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P80276 (ALDR_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 106. 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

Short name=AR
EC=1.1.1.21
Alternative name(s):
Aldehyde reductase
Gene names
Name:AKR1B1
Synonyms:ALR2
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 316315Aldose reductase
PRO_0000124625

Regions

Nucleotide binding10 – 1910NADP Potential
Nucleotide binding211 – 27363NADP

Sites

Active site491Proton donor
Binding site1111Substrate
Site781Lowers pKa of active site Tyr By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.2
Modified residue2221N6-acetyllysine By similarity
Modified residue2631N6-acetyllysine By similarity

Experimental info

Sequence conflict991D → N in AAA30989. Ref.1
Sequence conflict991D → N in AAC48515. Ref.1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P80276 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 7218B663AC1B4E92

FASTA31635,868
        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 

« Hide

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.
PIRA59021.
RefSeqNP_001001539.1. NM_001001539.2.
UniGeneSsc.3059.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AH0X-ray2.30A2-316[»]
1AH3X-ray2.30A2-316[»]
1AH4X-ray2.00A2-316[»]
1DLAX-ray3.00A/B/C/D3-316[»]
1EKOX-ray2.20A2-315[»]
ProteinModelPortalP80276.
SMRP80276. Positions 2-316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000017525.

Chemistry

BindingDBP80276.
ChEMBLCHEMBL4559.

Proteomic databases

PaxDbP80276.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000018009; ENSSSCP00000017525; ENSSSCG00000016539.
GeneID396816.
KEGGssc:396816.

Organism-specific databases

CTD231.

Phylogenomic databases

eggNOGCOG0656.
GeneTreeENSGT00670000097881.
HOGENOMHOG000250272.
HOVERGENHBG000020.
KOK00011.
OrthoDBEOG70KGQF.
TreeFamTF106492.

Enzyme and pathway databases

SABIO-RKP80276.

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.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP80276.

Entry information

Entry nameALDR_PIG
AccessionPrimary (citable) accession number: P80276
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 106 of the entry and version 2 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