P15122 (ALDR_RABIT) 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

Organism

Oryctolagus cuniculus (Rabbit) [Reference proteome]

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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 transcript 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	alditol:NADP+ 1-oxidoreductase 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		PRO_0000124626
Regions
	Nucleotide binding	10 – 19	10	NADP Potential
	Nucleotide binding	211 – 273	63	NADP By similarity
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
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	95	1	N6-acetyllysine By similarity
	Modified residue	222	1	N6-acetyllysine By similarity
	Modified residue	263	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P15122 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E52C078822BC2DFB	FASTA	316	35,763
	10 20 30 40 50 60 MATHLVLYNG AKMPILGLGT WKSPPGQVTE AVKTAIDLGY RHIDCAHVYQ NENEVGVALQ 70 80 90 100 110 120 EKLKEQVVKR EELFIVSKLW CTSHDKSLVK GACQKTLNDL KLDYLDLYLI HWPTGFKHGS 130 140 150 160 170 180 EYFPLDAAGN VIPSDTDFLD TWEAMEGLVD EGLVKSIGVS NFNHLQIERI LNKPGLKYKP 190 200 210 220 230 240 AVNQIECHPY LTQEKLIQYC HSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIADK 250 260 270 280 290 300 HKKTTAQVLI RFPMQRNLVV IPKSVTPARI AENFQVFDFE LSSEDMTTLL SYNRNWRVCA 310 LVSCASHKDY PFHAEF

References

[1]	"Cloning, genomic organization, and osmotic response of the aldose reductase gene." Ferraris J.D., Williams C.K., Martin B.M., Burg M.B., Garcia-Perez A. Proc. Natl. Acad. Sci. U.S.A. 91:10742-10746(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Spleen.
[2]	"Molecular cloning of cDNA coding for kidney aldose reductase. Regulation of specific mRNA accumulation by NaCl-mediated osmotic stress." Garcia-Perez A., Martin B., Murphy H.R., Uchida S., Murer H., Cowley B.D. Jr., Handler J.S., Burg M.B. J. Biol. Chem. 264:16815-16821(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-316. Tissue: Kidney.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U13694 , U13689, U13690, U13691, U13692, U13693 Genomic DNA. Translation: AAB60687.1. M32818 mRNA. Translation: AAA31160.1. U12316 mRNA. Translation: AAA50833.1. J05048 mRNA. Translation: AAA31157.1.
PIR	A34406.
RefSeq	NP_001075756.1. NM_001082287.1.
UniGene	Ocu.1743.
3D structure databases
ProteinModelPortal	P15122.
SMR	P15122. Positions 1-316.
ModBase	Search...
Protein-protein interaction databases
STRING	9986.ENSOCUP00000014272.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100009122.
Organism-specific databases
CTD	231.
Phylogenomic databases
eggNOG	COG0656.
HOGENOM	HOG000250272.
HOVERGEN	HBG000020.
OrthoDB	EOG4VMFFR.
Enzyme and pathway databases
SABIO-RK	P15122.
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
ChEMBL	CHEMBL3567.

Entry information

Entry name

ALDR_RABIT

Accession

Primary (citable) accession number: P15122

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program