ID   IFNA1_RAT               Reviewed;         192 AA.
AC   P05011;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Interferon alpha-1;
DE   Flags: Precursor;
GN   Name=Ifna1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GLYCOSYLATION AT ASN-190.
RX   PubMed=6320120; DOI=10.1093/nar/12.2.1227;
RA   Dijkema R., Pouwels P., de Reus A., Schellekens H.;
RT   "Structure and expression in Escherichia coli of a cloned rat interferon-
RT   alpha gene.";
RL   Nucleic Acids Res. 12:1227-1242(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3020354; DOI=10.1016/0076-6879(86)19064-1;
RA   van der Meide P.H., Dijkema R., Caspers M., Vijverberg K., Schellekens H.;
RT   "Cloning, expression, and purification of rat IFN-alpha 1.";
RL   Methods Enzymol. 119:441-453(1986).
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: There appear to be at least 12 rat interferon-alpha-1
CC       genes.
CC   -!- MISCELLANEOUS: The antiviral activity of this interferon appears to be
CC       independent of glycosylation.
CC   -!- SIMILARITY: Belongs to the alpha/beta interferon family. {ECO:0000305}.
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DR   EMBL; X00336; CAA25091.1; -; Genomic_DNA.
DR   PIR; A23179; IVRTA1.
DR   RefSeq; NP_001014786.1; NM_001014786.1.
DR   AlphaFoldDB; P05011; -.
DR   SMR; P05011; -.
DR   STRING; 10116.ENSRNOP00000051043; -.
DR   GlyGen; P05011; 1 site.
DR   iPTMnet; P05011; -.
DR   PaxDb; P05011; -.
DR   GeneID; 298210; -.
DR   KEGG; rno:298210; -.
DR   UCSC; RGD:1359312; rat.
DR   CTD; 3442; -.
DR   RGD; 1359312; Ifna1.
DR   eggNOG; ENOG502SQAC; Eukaryota.
DR   InParanoid; P05011; -.
DR   OrthoDB; 1358010at2759; -.
DR   PhylomeDB; P05011; -.
DR   Reactome; R-RNO-909733; Interferon alpha/beta signaling.
DR   Reactome; R-RNO-912694; Regulation of IFNA/IFNB signaling.
DR   PRO; PR:P05011; -.
DR   Proteomes; UP000002494; Unplaced.
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   Antiviral defense; Cytokine; Disulfide bond; Glycoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT   CHAIN           24..192
FT                   /note="Interferon alpha-1"
FT                   /id="PRO_0000016383"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305|PubMed:6320120"
FT   DISULFID        24..122
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..162
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   192 AA;  21935 MW;  9FD1ECE8554AE604 CRC64;
     MARLCAFLMS LVVVSYWSAC CLGCDLPHTH NLRNKRVFTL LAQMRRLSPV SCLKDRKYFG
     FPLEKVDGQQ IQKAQAIPVL HELTQQILSL FTSKESSTAW DATLLDSFCN DLQQQLSGLQ
     ACLMQQVGVQ ESPLTQEDSL LAVREYFHRI TVYLRENKHS PCAWEVVKAE VWRALSSSAN
     LMGRLREERN ES