IFNA6_MOUSE
ID IFNA6_MOUSE Reviewed; 189 AA.
AC P07350; B9EKS5; P17660;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Interferon alpha-6;
DE Short=IFN-alpha-6;
DE AltName: Full=Interferon alpha-8;
DE Short=IFN-alpha-8;
DE Flags: Precursor;
GN Name=Ifna6; Synonyms=Ifa6, Ifa8, Ifna8;
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].
RC STRAIN=BALB/cJ;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2471809; DOI=10.1099/0022-1317-70-6-1381;
RA Navarro S., Dion M., Vodjdani G., Berlot-Picard F., Doly J.;
RT "Isolation and characterization of a functional murine interferon alpha
RT gene which is not expressed in fibroblasts upon virus induction.";
RL J. Gen. Virol. 70:1381-1389(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- MISCELLANEOUS: Not expressed in fibroblasts upon virus induction.
CC -!- SIMILARITY: Belongs to the alpha/beta interferon family. {ECO:0000305}.
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DR EMBL; X01972; CAA26004.1; -; Genomic_DNA.
DR EMBL; D00460; BAA00349.1; -; Genomic_DNA.
DR EMBL; BC151087; AAI51088.1; -; mRNA.
DR PIR; D23087; IVMSA6.
DR PIR; I49773; I49773.
DR AlphaFoldDB; P07350; -.
DR SMR; P07350; -.
DR STRING; 10090.ENSMUSP00000100777; -.
DR GlyGen; P07350; 1 site.
DR PRIDE; P07350; -.
DR ABCD; P07350; 1 sequenced antibody.
DR MGI; MGI:107662; Ifna6.
DR InParanoid; P07350; -.
DR PhylomeDB; P07350; -.
DR Reactome; R-MMU-909733; Interferon alpha/beta signaling.
DR Reactome; R-MMU-912694; Regulation of IFNA/IFNB signaling.
DR ChiTaRS; Ifna6; mouse.
DR PRO; PR:P07350; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P07350; protein.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
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; 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; 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 2: Evidence at transcript level;
KW 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-6"
FT /id="PRO_0000016379"
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 89
FT /note="T -> A (in Ref. 2; BAA00349)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 21499 MW; A960BC2531330684 CRC64;
MARLCAFLMV LAVLSYWPTC SLGCDLPQTH NLRNKRALTL LVKMRRLSPL SCLKDRKDFG
FPQEKVGAQQ IQEAQAIPVL TELTQQILTL FTSKDSSAAW NATLLDSFCN DLHQLLNDLQ
GCLMQQVEIQ ALPLTQEDSL LAVRTYFHRI TVFLREKKHS PCAWEVVRAE VWRALSSSAK
LLARLNEDE