IFNG_VULVU
ID IFNG_VULVU Reviewed; 166 AA.
AC Q25BC0;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Interferon gamma;
DE Short=IFN-gamma;
DE Flags: Precursor;
GN Name=IFNG;
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16321447; DOI=10.1016/j.vetimm.2005.10.006;
RA Rolland-Turner M., Farre G., Boue F.;
RT "Cloning of fox (Vulpes vulpes) IL2, IL6, IL10 and IFNgamma and analysis of
RT their expression by quantitative RT-PCR in fox PBMC after in vitro
RT stimulation by concanavalin A.";
RL Vet. Immunol. Immunopathol. 110:369-375(2006).
CC -!- FUNCTION: Type II interferon produced by immune cells such as T-cells
CC and NK cells that plays crucial roles in antimicrobial, antiviral, and
CC antitumor responses by activating effector immune cells and enhancing
CC antigen presentation. Primarily signals through the JAK-STAT pathway
CC after interaction with its receptor IFNGR1 to affect gene regulation.
CC Upon IFNG binding, IFNGR1 intracellular domain opens out to allow
CC association of downstream signaling components JAK2, JAK1 and STAT1,
CC leading to STAT1 activation, nuclear translocation and transcription of
CC IFNG-regulated genes. Many of the induced genes are transcription
CC factors such as IRF1 that are able to further drive regulation of a
CC next wave of transcription. Plays a role in class I antigen
CC presentation pathway by inducing a replacement of catalytic proteasome
CC subunits with immunoproteasome subunits. In turn, increases the
CC quantity, quality, and repertoire of peptides for class I MHC loading.
CC Increases the efficiency of peptide generation also by inducing the
CC expression of activator PA28 that associates with the proteasome and
CC alters its proteolytic cleavage preference. Up-regulates as well MHC II
CC complexes on the cell surface by promoting expression of several key
CC molecules such as cathepsins B/CTSB, H/CTSH, and L/CTSL (By
CC similarity). Participates in the regulation of hematopoietic stem cells
CC during development and under homeostatic conditions by affecting their
CC development, quiescence, and differentiation (By similarity).
CC {ECO:0000250|UniProtKB:P01579, ECO:0000250|UniProtKB:P01580}.
CC -!- SUBUNIT: Homodimer. Interacts with IFNGR1 (via extracellular domain);
CC this interaction promotes IFNGR1 dimerization.
CC {ECO:0000250|UniProtKB:P01579}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01579}.
CC -!- TISSUE SPECIFICITY: Released primarily from activated T lymphocytes.
CC -!- SIMILARITY: Belongs to the type II (or gamma) interferon family.
CC {ECO:0000305}.
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DR EMBL; AJ621191; CAF18415.1; -; mRNA.
DR AlphaFoldDB; Q25BC0; -.
DR SMR; Q25BC0; -.
DR STRING; 9627.ENSVVUP00000014058; -.
DR OMA; GGPIFTE; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0005133; F:interferon-gamma receptor binding; IEA:InterPro.
DR GO; GO:0048143; P:astrocyte activation; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0002281; P:macrophage activation involved in immune response; IEA:Ensembl.
DR GO; GO:0030225; P:macrophage differentiation; IEA:Ensembl.
DR GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
DR GO; GO:0032700; P:negative regulation of interleukin-17 production; IEA:Ensembl.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:1902948; P:negative regulation of tau-protein kinase activity; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; IEA:Ensembl.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
DR GO; GO:0060559; P:positive regulation of calcidiol 1-monooxygenase activity; IEA:Ensembl.
DR GO; GO:0032834; P:positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation involved in immune response; IEA:Ensembl.
DR GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl.
DR GO; GO:1904798; P:positive regulation of core promoter binding; IEA:Ensembl.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:0060550; P:positive regulation of fructose 1,6-bisphosphate 1-phosphatase activity; IEA:Ensembl.
DR GO; GO:0060552; P:positive regulation of fructose 1,6-bisphosphate metabolic process; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IEA:Ensembl.
DR GO; GO:0032747; P:positive regulation of interleukin-23 production; IEA:Ensembl.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0051712; P:positive regulation of killing of cells of another organism; IEA:Ensembl.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IEA:Ensembl.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IEA:Ensembl.
DR GO; GO:1901216; P:positive regulation of neuron death; IEA:Ensembl.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0033141; P:positive regulation of peptidyl-serine phosphorylation of STAT protein; IEA:Ensembl.
DR GO; GO:0090312; P:positive regulation of protein deacetylation; IEA:Ensembl.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0034393; P:positive regulation of smooth muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:2000309; P:positive regulation of tumor necrosis factor (ligand) superfamily member 11 production; IEA:Ensembl.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR GO; GO:0060557; P:positive regulation of vitamin D biosynthetic process; IEA:Ensembl.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0050796; P:regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0010835; P:regulation of protein ADP-ribosylation; IEA:Ensembl.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR002069; Interferon_gamma.
DR PANTHER; PTHR11419; PTHR11419; 1.
DR Pfam; PF00714; IFN-gamma; 1.
DR PIRSF; PIRSF001936; IFN-gamma; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
PE 2: Evidence at transcript level;
KW Antiviral defense; Cytokine; Glycoprotein; Growth regulation;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..166
FT /note="Interferon gamma"
FT /id="PRO_0000235174"
FT MOD_RES 24
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P01579"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 166 AA; 19395 MW; 72179B0B637402DB CRC64;
MNYTSYILAF QLCVILCSSG CNCQAMFFKE IENLKEYFNA SNPDVSDGGS LFVDILKKWR
EESDKTIIQS QIVSFYLKLF DNFKDNQIIQ RSMDTIKEDM LGKFLNSSTS KREDFLKLIQ
IPVNDLQVQR KAINELIKVM NDLSPRSNLR KRKRSQNLFR GRRASK
