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Reviewed, UniProtKB/Swiss-Prot P16116 (ALDR_BOVIN)

Last modified June 16, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Aldose reductase
      Short name=AR
    EC=1.1.1.21
Alternative name(s):
    Aldehyde reductase
    20-alpha-hydroxysteroid dehydrogenase
      Short name=20-alpha-HSD
    EC=1.1.1.149
Gene names
Name: AKR1B1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length315 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function20-alpha-hydroxysteroid dehydrogenase activity

Inferred from electronic annotation. Source: EC

aldehyde reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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 residue221Phosphoserine By similarity
Modified residue391Phosphotyrosine 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
P16116-1 [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: 2105951] [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: 8431420] [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: 2515032] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-315.
Tissue: Lens.

Cross-references

Sequence databases

M31463 mRNA. Translation: AAA30370.1. Different initiation.
S54973 mRNA. Translation: AAB25333.1.
IPIIPI00700920.
PIRA35452.
UniGeneBt.63116

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2GO6model-A1-315[»]
SMRP16116. Positions 1-315.
ModBaseSearch...

Genome annotation databases

EnsemblENSBTAG00000009902. Bos taurus. [Contig view]

Phylogenomic databases

HOVERGENP16116.

Enzyme and pathway databases

BRENDA1.1.1.149. 251.
1.1.1.21. 251.

Family and domain databases

InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHERPTHR11732. Aldo/ket_red. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
ProDomPD000288. Aldo/ket_red. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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: June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents