IFNG_BOVIN
ID IFNG_BOVIN Reviewed; 166 AA.
AC P07353; A7L687; A9QWQ4;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Interferon gamma;
DE Short=BoIFNG;
DE Short=IFN-gamma;
DE Flags: Precursor;
GN Name=IFNG;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3086437;
RA Cerretti D.P., McKereghan K., Larsen A., Cosman D., Gillis S., Baker P.E.;
RT "Cloning, sequence, and expression of bovine interferon-gamma.";
RL J. Immunol. 136:4561-4564(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-14.
RC STRAIN=Deutsche Schwarzbunte;
RX PubMed=12396714; DOI=10.1089/10799900260286632;
RA Schmidt P., Kuehn C., Maillard J.-C., Pitra C., Tiemann U., Weikard R.,
RA Schwerin M.;
RT "A comprehensive survey for polymorphisms in the bovine IFN-gamma gene
RT reveals a highly polymorphic intronic DNA sequence allowing improved
RT genotyping of Bovinae.";
RL J. Interferon Cytokine Res. 22:923-934(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-166.
RA Li G., Hu Y., Ren X., Ma D., Gai R.;
RT "Cloning and sequence analysis of cattle interferon gamma.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Belted Galloway; TISSUE=Peripheral blood;
RG U.S. Veterinary Immune Reagent Network;
RA Hudgens T., Tompkins D., Baldwin C.L.;
RT "U.S. veterinary immune reagent network: expressed bovine gene sequences.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=15299487; DOI=10.1107/s0907444993006924;
RA Samudzi C.T., Rubin J.R.;
RT "Structure of recombinant bovine interferon-gamma at 3.0-A resolution.";
RL Acta Crystallogr. D 49:513-521(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10666622; DOI=10.1107/s0907444999014304;
RA Randal M., Kossiakoff A.A.;
RT "The 2.0-A structure of bovine interferon-gamma; assessment of the
RT structural differences between species.";
RL Acta Crystallogr. D 56:14-24(2000).
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; M29867; AAB64477.1; -; mRNA.
DR EMBL; Z54144; CAA90859.1; -; Genomic_DNA.
DR EMBL; EF675629; ABS11696.1; -; mRNA.
DR EMBL; EU276066; ABX72064.1; -; mRNA.
DR PIR; A24390; IVBOG.
DR RefSeq; NP_776511.1; NM_174086.1.
DR PDB; 1D9C; X-ray; 2.00 A; A/B=24-144.
DR PDB; 1D9G; X-ray; 2.90 A; A/B=24-144.
DR PDB; 1RFB; X-ray; 3.00 A; A/B=24-142.
DR PDBsum; 1D9C; -.
DR PDBsum; 1D9G; -.
DR PDBsum; 1RFB; -.
DR AlphaFoldDB; P07353; -.
DR SMR; P07353; -.
DR STRING; 9913.ENSBTAP00000016634; -.
DR PaxDb; P07353; -.
DR PRIDE; P07353; -.
DR Ensembl; ENSBTAT00000016634; ENSBTAP00000016634; ENSBTAG00000012529.
DR GeneID; 281237; -.
DR KEGG; bta:281237; -.
DR CTD; 3458; -.
DR VEuPathDB; HostDB:ENSBTAG00000012529; -.
DR VGNC; VGNC:30057; IFNG.
DR eggNOG; ENOG502SBGW; Eukaryota.
DR GeneTree; ENSGT00390000007831; -.
DR HOGENOM; CLU_135106_0_0_1; -.
DR InParanoid; P07353; -.
DR OMA; GGPIFTE; -.
DR OrthoDB; 1382686at2759; -.
DR TreeFam; TF336308; -.
DR Reactome; R-BTA-877300; Interferon gamma signaling.
DR Reactome; R-BTA-877312; Regulation of IFNG signaling.
DR EvolutionaryTrace; P07353; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000012529; Expressed in mesenteric lymph node and 40 other tissues.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005133; F:interferon-gamma receptor binding; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IBA:GO_Central.
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:0006959; P:humoral immune response; IBA:GO_Central.
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:0030890; P:positive regulation of B cell proliferation; IMP:AgBase.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:AgBase.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000016433"
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:0000250"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT VARIANT 14
FT /note="G -> V"
FT /evidence="ECO:0000269|PubMed:12396714"
FT VARIANT 166
FT /note="M -> T (may represent an allelic difference or a
FT cloning artifact)"
FT /evidence="ECO:0000269|Ref.3"
FT HELIX 25..38
FT /evidence="ECO:0007829|PDB:1D9C"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:1D9G"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:1D9G"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:1D9C"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1D9C"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1D9C"
FT HELIX 66..81
FT /evidence="ECO:0007829|PDB:1D9C"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:1D9C"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1D9C"
FT HELIX 90..104
FT /evidence="ECO:0007829|PDB:1D9C"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:1D9C"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:1D9C"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:1D9C"
SQ SEQUENCE 166 AA; 19393 MW; 27B268B950BB3B1F CRC64;
MKYTSYFLAL LLCGLLGFSG SYGQGQFFRE IENLKEYFNA SSPDVAKGGP LFSEILKNWK
DESDKKIIQS QIVSFYFKLF ENLKDNQVIQ RSMDIIKQDM FQKFLNGSSE KLEDFKKLIQ
IPVDDLQIQR KAINELIKVM NDLSPKSNLR KRKRSQNLFR GRRASM
