HIF3A

HIF3A
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesHIF3A, HIF-3A, IPAS, MOP7, PASD7, bHLHe17, HIF3-alpha-1, hypoxia inducible factor 3 alpha subunit
External IDsMGI: 1859778 HomoloGene: 9646 GeneCards: HIF3A
Gene location (Human)
Chr.Chromosome 19 (human)[1]
BandNo data availableStart46,297,046 bp[1]
End46,343,433 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

64344

53417

Ensembl

ENSG00000124440

ENSMUSG00000004328

UniProt

Q9Y2N7

Q0VBL6

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: 17.03 – 17.06 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

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

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

See also

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000124440 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000004328 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  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. PMID 11573933. doi:10.1006/bbrc.2001.5659.
  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. PMID 11734856. doi:10.1038/35107085.
  7. 1 2 "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. PMID 22884965. doi:10.1016/j.pathophys.2012.06.002.
  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. PMID 24630777. doi:10.1016/S0140-6736(13)62674-4.

Further reading

  • Gu YZ, Moran SM, Hogenesch JB, Wartman L, Bradfield CA (1998). "Molecular characterization and chromosomal localization of a third alpha-class hypoxia inducible factor subunit, HIF3alpha.". Gene Expr. 7 (3): 205–13. PMID 9840812. 
  • Makino Y, Kanopka A, Wilson WJ, Tanaka H, Poellinger L (2002). "Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxia-inducible factor-3alpha locus.". J. Biol. Chem. 277 (36): 32405–8. PMID 12119283. doi:10.1074/jbc.C200328200. 
  • Maynard MA, Qi H, Chung J, Lee EH, Kondo Y, Hara S, Conaway RC, Conaway JW, Ohh M (2003). "Multiple splice variants of the human HIF-3 alpha locus are targets of the von Hippel-Lindau E3 ubiquitin ligase complex.". J. Biol. Chem. 278 (13): 11032–40. PMID 12538644. doi:10.1074/jbc.M208681200. 
  • Maynard MA, Evans AJ, Hosomi T, Hara S, Jewett MA, Ohh M (2006). "Human HIF-3alpha4 is a dominant-negative regulator of HIF-1 and is down-regulated in renal cell carcinoma.". FASEB J. 19 (11): 1396–406. PMID 16126907. doi:10.1096/fj.05-3788com. 
  • Jang MS, Park JE, Lee JA, Park SG, Myung PK, Lee DH, Park BC, Cho S (2005). "Binding and regulation of hypoxia-inducible factor-1 by the inhibitory PAS proteins.". Biochem. Biophys. Res. Commun. 337 (1): 209–15. PMID 16182248. doi:10.1016/j.bbrc.2005.09.038. 
  • Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. PMC 1356129 Freely accessible. PMID 16344560. doi:10.1101/gr.4039406. 
  • Li QF, Wang XR, Yang YW, Lin H (2006). "Hypoxia upregulates hypoxia inducible factor (HIF)-3alpha expression in lung epithelial cells: characterization and comparison with HIF-1alpha.". Cell Res. 16 (6): 548–58. PMID 16775626. doi:10.1038/sj.cr.7310072. 
  • Kollers S, Musilova P, Rubes J, Rocha D (2007). "Comparative mapping reveals multiple rearrangements between pig chromosome 6 and human 19q13.". Anim. Genet. 37 (6): 595–6. PMID 17121608. doi:10.1111/j.1365-2052.2006.01516.x. 


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