Aldose reductase - Mus musculus (Mouse)

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P45376 (ALDR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › 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
Technical term	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 direct assay Ref.1. Source: MGI 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

Removed By similarity

Chain

2 – 316

315

Aldose reductase

PRO_0000124624

Regions

Nucleotide binding

10 – 19

NADP Potential

Nucleotide binding

211 – 273

NADP By similarity

Sites

Active site

Proton donor By similarity

Binding site

111

Substrate By similarity

Site

Lowers pKa of active site Tyr By similarity

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

222

N6-acetyllysine By similarity

Modified residue

263

N6-acetyllysine By similarity

Experimental info

Sequence conflict

A → S in BAA06980. Ref.1

Sequence conflict

221

A → G in AAC13358. Ref.4

Sequence conflict

281

V → L in AAH04725. Ref.7

Sequence conflict

281

V → L in AAH21655. Ref.7

Sequences

Sequence

Length

Mass (Da)

Tools

P45376 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E18759AD160B4A0E
Show »

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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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
EMBL GenBank DDBJ	D32250 mRNA. Translation: BAA06980.1. L39795 mRNA. Translation: AAA62176.1. U29152 mRNA. Translation: AAA69958.1. U89150 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. NM_009658.3.
UniGene	Mm.389126. Mm.451.
3D structure databases
ProteinModelPortal	P45376.
SMR	P45376. Positions 2-315.
ModBase	Search...
Protein-protein interaction databases
IntAct	P45376. 3 interactions.
PTM databases
PhosphoSite	P45376.
2D gel databases
COMPLUYEAST-2DPAGE	P45376.
REPRODUCTION-2DPAGE	IPI00223757. P45376.
SWISS-2DPAGE	P45376.
Proteomic databases
PaxDb	P45376.
PRIDE	P45376.
Protocols and materials databases
DNASU	11677.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000102980; ENSMUSP00000100045; ENSMUSG00000001642.
GeneID	11677.
KEGG	mmu:11677.
Organism-specific databases
CTD	11677.
MGI	MGI:1353494. Akr1b3.
Phylogenomic databases
eggNOG	COG0656.
HOGENOM	HOG000250272.
HOVERGEN	HBG000020.
InParanoid	P45376.
KO	K00011.
OMA	QEDHAAI.
OrthoDB	EOG4VMFFR.
Gene expression databases
ArrayExpress	P45376.
Bgee	P45376.
Genevestigator	P45376.
GermOnline	ENSMUSG00000071414. Mus musculus.
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
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:	April 3, 2013
This is version 116 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents