AKR7A2

AKR7A2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2BP1

Identifiers

Aliases

AKR7A2, AFAR, AFAR1, AFB1-AR1, AKR7, aldo-keto reductase family 7, member A2, aldo-keto reductase family 7 member A2

External IDs

OMIM: 603418 MGI: 107796 HomoloGene: 2737 GeneCards: AKR7A2

Gene location (Human)

Chr.	Chromosome 1 (human)^[1]

Band	1p36.13	Start	19,303,965 bp^[1]
Band	1p36.13	End	19,312,144 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 4 (mouse)^[2]

Band	4 D3\|4 70.64 cM	Start	139,038,055 bp^[2]
Band	4 D3\|4 70.64 cM	End	139,045,737 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

duodenum

right adrenal gland

right uterine tube

left adrenal gland

jejunal mucosa

kidney

canal of the cervix

right lobe of liver

body of stomach

body of pancreas

Top expressed in

proximal tubule

left lobe of liver

Paneth cell

kidney

internal carotid artery

crypt of lieberkuhn of small intestine

external carotid artery

right ventricle

motor neuron

maxillary prominence

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	alditol:NADP+ 1-oxidoreductase activity electron transfer activity oxidoreductase activity phenanthrene-9,10-epoxide hydrolase activity aldo-keto reductase (NADP) activity protein binding
Cellular component	cytoplasm Golgi apparatus extracellular exosome cytosol
Biological process	xenobiotic metabolic process cellular aldehyde metabolic process daunorubicin metabolic process doxorubicin metabolic process carbohydrate metabolic process electron transport chain
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


8574


110198

Ensembl


ENSG00000053371


ENSMUSG00000028743

UniProt


O43488


Q8CG76

RefSeq (mRNA)


NM_003689 NM_001320979


NM_025337

RefSeq (protein)


NP_001307908 NP_003680


NP_079613

Location (UCSC)

Chr 1: 19.3 – 19.31 Mb

Chr 4: 139.04 – 139.05 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Aflatoxin B1 aldehyde reductase member 2 is an enzyme that in humans is encoded by the AKR7A2 gene.^[5]^[6]

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Transcription

Function

Aldo-keto reductases, such as AKR7A2, are involved in the detoxification of aldehydes and ketones.[supplied by OMIM]^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000053371 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028743 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Ireland LS, Harrison DJ, Neal GE, Hayes JD (Aug 1998). "Molecular cloning, expression and catalytic activity of a human AKR7 member of the aldo-keto reductase superfamily: evidence that the major 2-carboxybenzaldehyde reductase from human liver is a homologue of rat aflatoxin B1-aldehyde reductase". Biochem J. 332 (1): 21–34. doi:10.1042/bj3320021. PMC 1219447. PMID 9576847.
^ ^a ^b "Entrez Gene: AKR7A2 aldo-keto reductase family 7, member A2 (aflatoxin aldehyde reductase)".

External links

Human AKR7A2 genome location and AKR7A2 gene details page in the UCSC Genome Browser.
Overview of all the structural information available in the PDB for UniProt: O43488 (Human Aflatoxin B1 aldehyde reductase member 2 (AKR7A2)) at the PDBe-KB.

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Praml C, Savelyeva L, Perri P, Schwab M (1998). "Cloning of the human aflatoxin B1-aldehyde reductase gene at 1p35-1p36.1 in a region frequently altered in human tumor cells". Cancer Res. 58 (22): 5014–8. PMID 9823300.
Kelly VP, Sherratt PJ, Crouch DH, Hayes JD (2002). "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". Biochem. J. 366 (Pt 3): 847–61. doi:10.1042/BJ20020342. PMC 1222835. PMID 12071861.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Praml C, Savelyeva L, Schwab M (2003). "Aflatoxin B1 aldehyde reductase (AFAR) genes cluster at 1p35-1p36.1 in a region frequently altered in human tumour cells". Oncogene. 22 (30): 4765–73. doi:10.1038/sj.onc.1206684. PMID 12879023.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Jordanova A, Irobi J, Thomas FP, et al. (2006). "Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy". Nat. Genet. 38 (2): 197–202. doi:10.1038/ng1727. PMID 16429158. S2CID 16668375.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.
Lyon RC, Johnston SM, Watson DG, et al. (2007). "Synthesis and catabolism of gamma-hydroxybutyrate in SH-SY5Y human neuroblastoma cells: role of the aldo-keto reductase AKR7A2". J. Biol. Chem. 282 (36): 25986–92. doi:10.1074/jbc.M702465200. PMID 17591773.

v t e PDB gallery
2bp1: STRUCTURE OF THE AFLATOXIN ALDEHYDE REDUCTASE IN COMPLEX WITH NADPH

v t e Oxidoreductases: alcohol oxidoreductases (EC 1.1)
1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Phosphogluconate dehydrogenase Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3β 3β-HSD NSDHL 11β 11β-HSD1 11β-HSD2 17β
1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)
1.1.3: oxygen acceptor	Glucose oxidase L-gulonolactone oxidase Xanthine oxidase Alcohol oxidase
1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)
1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase
1.1.99: other acceptors	Choline dehydrogenase L2HGDH

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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This page was last edited on 11 October 2022, at 13:10

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Transcription

Function

References

External links

Further reading