AKR1C1

From Wikipedia, the free encyclopedia

Aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase)

PDB rendering based on 1ihi.

Available structures: 1ihi, 1j96, 1mrq, 1xjb, 2hdj

Identifiers

AKR1C1; C9; 2-ALPHA-HSD; 20-ALPHA-HSD; DD1; DDH; DDH1; H-37; HAKRC; MBAB; MGC8954; DD; AKR1C-pseudo; BABP; DD2; DDH2; HAKRD; HBAB; MCDR2

External IDs

OMIM: 600449 MGI: 1933427 HomoloGene: 84695

Gene ontology
Molecular Function:	• aldo-keto reductase activity • oxidoreductase activity • bile acid binding • 20-alpha-hydroxysteroid dehydrogenase activity • 3-alpha-hydroxysteroid dehydrogenase (B-specific) activity • trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity • 3-alpha-hydroxysteroid dehydrogenase (A-specific) activity
Cellular Component:	• cytosol
Biological Process:	• electron transport • xenobiotic metabolic process • digestion • bile acid metabolic process • bile acid and bile salt transport • cholesterol absorption • cholesterol homeostasis • protein homooligomerization • lipid metabolic process • prostaglandin metabolic process • steroid metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001353 (mRNA)
NP_001344 (protein)

NM_030611 (mRNA)
NP_085114 (protein)

Location

Chr 10: 5.02 - 5.04 Mb

Chr 13: 4.43 - 4.46 Mb

Pubmed search

[1]

[2]

Aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase), also known as AKR1C1, is a human gene.^[1]

This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme catalyzes the reaction of progesterone to the inactive form 20-alpha-hydroxy-progesterone. This gene shares high sequence identity with three other gene members and is clustered with those three genes at chromosome 10p15-p14.^[1]

[edit] References

^ ^a ^b Entrez Gene: AKR1C1 aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase).

[edit] Further reading

Ciaccio PJ, Jaiswal AK, Tew KD (1994). "Regulation of human dihydrodiol dehydrogenase by Michael acceptor xenobiotics.". J. Biol. Chem. 269 (22): 15558–62. PMID 7515059.
Khanna M, Qin KN, Cheng KC (1995). "Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans.". J. Steroid Biochem. Mol. Biol. 53 (1-6): 41–6. PMID 7626489.
Khanna M, Qin KN, Klisak I, et al. (1995). "Localization of multiple human dihydrodiol dehydrogenase (DDH1 and DDH2) and chlordecone reductase (CHDR) genes in chromosome 10 by the polymerase chain reaction and fluorescence in situ hybridization.". Genomics 25 (2): 588–90. PMID 7789999.
Ciaccio PJ, Tew KD (1994). "cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase.". Biochim. Biophys. Acta 1186 (1-2): 129–32. PMID 8011662.
Lou H, Hammond L, Sharma V, et al. (1994). "Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding.". J. Biol. Chem. 269 (11): 8416–22. PMID 8132567.
Deyashiki Y, Ogasawara A, Nakayama T, et al. (1994). "Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder.". Biochem. J. 299 ( Pt 2): 545–52. PMID 8172617.
Qin KN, New MI, Cheng KC (1994). "Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase.". J. Steroid Biochem. Mol. Biol. 46 (6): 673–9. PMID 8274401.
Stolz A, Hammond L, Lou H, et al. (1993). "cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family.". J. Biol. Chem. 268 (14): 10448–57. PMID 8486699.
Hara A, Matsuura K, Tamada Y, et al. (1996). "Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells.". Biochem. J. 313 ( Pt 2): 373–6. PMID 8573067.
O'connor T, Ireland LS, Harrison DJ, Hayes JD (1999). "Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members.". Biochem. J. 343 Pt 2: 487–504. PMID 10510318.
Nishizawa M, Nakajima T, Yasuda K, et al. (2000). "Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes.". Genes Cells 5 (2): 111–25. PMID 10672042.
Zhang Y, Dufort I, Rheault P, Luu-The V (2000). "Characterization of a human 20alpha-hydroxysteroid dehydrogenase.". J. Mol. Endocrinol. 25 (2): 221–8. PMID 11013348.
Nahoum V, Gangloff A, Legrand P, et al. (2001). "Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolution.". J. Biol. Chem. 276 (45): 42091–8. doi:10.1074/jbc.M105610200. PMID 11514561.
Chen CY, Hsu CP, Hsu NY, et al. (2002). "Expression of dihydrodiol dehydrogenase in the resected stage I non-small cell lung cancer.". Oncol. Rep. 9 (3): 515–9. PMID 11956619.
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. doi:10.1073/pnas.242603899. PMID 12477932.
Yang MD, Wu CC, Chiou SH, et al. (2003). "Reduction of dihydrodiol dehydrogenase expression in resected hepatocellular carcinoma.". Oncol. Rep. 10 (2): 271–6. PMID 12579257.
Nakajima T, Yasuda K, Nishizawa M, et al. (2003). "Expression of 20alpha-hydroxysteroid dehydrogenase mRNA in human endometrium and decidua.". Endocr. J. 50 (1): 105–11. PMID 12733716.
Couture JF, Legrand P, Cantin L, et al. (2003). "Human 20alpha-hydroxysteroid dehydrogenase: crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids.". J. Mol. Biol. 331 (3): 593–604. PMID 12899831.
Agapova OA, Yang P, Wang WH, et al. (2003). "Altered expression of 3 alpha-hydroxysteroid dehydrogenases in human glaucomatous optic nerve head astrocytes.". Neurobiol. Dis. 14 (1): 63–73. PMID 13678667.
Deloukas P, Earthrowl ME, Grafham DV, et al. (2004). "The DNA sequence and comparative analysis of human chromosome 10.". Nature 429 (6990): 375–81. doi:10.1038/nature02462. PMID 15164054.