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{{Infobox_gene}}
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'''Aldo-keto reductase family 1 member C1''' also known as '''[[20α-hydroxysteroid dehydrogenase]]''', '''3α-hydroxysteroid dehydrogenase''', and '''dihydrodiol dehydrogenase 1/2''' is an [[enzyme]] that in humans is encoded by the ''AKR1C1'' [[gene]].<ref name="pmid8011662">{{cite journal | vauthors = Ciaccio PJ, Tew KD | title = cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase | journal = Biochimica et Biophysica Acta | volume = 1186 | issue = 1-2 | pages = 129–32 | date = Jun 1994 | pmid = 8011662 | pmc =  | doi = 10.1016/0005-2728(94)90144-9 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: AKR1C1 aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1645| accessdate = }}</ref>
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| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
This gene encodes a member of the [[aldo-keto reductase|aldo/keto reductase superfamily]], which consists of more than 40 known [[enzyme]]s 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 [[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.<ref name="entrez"/>
{{GNF_Protein_box
| image = PBB_Protein_AKR1C1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ihi.
| PDB = {{PDB2|1ihi}}, {{PDB2|1j96}}, {{PDB2|1mrq}}, {{PDB2|1xjb}}, {{PDB2|2hdj}}
| Name = Aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase)
| HGNCid = 384
| Symbol = AKR1C1
| AltSymbols =; C9; 2-ALPHA-HSD; 20-ALPHA-HSD; DD1; DDH; DDH1; H-37; HAKRC; MBAB; MGC8954; DD; AKR1C-pseudo; BABP; DD2; DDH2; HAKRD; HBAB; MCDR2
| OMIM = 600449
| ECnumber = 
| Homologene = 84695
| MGIid = 1933427
| GeneAtlas_image1 = PBB_GE_AKR1C1_204151_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_AKR1C1_209699_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_AKR1C1_211653_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004033 |text = aldo-keto reductase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0032052 |text = bile acid binding}} {{GNF_GO|id=GO:0047006 |text = 20-alpha-hydroxysteroid dehydrogenase activity}} {{GNF_GO|id=GO:0047042 |text = 3-alpha-hydroxysteroid dehydrogenase (B-specific) activity}} {{GNF_GO|id=GO:0047115 |text = trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity}} {{GNF_GO|id=GO:0047026 |text = 3-alpha-hydroxysteroid dehydrogenase (A-specific) activity}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006805 |text = xenobiotic metabolic process}} {{GNF_GO|id=GO:0007586 |text = digestion}} {{GNF_GO|id=GO:0008206 |text = bile acid metabolic process}} {{GNF_GO|id=GO:0015721 |text = bile acid and bile salt transport}} {{GNF_GO|id=GO:0030299 |text = cholesterol absorption}} {{GNF_GO|id=GO:0042632 |text = cholesterol homeostasis}} {{GNF_GO|id=GO:0051260 |text = protein homooligomerization}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006693 |text = prostaglandin metabolic process}} {{GNF_GO|id=GO:0008202 |text = steroid metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1645
    | Hs_Ensembl = ENSG00000151632
    | Hs_RefseqProtein = NP_001344
    | Hs_RefseqmRNA = NM_001353
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 5019967
    | Hs_GenLoc_end = 5036224
    | Hs_Uniprot = P52895
    | Mm_EntrezGene = 83702
    | Mm_Ensembl = ENSMUSG00000021210
    | Mm_RefseqmRNA = NM_030611
    | Mm_RefseqProtein = NP_085114
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 4433607
    | Mm_GenLoc_end = 4456649
    | Mm_Uniprot = Q3UEM0
  }}
}}
'''Aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase)''', also known as '''AKR1C1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AKR1C1 aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1645| accessdate = }}</ref>


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== References ==
{{PBB_Summary
{{reflist}}
| 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 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.<ref name="entrez">{{cite web | title = Entrez Gene: AKR1C1 aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1645| accessdate = }}</ref>
}}


==References==
==External links==
{{reflist|2}}
* {{UCSC gene info|AKR1C1}}
==Further reading==
* {{UCSC gene info|C9}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Ciaccio PJ, Jaiswal AK, Tew KD | title = Regulation of human dihydrodiol dehydrogenase by Michael acceptor xenobiotics | journal = The Journal of Biological Chemistry | volume = 269 | issue = 22 | pages = 15558–62 | date = Jun 1994 | pmid = 7515059 | doi =  }}
| citations =
* {{cite journal | vauthors = 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 = The Journal of Steroid Biochemistry and Molecular Biology | volume = 53 | issue = 1-6 | pages = 41–6 | date = Jun 1995 | pmid = 7626489 | doi = 10.1016/0960-0760(95)00019-V }}
*{{cite journal | author=Ciaccio PJ, Jaiswal AK, Tew KD |title=Regulation of human dihydrodiol dehydrogenase by Michael acceptor xenobiotics. |journal=J. Biol. Chem. |volume=269 |issue= 22 |pages= 15558-62 |year= 1994 |pmid= 7515059 |doi=  }}
* {{cite journal | vauthors = Khanna M, Qin KN, Klisak I, Belkin S, Sparkes RS, Cheng KC | 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 | date = Jan 1995 | pmid = 7789999 | doi = 10.1016/0888-7543(95)80066-U }}
*{{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 | vauthors = Lou H, Hammond L, Sharma V, Sparkes RS, Lusis AJ, Stolz A | title = Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding | journal = The Journal of Biological Chemistry | volume = 269 | issue = 11 | pages = 8416–22 | date = Mar 1994 | pmid = 8132567 | 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 | vauthors = Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A | title = Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder | journal = The Biochemical Journal | volume = 299 | issue = 2 | pages = 545–52 | date = Apr 1994 | pmid = 8172617 | pmc = 1138306 | doi =  10.1042/bj2990545}}
*{{cite journal  | author=Ciaccio PJ, Tew KD |title=cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase. |journal=Biochim. Biophys. Acta |volume=1186 |issue= 1-2 |pages= 129-32 |year= 1994 |pmid= 8011662 |doi=  }}
* {{cite journal | vauthors = Qin KN, New MI, Cheng KC | title = Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 46 | issue = 6 | pages = 673–9 | date = Dec 1993 | pmid = 8274401 | doi = 10.1016/0960-0760(93)90308-J }}
*{{cite journal | author=Lou H, Hammond L, Sharma V, ''et al.'' |title=Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding. |journal=J. Biol. Chem. |volume=269 |issue= 11 |pages= 8416-22 |year= 1994 |pmid= 8132567 |doi=  }}
* {{cite journal | vauthors = Stolz A, Hammond L, Lou H, Takikawa H, Ronk M, Shively JE | title = cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family | journal = The Journal of Biological Chemistry | volume = 268 | issue = 14 | pages = 10448–57 | date = May 1993 | pmid = 8486699 | doi =  }}
*{{cite journal | author=Deyashiki Y, Ogasawara A, Nakayama T, ''et al.'' |title=Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. |journal=Biochem. J. |volume=299 ( Pt 2) |issue= |pages= 545-52 |year= 1994 |pmid= 8172617 |doi=  }}
* {{cite journal | vauthors = Hara A, Matsuura K, Tamada Y, Sato K, Miyabe Y, Deyashiki Y, Ishida N | title = Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells | journal = The Biochemical Journal | volume = 313 | issue = 2 | pages = 373–6 | date = Jan 1996 | pmid = 8573067 | pmc = 1216918 | doi =  10.1042/bj3130373}}
*{{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 | vauthors = O'connor T, Ireland LS, Harrison DJ, Hayes JD | title = 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 | journal = The Biochemical Journal | volume = 343 | issue = 2 | pages = 487–504 | date = Oct 1999 | pmid = 10510318 | pmc = 1220579 | doi = 10.1042/0264-6021:3430487 }}
*{{cite journal | author=Stolz A, Hammond L, Lou H, ''et al.'' |title=cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family. |journal=J. Biol. Chem. |volume=268 |issue= 14 |pages= 10448-57 |year= 1993 |pmid= 8486699 |doi=  }}
* {{cite journal | vauthors = Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S | title = Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes | journal = Genes to Cells | volume = 5 | issue = 2 | pages = 111–25 | date = Feb 2000 | pmid = 10672042 | doi = 10.1046/j.1365-2443.2000.00310.x }}
*{{cite journal | author=Hara A, Matsuura K, Tamada Y, ''et al.'' |title=Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells. |journal=Biochem. J. |volume=313 ( Pt 2) |issue= |pages= 373-6 |year= 1996 |pmid= 8573067 |doi=  }}
* {{cite journal | vauthors = Zhang Y, Dufort I, Rheault P, Luu-The V | title = Characterization of a human 20alpha-hydroxysteroid dehydrogenase | journal = Journal of Molecular Endocrinology | volume = 25 | issue = 2 | pages = 221–8 | date = Oct 2000 | pmid = 11013348 | doi = 10.1677/jme.0.0250221 }}
*{{cite journal | author=O'connor T, Ireland LS, Harrison DJ, Hayes JD |title=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. |journal=Biochem. J. |volume=343 Pt 2 |issue= |pages= 487-504 |year= 1999 |pmid= 10510318 |doi= }}
* {{cite journal | vauthors = Nahoum V, Gangloff A, Legrand P, Zhu DW, Cantin L, Zhorov BS, Luu-The V, Labrie F, Breton R, Lin SX | title = Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolution | journal = The Journal of Biological Chemistry | volume = 276 | issue = 45 | pages = 42091–8 | date = Nov 2001 | pmid = 11514561 | doi = 10.1074/jbc.M105610200 }}
*{{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 | vauthors = Chen CY, Hsu CP, Hsu NY, Shih CS, Lin TY, Chow KC | title = Expression of dihydrodiol dehydrogenase in the resected stage I non-small cell lung cancer | journal = Oncology Reports | volume = 9 | issue = 3 | pages = 515–9 | year = 2002 | pmid = 11956619 | doi = 10.3892/or.9.3.515 }}
*{{cite journal | author=Zhang Y, Dufort I, Rheault P, Luu-The V |title=Characterization of a human 20alpha-hydroxysteroid dehydrogenase. |journal=J. Mol. Endocrinol. |volume=25 |issue= 2 |pages= 221-8 |year= 2000 |pmid= 11013348 |doi= }}
* {{cite journal | vauthors = Yang MD, Wu CC, Chiou SH, Chiu CF, Lin TY, Chiang IP, Chow KC | title = Reduction of dihydrodiol dehydrogenase expression in resected hepatocellular carcinoma | journal = Oncology Reports | volume = 10 | issue = 2 | pages = 271–6 | year = 2003 | pmid = 12579257 | doi = 10.3892/or.10.2.271 }}
*{{cite journal | author=Nahoum V, Gangloff A, Legrand P, ''et al.'' |title=Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolution. |journal=J. Biol. Chem. |volume=276 |issue= 45 |pages= 42091-8 |year= 2001 |pmid= 11514561 |doi= 10.1074/jbc.M105610200 }}
* {{cite journal | vauthors = Nakajima T, Yasuda K, Nishizawa M, Okada H, Yoshimura T, Ito S, Kanzaki H | title = Expression of 20alpha-hydroxysteroid dehydrogenase mRNA in human endometrium and decidua | journal = Endocrine Journal | volume = 50 | issue = 1 | pages = 105–11 | date = Feb 2003 | pmid = 12733716 | doi = 10.1507/endocrj.50.105 }}
*{{cite journal | author=Chen CY, Hsu CP, Hsu NY, ''et al.'' |title=Expression of dihydrodiol dehydrogenase in the resected stage I non-small cell lung cancer. |journal=Oncol. Rep. |volume=9 |issue= 3 |pages= 515-9 |year= 2002 |pmid= 11956619 |doi= }}
* {{cite journal | vauthors = Couture JF, Legrand P, Cantin L, Luu-The V, Labrie F, Breton R | title = Human 20alpha-hydroxysteroid dehydrogenase: crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids | journal = Journal of Molecular Biology | volume = 331 | issue = 3 | pages = 593–604 | date = Aug 2003 | pmid = 12899831 | doi = 10.1016/S0022-2836(03)00762-9 }}
*{{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 }}
* {{cite journal | vauthors = Agapova OA, Yang P, Wang WH, Lane DA, Clark AF, Weinstein BI, Hernandez MR | title = Altered expression of 3 alpha-hydroxysteroid dehydrogenases in human glaucomatous optic nerve head astrocytes | journal = Neurobiology of Disease | volume = 14 | issue = 1 | pages = 63–73 | date = Oct 2003 | pmid = 13678667 | doi = 10.1016/S0969-9961(03)00101-3 }}
*{{cite journal | author=Yang MD, Wu CC, Chiou SH, ''et al.'' |title=Reduction of dihydrodiol dehydrogenase expression in resected hepatocellular carcinoma. |journal=Oncol. Rep. |volume=10 |issue= 2 |pages= 271-6 |year= 2003 |pmid= 12579257 |doi= }}
*{{cite journal | author=Nakajima T, Yasuda K, Nishizawa M, ''et al.'' |title=Expression of 20alpha-hydroxysteroid dehydrogenase mRNA in human endometrium and decidua. |journal=Endocr. J. |volume=50 |issue= 1 |pages= 105-11 |year= 2003 |pmid= 12733716 |doi= }}
*{{cite journal | author=Couture JF, Legrand P, Cantin L, ''et al.'' |title=Human 20alpha-hydroxysteroid dehydrogenase: crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids. |journal=J. Mol. Biol. |volume=331 |issue= 3 |pages= 593-604 |year= 2003 |pmid= 12899831 |doi= }}
*{{cite journal | author=Agapova OA, Yang P, Wang WH, ''et al.'' |title=Altered expression of 3 alpha-hydroxysteroid dehydrogenases in human glaucomatous optic nerve head astrocytes. |journal=Neurobiol. Dis. |volume=14 |issue= 1 |pages= 63-73 |year= 2003 |pmid= 13678667 |doi= }}
*{{cite journal  | author=Deloukas P, Earthrowl ME, Grafham DV, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 10. |journal=Nature |volume=429 |issue= 6990 |pages= 375-81 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462 }}
}}
{{refend}}
{{refend}}


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Revision as of 17:55, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Aldo-keto reductase family 1 member C1 also known as 20α-hydroxysteroid dehydrogenase, 3α-hydroxysteroid dehydrogenase, and dihydrodiol dehydrogenase 1/2 is an enzyme that in humans is encoded by the AKR1C1 gene.[1][2]

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 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.[2]

References

  1. ↑ Ciaccio PJ, Tew KD (Jun 1994). "cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase". Biochimica et Biophysica Acta. 1186 (1–2): 129–32. doi:10.1016/0005-2728(94)90144-9. PMID 8011662.
  2. ↑ 2.0 2.1 "Entrez Gene: AKR1C1 aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase)".

External links

Further reading


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