] Ye Q., Hyndman D.J., Li X., Flynn T.G., Jia Z.; "Crystal structure of CHO reductase, a member of the aldo-keto reductase superfamily."; Proteins 38:41-48(2000).

Comments

FUNCTION: Reductase with a preference for aliphatic substrates. Can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates.
CATALYTIC ACTIVITY: Alditol + NAD(P)⁺ = aldose + NAD(P)H.
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
TISSUE SPECIFICITY: Detected at very low levels in urinary bladder, testis and jejunum.
INDUCTION: By FGF-1 (By similarity). Up-regulated by calpain inhibitor I (N-acetyl-leucyl-leucyl-norleucinal/ALLN).
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

U81045; AAC53199.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1C9W; X-ray; 2.40 A; A=1-316.

[ExPASy / RCSB / EBI]

PDBsum

1C9W; -.

ModBase

O08782.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004032;	Molecular function: aldehyde reductase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

ProtoNet

O08782.

Phylogenomic databases

HOVERGEN

O08782; -.

Other

UniRef

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

Keywords

3D-structure; Cytoplasm; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 316`	`315`	`Aldose reductase-related protein 2.`	`PRO_0000124630`
`NP_BIND`	`211 273`	`63`	`NADP.`
`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).`
`STRAND`	`4 6`	`3`
`STRAND`	`12 16`	`5`
`HELIX`	`25 38`	`14`
`STRAND`	`42 44`	`3`
`HELIX`	`47 49`	`3`
`HELIX`	`52 64`	`13`
`HELIX`	`70 72`	`3`
`STRAND`	`74 79`	`6`
`HELIX`	`81 83`	`3`
`HELIX`	`86 100`	`15`
`STRAND`	`105 111`	`7`
`HELIX`	`138 150`	`13`
`STRAND`	`153 155`	`3`
`STRAND`	`157 161`	`5`
`HELIX`	`164 171`	`8`
`STRAND`	`182 186`	`5`
`HELIX`	`194 202`	`9`
`STRAND`	`206 210`	`5`
`STRAND`	`218 220`	`3`
`TURN`	`228 230`	`3`
`HELIX`	`232 240`	`9`
`HELIX`	`245 254`	`10`
`TURN`	`255 257`	`3`
`HELIX`	`267 273`	`7`
`HELIX`	`283 290`	`8`
`HELIX`	`302 304`	`3`
`STRAND`	`305 307`	`3`

Sequence information

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

Molecular weight: 36340 Da [This is the MW of the unprocessed precursor]

CRC64: 80B4B8BF0F4FDDAE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTFVELSTK AKMPIVGLGT WQSPPGQVKE AVKVAIDAGY RHIDCAYAYY NEHEVGEAIQ 

        70         80         90        100        110        120 
EKIKEKAVRR EDLFIVSKLW PTCFERKLLK EAFQKTLTDL KLDYLDLYLI HWPQGLQPGK 

       130        140        150        160        170        180 
ELFPKDDQGN VLTSKITFLD AWEVMEELVD EGLVKALGVS NFNHFQIERI LNKPGLKHKP 

       190        200        210        220        230        240 
VTNQVECHPY LTQEKLIEYC HSKGITVTAY SPLGSPNRPW AKPEDPSLLE DPKIKEIAAK 

       250        260        270        280        290        300 
HKKTSAQVLI RFHIQRNVVV IPKSVTPARI HENFQVFDFQ LSDQEMATIL GFNRNWRACL 

       310 
LPETVNMEEY PYDAEY

O08782 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