Reviewed, UniProtKB/Swiss-Prot O08782 (ALD2_CRIGR)

Names and origin

Protein names

Recommended name:
    Aldose reductase-related protein 2
      Short name=AR
    EC=1.1.1.21
Alternative name(s):
    Aldehyde reductase
    Aldo-keto reductase

Gene names

Name:

AKR1B8

Organism

Cricetulus griseus (Chinese hamster)

Taxonomic identifier

10029 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Reductase with a preference for aliphatic substrates. Can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. Ref.1
Catalytic activity	Alditol + NAD(P)+ = aldose + NAD(P)H.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Detected at very low levels in urinary bladder, testis and jejunum. Ref.1
Induction	By FGF-1 By similarity. Up-regulated by calpain inhibitor I (N-acetyl-leucyl-leucyl-norleucinal/ALLN).
Sequence similarities	Belongs to the aldo/keto reductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aldehyde reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 316

315

Aldose reductase-related protein 2

PRO_0000124630

Regions

Nucleotide binding

211 – 273

63

NADP

Sites

Active site

49

1

Proton donor By similarity

Binding site

111

1

Substrate By similarity

Site

78

1

Lowers pKa of active site Tyr By similarity

Secondary structure

1

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316

Helix Strand Turn

Details...

Beta strand

4 – 6

3

Beta strand

12 – 16

5

Helix

25 – 38

14

Beta strand

42 – 44

3

Helix

47 – 49

3

Helix

52 – 64

13

Helix

70 – 72

3

Beta strand

74 – 79

6

Helix

81 – 83

3

Helix

86 – 100

15

Beta strand

105 – 111

7

Helix

138 – 150

13

Beta strand

153 – 155

3

Beta strand

157 – 161

5

Helix

164 – 171

8

Beta strand

182 – 186

5

Helix

194 – 202

9

Beta strand

206 – 210

5

Beta 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

Beta strand

305 – 307

3

Sequences

	Sequence		Length	Mass (Da)
	O08782-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 80B4B8BF0F4FDDAE	FASTA	316	36,340
	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

References

[1]	"Cloning, sequencing, and enzymatic activity of an inducible aldo-keto reductase from Chinese hamster ovary cells." Hyndman D.J., Takenoshita R., Vera N.L., Pang S.C., Flynn T.G. J. Biol. Chem. 272:13286-13291(1997) [PubMed: 9148949] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, TISSUE SPECIFICITY. Tissue: Ovary.
[2]	"Crystal structure of CHO reductase, a member of the aldo-keto reductase superfamily." Ye Q., Hyndman D.J., Li X., Flynn T.G., Jia Z. Proteins 38:41-48(2000) [PubMed: 10651037] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NADPH.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U81045 mRNA. Translation: AAC53199.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C9W	X-ray	2.40	A	2-316	[»]

ModBase

Search...

Phylogenomic databases

HOVERGEN

O08782.

Enzyme and pathway databases

BRENDA

1.1.1.21. 18.

Family and domain databases

InterPro

IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
[Graphical view]

Gene3D

G3DSA:3.20.20.100. Aldo/ket_red. 1 hit.

PANTHER

PTHR11732. Aldo/ket_red. 1 hit.

Pfam

PF00248. Aldo_ket_red. 1 hit.
[Graphical view]

ProDom

PD000288. Aldo/ket_red. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ALD2_CRIGR

Accession

Primary (citable) accession number: O08782

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 51 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)