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IFNAD_MOUSE
ID   IFNAD_MOUSE             Reviewed;         189 AA.
AC   Q80SU4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Interferon alpha-13;
DE            Short=IFN-alpha-13;
DE   Flags: Precursor;
GN   Name=Ifna13;
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], FUNCTION, AND INDUCTION.
RC   STRAIN=129/Sv;
RX   PubMed=12930842; DOI=10.1074/jbc.m302554200;
RA   van Pesch V., Michiels T.;
RT   "Characterization of interferon-alpha 13, a novel constitutive murine
RT   interferon-alpha subtype.";
RL   J. Biol. Chem. 278:46321-46328(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=15233997; DOI=10.1016/j.ygeno.2004.03.003;
RA   Hardy M.P., Owczarek C.M., Jermiin L.S., Ejdebaeck M., Hertzog P.J.;
RT   "Characterization of the type I interferon locus and identification of
RT   novel genes.";
RL   Genomics 84:331-345(2004).
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: Exhibits antiviral activity against Theiler's virus, Mengo
CC       virus and vesicular stomatitis virus. Interferons alpha stimulate the
CC       production of two enzymes: a protein kinase and an oligoadenylate
CC       synthetase. {ECO:0000269|PubMed:12930842}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: Transcribed constitutively. Not induces by viral infection.
CC       {ECO:0000269|PubMed:12930842}.
CC   -!- SIMILARITY: Belongs to the alpha/beta interferon family. {ECO:0000305}.
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DR   EMBL; AY190047; AAO38688.1; -; mRNA.
DR   EMBL; AY220461; AAO64454.1; -; Genomic_DNA.
DR   EMBL; BC120724; AAI20725.1; -; mRNA.
DR   EMBL; BC120750; AAI20751.1; -; mRNA.
DR   CCDS; CCDS18324.1; -.
DR   RefSeq; NP_796321.1; NM_177347.2.
DR   AlphaFoldDB; Q80SU4; -.
DR   SMR; Q80SU4; -.
DR   STRING; 10090.ENSMUSP00000072517; -.
DR   GlyGen; Q80SU4; 2 sites.
DR   iPTMnet; Q80SU4; -.
DR   PhosphoSitePlus; Q80SU4; -.
DR   PaxDb; Q80SU4; -.
DR   PRIDE; Q80SU4; -.
DR   DNASU; 230396; -.
DR   Ensembl; ENSMUST00000105149; ENSMUSP00000100780; ENSMUSG00000063376.
DR   GeneID; 230396; -.
DR   KEGG; mmu:230396; -.
DR   UCSC; uc008tng.1; mouse.
DR   CTD; 3447; -.
DR   MGI; MGI:2667155; Ifna13.
DR   VEuPathDB; HostDB:ENSMUSG00000063376; -.
DR   eggNOG; ENOG502SQAC; Eukaryota.
DR   GeneTree; ENSGT01000000214430; -.
DR   HOGENOM; CLU_109427_0_0_1; -.
DR   InParanoid; Q80SU4; -.
DR   OMA; QYCAWEF; -.
DR   OrthoDB; 1358010at2759; -.
DR   PhylomeDB; Q80SU4; -.
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; 230396; 2 hits in 68 CRISPR screens.
DR   PRO; PR:Q80SU4; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q80SU4; protein.
DR   Bgee; ENSMUSG00000063376; Expressed in embryo.
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   2: Evidence at transcript level;
KW   Antiviral defense; Cytokine; Disulfide bond; Glycoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..189
FT                   /note="Interferon alpha-13"
FT                   /id="PRO_5000090349"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        24..122
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..162
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   189 AA;  21567 MW;  C0CB2AA2813186CE CRC64;
     MARPCAFLMV LVVLSYWSAC SLGCDLPQTH NLRNKRALTL LEQMRRLSPL SCLKDRKDFG
     FPQEKVDAQQ IKKAQAIPFV HELTQQILTL FTSNDSSAAW NATLLDSFCN DLHQQLNDLK
     ACLMQQVGVQ EFPLTQEDSL LAVRKYFHSI TVYLREKKHS PCAWEVVRAE VQRTLSSSAN
     LLARLSKEE
 
 
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