IFNG_EQUAS
ID IFNG_EQUAS Reviewed; 166 AA.
AC O77763;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Interferon gamma;
DE Short=IFN-gamma;
DE Flags: Precursor;
GN Name=IFNG;
OS Equus asinus (Donkey) (Equus africanus asinus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9793;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Burr P.D., Nasir L., Nicolson L., Argyle D.J., Reid S.W.J.;
RT "Nucleotide sequence of the donkey interferon gamma cDNA.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
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; AF055341; AAC42595.1; -; mRNA.
DR RefSeq; XP_014716180.1; XM_014860694.1.
DR AlphaFoldDB; O77763; -.
DR SMR; O77763; -.
DR GeneID; 106843591; -.
DR KEGG; eai:106843591; -.
DR CTD; 3458; -.
DR OMA; GGPIFTE; -.
DR OrthoDB; 1382686at2759; -.
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:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..166
FT /note="Interferon gamma"
FT /id="PRO_0000016441"
FT REGION 147..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..166
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 19311 MW; A335B4E05B7132AD CRC64;
MNYTSFILAF QLCAILGSST YYCQAAFFKE IENLKEYFNA SSPDVGDGGP LFLDILKNWK
EDSDKKIIQS QIVSFYFKLF ENLKDNQVIQ KSMDTIKEDL FVKFFNSSTS KLEDFQKLIQ
IPVNDLKVQR KAISELIKVM NDLSPKANLR KRKRSQNPFR GRRALQ