AKR1C3

Aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II), also known as AKR1C3, is a human gene.cite web | title = Entrez Gene: AKR1C3 aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8644| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: AKR1C3 aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8644| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Lin SX, Shi R, Qiu W, "et al." |title=Structural basis of the multispecificity demonstrated by 17beta-hydroxysteroid dehydrogenase types 1 and 5. |journal=Mol. Cell. Endocrinol. |volume=248 |issue= 1-2 |pages= 38–46 |year= 2006 |pmid= 16480815 |doi= 10.1016/j.mce.2005.11.035
*cite journal | author=Khanna M, Qin KN, Cheng KC |title=Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans. |journal=J. Steroid Biochem. Mol. Biol. |volume=53 |issue= 1-6 |pages= 41–6 |year= 1995 |pmid= 7626489 |doi=
*cite journal | author=Khanna M, Qin KN, Wang RW, Cheng KC |title=Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases. |journal=J. Biol. Chem. |volume=270 |issue= 34 |pages= 20162–8 |year= 1995 |pmid= 7650035 |doi=
*cite journal | author=Nagase T, Miyajima N, Tanaka A, "et al." |title=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. |journal=DNA Res. |volume=2 |issue= 1 |pages= 37–43 |year= 1995 |pmid= 7788527 |doi=
*cite journal | author=Khanna M, Qin KN, Klisak I, "et al." |title=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. |journal=Genomics |volume=25 |issue= 2 |pages= 588–90 |year= 1995 |pmid= 7789999 |doi=
*cite journal | author=Qin KN, New MI, Cheng KC |title=Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. |journal=J. Steroid Biochem. Mol. Biol. |volume=46 |issue= 6 |pages= 673–9 |year= 1994 |pmid= 8274401 |doi=
*cite journal | author=Bennett MJ, Schlegel BP, Jez JM, "et al." |title=Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+. |journal=Biochemistry |volume=35 |issue= 33 |pages= 10702–11 |year= 1996 |pmid= 8718859 |doi= 10.1021/bi9604688
*cite journal | author=Lin HK, Jez JM, Schlegel BP, "et al." |title=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. |journal=Mol. Endocrinol. |volume=11 |issue= 13 |pages= 1971–84 |year= 1998 |pmid= 9415401 |doi=
*cite journal | author=Matsuura K, Shiraishi H, Hara A, "et al." |title=Identification of a principal mRNA species for human 3alpha-hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D2 11-ketoreductase activity. |journal=J. Biochem. |volume=124 |issue= 5 |pages= 940–6 |year= 1999 |pmid= 9792917 |doi=
*cite journal | author=Mills KI, Gilkes AF, Sweeney M, "et al." |title=Identification of a retinoic acid responsive aldoketoreductase expressed in HL60 leukaemic cells. |journal=FEBS Lett. |volume=440 |issue= 1-2 |pages= 158–62 |year= 1999 |pmid= 9862446 |doi=
*cite journal | author=Dufort I, Rheault P, Huang XF, "et al." |title=Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase. |journal=Endocrinology |volume=140 |issue= 2 |pages= 568–74 |year= 1999 |pmid= 9927279 |doi=
*cite journal | author=Rheault P, Dufort I, Soucy P, Luu-The V |title=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. |journal=Cytogenet. Cell Genet. |volume=84 |issue= 3-4 |pages= 241–2 |year= 1999 |pmid= 10393440 |doi=
*cite journal | author=Griffin LD, Mellon SH |title=Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 23 |pages= 13512–7 |year= 1999 |pmid= 10557352 |doi=
*cite journal | author=Suzuki-Yamamoto T, Nishizawa M, Fukui M, "et al." |title=cDNA cloning, expression and characterization of human prostaglandin F synthase. |journal=FEBS Lett. |volume=462 |issue= 3 |pages= 335–40 |year= 2000 |pmid= 10622721 |doi=
*cite journal | author=Nishizawa M, Nakajima T, Yasuda K, "et al." |title=Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. |journal=Genes Cells |volume=5 |issue= 2 |pages= 111–25 |year= 2000 |pmid= 10672042 |doi=
*cite journal | author=Penning TM, Burczynski ME, Jez JM, "et al." |title=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. |journal=Biochem. J. |volume=351 |issue= Pt 1 |pages= 67–77 |year= 2001 |pmid= 10998348 |doi=
*cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=
*cite journal | author=Penning TM, Burczynski ME, Jez JM, "et al." |title=Structure-function aspects and inhibitor design of type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3). |journal=Mol. Cell. Endocrinol. |volume=171 |issue= 1-2 |pages= 137–49 |year= 2001 |pmid= 11165022 |doi=
*cite journal | author=Simpson JC, Wellenreuther R, Poustka A, "et al." |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287–92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899

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