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Protein

Aldose reductase

Gene

AKR1B1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei48 – 481Proton donorBy similarity
Sitei77 – 771Lowers pKa of active site TyrBy similarity
Binding sitei110 – 1101SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 1810NADPSequence Analysis
Nucleotide bindingi210 – 27263NADPBy similarityAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

SABIO-RKP16116.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldose reductase (EC:1.1.1.21)
Short name:
AR
Alternative name(s):
20-alpha-hydroxysteroid dehydrogenase (EC:1.1.1.149)
Short name:
20-alpha-HSD
Aldehyde reductase
Gene namesi
Name:AKR1B1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 315315Aldose reductasePRO_0000124622Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylalanine1 Publication
Modified residuei94 – 941N6-acetyllysineBy similarity
Modified residuei221 – 2211N6-acetyllysineBy similarity
Modified residuei262 – 2621N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP16116.
PRIDEiP16116.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000013082.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GO6model-A1-315[»]
ProteinModelPortaliP16116.
SMRiP16116. Positions 1-315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiCOG0656.
HOVERGENiHBG000020.
InParanoidiP16116.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16116-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AHNIVLYTGA KMPILGLGTW KSPPGKVTEA VKVAIDLGYR HIDCAHVYQN
60 70 80 90 100
ENEVGLALQA KLQEQVVKRE DLFIVSKLWC TYHDKDLVKG ACQKTLSDLK
110 120 130 140 150
LDYLDLYLIH WPTGFKPGKD FFPLDEDGNV IPSEKDFVDT WTAMEELVDE
160 170 180 190 200
GLVKAIGVSN FNHLQVEKIL NKPGLKYKPA VNQIECHPYL TQEKLIQYCN
210 220 230 240 250
SKGIVVTAYS PLGSPDRPWA KPEDPSILED PRIKAIADKY NKTTAQVLIR
260 270 280 290 300
FPIQRNLIVI PKSVTPERIA ENFQVFDFEL DKEDMNTLLS YNRDWRACAL
310
VSCASHRDYP FHEEF
Length:315
Mass (Da):35,919
Last modified:April 1, 1990 - v1
Checksum:i18597E7332A3F9C2
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651Q → K in AAA30370 (PubMed:8431420).Curated
Sequence conflicti65 – 651Q → K in AAB25333 (PubMed:8431420).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41I → L.
Natural varianti6 – 61L → I.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31463 mRNA. Translation: AAA30370.1. Different initiation.
S54973 mRNA. Translation: AAB25333.1.
PIRiA35452.
UniGeneiBt.63116.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31463 mRNA. Translation: AAA30370.1. Different initiation.
S54973 mRNA. Translation: AAB25333.1.
PIRiA35452.
UniGeneiBt.63116.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GO6model-A1-315[»]
ProteinModelPortaliP16116.
SMRiP16116. Positions 1-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000013082.

Chemistry

BindingDBiP16116.
ChEMBLiCHEMBL3081.

Proteomic databases

PaxDbiP16116.
PRIDEiP16116.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG0656.
HOVERGENiHBG000020.
InParanoidiP16116.

Enzyme and pathway databases

SABIO-RKP16116.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiALDR_BOVIN
AccessioniPrimary (citable) accession number: P16116
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 24, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.