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Aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II)

PDB rendering based on 1ry0.
Available structures
1ry0, 1ry8, 1s1p, 1s1r, 1s2a, 1s2c, 1xf0, 1zq5, 2f38, 2fgb
Identifiers
Symbols AKR1C3; DD3; HA1753; HAKRB; HAKRe; HSD17B5; KIAA0119; hluPGFS
External IDs OMIM603966 MGI2145420 HomoloGene81636 GeneCards: AKR1C3 Gene
RNA expression pattern
PBB GE AKR1C3 209160 at tn.png
PBB GE AKR1C3 211653 x at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 8644 105349
Ensembl ENSG00000196139 ENSMUSG00000021214
UniProt P42330 Q3U538
RefSeq (mRNA) NM_003739 NM_134066
RefSeq (protein) NP_003730 NP_598827
Location (UCSC) Chr 10:
5.13 - 5.14 Mb
Chr 13:
4.13 - 4.15 Mb
PubMed search [1] [2]

Aldo-keto reductase family 1 member C3 is an enzyme that in humans is encoded by the AKR1C3 gene.[1][2][3]

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.[3]

References

  1. ^ Khanna M, Qin KN, Wang RW, Cheng KC (Sep 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.  
  2. ^ Matsuura K, Shiraishi H, Hara A, Sato K, Deyashiki Y, Ninomiya M, Sakai S (Feb 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.  
  3. ^ a b "Entrez Gene: AKR1C3 aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8644.  

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. doi:10.1016/0960-0760(95)00019-V. PMID 7626489.  
  • 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. doi:10.1093/dnares/2.1.37. 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. doi:10.1016/0888-7543(95)80066-U. 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. doi:10.1016/0960-0760(93)90308-J. 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. doi:10.1210/me.11.13.1971. PMID 9415401.  
  • 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. doi:10.1016/S0014-5793(98)01435-5. 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. doi:10.1210/en.140.2.568. 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. doi:10.1159/000015267. 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. doi:10.1073/pnas.96.23.13512. 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. doi:10.1016/S0014-5793(99)01551-3. 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. doi:10.1046/j.1365-2443.2000.00310.x. 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. doi:10.1042/0264-6021:3510067. PMID 10998348.  
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. 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. doi:10.1016/S0303-7207(00)00426-3. 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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