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Q5RJP0 (ALD1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldose reductase-related protein 1

EC=1.1.1.21
Alternative name(s):
Aldehyde reductase
Aldo-keto reductase family 1 member B7
Aldose reductase-like protein AKR1B14
Gene names
Name:Akr1b7
Synonyms:Akr1b14
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. May play a role in the metabolism of xenobiotic aromatic aldehydes. Ref.4

Catalytic activity

Alditol + NAD(P)+ = aldose + NAD(P)H. Ref.4 Ref.5

Enzyme regulation

Inhibited by tolrestat and epalrestat. Ref.4

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the aldo/keto reductase family.

Biophysicochemical properties

Kinetic parameters:

KM=1.5 µM for NADPH Ref.4 Ref.5

KM=220 µM for NADH

KM=0.16 µM for 4-oxo-2-nonenal

KM=37 µM for geraniol

KM=1.5 µM for 4-nitrobenzaldehyde

pH dependence:

Optimum pH is 6.5-7.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316Aldose reductase-related protein 1
PRO_0000415351

Regions

Nucleotide binding20 – 212NADP
Nucleotide binding160 – 1612NADP
Nucleotide binding210 – 2156NADP
Nucleotide binding263 – 2697NADP

Sites

Active site491Proton donor By similarity
Binding site441NADP
Binding site1841NADP
Binding site2731NADP
Site781Lowers pKa of active site Tyr By similarity

Experimental info

Mutagenesis2691H → F or R: Reduced affinity for NADP. Ref.5
Mutagenesis2691H → M: Strongly reduced affinity for NADP. Ref.5

Secondary structure

................................................... 316
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5RJP0 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: E5733ADA0ED5FF21

FASTA31636,122
        10         20         30         40         50         60 
MTTFVKLRTK AKMPLVGLGT WKSPPGQVKE AVKAAIDAGY RHFDCAYVYQ NESEVGEAIQ 

        70         80         90        100        110        120 
EKIKEKAVRR EDLFIVSKLW STFFEKSLMK EAFQKTLSDL KLDYLDLYLI HWPQGLQAGK 

       130        140        150        160        170        180 
EFLPKDSQGK VLMSKSTFLD AWEGMEELVD QGLVKALGVS NFNHFQIERL LNKPGLKHKP 

       190        200        210        220        230        240 
VTNQVECHPY LTQEKLIQYC HSKGIAVIAY SPLGSPDRPY AKPEDPVVLE IPKIKEIAAK 

       250        260        270        280        290        300 
HKKTIAQVLI RFHVQRNVAV IPKSVTLSHI KENIQVFDFQ LSEEDMAAIL SLNRNWRACG 

       310 
LFVTSDEEDF PFHEEY 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[3]"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: Ovary.
[4]"Rat aldose reductase-like protein (AKR1B14) efficiently reduces the lipid peroxidation product 4-oxo-2-nonenal."
Endo S., Matsunaga T., Fujita A., Tajima K., El-Kabbani O., Hara A.
Biol. Pharm. Bull. 33:1886-1890(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[5]"Structure of rat aldose reductase-like protein AKR1B14 holoenzyme: Probing the role of His269 in coenzyme binding by site-directed mutagenesis."
Sundaram K., Dhagat U., Endo S., Chung R., Matsunaga T., Hara A., El-Kabbani O.
Bioorg. Med. Chem. Lett. 21:801-804(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH NADP, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-269.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH473959 Genomic DNA. Translation: EDM15308.1.
BC086563 mRNA. Translation: AAH86563.1.
RefSeqNP_446233.2. NM_053781.2.
UniGeneRn.32702.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3O3RX-ray1.86A/B1-316[»]
3QKZX-ray1.87A/B1-316[»]
ProteinModelPortalQ5RJP0.
SMRQ5RJP0. Positions 1-316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000013423.

Proteomic databases

PaxDbQ5RJP0.
PRIDEQ5RJP0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000013423; ENSRNOP00000013423; ENSRNOG00000009875.
GeneID116463.
KEGGrno:116463.
UCSCRGD:620257. rat.

Organism-specific databases

CTD11997.
RGD620257. Akr1b7.

Phylogenomic databases

eggNOGCOG0656.
GeneTreeENSGT00670000097881.
HOGENOMHOG000250272.
HOVERGENHBG000020.
InParanoidQ5RJP0.
KOK00011.
OMAFQIENIL.
OrthoDBEOG70KGQF.
PhylomeDBQ5RJP0.
TreeFamTF106492.

Gene expression databases

GenevestigatorQ5RJP0.

Family and domain databases

Gene3D3.20.20.100. 1 hit.
InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERPTHR11732. PTHR11732. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFPIRSF000097. AKR. 1 hit.
PRINTSPR00069. ALDKETRDTASE.
SUPFAMSSF51430. SSF51430. 1 hit.
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ5RJP0.
NextBio618984.
PROQ5RJP0.

Entry information

Entry nameALD1_RAT
AccessionPrimary (citable) accession number: Q5RJP0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: December 21, 2004
Last modified: May 14, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references