Reviewed, UniProtKB/Swiss-Prot P45376 (ALDR_MOUSE)

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:	Akr1b3, Aldor1, Aldr1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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.
Tissue specificity	Abundant in the testis, skeletal muscle and kidney.
Sequence similarities	Belongs to the aldo/keto reductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
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 Ref.1 Inferred from direct assay. Source: MGI
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_0000124624
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	23	1	Phosphoserine By similarity
	Modified residue	40	1	Phosphotyrosine 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
Experimental info
	Sequence conflict	46	1	A → S in BAA06980. Ref.1
	Sequence conflict	221	1	A → G in AAC13358. Ref.4
	Sequence conflict	281	1	V → L in AAH04725. Ref.7
	Sequence conflict	281	1	V → L in AAH21655. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P45376-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E18759AD160B4A0E	FASTA	316	35,732
	10 20 30 40 50 60 MASHLELNNG TKMPTLGLGT WKSPPGQVTE AVKVAIDLGY RHIDCAQVYQ NEKEVGVALQ 70 80 90 100 110 120 EKLKEQVVKR QDLFIVSKLW CTFHDKSMVK GAFQKTLSDL QLDYLDLYLI HWPTGFKPGP 130 140 150 160 170 180 DYFPLDASGN VIPSDTDFVD TWTAMEQLVD EGLVKTIGVS NFNPLQIERI LNKPGLKYKP 190 200 210 220 230 240 AVNQIECHPY LTQEKLIEYC HSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK 250 260 270 280 290 300 YNKTTAQVLI RFPIQRNLVV IPKSVTPVRI AENLKVFDFE VSSEDMATLL SYNRNWRVCA 310 LMSCAKHKDY PFHAEV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Presence of a closely related subgroup in the aldo-ketoreductase family of the mouse." Gui T., Tanimoto T., Kokai Y., Nishimura C. Eur. J. Biochem. 227:448-453(1995) [PubMed: 7851421] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6. Tissue: Kidney.
[2]	Iwata T., Carper D. Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ICR X Swiss Webster. Tissue: Liver.
[3]	Daoudal S., Berger M., Pailhoux E., Tournaire C., Veyssiere G., Jean C. Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: CD-1. Tissue: Kidney.
[4]	"Characterization of the mouse aldose reductase gene and promoter in a lens epithelial cell line." McGowan M.H., Iwata T., Carper D.A. Mol. Vis. 4:2-2(1998) [PubMed: 9485485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/Ola.
[5]	"Comparisons of genomic structures and chromosomal locations of the mouse aldose reductase and aldose reductase-like genes." Ho H.T.B., Jenkins N.A., Copeland N.G., Gilbert D.J., Winkles J.A., Louie H.W.Y., Lee F.K., Chung S.S.M., Chung S.K. Eur. J. Biochem. 259:726-730(1999) [PubMed: 10092857] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/SvJ.
[6]	"Characterization of genomic regions directing the cell-specific expression of the mouse aldose reductase gene." Li H., Nobukuni Y., Gui T., Yabe-Nishimura C. Biochem. Biophys. Res. Commun. 255:759-764(1999) [PubMed: 10049784] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BALB/c.
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary tumor.
[8]	Lubec G., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 156-169. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D32250 mRNA. Translation: BAA06980.1. L39795 mRNA. Translation: AAA62176.1. U29152 mRNA. Translation: AAA69958.1. U89150 , U89140, U89142, U89143, U89144, U89145, U89146, U89147, U89148, U89149 Genomic DNA. Translation: AAC13358.1. U93231, U93230 Genomic DNA. Translation: AAD32300.1. AB016665 Genomic DNA. Translation: BAA76413.1. BC004725 mRNA. Translation: AAH04725.1. BC021655 mRNA. Translation: AAH21655.1.
IPI	IPI00223757.
PIR	I49484.
RefSeq	NP_033788.3.
UniGene	Mm.389126 Mm.451
3D structure databases
HSSP	HSSP built from PDB template 2ACQ based on UniProtKB P15121.
SMR	P45376. Positions 1-315.
ModBase	Search...
Protein-protein interaction databases
STRING	P45376.
PTM databases
PhosphoSite	P45376.
2-D gel databases
SWISS-2DPAGE	P45376.
PMMA-2DPAGE	P45376.
REPRODUCTION-2DPAGE	P45376.
Proteomic databases
PRIDE	P45376.
Genome annotation databases
Ensembl	ENSMUST00000102980; ENSMUSP00000100045; ENSMUSG00000001642; Mus musculus. [Genome view]
GeneID	11677.
KEGG	mmu:11677.
Organism-specific databases
CTD	11677.
MGI	MGI:1353494. Akr1b3.
Phylogenomic databases
HOGENOM	P45376.
HOVERGEN	P45376.
OMA	CTYHEKS.
Enzyme and pathway databases
BRENDA	1.1.1.21. 244.
Gene expression databases
ArrayExpress	P45376.
Bgee	P45376.
Genevestigator	P45376.
GermOnline	ENSMUSG00000071414. Mus musculus.
Family and domain databases
InterPro	IPR001395. Aldo/ket_red. IPR018170. Aldo/ket_reductase_CS. IPR020471. Aldo/keto_reductase_sg. [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]
PRINTS	PR00069. ALDKETRDTASE.
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...
Other Resources
NextBio	279311.
SOURCE	Search...

Entry information

Entry name

ALDR_MOUSE

Accession

Primary (citable) accession number: P45376
Secondary accession number(s): O70130, Q99KC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)