ID   IFNG_PAROL              Reviewed;         198 AA.
AC   B3IXK1; B3IXK0;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Interferon gamma {ECO:0000303|Ref.1};
DE   Flags: Precursor;
GN   Name=ifng {ECO:0000303|Ref.1};
OS   Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Paralichthyidae;
OC   Paralichthys.
OX   NCBI_TaxID=8255 {ECO:0000312|EMBL:BAG50577.1};
RN   [1] {ECO:0000312|EMBL:BAG50577.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX   DOI=10.1007/s12562-008-0019-3;
RA   Matsuyama T., Fujiwara A., Sakai T., Nakayasu C.;
RT   "Molecular cloning and expression analysis of interferon gamma gene in
RT   Japanese flounder Paralichthys olivaceus.";
RL   Fish. Sci. 75:253-255(2009).
RN   [2] {ECO:0000305}
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-198, FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=29742458; DOI=10.1016/j.fsi.2018.05.008;
RA   Zahradnik J., Kolarova L., Parizkova H., Kolenko P., Schneider B.;
RT   "Interferons type II and their receptors R1 and R2 in fish species:
RT   Evolution, structure, and function.";
RL   Fish Shellfish Immunol. 79:140-152(2018).
CC   -!- FUNCTION: Cytokine which binds to interferon gamma receptor 1 (ifngr1)
CC       (PubMed:29742458). Also binds with lower affinity to interferon gamma
CC       receptor 1-like (ifngr1l) (PubMed:29742458). Has activating effects on
CC       macrophages and neutrophils (By similarity).
CC       {ECO:0000250|UniProtKB:B5B3U4, ECO:0000269|PubMed:29742458}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:29742458}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:29742458}.
CC   -!- INDUCTION: Strongly up-regulated in response to viral hemorrhagic
CC       septicaemia virus infection. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the type II (or gamma) interferon family.
CC       {ECO:0000305}.
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DR   EMBL; AB435093; BAG50576.1; -; mRNA.
DR   EMBL; AB435094; BAG50577.1; -; mRNA.
DR   RefSeq; XP_019964836.1; XM_020109277.1.
DR   PDB; 6F1E; X-ray; 2.30 A; A/B=24-198.
DR   PDBsum; 6F1E; -.
DR   AlphaFoldDB; B3IXK1; -.
DR   SMR; B3IXK1; -.
DR   GeneID; 109644000; -.
DR   KEGG; pov:109644000; -.
DR   CTD; 405790; -.
DR   OrthoDB; 1236990at2759; -.
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; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
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   SUPFAM; SSF47266; SSF47266; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytokine; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..198
FT                   /note="Interferon gamma"
FT                   /id="PRO_5002789827"
FT   REGION          173..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..198
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        98..99
FT                   /note="GS -> VA (in Ref. 1; BAG50576)"
FT                   /evidence="ECO:0000305"
FT   HELIX           28..40
FT                   /evidence="ECO:0007829|PDB:6F1E"
FT   HELIX           45..48
FT                   /evidence="ECO:0007829|PDB:6F1E"
FT   STRAND          60..62
FT                   /evidence="ECO:0007829|PDB:6F1E"
FT   HELIX           64..87
FT                   /evidence="ECO:0007829|PDB:6F1E"
FT   HELIX           112..130
FT                   /evidence="ECO:0007829|PDB:6F1E"
FT   HELIX           132..145
FT                   /evidence="ECO:0007829|PDB:6F1E"
FT   HELIX           152..160
FT                   /evidence="ECO:0007829|PDB:6F1E"
FT   HELIX           162..172
FT                   /evidence="ECO:0007829|PDB:6F1E"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:6F1E"
FT   HELIX           178..184
FT                   /evidence="ECO:0007829|PDB:6F1E"
SQ   SEQUENCE   198 AA;  22822 MW;  91838A05F5459CCB CRC64;
     MMVSTARAVV CLSLCLCVCQ VRGSHIPARM NKTIQNLLQH YNISNKDRFN GKPVFPKEPL
     SGRMETKMLF MGGVLETYEK LIGQMLEQLP NTTPPTAGSR EGLNSAAPEV SVRTDLNYIL
     KKVQELRTNR FKEQSKLLQG LHDLGDIKMN NFIIQSKALW ELQWMYEEAS SLSNNTKMQR
     RRRRRRRQAR KVKTPTRA