HNF1A

Last updated
HNF1A
Protein TCF1 PDB 1ic8.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases HNF1A , HNF-1A, HNF1, IDDM20, LFB1, MODY3, TCF-1, TCF1, HNF1 homeobox A, HNF4A, HNF1alpha
External IDs OMIM: 142410 MGI: 98504 HomoloGene: 459 GeneCards: HNF1A
Orthologs
SpeciesHumanMouse
Entrez

6927

21405

Ensembl

ENSG00000135100

ENSMUSG00000029556

UniProt

P20823

P22361

RefSeq (mRNA)

NM_000545
NM_001306179

NM_009327

RefSeq (protein)

NP_000536
NP_001293108
NP_000536.5
NP_001293108.1

NP_033353

Location (UCSC) Chr 12: 120.98 – 121 Mb Chr 5: 115.09 – 115.11 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

HNF1 homeobox A (hepatocyte nuclear factor 1 homeobox A), also known as HNF1A, is a human gene on chromosome 12. [5] [6] [7] It is ubiquitously expressed in many tissues and cell types. [8] The protein encoded by this gene is a transcription factor that is highly expressed in the liver and is involved in the regulation of the expression of several liver-specific genes. [9] Mutations in the HNF1A gene have been known to cause diabetes. [10] The HNF1A gene also contains a SNP associated with increased risk of coronary artery disease. [11]

Contents

Structure

Gene

The HNF1A gene resides on chromosome 12 at the band 12q24.2 and contains 10 [12] exons. [7] This gene produces 8 isoforms through alternative splicing. [13]

Protein

This protein belongs to the HNF1 homeobox family. [13] It contains 3 functional domains: an N-terminal dimerization domain (residues 1–32), a bipartite DNA-binding motif containing an atypical POU-homeodomain (residues 98–280), and a C-terminal transactivation domain (residues 281–631). [14] [15] There is also a flexible linker (residues 33–97) which connects the dimerization and DNA binding domains. [15] Crystal structures have been solved for the dimerization domain, which forms a four-helix bundle where two α helices are separated by a turn; the DNA-binding motif, which forms a helix-turn-helix structure; and the POU-homeodomain, which is composed of three α helices, contained in the motif. This homeodomain is considered atypical due to an extended loop inserted between the second and third helices relative to the canonical homeodomain fold. The atypical insertion is thought to stabilize the interface to improve transcriptional efficiency. [14] Meanwhile, the dimerization domain is responsible for the homo- and heterodimerization of HNF-1α. The resulting dimer contains a rigid “mini-zipper”, comprising α-helices 1 and 1′, linked by a non-canonical tight turn to a flexible C-terminal comprising α-helices 2 and 2′. [15]

Function

HNF-1α is a transcription factor expressed in organs of endoderm origin, including liver, kidneys, pancreas, intestines, stomach, spleen, thymus, testis, and keratinocytes and melanocytes in human skin. [16] It has been shown to affect intestinal epithelial cell growth and cell lineages differentiation. For instance, HNF1A is an important cell-intrinsic transcription factor in adult B lymphopoiesis. [17] [18] [19] The participation of HNF-1α in glucose metabolism and diabetes has been reported, including the involvement in GLUT1 and GLUT2 transporter expression in pancreatic β-cells and angiotensin-converting enzyme 2 gene expression in pancreatic islets. [20] [21] HNF-1α could promote the transcription of several proteins involved in the management of type II diabetes including dipeptidyl peptidase-IV (DPP-IV/CD26). [22] [23] HNF-1α is also involved in various metabolic pathways of other organs, such as being a transcriptional regulator of bile acid transporters in the intestine and kidneys. [24] HNF-1α is involved in the promotion of hepatic organic cation transporters, which uptake certain classes of pharmaceuticals; hence, the loss of its function can lead to drug metabolism problems. [25] In addition, HNF-1α regulates the expression of acute phase proteins, such as fibrinogen, c-reactive protein, and interleukin 1 receptor, which are involved with inflammation. [26] Moreover, significantly lower levels of HNF-1α in pancreatic tumors and hepatocellular adenomas than in normal adjacent tissues was observed, suggesting that HNF-1α might play a possible tumor suppressor role. [27] [28]

Clinical significance

HNF1A mutations can cause maturity onset diabetes of the young type 3, one of the forms of "monogenic diabetes", [6] as well as hepatocellular adenoma. HNF-1 protein is present in ovarian clear-cell carcinoma. [29] [30]

In humans, mutations in HNF1A cause diabetes that responds to low dose sulfonylurea agents. [31] The identification of extreme sulfonylurea sensitivity in patients with diabetes mellitus owing to heterozygous mutations in HNF1A presents a clear example of the relevance of HNF1A in diabetes patients and how pharmacogenetics can contribute in patient care. [32] For example, patients with maturity onset diabetes of the young owing to mutations in HNF1A (which accounts for ~3% of all diabetes mellitus cases diagnosed under the age of 30 years) are extremely sensitive to sulfonylurea treatment and can successfully transition off insulin treatment. [10] Likewise, patients with diabetes caused by mutations in the HNF1A gene have been described as sensitive to the hypoglycemic effects of sulphonylureas. The cause of hyperglycemia appears to alter the response to hypoglycemic drugs. Accordingly, HNF-1α-induced diabetes has marked sulphonylurea sensitivity. This pharmacogenetic effect is consistent with models of HNF-1α deficiency, and the genetic basis of hyperglycemia may have implications for patient management. [10] Common genetic variation within HNF1A is also associated with risk of developing type 2 diabetes and increased penetrance of early-onset diabetes [33]

Clinical marker

A multi-locus genetic risk score study based on a combination of 27 loci, including the HNF1A gene, identified individuals at increased risk for both incident and recurrent coronary artery disease events, as well as an enhanced clinical benefit from statin therapy. The study was based on a community cohort study (the Malmo Diet and Cancer study) and four additional randomized controlled trials of primary prevention cohorts (JUPITER and ASCOT) and secondary prevention cohorts (CARE and PROVE IT-TIMI 22). [11]

Interactions

HNF1A has been shown to interact with:

See also

Related Research Articles

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<span class="mw-page-title-main">Hepatocyte nuclear factor 4 alpha</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">PDX1</span> A protein involved in the pancreas and duodenum differentiation

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<span class="mw-page-title-main">HNF1B</span> Mammalian protein found in Homo sapiens

HNF1 homeobox B, also known as HNF1B or transcription factor 2 (TCF2), is a human gene.

<span class="mw-page-title-main">PCBD1</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">PROX1</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">HOXB2</span> Protein-coding gene in humans

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<span class="mw-page-title-main">3α-Hydroxysteroid dehydrogenase</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">GATA5</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">HOXD1</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">MODY 1</span> Medical condition

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<span class="mw-page-title-main">Neurogenin-3</span> Mammalian protein found in Homo sapiens

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<span class="mw-page-title-main">FOXA1</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">FOXA2</span> Mammalian protein found in Homo sapiens

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<span class="mw-page-title-main">FOXA3</span> Protein-coding gene in the species Homo sapiens

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References

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  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000029556 - Ensembl, May 2017
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  33. ↑ "The Common HNF1A Variant I27L Is a Modifier of Age at Diabetes Diagnosis in Individuals With HNF1A-MODY"
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  35. ↑ Ban N, Yamada Y, Someya Y, Miyawaki K, Ihara Y, Hosokawa M, Toyokuni S, Tsuda K, Seino Y (May 2002). "Hepatocyte nuclear factor-1alpha recruits the transcriptional co-activator p300 on the GLUT2 gene promoter". Diabetes. 51 (5): 1409–18. doi: 10.2337/diabetes.51.5.1409 . PMID   11978637.
  36. ↑ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3: 89. doi:10.1038/msb4100134. PMC   1847948 . PMID   17353931.
  37. ↑ Sourdive DJ, Transy C, Garbay S, Yaniv M (April 1997). "The bifunctional DCOH protein binds to HNF1 independently of its 4-alpha-carbinolamine dehydratase activity". Nucleic Acids Research. 25 (8): 1476–84. doi:10.1093/nar/25.8.1476. PMC   146627 . PMID   9092652.
  38. ↑ Ficner, R.; Sauer, U.H.; Stier, G.; Suck, D. (May 1995). "Three-dimensional structure of the bifunctional protein PCD/DCoH, a cytoplasmic enzyme interacting with transcription factor HNF1". The EMBO Journal. 14 (9): 2034–2042. doi:10.1002/j.1460-2075.1995.tb07195.x. hdl: 11858/00-001M-0000-0019-A7D6-3 . PMC   398303 . PMID   7744010.
  39. ↑ Alber, Tom; Rose, Robert B.; Bayle, J. Henri; Endrizzi, James A.; Cronk, Jeff D.; Crabtree, Gerald R. (2000-09-01). "[No title found]". Nature Structural Biology. 7 (9): 744–748. doi:10.1038/78966. PMID   10966642. S2CID   22528806.
  40. ↑ Hines RN, Luo Z, Cresteil T, Ding X, Prough RA, Fitzpatrick JL, Ripp SL, Falkner KC, Ge NL, Levine A, Elferink CJ (May 2001). "Molecular regulation of genes encoding xenobiotic-metabolizing enzymes: mechanisms involving endogenous factors". Drug Metabolism and Disposition. 29 (5): 623–33. PMID   11302926.
  41. ↑ Rufibach LE, Duncan SA, Battle M, Deeb SS (July 2006). "Transcriptional regulation of the human hepatic lipase (LIPC) gene promoter". Journal of Lipid Research. 47 (7): 1463–77. doi: 10.1194/jlr.M600082-JLR200 . PMID   16603721.
  42. 1 2 Bulla GA, Kraus DM (December 2004). "Dissociation of the hepatic phenotype from HNF4 and HNF1alpha expression". Bioscience Reports. 24 (6): 595–608. doi:10.1007/s10540-005-2794-8. PMID   16158197. S2CID   55553843.

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