ID   IFNG_MOSBE              Reviewed;         166 AA.
AC   Q647G2;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Interferon gamma;
DE            Short=IFN-gamma;
DE   Flags: Precursor;
GN   Name=IFNG;
OS   Moschus berezovskii (Chinese forest musk deer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Moschidae;
OC   Moschus.
OX   NCBI_TaxID=68408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zou F., Liu S., Lai B., Yue B.;
RT   "Cloning and expression of gamma interferon gene from musk deer (Moschus
RT   berezovskii).";
RL   Submitted (AUG-2004) 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; AY722800; AAU14169.1; -; mRNA.
DR   AlphaFoldDB; Q647G2; -.
DR   SMR; Q647G2; -.
DR   PRIDE; Q647G2; -.
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_0000016452"
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;  19477 MW;  0D86178DEF3DC4A0 CRC64;
     MKYTSYFLAL QLCLLLGFSG SYGQGPFFKE IENLKEYFNA SNPDVATGGP LFLEILKNWK
     EESDKKIIQS QIVSFYFKLF ENFKDDQVIQ RSMDIIKQDM FQKFLNGSSE KLEDFKKLIQ
     IPVDDLQIQR KAINELIKVM NDLLPKSNLR KRKRSQNLFR GRRAST