P80276 (ALDR_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aldose reductase
Short name=AR
EC=1.1.1.21

Alternative name(s):
Aldehyde reductase

Gene names

Name:	AKR1B1
Synonyms:	ALR2

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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	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 structure	Monomer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the aldo/keto reductase family.
Mass spectrometry	Molecular mass is 35778±3 Da from positions 2 - 316. Determined by ESI. Ref.2

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	daunorubicin metabolic process Inferred from electronic annotation. Source: Compara doxorubicin metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	alditol:NADP+ 1-oxidoreductase activity Inferred from electronic annotation. Source: EC glyceraldehyde oxidoreductase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 316

315

Aldose reductase

PRO_0000124625

Regions

Nucleotide binding

10 – 19

10

NADP Potential

Nucleotide binding

211 – 273

63

NADP

Sites

Active site

49

1

Proton donor

Binding site

111

1

Substrate

Site

78

1

Lowers pKa of active site Tyr By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.2

Modified residue

222

1

N6-acetyllysine By similarity

Modified residue

263

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

99

1

D → N in AAA30989. Ref.1

Sequence conflict

99

1

D → N in AAC48515. Ref.1

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 – 88

3

Helix

89 – 100

12

Beta strand

105 – 110

6

Beta strand

118 – 120

3

Beta strand

129 – 131

3

Helix

138 – 150

13

Beta strand

153 – 155

3

Beta strand

157 – 161

5

Helix

164 – 171

8

Beta strand

181 – 186

6

Helix

194 – 203

10

Beta strand

206 – 210

5

Beta strand

223 – 225

3

Helix

228 – 230

3

Helix

232 – 241

10

Helix

245 – 255

11

Helix

267 – 272

6

Turn

273 – 278

6

Helix

283 – 290

8

Helix

302 – 304

3

Helix

311 – 313

3

Sequences

	Sequence		Length	Mass (Da)
	P80276 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 7218B663AC1B4E92	FASTA	316	35,868
	10 20 30 40 50 60 MASHLVLYTG AKMPILGLGT WKSPPGKVTE AVKVAIDLGY RHIDCAHVYQ NENEVGLGLQ 70 80 90 100 110 120 EKLQGQVVKR EDLFIVSKLW CTDHEKNLVK GACQTTLRDL KLDYLDLYLI HWPTGFKPGK 130 140 150 160 170 180 DPFPLDGDGN VVPDESDFVE TWEAMEELVD EGLVKAIGVS NFNHLQVEKI LNKPGLKYKP 190 200 210 220 230 240 AVNQIEVHPY LTQEKLIEYC KSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK 250 260 270 280 290 300 YNKTTAQVLI RFPMQRNLIV IPKSVTPERI AENFQVFDFE LSPEDMNTLL SYNRNWRVCA 310 LMSCASHKDY PFHEEY

References

[1]	"Location of an essential arginine residue in the primary structure of pig aldose reductase." Kubiseski T.J., Green N.C., Flynn T.G. Adv. Exp. Med. Biol. 328:259-265(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes." Jaquinod M., Potier N., Klarskov K., Reymann J.-M., Sorokine O., Kieffer S., Barth P., Andriantomanga V., Biellmann J.-F., van Dorsselaer A. Eur. J. Biochem. 218:893-903(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-316, MASS SPECTROMETRY. Tissue: Lens.
[3]	"Novel NADPH-binding domain revealed by the crystal structure of aldose reductase." Rondeau J.-M., Tete-Favier F., Podjarny A., Reymann J.-M., Barth P., Biellmann J.-F., Moras D. Nature 355:469-472(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[4]	"A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil." Urzhumtsev A., Tete-Favier F., Mitschler A., Barbanton J., Barth P., Urzhumtseva L., Biellmann J.-F., Podjarny A.D., Moras D. Structure 5:601-612(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L14950 mRNA. Translation: AAA30989.1.
U46065 mRNA. Translation: AAC48515.1.

PIR

A59021.

RefSeq

NP_001001539.1. NM_001001539.2.

UniGene

Ssc.3059.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AH0	X-ray	2.30	A	2-316	[»]
1AH3	X-ray	2.30	A	2-316	[»]
1AH4	X-ray	2.00	A	2-316	[»]
1DLA	X-ray	3.00	A/B/C/D	3-316	[»]
1EKO	X-ray	2.20	A	2-315	[»]

ProteinModelPortal

P80276.

SMR

P80276. Positions 2-316.

ModBase

Search...

Protein-protein interaction databases

STRING

9823.ENSSSCP00000017525.

Proteomic databases

PaxDb

P80276.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSSSCT00000018009; ENSSSCP00000017525; ENSSSCG00000016539.

GeneID

396816.

KEGG

ssc:396816.

Organism-specific databases

CTD

231.

Phylogenomic databases

eggNOG

COG0656.

GeneTree

ENSGT00670000097881.

HOGENOM

HOG000250272.

HOVERGEN

HBG000020.

KO

K00011.

OrthoDB

EOG4VMFFR.

Enzyme and pathway databases

SABIO-RK

P80276.

Family and domain databases

Gene3D

3.20.20.100. 1 hit.

InterPro

IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]

PANTHER

PTHR11732. PTHR11732. 1 hit.

Pfam

PF00248. Aldo_ket_red. 1 hit.
[Graphical view]

PIRSF

PIRSF000097. AKR. 1 hit.

PRINTS

PR00069. ALDKETRDTASE.

SUPFAM

SSF51430. Aldo/ket_red. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

BindingDB

P80276.

ChEMBL

CHEMBL4559.

EvolutionaryTrace

P80276.

Entry information

Entry name

ALDR_PIG

Accession

Primary (citable) accession number: P80276

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program