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P16116

- ALDR_BOVIN

UniProt

P16116 - ALDR_BOVIN

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Protein

Aldose reductase

Gene
AKR1B1
Organism
Bos taurus (Bovine)
Status
Reviewed - 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 donor By similarity
Sitei77 – 771Lowers pKa of active site Tyr By similarity
Binding sitei110 – 1101Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 1810NADP Reviewed prediction
Nucleotide bindingi210 – 27263NADP By similarityAdd
BLAST

GO - Molecular functioni

  1. 17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity Source: UniProtKB-EC
  2. alditol:NADP+ 1-oxidoreductase activity Source: UniProtKB-EC
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: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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-acetyllysine By similarity
Modified residuei221 – 2211N6-acetyllysine By similarity
Modified residuei262 – 2621N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP16116.
PRIDEiP16116.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GO6model-A1-315[»]
ProteinModelPortaliP16116.
SMRiP16116. Positions 1-315.

Family & Domainsi

Sequence similaritiesi

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

AHNIVLYTGA KMPILGLGTW KSPPGKVTEA VKVAIDLGYR HIDCAHVYQN    50
ENEVGLALQA KLQEQVVKRE DLFIVSKLWC TYHDKDLVKG ACQKTLSDLK 100
LDYLDLYLIH WPTGFKPGKD FFPLDEDGNV IPSEKDFVDT WTAMEELVDE 150
GLVKAIGVSN FNHLQVEKIL NKPGLKYKPA VNQIECHPYL TQEKLIQYCN 200
SKGIVVTAYS PLGSPDRPWA KPEDPSILED PRIKAIADKY NKTTAQVLIR 250
FPIQRNLIVI PKSVTPERIA ENFQVFDFEL DKEDMNTLLS YNRDWRACAL 300
VSCASHRDYP FHEEF 315
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.

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651Q → K in AAA30370. 1 Publication
Sequence conflicti65 – 651Q → K in AAB25333. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M31463 mRNA. Translation: AAA30370.1 . Different initiation.
S54973 mRNA. Translation: AAB25333.1 .
PIRi A35452.
UniGenei Bt.63116.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GO6 model - A 1-315 [» ]
ProteinModelPortali P16116.
SMRi P16116. Positions 1-315.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P16116.
ChEMBLi CHEMBL3081.

Proteomic databases

PaxDbi P16116.
PRIDEi P16116.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0656.
HOVERGENi HBG000020.
InParanoidi P16116.

Enzyme and pathway databases

SABIO-RK P16116.

Family and domain databases

Gene3Di 3.20.20.100. 1 hit.
InterProi IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view ]
PANTHERi PTHR11732. PTHR11732. 1 hit.
Pfami PF00248. Aldo_ket_red. 1 hit.
[Graphical view ]
PIRSFi PIRSF000097. AKR. 1 hit.
PRINTSi PR00069. ALDKETRDTASE.
SUPFAMi SSF51430. SSF51430. 1 hit.
PROSITEi PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: January 22, 2014
This is version 102 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

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