AKR1C2

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AKR1C2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesAKR1C2, AKR1C-pseudo, BABP, DD, DD2, DDH2, HAKRD, HBAB, MCDR2, SRXY8, TDD, DD-2, DD/BABP, aldo-keto reductase family 1, member C2, aldo-keto reductase family 1 member C2
External IDsOMIM: 600450 MGI: 1924587 HomoloGene: 134114 GeneCards: AKR1C2
EC number1.1.1.357
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001135241
NM_001354
NM_205845
NM_001321027
NM_001393392

NM_029901

RefSeq (protein)

NP_001128713
NP_001307956
NP_001345
NP_995317

NP_084177

Location (UCSC)Chr 10: 4.99 – 5.02 MbChr 13: 4.62 – 4.64 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Aldo-keto reductase family 1 member C2, also known as bile acid binding protein, 3α-hydroxysteroid dehydrogenase type 3, and dihydrodiol dehydrogenase type 2, is an enzyme that in humans is encoded by the AKR1C2 gene.[5]

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 using NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme binds bile acid with high affinity, and shows minimal 3α-hydroxysteroid dehydrogenase activity. This gene shares high sequence identity with three other gene members and is clustered with those three genes at chromosome 10p15-p14. Three transcript variants encoding two different isoforms have been found for this gene.[5]

References[]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000151632 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000021207 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: AKR1C2 aldo-keto reductase family 1, member C2 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase)". National Center for Biotechnology Information, U.S. National Library of Medicine. Public Domain This article incorporates text from this source, which is in the public domain.

External links[]


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