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Showing Protein Aldo-keto reductase family 1 member C1 (HMDBP00386)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 26 metabolites
Identification
HMDB Protein ID HMDBP00386
Secondary Accession Numbers
  • 5623
  • HMDBP04812
Name Aldo-keto reductase family 1 member C1
Synonyms
  1. 20-alpha-HSD
  2. 20-alpha-hydroxysteroid dehydrogenase
  3. Chlordecone reductase homolog HAKRC
  4. DD1/DD2
  5. Dihydrodiol dehydrogenase 1/2
  6. HBAB
  7. High-affinity hepatic bile acid-binding protein
  8. Indanol dehydrogenase
  9. Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
Gene Name AKR1C1
Protein Type Unknown
Biological Properties
General Function Involved in oxidoreductase activity
Specific Function Converts progesterone to its inactive form, 20-alpha-dihydroxyprogesterone (20-alpha-OHP). In the liver and intestine, may have a role in the transport of bile. May have a role in monitoring the intrahepatic bile acid concentration. Has a low bile-binding ability. May play a role in myelin formation.
Pathways
  • Metabolism of xenobiotics by cytochrome P450
  • Steroid hormone biosynthesis
Reactions
17alpha,20alpha-Dihydroxypregn-4-en-3-one + NAD(P)(+) → 17-Hydroxyprogesterone + NAD(P)H details
trans-1,2-Dihydrobenzene-1,2-diol + NADP → Pyrocatechol + NADPH details
Indan-1-ol + NAD(P)(+) → Indanone + NAD(P)H details
5alpha-Dihydrodeoxycorticosterone + NADPH + Hydrogen Ion → Tetrahydrodeoxycorticosterone + NADP details
5a-Pregnane-3,20-dione + NADPH + Hydrogen Ion → Allopregnanolone + NADP details
5alpha-Pregnan-20alpha-ol-3-one + NADPH + Hydrogen Ion → 5alpha-Pregnane-3alpha,20alpha-diol + NADP details
GO Classification
Biological Process
daunorubicin metabolic process
doxorubicin metabolic process
xenobiotic metabolic process
bile acid and bile salt transport
bile acid metabolic process
cellular response to jasmonic acid stimulus
intestinal cholesterol absorption
progesterone metabolic process
protein homooligomerization
response to organophosphorus
retinal metabolic process
cholesterol homeostasis
Cellular Component
cytosol
Function
catalytic activity
oxidoreductase activity
Molecular Function
alditol:NADP+ 1-oxidoreductase activity
indanol dehydrogenase activity
17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity
androsterone dehydrogenase (B-specific) activity
bile acid binding
ketosteroid monooxygenase activity
oxidoreductase activity, acting on NADH or NADPH, quinone or similar compound as acceptor
phenanthrene 9,10-monooxygenase activity
trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity
Process
metabolic process
oxidation reduction
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 10
Locus 10p15-p14
SNPs AKR1C1
Gene Sequence 
>972 bp
ATGGATTCGAAATATCAGTGTGTGAAGCTGAATGATGGTCACTTCATGCCTGTCCTGGGA
TTTGGCACCTATGCGCCTGCAGAGGTTCCTAAAAGTAAAGCTTTAGAGGCCACCAAATTG
GCAATTGAAGCTGGCTTCCGCCATATTGATTCTGCTCATTTATACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGTGCAATTCCCATCGACCAGAGTTGGTCCGACCAGCCTTGGAA
AGGTCACTGAAAAATCTTCAATTGGATTATGTTGACCTCTACCTTATTCATTTTCCAGTG
TCTGTAAAGCCAGGTGAGGAAGTGATCCCAAAAGATGAAAATGGAAAAATACTATTTGAC
ACAGTGGATCTCTGTGCCACGTGGGAGGCCGTGGAGAAGTGTAAAGATGCAGGATTGGCC
AAGTCCATCGGGGTGTCCAACTTCAACCGCAGGCAGCTGGAGATGATCCTCAACAAGCCA
GGGCTCAAGTACAAGCCTGTCTGCAACCAGGTGGAATGTCATCCTTACTTCAACCAGAGA
AAACTGCTGGATTTCTGCAAGTCAAAAGACATTGTTCTGGTTGCCTATAGTGCTCTGGGA
TCCCACCGAGAAGAACCATGGGTGGACCCGAACTCCCCGGTGCTCTTGGAGGACCCAGTC
CTTTGTGCCTTGGCAAAAAAGCACAAGCGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTACAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGCATCAGACAGAAC
GTGCAGGTGTTTGAATTCCAGTTGACTTCAGAGGAGATGAAAGCCATAGATGGCCTAAAC
AGAAATGTGCGATATTTGACCCTTGATATTTTTGCTGGCCCCCCTAATTATCCATTTTCT
GATGAATATTAA
Protein Properties
Number of Residues 323
Molecular Weight 36788.02
Theoretical pI 7.891
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Aldo-keto reductase family 1 member C1
MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV
SVKPGEEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQLEMILNKP
GLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN
RNVRYLTLDIFAGPPNYPFSDEY
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q04828
UniProtKB/Swiss-Prot Entry Name AK1C1_HUMAN
PDB IDs
GenBank Gene ID M86609
GeneCard ID AKR1C1
GenAtlas ID AKR1C1
HGNC ID HGNC:384
References
General References
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  3. Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed:8274401 ]
  4. Khanna M, Qin KN, Cheng KC: 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. 1995 Jun;53(1-6):41-6. [PubMed:7626489 ]
  5. Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed:10672042 ]
  6. Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A: Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. Biochem J. 1994 Apr 15;299 ( Pt 2):545-52. [PubMed:8172617 ]
  7. Stolz A, Hammond L, Lou H, Takikawa H, Ronk M, Shively JE: cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family. J Biol Chem. 1993 May 15;268(14):10448-57. [PubMed:8486699 ]
  8. Lou H, Hammond L, Sharma V, Sparkes RS, Lusis AJ, Stolz A: Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding. J Biol Chem. 1994 Mar 18;269(11):8416-22. [PubMed:8132567 ]
  9. Ciaccio PJ, Jaiswal AK, Tew KD: Regulation of human dihydrodiol dehydrogenase by Michael acceptor xenobiotics. J Biol Chem. 1994 Jun 3;269(22):15558-62. [PubMed:7515059 ]
  10. Zhang Y, Dufort I, Rheault P, Luu-The V: Characterization of a human 20alpha-hydroxysteroid dehydrogenase. J Mol Endocrinol. 2000 Oct;25(2):221-8. [PubMed:11013348 ]
  11. Hara A, Matsuura K, Tamada Y, Sato K, Miyabe Y, Deyashiki Y, Ishida N: Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells. Biochem J. 1996 Jan 15;313 ( Pt 2):373-6. [PubMed:8573067 ]
  12. Couture JF, Legrand P, Cantin L, Luu-The V, Labrie F, Breton R: 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. 2003 Aug 15;331(3):593-604. [PubMed:12899831 ]