IFNA1_MOUSE
ID IFNA1_MOUSE Reviewed; 189 AA.
AC P01572; Q7M0A3; Q810G7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Interferon alpha-1;
DE Short=IFN-alpha-1;
DE Flags: Precursor;
GN Name=Ifna1;
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].
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND GLYCOSYLATION.
RC STRAIN=C57BL/6J;
RX PubMed=15254193; DOI=10.1128/jvi.78.15.8219-8228.2004;
RA van Pesch V., Lanaya H., Renauld J.C., Michiels T.;
RT "Characterization of the murine alpha interferon gene family.";
RL J. Virol. 78:8219-8228(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 24-51; 124-146 AND 175-181.
RX PubMed=9244179; DOI=10.1016/0167-4889(95)00159-x;
RA Beare D., Learmonth M., Wells V., Aitken A., Mallucci L.;
RT "Characterisation and antiproliferative activity of an alpha-type murine
RT interferon from embryonic fibroblasts.";
RL Biochim. Biophys. Acta 1310:81-85(1996).
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. {ECO:0000269|PubMed:15254193}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:15254193}.
CC -!- SIMILARITY: Belongs to the alpha/beta interferon family. {ECO:0000305}.
CC -!- CAUTION: Was named interferon alpha-E (embryonic) based on peptide
CC sequencing (PubMed:9244179). The differences found may be sequencing
CC erros and have not been confirmed by other studies.
CC {ECO:0000305|PubMed:9244179}.
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DR EMBL; X01974; CAA26006.1; -; Genomic_DNA.
DR EMBL; AY225950; AAO63592.1; -; Genomic_DNA.
DR EMBL; BX530016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466527; EDL30958.1; -; Genomic_DNA.
DR CCDS; CCDS18347.1; -.
DR PIR; A01836; IVMSA1.
DR PIR; S62682; S62682.
DR RefSeq; NP_034632.2; NM_010502.2.
DR AlphaFoldDB; P01572; -.
DR SMR; P01572; -.
DR STRING; 10090.ENSMUSP00000092580; -.
DR GlyGen; P01572; 1 site.
DR iPTMnet; P01572; -.
DR PhosphoSitePlus; P01572; -.
DR PaxDb; P01572; -.
DR PRIDE; P01572; -.
DR ABCD; P01572; 1 sequenced antibody.
DR DNASU; 15962; -.
DR Ensembl; ENSMUST00000094972; ENSMUSP00000092580; ENSMUSG00000095498.
DR GeneID; 15962; -.
DR KEGG; mmu:15962; -.
DR UCSC; uc008toc.1; mouse.
DR CTD; 3439; -.
DR MGI; MGI:107668; Ifna1.
DR VEuPathDB; HostDB:ENSMUSG00000095498; -.
DR eggNOG; ENOG502SQAC; Eukaryota.
DR GeneTree; ENSGT01000000214430; -.
DR HOGENOM; CLU_109427_0_0_1; -.
DR InParanoid; P01572; -.
DR OMA; RRTLMIM; -.
DR OrthoDB; 1358010at2759; -.
DR PhylomeDB; P01572; -.
DR TreeFam; TF336177; -.
DR Reactome; R-MMU-909733; Interferon alpha/beta signaling.
DR Reactome; R-MMU-912694; Regulation of IFNA/IFNB signaling.
DR SABIO-RK; P01572; -.
DR BioGRID-ORCS; 15962; 8 hits in 38 CRISPR screens.
DR PRO; PR:P01572; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P01572; protein.
DR Genevisible; P01572; MM.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:0005125; F:cytokine activity; IDA:MGI.
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:0042742; P:defense response to bacterium; IDA:MGI.
DR GO; GO:0051607; P:defense response to virus; IDA:MGI.
DR GO; GO:0006959; P:humoral immune response; IBA:GO_Central.
DR GO; GO:0002323; P:natural killer cell activation involved in immune response; IDA:MGI.
DR GO; GO:0033141; P:positive regulation of peptidyl-serine phosphorylation of STAT protein; IBA:GO_Central.
DR GO; GO:0050691; P:regulation of defense response to virus by host; IDA:CAFA.
DR GO; GO:0043330; P:response to exogenous dsRNA; IBA:GO_Central.
DR GO; GO:0002286; P:T cell activation involved in immune response; IDA:MGI.
DR GO; GO:0060337; P:type I interferon signaling pathway; IDA:CAFA.
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 Antiviral defense; Cytokine; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:9244179"
FT CHAIN 24..189
FT /note="Interferon alpha-1"
FT /id="PRO_0000016375"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:15254193"
FT DISULFID 24..122
FT /evidence="ECO:0000250"
FT DISULFID 52..162
FT /evidence="ECO:0000250"
FT CONFLICT 14
FT /note="L -> M (in Ref. 1; no nucleotide entry and 2;
FT CAA26006)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="T -> A (in Ref. 1; no nucleotide entry and 2;
FT CAA26006)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="Q -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="F -> P (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="A -> Y (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="K -> T (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="L -> M (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 180..181
FT /note="NV -> KL (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 21646 MW; D6F4BC96DCE7D67E CRC64;
MARLCAFLMV LAVLSYWPTC SLGCDLPQTH NLRNKRALTL LVQMRRLSPL SCLKDRKDFG
FPQEKVDAQQ IKKAQAIPVL SELTQQILNI FTSKDSSAAW NTTLLDSFCN DLHQQLNDLQ
GCLMQQVGVQ EFPLTQEDAL LAVRKYFHRI TVYLREKKHS PCAWEVVRAE VWRALSSSAN
VLGRLREEK
