IFNB_MOUSE
ID IFNB_MOUSE Reviewed; 182 AA.
AC P01575;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Interferon beta;
DE Short=IFN-beta;
DE Flags: Precursor;
GN Name=Ifnb1; Synonyms=Ifb, Ifnb;
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 [MRNA].
RX PubMed=6688252; DOI=10.1016/s0021-9258(17)44698-9;
RA Higashi Y., Sokawa Y., Watanabe Y., Kawade Y., Ohno S., Takaoka C.,
RA Taniguchi T.;
RT "Structure and expression of a cloned cDNA for mouse interferon-beta.";
RL J. Biol. Chem. 258:9522-9529(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2726460; DOI=10.1093/nar/17.8.3291;
RA Kuga T., Fujita T., Taniguchi T.;
RT "Nucleotide sequence of the mouse interferon-beta gene.";
RL Nucleic Acids Res. 17:3291-3291(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3221389; DOI=10.1016/0022-2836(88)90571-2;
RA Vodjdani G., Coulombel C., Doly J.;
RT "Structure and characterization of a murine chromosomal fragment containing
RT the interferon beta gene.";
RL J. Mol. Biol. 204:221-231(1988).
RN [4]
RP STRUCTURE OF CARBOHYDRATES.
RX PubMed=3360010; DOI=10.1111/j.1432-1033.1988.tb14000.x;
RA Civas A., Fournet B., Coulombel C., le Roscouet D., Honvault A., Petek F.,
RA Montreuil J., Doly J.;
RT "Purification and carbohydrate structure of natural murine interferon-
RT beta.";
RL Eur. J. Biochem. 173:311-316(1988).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
RA Senda T., Matsuda S., Kurihara H., Nakamura K.T., Kawano G., Shimizu H.,
RA Mizuno H., Mitsui Y.;
RT "Three-dimensional structure of recombinant murine interferon-beta.";
RL Proc. Jpn. Acad., B, Phys. Biol. Sci. 66:77-80(1990).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=1505514; DOI=10.1002/j.1460-2075.1992.tb05396.x;
RA Senda T., Shimazu T., Matsuda S., Kawano G., Shimizu H., Nakamura K.T.,
RA Mitsui Y.;
RT "Three-dimensional crystal structure of recombinant murine interferon-
RT beta.";
RL EMBO J. 11:3193-3201(1992).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RX PubMed=7473712; DOI=10.1006/jmbi.1995.0544;
RA Senda T., Saitoh S., Mitsui Y.;
RT "Refined crystal structure of recombinant murine interferon-beta at 2.15-A
RT resolution.";
RL J. Mol. Biol. 253:187-207(1995).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 22-182 IN COMPLEX WITH IFNAR1, AND
RP SUBUNIT.
RX PubMed=23872679; DOI=10.1038/ni.2667;
RA de Weerd N.A., Vivian J.P., Nguyen T.K., Mangan N.E., Gould J.A.,
RA Braniff S.J., Zaker-Tabrizi L., Fung K.Y., Forster S.C., Beddoe T.,
RA Reid H.H., Rossjohn J., Hertzog P.J.;
RT "Structural basis of a unique interferon-beta signaling axis mediated via
RT the receptor IFNAR1.";
RL Nat. Immunol. 14:901-907(2013).
CC -!- FUNCTION: Has antiviral, antibacterial and anticancer activities.
CC -!- SUBUNIT: Monomer. Signals mostly via binding to a IFNAR1-IFNAR2
CC heterodimeric receptor, but can also function with IFNAR1 alone and
CC independently of Jak-STAT pathways. {ECO:0000269|PubMed:23872679}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: This beta interferon does not have a disulfide bond.
CC -!- SIMILARITY: Belongs to the alpha/beta interferon family. {ECO:0000305}.
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DR EMBL; K00020; AAA37891.1; -; mRNA.
DR EMBL; X14455; CAA32625.1; -; Genomic_DNA.
DR EMBL; X14029; CAA32190.1; -; Genomic_DNA.
DR CCDS; CCDS18318.1; -.
DR PIR; S02020; IVMSB.
DR RefSeq; NP_034640.1; NM_010510.1.
DR PDB; 1IFA; X-ray; 2.60 A; A=24-181.
DR PDB; 1WU3; X-ray; 2.15 A; I=22-182.
DR PDB; 3WCY; X-ray; 2.90 A; I=22-182.
DR PDBsum; 1IFA; -.
DR PDBsum; 1WU3; -.
DR PDBsum; 3WCY; -.
DR AlphaFoldDB; P01575; -.
DR SMR; P01575; -.
DR STRING; 10090.ENSMUSP00000056720; -.
DR GlyConnect; 292; 9 N-Linked glycans.
DR GlyGen; P01575; 4 sites, 16 N-linked glycans (1 site).
DR PhosphoSitePlus; P01575; -.
DR PaxDb; P01575; -.
DR PRIDE; P01575; -.
DR Antibodypedia; 3995; 1010 antibodies from 43 providers.
DR DNASU; 15977; -.
DR Ensembl; ENSMUST00000055671; ENSMUSP00000056720; ENSMUSG00000048806.
DR GeneID; 15977; -.
DR KEGG; mmu:15977; -.
DR UCSC; uc008tmz.1; mouse.
DR CTD; 3456; -.
DR MGI; MGI:107657; Ifnb1.
DR VEuPathDB; HostDB:ENSMUSG00000048806; -.
DR eggNOG; ENOG502SQGR; Eukaryota.
DR GeneTree; ENSGT01000000214430; -.
DR HOGENOM; CLU_109427_1_0_1; -.
DR InParanoid; P01575; -.
DR OMA; HWQKEHL; -.
DR OrthoDB; 1358010at2759; -.
DR PhylomeDB; P01575; -.
DR TreeFam; TF336177; -.
DR Reactome; R-MMU-909733; Interferon alpha/beta signaling.
DR Reactome; R-MMU-912694; Regulation of IFNA/IFNB signaling.
DR BioGRID-ORCS; 15977; 1 hit in 71 CRISPR screens.
DR EvolutionaryTrace; P01575; -.
DR PRO; PR:P01575; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P01575; protein.
DR Bgee; ENSMUSG00000048806; Expressed in sternocleidomastoid and 10 other tissues.
DR ExpressionAtlas; P01575; baseline and differential.
DR Genevisible; P01575; MM.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0008811; F:chloramphenicol O-acetyltransferase activity; ISO:MGI.
DR GO; GO:0005125; F:cytokine activity; IDA:MGI.
DR GO; GO:0005132; F:type I interferon receptor binding; IPI:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IDA:MGI.
DR GO; GO:0002312; P:B cell activation involved in immune response; ISO:MGI.
DR GO; GO:0030183; P:B cell differentiation; IBA:GO_Central.
DR GO; GO:0042100; P:B cell proliferation; IMP:UniProtKB.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:MGI.
DR GO; GO:0071359; P:cellular response to dsRNA; IEP:UniProtKB.
DR GO; GO:0035458; P:cellular response to interferon-beta; ISO:MGI.
DR GO; GO:0098586; P:cellular response to virus; IDA:UniProtKB.
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; IDA:MGI.
DR GO; GO:0002281; P:macrophage activation involved in immune response; ISO:MGI.
DR GO; GO:0002323; P:natural killer cell activation involved in immune response; IBA:GO_Central.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IDA:MGI.
DR GO; GO:0045581; P:negative regulation of T cell differentiation; ISO:MGI.
DR GO; GO:2000552; P:negative regulation of T-helper 2 cell cytokine production; ISO:MGI.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISO:MGI.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0033141; P:positive regulation of peptidyl-serine phosphorylation of STAT protein; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0043330; P:response to exogenous dsRNA; ISO:MGI.
DR GO; GO:0002286; P:T cell activation involved in immune response; IBA:GO_Central.
DR GO; GO:0060337; P:type I interferon signaling pathway; IMP:UniProtKB.
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 InterPro; IPR015588; Interferon_beta.
DR PANTHER; PTHR11691; PTHR11691; 1.
DR PANTHER; PTHR11691:SF68; PTHR11691:SF68; 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 Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT CHAIN 22..182
FT /note="Interferon beta"
FT /id="PRO_0000016403"
FT MOD_RES 24
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P70499"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT HELIX 24..43
FT /evidence="ECO:0007829|PDB:1WU3"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:1WU3"
FT HELIX 69..86
FT /evidence="ECO:0007829|PDB:1WU3"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1WU3"
FT HELIX 98..118
FT /evidence="ECO:0007829|PDB:1WU3"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:1WU3"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:1WU3"
FT HELIX 133..151
FT /evidence="ECO:0007829|PDB:1WU3"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:1WU3"
FT HELIX 156..176
FT /evidence="ECO:0007829|PDB:1WU3"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:1WU3"
SQ SEQUENCE 182 AA; 22127 MW; 8C4C32947FD1B917 CRC64;
MNNRWILHAA FLLCFSTTAL SINYKQLQLQ ERTNIRKCQE LLEQLNGKIN LTYRADFKIP
MEMTEKMQKS YTAFAIQEML QNVFLVFRNN FSSTGWNETI VVRLLDELHQ QTVFLKTVLE
EKQEERLTWE MSSTALHLKS YYWRVQRYLK LMKYNSYAWM VVRAEIFRNF LIIRRLTRNF
QN
