IFNA2_MOUSE
ID IFNA2_MOUSE Reviewed; 190 AA.
AC P01573; Q61717;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Interferon alpha-2;
DE Short=IFN-alpha-2;
DE Flags: Precursor;
GN Name=Ifna2;
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=6188104; DOI=10.1093/nar/11.3.555;
RA Shaw G.D., Boll W., Taira H., Mantei N., Lengyel P., Weissmann C.;
RT "Structure and expression of cloned murine IFN-alpha genes.";
RL Nucleic Acids Res. 11:555-573(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2987810; DOI=10.1093/nar/13.3.791;
RA Zwarthoff E.C., Mooren A.T.A., Trapman J.;
RT "Organization, structure and expression of murine interferon alpha genes.";
RL Nucleic Acids Res. 13:791-804(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 55-190.
RX PubMed=6689487; DOI=10.1016/0378-1119(83)90188-9;
RA Kelly K.A., Kozak C.A., Dandoy F., Sor F., Skup D., Windass J.D.,
RA DeMaeyer-Guignard J., Pitha P.M., DeMaeyer E.;
RT "Mapping of murine interferon-alpha genes to chromosome 4.";
RL Gene 26:181-188(1983).
CC -!- FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities.
CC {ECO:0000269|PubMed:2987810}.
CC -!- SUBUNIT: Interacts with IFNAR2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alpha/beta interferon family. {ECO:0000305}.
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DR EMBL; X01969; CAA26002.1; -; Genomic_DNA.
DR EMBL; K01411; AAA37885.1; -; mRNA.
DR CCDS; CCDS18326.1; -.
DR PIR; A01837; IVMSA2.
DR PDB; 7E0E; X-ray; 2.10 A; A=24-190.
DR PDBsum; 7E0E; -.
DR AlphaFoldDB; P01573; -.
DR SMR; P01573; -.
DR STRING; 10090.ENSMUSP00000100778; -.
DR GlyGen; P01573; 1 site.
DR PaxDb; P01573; -.
DR PRIDE; P01573; -.
DR ABCD; P01573; 1 sequenced antibody.
DR MGI; MGI:107666; Ifna2.
DR eggNOG; ENOG502SQAC; Eukaryota.
DR InParanoid; P01573; -.
DR PhylomeDB; P01573; -.
DR Reactome; R-MMU-909733; Interferon alpha/beta signaling.
DR Reactome; R-MMU-912694; Regulation of IFNA/IFNB signaling.
DR PRO; PR:P01573; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01573; 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..190
FT /note="Interferon alpha-2"
FT /id="PRO_0000016376"
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 CONFLICT 123
FT /note="L -> P (in Ref. 3; AAA37885)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="Q -> K (in Ref. 3; AAA37885)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="A -> T (in Ref. 3; AAA37885)"
FT /evidence="ECO:0000305"
FT HELIX 28..43
FT /evidence="ECO:0007829|PDB:7E0E"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:7E0E"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:7E0E"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:7E0E"
FT HELIX 73..91
FT /evidence="ECO:0007829|PDB:7E0E"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:7E0E"
FT HELIX 102..121
FT /evidence="ECO:0007829|PDB:7E0E"
FT HELIX 136..156
FT /evidence="ECO:0007829|PDB:7E0E"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:7E0E"
FT HELIX 161..178
FT /evidence="ECO:0007829|PDB:7E0E"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:7E0E"
SQ SEQUENCE 190 AA; 21922 MW; EFA97FC69C300FD5 CRC64;
MARLCAFLVM LIVMSYWSIC SLGCDLPHTY NLRNKRALKV LAQMRRLPFL SCLKDRQDFG
FPLEKVDNQQ IQKAQAIPVL RDLTQQTLNL FTSKASSAAW NATLLDSFCN DLHQQLNDLQ
TCLMQQVGVQ EPPLTQEDAL LAVRKYFHRI TVYLREKKHS PCAWEVVRAE VWRALSSSVN
LLPRLSEEKE
