AKR1C3
Aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II) | |||||||||||||
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PDB rendering based on 1ry0. | |||||||||||||
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Identifiers | |||||||||||||
Symbols | AKR1C3 ; DD3; HA1753; HAKRB; HAKRe; HSD17B5; KIAA0119; hluPGFS | ||||||||||||
External IDs | Template:OMIM5 Template:MGI HomoloGene: 81636 | ||||||||||||
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RNA expression pattern | |||||||||||||
File:PBB GE AKR1C3 211653 x at tn.png | |||||||||||||
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Species | Human | Mouse | |||||||||||
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RefSeq (protein) | n/a | n/a | |||||||||||
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PubMed search | n/a | n/a |
Aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II), also known as AKR1C3, 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 reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the oxidation of 9alpha,11beta-PGF2 to PGD2. It may play an important role in the pathogenesis of allergic diseases such as asthma, and may also have a role in controlling cell growth and/or differentiation. This gene shares high sequence identity with three other gene members and is clustered with those three genes at chromosome 10p15-p14.[1]
References
Further reading
- Lin SX, Shi R, Qiu W; et al. (2006). "Structural basis of the multispecificity demonstrated by 17beta-hydroxysteroid dehydrogenase types 1 and 5". Mol. Cell. Endocrinol. 248 (1–2): 38–46. doi:10.1016/j.mce.2005.11.035. PMID 16480815.
- 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, Wang RW, Cheng KC (1995). "Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases". J. Biol. Chem. 270 (34): 20162–8. PMID 7650035.
- Nagase T, Miyajima N, Tanaka A; et al. (1995). "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1". DNA Res. 2 (1): 37–43. PMID 7788527.
- 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.
- 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.
- Bennett MJ, Schlegel BP, Jez JM; et al. (1996). "Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+". Biochemistry. 35 (33): 10702–11. doi:10.1021/bi9604688. PMID 8718859.
- Lin HK, Jez JM, Schlegel BP; et al. (1998). "Expression and characterization of recombinant type 2 3 alpha-hydroxysteroid dehydrogenase (HSD) from human prostate: demonstration of bifunctional 3 alpha/17 beta-HSD activity and cellular distribution". Mol. Endocrinol. 11 (13): 1971–84. PMID 9415401.
- Matsuura K, Shiraishi H, Hara A; et al. (1999). "Identification of a principal mRNA species for human 3alpha-hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D2 11-ketoreductase activity". J. Biochem. 124 (5): 940–6. PMID 9792917.
- Mills KI, Gilkes AF, Sweeney M; et al. (1999). "Identification of a retinoic acid responsive aldoketoreductase expressed in HL60 leukaemic cells". FEBS Lett. 440 (1–2): 158–62. PMID 9862446.
- Dufort I, Rheault P, Huang XF; et al. (1999). "Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase". Endocrinology. 140 (2): 568–74. PMID 9927279.
- Rheault P, Dufort I, Soucy P, Luu-The V (1999). "Assignment of HSD17B5 encoding type 5 17 beta-hydroxysteroid dehydrogenase to human chromosome bands 10p15-->p14 and mouse chromosome 13 region A2 by in situ hybridization: identification of a new syntenic relationship". Cytogenet. Cell Genet. 84 (3–4): 241–2. PMID 10393440.
- Griffin LD, Mellon SH (1999). "Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes". Proc. Natl. Acad. Sci. U.S.A. 96 (23): 13512–7. PMID 10557352.
- Suzuki-Yamamoto T, Nishizawa M, Fukui M; et al. (2000). "cDNA cloning, expression and characterization of human prostaglandin F synthase". FEBS Lett. 462 (3): 335–40. PMID 10622721.
- 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.
- Penning TM, Burczynski ME, Jez JM; et al. (2001). "Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones". Biochem. J. 351 (Pt 1): 67–77. PMID 10998348.
- Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. PMID 11076863.
- Penning TM, Burczynski ME, Jez JM; et al. (2001). "Structure-function aspects and inhibitor design of type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3)". Mol. Cell. Endocrinol. 171 (1–2): 137–49. PMID 11165022.
- Simpson JC, Wellenreuther R, Poustka A; et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMID 11256614.
- 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.
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