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SRD5A2

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(Redirected from 5α reductase II)
SRD5A2
Identifiers
AliasesSRD5A2, entrez:6716, steroid 5 alpha-reductase 2
External IDsOMIM: 607306; MGI: 2150380; HomoloGene: 37292; GeneCards: SRD5A2; OMA:SRD5A2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000348

NM_053188

RefSeq (protein)

NP_000339

NP_444418

Location (UCSC)Chr 2: 31.52 – 31.58 MbChr 17: 74.32 – 74.35 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

The human gene SRD5A2 encodes the 3-oxo-5α-steroid 4-dehydrogenase 2 enzyme, also known as 5α-reductase type 2 (5αR2),[5][6] one of three isozymes of 5α-reductase.

5αR2 catalyzes the conversion of the male sex hormone testosterone into the more potent androgen, dihydrotestosterone.

5αR2 is a microsomal protein expressed at high levels in androgen-sensitive tissues such as the prostate. The enzyme is active at acidic pH and is sensitive to the 4-azasteroid inhibitor finasteride. Deficiencies in 5αR2 activity of the can lead to a condition known as 5α-reductase 2 deficiency, which is a cause of 46,XY DSD that presents as atypical male genitalia.

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000277893Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000038541Ensembl, 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. ^ Thigpen AE, Davis DL, Milatovich A, Mendonca BB, Imperato-McGinley J, Griffin JE, Francke U, Wilson JD, Russell DW (Oct 1992). "Molecular genetics of steroid 5 alpha-reductase 2 deficiency". J Clin Invest. 90 (3): 799–809. doi:10.1172/JCI115954. PMC 329933. PMID 1522235.
  6. ^ "SRD5A2 steroid 5 alpha-reductase 2 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 31 August 2021.

Further reading

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.