ID   IFNA5_MOUSE             Reviewed;         189 AA.
AC   P07349;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Interferon alpha-5;
DE            Short=IFN-alpha-5;
DE   Flags: Precursor;
GN   Name=Ifna5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2987811; DOI=10.1093/nar/13.3.805;
RA   Kelly K.A., Pitha P.M.;
RT   "Characterization of a mouse interferon gene locus I. Isolation of a
RT   cluster of four alpha interferon genes.";
RL   Nucleic Acids Res. 13:805-823(1985).
CC   -!- FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities.
CC       Interferon stimulates the production of two enzymes: a protein kinase
CC       and an oligoadenylate synthetase.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the alpha/beta interferon family. {ECO:0000305}.
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DR   EMBL; X01971; CAA26003.1; ALT_SEQ; Genomic_DNA.
DR   CCDS; CCDS18345.1; -.
DR   PIR; C23087; IVMSA5.
DR   PDB; 3OQ3; X-ray; 2.10 A; A=24-189.
DR   PDBsum; 3OQ3; -.
DR   AlphaFoldDB; P07349; -.
DR   SMR; P07349; -.
DR   STRING; 10090.ENSMUSP00000099868; -.
DR   GlyGen; P07349; 1 site.
DR   PaxDb; P07349; -.
DR   PRIDE; P07349; -.
DR   ABCD; P07349; 1 sequenced antibody.
DR   MGI; MGI:107663; Ifna5.
DR   eggNOG; ENOG502SQAC; Eukaryota.
DR   InParanoid; P07349; -.
DR   PhylomeDB; P07349; -.
DR   Reactome; R-MMU-909733; Interferon alpha/beta signaling.
DR   Reactome; R-MMU-912694; Regulation of IFNA/IFNB signaling.
DR   EvolutionaryTrace; P07349; -.
DR   PRO; PR:P07349; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P07349; protein.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0005132; F:type I interferon receptor binding; IBA:GO_Central.
DR   GO; GO:0002250; P:adaptive immune response; IBA:GO_Central.
DR   GO; GO:0030183; P:B cell differentiation; IBA:GO_Central.
DR   GO; GO:0042100; P:B cell proliferation; IBA:GO_Central.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0006959; P:humoral immune response; IBA:GO_Central.
DR   GO; GO:0002323; P:natural killer cell activation involved in immune response; IBA:GO_Central.
DR   GO; GO:0033141; P:positive regulation of peptidyl-serine phosphorylation of STAT protein; IBA:GO_Central.
DR   GO; GO:0043330; P:response to exogenous dsRNA; IBA:GO_Central.
DR   GO; GO:0002286; P:T cell activation involved in immune response; IBA:GO_Central.
DR   CDD; cd00095; IFab; 1.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR000471; Interferon_alpha/beta/delta.
DR   PANTHER; PTHR11691; PTHR11691; 1.
DR   Pfam; PF00143; Interferon; 1.
DR   PRINTS; PR00266; INTERFERONAB.
DR   SMART; SM00076; IFabd; 1.
DR   SUPFAM; SSF47266; SSF47266; 1.
DR   PROSITE; PS00252; INTERFERON_A_B_D; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; Cytokine; Disulfide bond; Glycoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..189
FT                   /note="Interferon alpha-5"
FT                   /id="PRO_0000016378"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        24..122
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..162
FT                   /evidence="ECO:0000250"
FT   HELIX           32..44
FT                   /evidence="ECO:0007829|PDB:3OQ3"
FT   HELIX           49..51
FT                   /evidence="ECO:0007829|PDB:3OQ3"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:3OQ3"
FT   TURN            68..70
FT                   /evidence="ECO:0007829|PDB:3OQ3"
FT   HELIX           73..91
FT                   /evidence="ECO:0007829|PDB:3OQ3"
FT   HELIX           94..99
FT                   /evidence="ECO:0007829|PDB:3OQ3"
FT   HELIX           102..125
FT                   /evidence="ECO:0007829|PDB:3OQ3"
FT   HELIX           133..156
FT                   /evidence="ECO:0007829|PDB:3OQ3"
FT   TURN            157..159
FT                   /evidence="ECO:0007829|PDB:3OQ3"
FT   HELIX           161..187
FT                   /evidence="ECO:0007829|PDB:3OQ3"
SQ   SEQUENCE   189 AA;  21514 MW;  8BB9CDFD15F5C3BD CRC64;
     MARLCAFLMV LPVLSYWPTC SLGCDLPQTH NLRNKRALTL LVKMRRLSPL SCLKDRKDFG
     FPQEKVGAQQ IQEAQAIPVL SELTQQVLNI FTSKDSSAAW NATLLDSFCN EVHQQLNDLK
     ACVMQQVGVQ ESPLTQEDSL LAVRKYFHRI TVYLREKKHS PCAWEVVRAE VWRALSSSVN
     LLARLSKEE