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P16116 (ALDR_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 102. 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):
20-alpha-hydroxysteroid dehydrogenase
Short name=20-alpha-HSD
EC=1.1.1.149
Aldehyde reductase
Gene names
Name:AKR1B1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length315 AA.
Sequence statusComplete.
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.

17-alpha,20-alpha-dihydroxypregn-4-en-3-one + NAD(P)+ = 17-alpha-hydroxyprogesterone + NAD(P)H.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the aldo/keto reductase family.

Sequence caution

The sequence AAA30370.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 315315Aldose reductase
PRO_0000124622

Regions

Nucleotide binding9 – 1810NADP Potential
Nucleotide binding210 – 27263NADP By similarity

Sites

Active site481Proton donor By similarity
Binding site1101Substrate By similarity
Site771Lowers pKa of active site Tyr By similarity

Amino acid modifications

Modified residue11N-acetylalanine Ref.1
Modified residue941N6-acetyllysine By similarity
Modified residue2211N6-acetyllysine By similarity
Modified residue2621N6-acetyllysine By similarity

Natural variations

Natural variant41I → L.
Natural variant61L → I.

Experimental info

Sequence conflict651Q → K in AAA30370. Ref.2
Sequence conflict651Q → K in AAB25333. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P16116 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 18597E7332A3F9C2

FASTA31535,919
        10         20         30         40         50         60 
AHNIVLYTGA KMPILGLGTW KSPPGKVTEA VKVAIDLGYR HIDCAHVYQN ENEVGLALQA 

        70         80         90        100        110        120 
KLQEQVVKRE DLFIVSKLWC TYHDKDLVKG ACQKTLSDLK LDYLDLYLIH WPTGFKPGKD 

       130        140        150        160        170        180 
FFPLDEDGNV IPSEKDFVDT WTAMEELVDE GLVKAIGVSN FNHLQVEKIL NKPGLKYKPA 

       190        200        210        220        230        240 
VNQIECHPYL TQEKLIQYCN SKGIVVTAYS PLGSPDRPWA KPEDPSILED PRIKAIADKY 

       250        260        270        280        290        300 
NKTTAQVLIR FPIQRNLIVI PKSVTPERIA ENFQVFDFEL DKEDMNTLLS YNRDWRACAL 

       310 
VSCASHRDYP FHEEF 

« Hide

References

[1]"Sequence analysis of bovine lens aldose reductase."
Schade S.Z., Early S.L., Williams T.R., Kezdy F.J., Heinrikson R.L., Grimshaw C.E., Doughty C.C.
J. Biol. Chem. 265:3628-3635(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Lens.
[2]"Molecular cloning of testicular 20 alpha-hydroxysteroid dehydrogenase: identity with aldose reductase."
Warren J.C., Murdock G.L., Ma Y., Goodman S.R., Zimmer W.E.
Biochemistry 32:1401-1406(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-315.
Tissue: Testis.
[3]"Isolation and characterization of cDNA clones encoding aldose reductase."
Petrash J.M., Favello A.D.
Curr. Eye Res. 8:1021-1027(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-315.
Tissue: Lens.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31463 mRNA. Translation: AAA30370.1. Different initiation.
S54973 mRNA. Translation: AAB25333.1.
PIRA35452.
UniGeneBt.63116.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GO6model-A1-315[»]
ProteinModelPortalP16116.
SMRP16116. Positions 1-315.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP16116.
ChEMBLCHEMBL3081.

Proteomic databases

PaxDbP16116.
PRIDEP16116.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0656.
HOVERGENHBG000020.
InParanoidP16116.

Enzyme and pathway databases

SABIO-RKP16116.

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...

Entry information

Entry nameALDR_BOVIN
AccessionPrimary (citable) accession number: P16116
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: January 22, 2014
This is version 102 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