Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aflatoxin B1 aldehyde reductase member 3

Gene

Akr7a3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. Probably involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei40 – 401NADP1 Publication
Active sitei45 – 451Proton donor
Sitei73 – 731Lowers pKa of active site TyrBy similarity
Binding sitei109 – 1091Substrate1 Publication
Binding sitei165 – 1651NADP1 Publication
Binding sitei218 – 2181NADP1 Publication
Binding sitei228 – 2281Substrate1 Publication
Binding sitei231 – 2311Substrate1 Publication
Binding sitei327 – 3271NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi139 – 1402NADP1 Publication
Nucleotide bindingi194 – 20411NADP1 PublicationAdd
BLAST
Nucleotide bindingi286 – 2949NADP1 Publication

GO - Molecular functioni

  • alditol:NADP+ 1-oxidoreductase activity Source: RGD
  • aldo-keto reductase (NADP) activity Source: RGD

GO - Biological processi

  • aflatoxin catabolic process Source: RGD
  • aflatoxin metabolic process Source: RGD
  • response to toxic substance Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Detoxification

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

SABIO-RKP38918.

Names & Taxonomyi

Protein namesi
Recommended name:
Aflatoxin B1 aldehyde reductase member 3 (EC:1.-.-.-)
Short name:
AFB1-AR
Alternative name(s):
Aflatoxin B1 aldehyde reductase member 1
Short name:
rAFAR1
Gene namesi
Name:Akr7a3
Synonyms:Afar, Akr7a1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi628635. Akr7a3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2697.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327Aflatoxin B1 aldehyde reductase member 3PRO_0000070374Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP38918.
PRIDEiP38918.

PTM databases

iPTMnetiP38918.
PhosphoSiteiP38918.

Expressioni

Inductioni

By the phenolic antioxidant ethoxyquin.

Gene expression databases

GenevisibleiP38918. RN.

Interactioni

Subunit structurei

Homodimer. Heterodimer with AKR7A2.2 Publications

Protein-protein interaction databases

MINTiMINT-4564936.
STRINGi10116.ENSRNOP00000024160.

Structurei

Secondary structure

1
327
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115Combined sources
Turni16 – 183Combined sources
Helixi21 – 3313Combined sources
Beta strandi38 – 403Combined sources
Helixi45 – 484Combined sources
Helixi49 – 546Combined sources
Beta strandi68 – 747Combined sources
Helixi84 – 9714Combined sources
Beta strandi103 – 1086Combined sources
Helixi117 – 12913Combined sources
Beta strandi132 – 1409Combined sources
Helixi143 – 15614Combined sources
Beta strandi161 – 1677Combined sources
Helixi174 – 1763Combined sources
Helixi179 – 1868Combined sources
Beta strandi189 – 1935Combined sources
Helixi197 – 2026Combined sources
Helixi207 – 2115Combined sources
Beta strandi216 – 2216Combined sources
Helixi225 – 2328Combined sources
Helixi235 – 25218Combined sources
Helixi259 – 26911Combined sources
Helixi275 – 2773Combined sources
Beta strandi280 – 2834Combined sources
Helixi288 – 29710Combined sources
Helixi305 – 31814Combined sources
Helixi319 – 3213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GVEX-ray1.38A/B1-327[»]
ProteinModelPortaliP38918.
SMRiP38918. Positions 4-327.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38918.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IDYD. Eukaryota.
COG0667. LUCA.
GeneTreeiENSGT00550000074567.
HOGENOMiHOG000250286.
HOVERGENiHBG050576.
InParanoidiP38918.
KOiK15303.
OMAiNGLHRAV.
OrthoDBiEOG77127F.
PhylomeDBiP38918.
TreeFamiTF329173.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.

Sequencei

Sequence statusi: Complete.

P38918-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQARPATVL GAMEMGRRMD VTSSSASVRA FLQRGHTEID TAFVYANGQS
60 70 80 90 100
ETILGDLGLG LGRSGCKVKI ATKAAPMFGK TLKPADVRFQ LETSLKRLQC
110 120 130 140 150
PRVDLFYLHF PDHGTPIEET LQACHQLHQE GKFVELGLSN YVSWEVAEIC
160 170 180 190 200
TLCKKNGWIM PTVYQGMYNA ITRQVETELF PCLRHFGLRF YAFNPLAGGL
210 220 230 240 250
LTGRYKYQDK DGKNPESRFF GNPFSQLYMD RYWKEEHFNG IALVEKALKT
260 270 280 290 300
TYGPTAPSMI SAAVRWMYHH SQLKGTQGDA VILGMSSLEQ LEQNLALVEE
310 320
GPLEPAVVDA FDQAWNLVAH ECPNYFR
Length:327
Mass (Da):36,747
Last modified:December 15, 2003 - v2
Checksum:iF0C908C014DF672D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti126 – 1272QL → HV in CAA52740 (PubMed:8234296).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74673 mRNA. Translation: CAA52740.1.
AF045464 mRNA. Translation: AAD02413.1.
AY230497
, AY230491, AY230492, AY230493, AY230494, AY230495, AY230496 Genomic DNA. Translation: AAO48423.1.
BC078872 mRNA. Translation: AAH78872.2.
BC089811 mRNA. Translation: AAH89811.1.
PIRiA48804.
RefSeqiNP_037347.1. NM_013215.1.
UniGeneiRn.6043.

Genome annotation databases

EnsembliENSRNOT00000024160; ENSRNOP00000024160; ENSRNOG00000017899.
GeneIDi26760.
KEGGirno:26760.
UCSCiRGD:628635. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74673 mRNA. Translation: CAA52740.1.
AF045464 mRNA. Translation: AAD02413.1.
AY230497
, AY230491, AY230492, AY230493, AY230494, AY230495, AY230496 Genomic DNA. Translation: AAO48423.1.
BC078872 mRNA. Translation: AAH78872.2.
BC089811 mRNA. Translation: AAH89811.1.
PIRiA48804.
RefSeqiNP_037347.1. NM_013215.1.
UniGeneiRn.6043.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GVEX-ray1.38A/B1-327[»]
ProteinModelPortaliP38918.
SMRiP38918. Positions 4-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4564936.
STRINGi10116.ENSRNOP00000024160.

Chemistry

ChEMBLiCHEMBL2697.

PTM databases

iPTMnetiP38918.
PhosphoSiteiP38918.

Proteomic databases

PaxDbiP38918.
PRIDEiP38918.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000024160; ENSRNOP00000024160; ENSRNOG00000017899.
GeneIDi26760.
KEGGirno:26760.
UCSCiRGD:628635. rat.

Organism-specific databases

CTDi22977.
RGDi628635. Akr7a3.

Phylogenomic databases

eggNOGiENOG410IDYD. Eukaryota.
COG0667. LUCA.
GeneTreeiENSGT00550000074567.
HOGENOMiHOG000250286.
HOVERGENiHBG050576.
InParanoidiP38918.
KOiK15303.
OMAiNGLHRAV.
OrthoDBiEOG77127F.
PhylomeDBiP38918.
TreeFamiTF329173.

Enzyme and pathway databases

SABIO-RKP38918.

Miscellaneous databases

EvolutionaryTraceiP38918.
NextBioi608018.
PROiP38918.

Gene expression databases

GenevisibleiP38918. RN.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An ethoxyquin-inducible aldehyde reductase from rat liver that metabolizes aflatoxin B1 defines a subfamily of aldo-keto reductases."
    Ellis E.M., Judah D.J., Neal G.E., Hayes J.D.
    Proc. Natl. Acad. Sci. U.S.A. 90:10350-10354(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Fischer 344.
    Tissue: Liver.
  2. "cDNA cloning, expression and activity of a second human aflatoxin B1-metabolizing member of the aldo-keto reductase superfamily, AKR7A3."
    Knight L.P., Primiano T., Groopman J.D., Kensler T.W., Sutter T.R.
    Carcinogenesis 20:1215-1223(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Strain: Fischer 344.
    Tissue: Liver.
  3. "Characterization of the rat aflatoxin B1 aldehyde reductase gene, AKR7A1. Structure and chromosomal localization of AKR7A1 as well as identification of antioxidant response elements in the gene promoter."
    Ellis E.M., Slattery C.M., Hayes J.D.
    Carcinogenesis 24:727-737(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Fischer 344.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  5. Raymackers J., Anderson L.
    Submitted (NOV-1994) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 6-17; 89-97; 156-184; 232-246 AND 250-274.
    Tissue: Liver.
  6. "Resistance to aflatoxin B1 is associated with the expression of a novel aldo-keto reductase which has catalytic activity towards a cytotoxic aldehyde-containing metabolite of the toxin."
    Hayes J.D., Judah D.J., Neal G.E.
    Cancer Res. 53:3887-3894(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  7. "Novel homodimeric and heterodimeric rat gamma-hydroxybutyrate synthases that associate with the Golgi apparatus define a distinct subclass of aldo-keto reductase 7 family proteins."
    Kelly V.P., Sherratt P.J., Crouch D.H., Hayes J.D.
    Biochem. J. 366:847-861(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  8. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "The crystal structure of rat liver AKR7A1. A dimeric member of the aldo-keto reductase superfamily."
    Kozma E., Brown E., Ellis E.M., Lapthorn A.J.
    J. Biol. Chem. 277:16285-16293(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) IN COMPLEX WITH NADP AND CITRATE, SUBUNIT.

Entry informationi

Entry nameiARK73_RAT
AccessioniPrimary (citable) accession number: P38918
Secondary accession number(s): Q5EBB7, Q68FZ3, Q9QX16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: December 15, 2003
Last modified: February 17, 2016
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

With succinic semialdehyde or 4-nitrobenzaldehyde as substrate, it exhibits a substantially greater specic activity whit NADPH than with NADH Conversely, it has a 3-fold higher activity towards 2-carboxybenzaldehyde with NADH than with NADPH.

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

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 one 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.