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HIF3A

From Wikipedia, the free encyclopedia
(Redirected from Hypoxia inducible factor 3)
HIF3A
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesHIF3A, HIF-3A, IPAS, MOP7, PASD7, bHLHe17, HIF3-alpha-1, hypoxia inducible factor 3 alpha subunit, hypoxia inducible factor 3 subunit alpha
External IDsOMIM: 609976; MGI: 1859778; HomoloGene: 9646; GeneCards: HIF3A; OMA:HIF3A - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_022462
NM_152794
NM_152795
NM_152796

NM_001162950
NM_016868

RefSeq (protein)

NP_071907
NP_690007
NP_690008
NP_690009

NP_001156422
NP_058564

Location (UCSC)Chr 19: 46.3 – 46.34 MbChr 7: 16.77 – 16.8 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Hypoxia-inducible factor 3 alpha is a protein that in humans is encoded by the HIF3A gene.[5][6][7]

Function

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The protein encoded by this gene is the alpha-3 subunit of one of several alpha/beta-subunit heterodimeric transcription factors that regulate many adaptive responses to low oxygen tension (hypoxia). The alpha-3 subunit lacks the transactivation domain found in factors containing either the alpha-1 or alpha-2 subunits. It is thought that factors containing the alpha-3 subunit are negative regulators of hypoxia-inducible gene expression. At least three transcript variants encoding three different isoforms have been found for this gene.[7]

In rats, it plays a negative role in the adaptation to hypoxia, because the inhibition of HIF-3α expression leads to an increase in physical endurance.[8]

Clinical significance

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DNA methylation in the introns of HIF3A is associated with BMI an adiposity.[9]

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000124440Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000004328Ensembl, 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. ^ Hara S, Hamada J, Kobayashi C, Kondo Y, Imura N (Sep 2001). "Expression and characterization of hypoxia-inducible factor (HIF)-3alpha in human kidney: suppression of HIF-mediated gene expression by HIF-3alpha". Biochem Biophys Res Commun. 287 (4): 808–13. doi:10.1006/bbrc.2001.5659. PMID 11573933.
  6. ^ Makino Y, Cao R, Svensson K, Bertilsson G, Asman M, Tanaka H, Cao Y, Berkenstam A, Poellinger L (Dec 2001). "Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression". Nature. 414 (6863): 550–4. Bibcode:2001Natur.414..550M. doi:10.1038/35107085. PMID 11734856. S2CID 4389117.
  7. ^ a b "Entrez Gene: HIF3A hypoxia inducible factor 3, alpha subunit".
  8. ^ Drevytska T, Gavenauskas B, Drozdovska S, Nosar V, Dosenko V, Mankovska I (2012). "HIF-3α mRNA expression changes in different tissues and their role in adaptation to intermittent hypoxia and physical exercise". Pathophysiology. 19 (3): 205–14. doi:10.1016/j.pathophys.2012.06.002. PMID 22884965.
  9. ^ Dick KJ, Nelson CP, Tsaprouni L, Sandling JK, Aïssi D, Wahl S, Meduri E, Morange PE, Gagnon F, Grallert H, Waldenberger M, Peters A, Erdmann J, Hengstenberg C, Cambien F, Goodall AH, Ouwehand WH, Schunkert H, Thompson JR, Spector TD, Gieger C, Trégouët DA, Deloukas P, Samani NJ (2014). "DNA methylation and body-mass index: a genome-wide analysis". Lancet. 383 (9933): 1990–1998. doi:10.1016/S0140-6736(13)62674-4. PMID 24630777. S2CID 18026508.

Further reading

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