Interferon gamma

Details

Name
Interferon gamma
Synonyms
  • IFN-gamma
  • Immune interferon
Gene Name
IFNG
Organism
Humans
Amino acid sequence
>lcl|BSEQ0010663|Interferon gamma
MKYTSYILAFQLCIVLGSLGCYCQDPYVKEAENLKKYFNAGHSDVADNGTLFLGILKNWK
EESDRKIMQSQIVSFYFKLFKNFKDDQSIQKSVETIKEDMNVKFFNSNKKKRDDFEKLTN
YSVTDLNVQRKAIHELIQVMAELSPAAKTGKRKRSQMLFRGRRASQ
Number of residues
166
Molecular Weight
19348.165
Theoretical pI
10.01
GO Classification
Functions
cytokine activity / interferon-gamma receptor binding
Processes
adaptive immune response / antigen processing and presentation / apoptotic process / CD8-positive, alpha-beta T cell differentiation involved in immune response / cell cycle arrest / cell surface receptor signaling pathway / cellular response to interleukin-18 / cellular response to lipopolysaccharide / cytokine-mediated signaling pathway / defense response to bacterium / defense response to protozoan / defense response to virus / endoplasmic reticulum unfolded protein response / extrinsic apoptotic signaling pathway / humoral immune response / interferon-gamma-mediated signaling pathway / movement of cell or subcellular component / negative regulation of epithelial cell differentiation / negative regulation of gene expression / negative regulation of growth of symbiont in host / negative regulation of interleukin-17 production / negative regulation of myelination / negative regulation of smooth muscle cell proliferation / negative regulation of transcription from RNA polymerase II promoter / neutrophil apoptotic process / neutrophil chemotaxis / positive regulation of autophagy / positive regulation of calcidiol 1-monooxygenase activity / positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation involved in immune response / positive regulation of cell proliferation / positive regulation of chemokine biosynthetic process / positive regulation of epithelial cell migration / positive regulation of fructose 1,6-bisphosphate 1-phosphatase activity / positive regulation of fructose 1,6-bisphosphate metabolic process / positive regulation of gene expression / positive regulation of interleukin-1 beta secretion / positive regulation of interleukin-12 biosynthetic process / positive regulation of interleukin-12 production / positive regulation of interleukin-23 production / positive regulation of interleukin-6 biosynthetic process / positive regulation of isotype switching to IgG isotypes / positive regulation of killing of cells of other organism / positive regulation of membrane protein ectodomain proteolysis / positive regulation of MHC class II biosynthetic process / positive regulation of neuron differentiation / positive regulation of nitric oxide biosynthetic process / positive regulation of osteoclast differentiation / positive regulation of peptidyl-serine phosphorylation of STAT protein / positive regulation of smooth muscle cell apoptotic process / positive regulation of synaptic transmission, cholinergic / positive regulation of T cell proliferation / positive regulation of transcription from RNA polymerase II promoter / positive regulation of tumor necrosis factor (ligand) superfamily member 11 production / positive regulation of tumor necrosis factor production / positive regulation of tyrosine phosphorylation of Stat1 protein / positive regulation of vitamin D biosynthetic process / protein import into nucleus, translocation / regulation of hepatocyte proliferation / regulation of insulin secretion / regulation of interferon-gamma-mediated signaling pathway / regulation of neuronal action potential / regulation of the force of heart contraction / response to drug / response to virus / sensory perception of mechanical stimulus
Components
external side of plasma membrane / extracellular region / extracellular space / intracellular
General Function
Interferon-gamma receptor binding
Specific Function
Produced by lymphocytes activated by specific antigens or mitogens. IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions. It is a potent activator of macrophages, it has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0010664|Interferon gamma (IFNG)
ATGAAATATACAAGTTATATCTTGGCTTTTCAGCTCTGCATCGTTTTGGGTTCTCTTGGC
TGTTACTGCCAGGACCCATATGTAAAAGAAGCAGAAAACCTTAAGAAATATTTTAATGCA
GGTCATTCAGATGTAGCGGATAATGGAACTCTTTTCTTAGGCATTTTGAAGAATTGGAAA
GAGGAGAGTGACAGAAAAATAATGCAGAGCCAAATTGTCTCCTTTTACTTCAAACTTTTT
AAAAACTTTAAAGATGACCAGAGCATCCAAAAGAGTGTGGAGACCATCAAGGAAGACATG
AATGTCAAGTTTTTCAATAGCAACAAAAAGAAACGAGATGACTTCGAAAAGCTGACTAAT
TATTCGGTAACTGACTTGAATGTCCAACGCAAAGCAATACATGAACTCATCCAAGTGATG
GCTGAACTGTCGCCAGCAGCTAAAACAGGGAAGCGAAAAAGGAGTCAGATGCTGTTTCGA
GGTCGAAGAGCATCCCAGTAA
Chromosome Location
12
Locus
12q14
External Identifiers
ResourceLink
UniProtKB IDP01579
UniProtKB Entry NameIFNG_HUMAN
GenBank Protein ID32692
GenBank Gene IDX13274
GenAtlas IDIFNG
HGNC IDHGNC:5438
General References
  1. Gray PW, Goeddel DV: Structure of the human immune interferon gene. Nature. 1982 Aug 26;298(5877):859-63. [Article]
  2. Gray PW, Leung DW, Pennica D, Yelverton E, Najarian R, Simonsen CC, Derynck R, Sherwood PJ, Wallace DM, Berger SL, Levinson AD, Goeddel DV: Expression of human immune interferon cDNA in E. coli and monkey cells. Nature. 1982 Feb 11;295(5849):503-8. [Article]
  3. Nishi T, Fujita T, Nishi-Takaoka C, Saito A, Matsumoto T, Sato M, Oka T, Itoh S, Yip YK, Vilcek J, et al.: Cloning and expression of a novel variant of human interferon-gamma cDNA. J Biochem. 1985 Jan;97(1):153-9. [Article]
  4. Taya Y, Devos R, Tavernier J, Cheroutre H, Engler G, Fiers W: Cloning and structure of the human immune interferon-gamma chromosomal gene. EMBO J. 1982;1(8):953-8. [Article]
  5. Devos R, Cheroutre H, Taya Y, Degrave W, Van Heuverswyn H, Fiers W: Molecular cloning of human immune interferon cDNA and its expression in eukaryotic cells. Nucleic Acids Res. 1982 Apr 24;10(8):2487-501. [Article]
  6. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [Article]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  8. Rinderknecht E, O'Connor BH, Rodriguez H: Natural human interferon-gamma. Complete amino acid sequence and determination of sites of glycosylation. J Biol Chem. 1984 Jun 10;259(11):6790-7. [Article]
  9. Pan YC, Stern AS, Familletti PC, Khan FR, Chizzonite R: Structural characterization of human interferon gamma. Heterogeneity of the carboxyl terminus. Eur J Biochem. 1987 Jul 1;166(1):145-9. [Article]
  10. Yamamoto S, Hase S, Yamauchi H, Tanimoto T, Ikenaka T: Studies on the sugar chains of interferon-gamma from human peripheral-blood lymphocytes. J Biochem. 1989 Jun;105(6):1034-9. [Article]
  11. Ealick SE, Cook WJ, Vijay-Kumar S, Carson M, Nagabhushan TL, Trotta PP, Bugg CE: Three-dimensional structure of recombinant human interferon-gamma. Science. 1991 May 3;252(5006):698-702. [Article]
  12. Walter MR, Windsor WT, Nagabhushan TL, Lundell DJ, Lunn CA, Zauodny PJ, Narula SK: Crystal structure of a complex between interferon-gamma and its soluble high-affinity receptor. Nature. 1995 Jul 20;376(6537):230-5. [Article]
  13. Landar A, Curry B, Parker MH, DiGiacomo R, Indelicato SR, Nagabhushan TL, Rizzi G, Walter MR: Design, characterization, and structure of a biologically active single-chain mutant of human IFN-gamma. J Mol Biol. 2000 May 26;299(1):169-79. [Article]
  14. Thiel DJ, le Du MH, Walter RL, D'Arcy A, Chene C, Fountoulakis M, Garotta G, Winkler FK, Ealick SE: Observation of an unexpected third receptor molecule in the crystal structure of human interferon-gamma receptor complex. Structure. 2000 Sep 15;8(9):927-36. [Article]
  15. Grzesiek S, Dobeli H, Gentz R, Garotta G, Labhardt AM, Bax A: 1H, 13C, and 15N NMR backbone assignments and secondary structure of human interferon-gamma. Biochemistry. 1992 Sep 8;31(35):8180-90. [Article]
  16. Dufour C, Capasso M, Svahn J, Marrone A, Haupt R, Bacigalupo A, Giordani L, Longoni D, Pillon M, Pistorio A, Di Michele P, Iori AP, Pongiglione C, Lanciotti M, Iolascon A: Homozygosis for (12) CA repeats in the first intron of the human IFN-gamma gene is significantly associated with the risk of aplastic anaemia in Caucasian population. Br J Haematol. 2004 Sep;126(5):682-5. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01296Glucosamineapproved, investigationalunknowninhibitorDetails
DB05110VIR201investigationalunknownDetails
DB05111FontolizumabinvestigationalunknownDetails
DB01250OlsalazineapprovedyesDetails
DB10770Foreskin fibroblast (neonatal)approvedunknownagonistDetails
DB10772Foreskin keratinocyte (neonatal)approvedyesagonistDetails
DB14724Emapalumabapproved, investigationalyesneutralizerDetails