ID   IFNG_CERAT              Reviewed;         165 AA.
AC   P42162;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Interferon gamma;
DE            Short=IFN-gamma;
DE   Flags: Precursor;
GN   Name=IFNG;
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7561102;
RA   Villinger F.J., Brar S.S., Mayne A.E., Chikkala N., Ansari A.A.;
RT   "Comparative sequence analysis of cytokine genes from human and nonhuman
RT   primates.";
RL   J. Immunol. 155:3946-3954(1995).
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; L26025; AAA99969.1; -; mRNA.
DR   RefSeq; XP_011947219.1; XM_012091829.1.
DR   AlphaFoldDB; P42162; -.
DR   SMR; P42162; -.
DR   STRING; 9531.ENSCATP00000022573; -.
DR   Ensembl; ENSCATT00000046784; ENSCATP00000022573; ENSCATG00000034911.
DR   GeneID; 105600509; -.
DR   KEGG; caty:105600509; -.
DR   CTD; 3458; -.
DR   GeneTree; ENSGT00390000007831; -.
DR   OMA; GGPIFTE; -.
DR   OrthoDB; 1382686at2759; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000034911; Expressed in lymph node and 1 other tissue.
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; ISS:UniProtKB.
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..165
FT                   /note="Interferon gamma"
FT                   /id="PRO_0000016440"
FT   MOD_RES         24
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P01579"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   165 AA;  19301 MW;  5CF80CE233C4B153 CRC64;
     MKYTSYILAF QLCIVLGSLG CYCQDPYVKE AENLKKYFNA GDPDVADNGT LFLDILRNWK
     EESDRKIMQS QIVSFYFKLF KSFKDDQRIQ KSVETIKEDI NVKFFNSNKK KRDDFEKLTN
     YSVTDLNVQR KAVHELIQVM AELSPAAKIG KRKRSQTFRG RRASQ