Gene Symbol | Akr1c21 |
Entrez Gene ID | 77337 |
Full Name | aldo-keto reductase family 1, member C21 |
Synonyms | 9430025F20Rik,AI315367 |
General protein information |
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Gene Type | protein-coding |
Organism | Mus musculus(house mouse) |
Genome |
ORF » Species Summary » Mus musculus » Akr1c21 cDNA ORF clone
gRNAs
Gene Symbol | Akr1c21 |
Entrez Gene ID | 77337 |
Full Name | aldo-keto reductase family 1, member C21 |
Synonyms | 9430025F20Rik,AI315367 |
General protein information |
|
Gene Type | protein-coding |
Organism | Mus musculus(house mouse) |
Genome |
mRNA | Protein | Name |
---|---|---|
NM_029901.2 | NP_084177.2 | aldo-keto reductase family 1 member C21 |
Homo sapiens (human) | AKR1C1 | NP_001344.2 |
Arabidopsis thaliana (thale cress) | AT1G59950 | NP_176203.1 |
Rattus norvegicus (Norway rat) | Akr1c2 | NP_001013075.1 |
Arabidopsis thaliana (thale cress) | AT1G59960 | NP_176204.1 |
Homo sapiens (human) | AKR1C2 | NP_995317.1 |
Mus musculus (house mouse) | Akr1c21 | NP_084177.2 |
AKR1C4 | XP_001104300.1 | |
Pan troglodytes (chimpanzee) | AKR1C1 | XP_003951630.1 |
Studies on a Tyr residue critical for the binding of coenzyme and substrate in mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21): structure of the Y224D mutant enzyme.
Dhagat U, Endo S, Mamiya H, Hara A, El-Kabbani O
Acta crystallographica. Section D, Biological crystallography66(Pt 2)198-204(2010 Feb)
Structure of the G225P/G226P mutant of mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) ternary complex: implications for the binding of inhibitor and substrate.
Dhagat U, Endo S, Mamiya H, Hara A, El-Kabbani O
Acta crystallographica. Section D, Biological crystallography65(Pt 3)257-65(2009 Mar)
Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto reductases: identification and characterization of amino acid residues critical for substrate binding.
Faucher F, Cantin L, Pereira de J?sus-Tran K, Lemieux M, Luu-The V, Labrie F, Breton R
Journal of molecular biology369(2)525-40(2007 Jun)
Crystal structures of mouse 17alpha-hydroxysteroid dehydrogenase (apoenzyme and enzyme-NADP(H) binary complex): identification of molecular determinants responsible for the unique 17alpha-reductive activity of this enzyme.
Faucher F, Pereira de J?sus-Tran K, Cantin L, Luu-The V, Labrie F, Breton R
Journal of molecular biology364(4)747-63(2006 Dec)
Crystallization and preliminary X-ray diffraction analysis of mouse 3(17)alpha-hydroxysteroid dehydrogenase.
El-Kabbani O, Ishikura S, Wagner A, Schulze-Briese C, Hara A
Acta crystallographica. Section F, Structural biology and crystallization communications61(Pt 7)688-90(2005 Jul)
GeneRIFs: Gene References Into Functions What's a GeneRIF?
mutation resulted in a change in the conformation of the flexible loop B, including the V-shaped groove, which is a unique feature of the active-site architecture of wild-type AKR1C21 and is formed by the side chains of Tyr224 and Trp227.
Title: Studies on a Tyr residue critical for the binding of coenzyme and substrate in mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21): structure of the Y224D mutant enzyme.
Gly225 & Gly226 help determine the substrate stereospecificity. The G225P/G226P mutation reduced the affinity for both 3alpha- & 17alpha-hydroxysteroid substrates by up to 160-fold, indicating that these residues are critical for substrate binding.
Title: Structure of the G225P/G226P mutant of mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) ternary complex: implications for the binding of inhibitor and substrate.
study reports a ternary complex crystal structure (m17alpha-HSD:NADP(+):epi-T) determined at 1.85 A resolution reveals a unique steroid-binding mode for an AKR enzyme
Title: Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto reductases: identification and characterization of amino acid residues critical for substrate binding.
crystal structure of the m17alpha-HSD enzyme in its apo-form (1.9 A resolution) as well as those of two different forms of this enzyme in binary complex with NADP(H) (2.9 A and 1.35 A resolution)(
Title: Crystal structures of mouse 17alpha-hydroxysteroid dehydrogenase (apoenzyme and enzyme-NADP(H) binary complex): identification of molecular determinants responsible for the unique 17alpha-reductive activity of this enzyme.
X-ray diffraction analysis of mouse 3(17)alpha-hydroxysteroid dehydrogenase
Title: Crystallization and preliminary X-ray diffraction analysis of mouse 3(17)alpha-hydroxysteroid dehydrogenase.
The following Akr1c21 gene cDNA ORF clone sequences were retrieved from the NCBI Reference Sequence Database (RefSeq). These sequences represent the protein coding region of the Akr1c21 cDNA ORF which is encoded by the open reading frame (ORF) sequence. ORF sequences can be delivered in our standard vector, pcDNA3.1+/C-(K)DYK or the vector of your choice as an expression/transfection-ready ORF clone. Not the clone you want? Click here to find your clone.
CloneID | OMu07654 | |
Clone ID Related Accession (Same CDS sequence) | NM_029901.2 | |
Accession Version | NM_029901.2 Latest version! | Documents for ORF clone product in default vector |
Sequence Information | ORF Nucleotide Sequence (Length: 972bp) Protein sequence SNP |
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Vector | pcDNA3.1-C-(k)DYK or customized vector | ![]() |
Clone information | Clone Map | ![]() |
Tag on pcDNA3.1+/C-(K)DYK | C terminal DYKDDDDK tags | |
ORF Insert Method | CloneEZ™ Seamless cloning technology | |
Insert Structure | linear | |
Update Date | 2019-12-26 | |
Organism | Mus musculus(house mouse) | |
Product | aldo-keto reductase family 1 member C21 | |
Comment | Comment: VALIDATED REFSEQ: This record has undergone validation or preliminary review. The reference sequence was derived from BY721648.1, AY742217.1, AI882115.1 and AI035317.1. On Feb 23, 2007 this sequence version replaced NM_029901.1. ##Evidence-Data-START## Transcript exon combination :: AK020439.1, BC061057.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMN00849385 [ECO:0000348] ##Evidence-Data-END## COMPLETENESS: complete on the 3' end. |
1 | ATGAACTCCA AATGTCATTG TGTCATATTG AATGATGGTA ACTTCATTCC AGTGCTGGGT |
The stop codons will be deleted if pcDNA3.1+/C-(K)DYK vector is selected.
RefSeq | NP_084177.2 |
CDS | 75..1046 |
Translation |
Target ORF information:
Target ORF information:
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1 | ATGAACTCCA AATGTCATTG TGTCATATTG AATGATGGTA ACTTCATTCC AGTGCTGGGT |
The stop codons will be deleted if pcDNA3.1+/C-(K)DYK vector is selected.
Studies on a Tyr residue critical for the binding of coenzyme and substrate in mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21): structure of the Y224D mutant enzyme. |
Structure of the G225P/G226P mutant of mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) ternary complex: implications for the binding of inhibitor and substrate. |
Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto reductases: identification and characterization of amino acid residues critical for substrate binding. |
Crystal structures of mouse 17alpha-hydroxysteroid dehydrogenase (apoenzyme and enzyme-NADP(H) binary complex): identification of molecular determinants responsible for the unique 17alpha-reductive activity of this enzyme. |
Crystallization and preliminary X-ray diffraction analysis of mouse 3(17)alpha-hydroxysteroid dehydrogenase. |