HLA-F

Major histocompatibility complex, class I, F
Identifiers
Symbols HLA-F ; CDA12; HLA-5.4; HLA-CDA12; HLAF
External IDs OMIM: 143110 MGI: 95931 HomoloGene: 133121 GeneCards: HLA-F Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 3134 630294
Ensembl ENSG00000137403 ENSMUSG00000092243
UniProt P30511 A7VMS3
RefSeq (mRNA) NM_001098478 NM_001177467
RefSeq (protein) NP_001091948 NP_001170938
Location (UCSC) Chr 6:
29.72 – 29.74 Mb		 Chr 17:
36.11 – 36.13 Mb
PubMed search

HLA class I histocompatibility antigen, alpha chain F is a protein that in humans is encoded by the HLA-F gene.[1][2]

Function

HLA-F belongs to the non-classical HLA class I heavy chain paralogues. Compared to classical HLA I molecules it exhibits very few polymorphisms. This class I molecule mainly exists as a heterodimer associated with the invariant light chain beta-2 microglobulin. The heavy chain is approximately 42 kDa and its gene contains 8 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the alpha1 and alpha2 domains, the putative peptide binding sites, exon 4 encodes the alpha3 domain, exon 5 and 6 encode the transmembrane region and exons 7 and 8 the cytoplasmic tail. However, exons 7 and 8 (the cytoplasmic tail) are not translated due to an in-frame translation termination codon in exon 6.[2]

HLA-F is currently the most enigmatic of the HLA molecules. Hence, its precise functions still remain to be resolved. Though, in contrast to other HLA molecules, it mainly resides intracellularly and rarely reaches the cell surface, e.g. upon activation of NK, B and T cells. Unlike classical HLA class I molecules, which possess ten highly conserved amino acids responsible for antigen recognition, HLA-F only has 5, suggesting a biological function different from peptide presentation. Data suggest that upon immune cell activation HLA-F binds free forms of HLA I and reaches the cell surface as heterodimer. In this way HLA-F stabilizes HLA I molecules that haven´t yet bound peptides, thereby acting as a chaperone and transporting the free HLA I to, on, and from the cell surface.[3]

References

  1. ↑ Geraghty DE, Wei XH, Orr HT, Koller BH (Jan 1990). "Human leukocyte antigen F (HLA-F). An expressed HLA gene composed of a class I coding sequence linked to a novel transcribed repetitive element". The Journal of Experimental Medicine 171 (1): 1–18. doi:10.1084/jem.171.1.1. PMC 2187653. PMID 1688605.
  2. 1 2 "Entrez Gene: HLA-F major histocompatibility complex, class I, F".
  3. ↑ Foroni I, Rita A, Filipe B, Santos M, Lima M, Bruges-Armas J (2014-03-19). HLA-E, HLA-F and HLA-G — The Non-Classical Side of the MHC Cluster. InTech. doi:10.5772/57507.

Further reading

  • Geyer M, Fackler OT, Peterlin BM (Jul 2001). "Structure--function relationships in HIV-1 Nef". EMBO Reports 2 (7): 580–5. doi:10.1093/embo-reports/kve141. PMC 1083955. PMID 11463741. 
  • Greenway AL, Holloway G, McPhee DA, Ellis P, Cornall A, Lidman M (Apr 2003). "HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication". Journal of Biosciences 28 (3): 323–35. doi:10.1007/BF02970151. PMID 12734410. 
  • Bénichou S, Benmerah A (Jan 2003). "[The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: "parasites"of the endocytosis pathway]". Médecine Sciences 19 (1): 100–6. doi:10.1051/medsci/2003191100. PMID 12836198. 
  • Leavitt SA, SchOn A, Klein JC, Manjappara U, Chaiken IM, Freire E (Feb 2004). "Interactions of HIV-1 proteins gp120 and Nef with cellular partners define a novel allosteric paradigm". Current Protein & Peptide Science 5 (1): 1–8. doi:10.2174/1389203043486955. PMID 14965316. 
  • Tolstrup M, Ostergaard L, Laursen AL, Pedersen SF, Duch M (Apr 2004). "HIV/SIV escape from immune surveillance: focus on Nef". Current HIV Research 2 (2): 141–51. doi:10.2174/1570162043484924. PMID 15078178. 
  • Joseph AM, Kumar M, Mitra D (Jan 2005). "Nef: "necessary and enforcing factor" in HIV infection". Current HIV Research 3 (1): 87–94. doi:10.2174/1570162052773013. PMID 15638726. 
  • Anderson JL, Hope TJ (Apr 2004). "HIV accessory proteins and surviving the host cell". Current HIV/AIDS Reports 1 (1): 47–53. doi:10.1007/s11904-004-0007-x. PMID 16091223. 
  • Kozlowski S, Corr M, Takeshita T, Boyd LF, Pendleton CD, Germain RN, Berzofsky JA, Margulies DH (Jun 1992). "Serum angiotensin-1 converting enzyme activity processes a human immunodeficiency virus 1 gp160 peptide for presentation by major histocompatibility complex class I molecules". The Journal of Experimental Medicine 175 (6): 1417–22. doi:10.1084/jem.175.6.1417. PMC 2119225. PMID 1316930. 
  • Lury D, Epstein H, Holmes N (1991). "The human class I MHC gene HLA-F is expressed in lymphocytes". International Immunology 2 (6): 531–7. doi:10.1093/intimm/2.6.531. PMID 1707659. 
  • Takahashi H, Merli S, Putney SD, Houghten R, Moss B, Germain RN, Berzofsky JA (Oct 1989). "A single amino acid interchange yields reciprocal CTL specificities for HIV-1 gp160". Science 246 (4926): 118–21. doi:10.1126/science.2789433. PMID 2789433. 
  • Dianzani U, Bragardo M, Buonfiglio D, Redoglia V, Funaro A, Portoles P, Rojo J, Malavasi F, Pileri A (May 1995). "Modulation of CD4 lateral interaction with lymphocyte surface molecules induced by HIV-1 gp120". European Journal of Immunology 25 (5): 1306–11. doi:10.1002/eji.1830250526. PMID 7539755. 
  • Howcroft TK, Palmer LA, Brown J, Rellahan B, Kashanchi F, Brady JN, Singer DS (Jul 1995). "HIV Tat represses transcription through Sp1-like elements in the basal promoter". Immunity 3 (1): 127–38. doi:10.1016/1074-7613(95)90165-5. PMID 7621073. 
  • Chen YH, Böck G, Vornhagen R, Steindl F, Katinger H, Dierich MP (Jul 1994). "HIV-1 gp41 enhances major histocompatibility complex class I and ICAM-1 expression on H9 and U937 cells". International Archives of Allergy and Immunology 104 (3): 227–31. doi:10.1159/000236670. PMID 7913356. 
  • Chen YH, Böck G, Vornhagen R, Steindl F, Katinger H, Dierich MP (Sep 1994). "HIV-1 gp41 binding proteins and antibodies to gp41 could inhibit enhancement of human Raji cell MHC class I and II expression by gp41". Molecular Immunology 31 (13): 977–82. doi:10.1016/0161-5890(94)90092-2. PMID 8084338. 
  • Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
  • Howcroft TK, Strebel K, Martin MA, Singer DS (May 1993). "Repression of MHC class I gene promoter activity by two-exon Tat of HIV". Science 260 (5112): 1320–2. doi:10.1126/science.8493575. PMID 8493575. 
  • Gasparini P, Borgato L, Piperno A, Girelli D, Olivieri O, Gottardi E, Roetto A, Dianzani I, Fargion S, Schinaia G (May 1993). "Linkage analysis of 6p21 polymorphic markers and the hereditary hemochromatosis: localization of the gene centromeric to HLA-F". Human Molecular Genetics 2 (5): 571–6. doi:10.1093/hmg/2.5.571. PMID 8518796. 
  • Schwartz O, Maréchal V, Le Gall S, Lemonnier F, Heard JM (Mar 1996). "Endocytosis of major histocompatibility complex class I molecules is induced by the HIV-1 Nef protein". Nature Medicine 2 (3): 338–42. doi:10.1038/nm0396-338. PMID 8612235. 
  • Alexander-Miller MA, Parker KC, Tsukui T, Pendleton CD, Coligan JE, Berzofsky JA (May 1996). "Molecular analysis of presentation by HLA-A2.1 of a promiscuously binding V3 loop peptide from the HIV-envelope protein to human cytotoxic T lymphocytes". International Immunology 8 (5): 641–9. doi:10.1093/intimm/8.5.641. PMID 8671651. 


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