IFNA2_HUMAN
ID IFNA2_HUMAN Reviewed; 188 AA.
AC P01563; H2DF54; H2DF55; P01564; Q14606; Q6DJX8; Q96KI6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Interferon alpha-2;
DE Short=IFN-alpha-2;
DE AltName: Full=Interferon alpha-A;
DE Short=LeIF A {ECO:0000303|PubMed:6159538};
DE Flags: Precursor;
GN Name=IFNA2; Synonyms=IFNA2A, IFNA2B, IFNA2C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELES ALPHA-2A AND ALPHA-2B),
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=6159538; DOI=10.1038/287411a0;
RA Goeddel D.V., Yelverton E., Ullrich A., Heyneker H.L., Miozzari G.,
RA Holmes W., Seeburg P.H., Dull T.J., May L., Stebbing N., Crea R., Maeda S.,
RA McCandliss R., Sloma A., Tabor J.M., Gross M., Familletti P.C., Pestka S.;
RT "Human leukocyte interferon produced by E. coli is biologically active.";
RL Nature 287:411-416(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELES ALPHA-2A AND ALPHA-2B).
RX PubMed=6163083; DOI=10.1038/290020a0;
RA Goeddel D.V., Leung D.W., Dull T.J., Gross M., Lawn R.M., McCandliss R.,
RA Seeburg P.H., Ullrich A., Yelverton E., Gray P.W.;
RT "The structure of eight distinct cloned human leukocyte interferon cDNAs.";
RL Nature 290:20-26(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELE ALPHA-2B).
RX PubMed=6170983; DOI=10.1073/pnas.78.9.5435;
RA Lawn R.M., Gross M., Houck C.M., Franke A.E., Gray P.V., Goeddel D.V.;
RT "DNA sequence of a major human leukocyte interferon gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:5435-5439(1981).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES ALPHA-2A AND ALPHA-2B).
RC TISSUE=Bone marrow tumor;
RX PubMed=3906813;
RA Oliver G., Balbas P., Valle F., Soberon X., Bolivar F.;
RT "Cloning of human leukocyte interferon cDNA and a strategy for its
RT production in E. coli.";
RL Rev. Latinoam. Microbiol. 27:141-150(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE ALPHA-2B).
RC TISSUE=Placenta;
RX PubMed=9694076;
RA Austruy E., Bagnis C., Carbuccia N., Maroc C., Birg F., Dubreuil P.,
RA Mannoni P., Chabannon C.;
RT "A defective retroviral vector encoding human interferon alpha 2 can
RT transduce human leukemic cell lines.";
RL Cancer Gene Ther. 5:247-256(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE ALPHA-2B).
RX PubMed=23875128; DOI=10.1186/2193-1801-2-264;
RA Gull I., Samra Z.Q., Aslam M.S., Athar M.A.;
RT "Heterologous expression, immunochemical and computational analysis of
RT recombinant human interferon alpha 2b.";
RL Springerplus 2:264-264(2013).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE ALPHA-2B).
RA Hanif K., Noor S., Naveed Y., Bashir B., Hussain T., Kanwal N.;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE ALPHA-2B).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE ALPHA-2B).
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).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 7-188 (ALLELE ALPHA-2B).
RX PubMed=6158094; DOI=10.1126/science.6158094;
RA Streuli M., Nagata S., Weissmann C.;
RT "At least three human type alpha interferons: structure of alpha 2.";
RL Science 209:1343-1347(1980).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-188.
RX PubMed=6310510; DOI=10.1093/nar/11.16.5661;
RA Weber H., Weissmann C.;
RT "Formation of genes coding for hybrid proteins by recombination between
RT related, cloned genes in E. coli.";
RL Nucleic Acids Res. 11:5661-5669(1983).
RN [14]
RP PROTEIN SEQUENCE OF 24-112 AND 136-188.
RX PubMed=6159537; DOI=10.1038/287408a0;
RA Allen G., Fantes K.H.;
RT "A family of structural genes for human lymphoblastoid (leukocyte-type)
RT interferon.";
RL Nature 287:408-411(1980).
RN [15]
RP PROTEIN SEQUENCE OF 24-58.
RX PubMed=9425112; DOI=10.1042/bj3290295;
RA Nyman T.A., Toeloe H., Parkkinen J., Kalkkinen N.;
RT "Identification of nine interferon-alpha subtypes produced by Sendai virus-
RT induced human peripheral blood leucocytes.";
RL Biochem. J. 329:295-302(1998).
RN [16]
RP DISULFIDE BONDS.
RX PubMed=6162107; DOI=10.1038/289606a0;
RA Wetzel R.;
RT "Assignment of the disulphide bonds of leukocyte interferon.";
RL Nature 289:606-607(1981).
RN [17]
RP GLYCOSYLATION AT THR-129, AND ALLELES ALPHA-2B AND ALPHA-2C.
RX PubMed=2049076; DOI=10.1042/bj2760511;
RA Adolf G.R., Kalsner I., Ahorn H., Maurer-Fogy I., Cantell K.;
RT "Natural human interferon-alpha 2 is O-glycosylated.";
RL Biochem. J. 276:511-518(1991).
RN [18]
RP POLYMORPHISM.
RX PubMed=7627809; DOI=10.1089/jir.1995.15.341;
RA Lee N., Ni D., Brissette R., Chou M., Hussain M., Gill D.S., Liao M.-J.,
RA Testa D.;
RT "Interferon-alpha 2 variants in the human genome.";
RL J. Interferon Cytokine Res. 15:341-349(1995).
RN [19]
RP 3D-STRUCTURE MODELING.
RX PubMed=8234245; DOI=10.1002/prot.340170109;
RA Murgolo N.J., Windsor W.T., Hruza A., Reichert P., Tsarbopoulos A.,
RA Baldwin S., Huang E., Pramanik B., Ealick S., Trotta P.P.;
RT "A homology model of human interferon alpha-2.";
RL Proteins 17:62-74(1993).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=8994971; DOI=10.1016/s0969-2126(96)00152-9;
RA Radhakrishnan R., Walter L.J., Hruza A., Reichert P., Trotta P.P.,
RA Nagabhushan T.L., Walter M.R.;
RT "Zinc mediated dimer of human interferon-alpha 2b revealed by X-ray
RT crystallography.";
RL Structure 4:1453-1463(1996).
RN [21]
RP STRUCTURE BY NMR.
RX PubMed=9417943; DOI=10.1006/jmbi.1997.1396;
RA Klaus W., Gsell B., Labhardt A.M., Wipf B., Senn H.;
RT "The three-dimensional high resolution structure of human interferon alpha-
RT 2a determined by heteronuclear NMR spectroscopy in solution.";
RL J. Mol. Biol. 274:661-675(1997).
RN [22]
RP STRUCTURE BY NMR OF 24-188 IN COMPLEX WITH IFNAR2, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=17001036; DOI=10.1110/ps.062283006;
RA Quadt-Akabayov S.R., Chill J.H., Levy R., Kessler N., Anglister J.;
RT "Determination of the human type I interferon receptor binding site on
RT human interferon-alpha2 by cross saturation and an NMR-based model of the
RT complex.";
RL Protein Sci. 15:2656-2668(2006).
RN [23]
RP STRUCTURE BY NMR OF 24-188 IN COMPLEX WITH IFNAR2, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=20496919; DOI=10.1021/bi100041f;
RA Nudelman I., Akabayov S.R., Schnur E., Biron Z., Levy R., Xu Y., Yang D.,
RA Anglister J.;
RT "Intermolecular interactions in a 44 kDa interferon-receptor complex
RT detected by asymmetric reverse-protonation and two-dimensional NOESY.";
RL Biochemistry 49:5117-5133(2010).
RN [24]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-177.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities.
CC {ECO:0000269|PubMed:6159538}.
CC -!- SUBUNIT: Interacts with IFNAR2. {ECO:0000269|PubMed:17001036,
CC ECO:0000269|PubMed:20496919}.
CC -!- INTERACTION:
CC P01563; P48551: IFNAR2; NbExp=2; IntAct=EBI-4394394, EBI-958408;
CC P01563; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-4394394, EBI-6268651;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6159538}.
CC -!- POLYMORPHISM: Three alleles exist; alpha-2A, alpha-2B (shown here) and
CC alpha-2C (PubMed:7627809). Allele alpha-2B is the predominant allele
CC while allele alpha-2A is less predominant and alpha-2C only a minor
CC allelic variant. {ECO:0000269|PubMed:7627809}.
CC -!- PHARMACEUTICAL: Available under the names Roferon-A (Roche) or Intron-A
CC (Schering-Plough). Used as an anticancer drug for its antiproliferative
CC activity.
CC -!- SIMILARITY: Belongs to the alpha/beta interferon family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J00207; AAB59402.1; -; Genomic_DNA.
DR EMBL; V00544; CAA23805.1; -; mRNA.
DR EMBL; V00548; CAA23809.1; -; mRNA.
DR EMBL; V00549; CAA23810.1; -; mRNA.
DR EMBL; Y11834; CAA72532.1; -; Genomic_DNA.
DR EMBL; JN591568; AEX60802.1; -; mRNA.
DR EMBL; JN591569; AEX60803.1; -; mRNA.
DR EMBL; JN591570; AEX60804.1; -; mRNA.
DR EMBL; JN848522; AET86951.1; -; mRNA.
DR EMBL; CR541921; CAG46719.1; -; mRNA.
DR EMBL; AL353732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58611.1; -; Genomic_DNA.
DR EMBL; BC074936; AAH74936.1; -; mRNA.
DR EMBL; BC074937; AAH74937.1; -; mRNA.
DR EMBL; BC104163; AAI04164.1; -; mRNA.
DR EMBL; BC104164; AAI04165.1; -; mRNA.
DR EMBL; M54886; AAA59181.1; -; mRNA.
DR EMBL; M29883; AAA52715.1; -; Genomic_DNA.
DR CCDS; CCDS6506.1; -.
DR PIR; A93234; IVHUA2.
DR PIR; I78570; I78570.
DR RefSeq; NP_000596.2; NM_000605.3.
DR PDB; 1ITF; NMR; -; A=24-188.
DR PDB; 1RH2; X-ray; 2.90 A; A/B/C/D/E/F=24-188.
DR PDB; 2HYM; NMR; -; B=24-188.
DR PDB; 2KZ1; NMR; -; A=24-188.
DR PDB; 2LAG; NMR; -; A=24-188.
DR PDB; 2LMS; NMR; -; A=24-188.
DR PDB; 3S9D; X-ray; 2.00 A; A/C=24-188.
DR PDB; 3SE3; X-ray; 4.00 A; B=24-188.
DR PDB; 4YPG; X-ray; 3.00 A; C/D=24-182.
DR PDB; 4Z5R; X-ray; 3.00 A; D/E/F/G/H/I/N/X=24-188.
DR PDBsum; 1ITF; -.
DR PDBsum; 1RH2; -.
DR PDBsum; 2HYM; -.
DR PDBsum; 2KZ1; -.
DR PDBsum; 2LAG; -.
DR PDBsum; 2LMS; -.
DR PDBsum; 3S9D; -.
DR PDBsum; 3SE3; -.
DR PDBsum; 4YPG; -.
DR PDBsum; 4Z5R; -.
DR AlphaFoldDB; P01563; -.
DR BMRB; P01563; -.
DR SMR; P01563; -.
DR BioGRID; 109663; 11.
DR ComplexPortal; CPX-5995; Interferon alpha receptor-ligand complex, IFNA2 variant.
DR CORUM; P01563; -.
DR DIP; DIP-481N; -.
DR IntAct; P01563; 11.
DR STRING; 9606.ENSP00000369554; -.
DR ChEMBL; CHEMBL3856161; -.
DR DrugBank; DB12773; Sifalimumab.
DR Allergome; 9876; Hom s IFN alpha.
DR GlyConnect; 289; 7 O-Linked glycans (1 site).
DR GlyGen; P01563; 1 site, 11 O-linked glycans (1 site).
DR iPTMnet; P01563; -.
DR PhosphoSitePlus; P01563; -.
DR BioMuta; IFNA2; -.
DR DMDM; 124449; -.
DR jPOST; P01563; -.
DR MassIVE; P01563; -.
DR PaxDb; P01563; -.
DR PeptideAtlas; P01563; -.
DR PRIDE; P01563; -.
DR ProteomicsDB; 51381; -.
DR ABCD; P01563; 2 sequenced antibodies.
DR Antibodypedia; 10443; 1093 antibodies from 35 providers.
DR DNASU; 3440; -.
DR Ensembl; ENST00000380206.4; ENSP00000369554.2; ENSG00000188379.7.
DR GeneID; 3440; -.
DR KEGG; hsa:3440; -.
DR MANE-Select; ENST00000380206.4; ENSP00000369554.2; NM_000605.4; NP_000596.2.
DR UCSC; uc003zpb.4; human.
DR CTD; 3440; -.
DR DisGeNET; 3440; -.
DR GeneCards; IFNA2; -.
DR HGNC; HGNC:5423; IFNA2.
DR HPA; ENSG00000188379; Tissue enriched (brain).
DR MIM; 147562; gene.
DR neXtProt; NX_P01563; -.
DR OpenTargets; ENSG00000188379; -.
DR PharmGKB; PA29662; -.
DR VEuPathDB; HostDB:ENSG00000188379; -.
DR eggNOG; ENOG502SQAC; Eukaryota.
DR GeneTree; ENSGT01000000214430; -.
DR HOGENOM; CLU_109427_0_0_1; -.
DR InParanoid; P01563; -.
DR OrthoDB; 1358010at2759; -.
DR PhylomeDB; P01563; -.
DR TreeFam; TF336177; -.
DR PathwayCommons; P01563; -.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR Reactome; R-HSA-912694; Regulation of IFNA/IFNB signaling.
DR Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P01563; -.
DR SIGNOR; P01563; -.
DR BioGRID-ORCS; 3440; 10 hits in 1029 CRISPR screens.
DR EvolutionaryTrace; P01563; -.
DR GeneWiki; IFNA2; -.
DR GenomeRNAi; 3440; -.
DR Pharos; P01563; Tbio.
DR PRO; PR:P01563; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P01563; protein.
DR Bgee; ENSG00000188379; Expressed in corpus callosum and 29 other tissues.
DR Genevisible; P01563; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
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:0006915; P:apoptotic process; TAS:ProtInc.
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:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0098586; P:cellular response to virus; IC:ComplexPortal.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IDA:BHF-UCL.
DR GO; GO:0006959; P:humoral immune response; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0002323; P:natural killer cell activation involved in immune response; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0032696; P:negative regulation of interleukin-13 production; IDA:UniProtKB.
DR GO; GO:0032714; P:negative regulation of interleukin-5 production; IDA:UniProtKB.
DR GO; GO:0045581; P:negative regulation of T cell differentiation; IDA:UniProtKB.
DR GO; GO:2000552; P:negative regulation of T-helper 2 cell cytokine production; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:BHF-UCL.
DR GO; GO:0033141; P:positive regulation of peptidyl-serine phosphorylation of STAT protein; IBA:GO_Central.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IMP:AgBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:AgBase.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
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 GO; GO:0060337; P:type I interferon signaling pathway; IC:ComplexPortal.
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 3D-structure; Antiviral defense; Cytokine; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Pharmaceutical; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:6159537,
FT ECO:0000269|PubMed:9425112"
FT CHAIN 24..188
FT /note="Interferon alpha-2"
FT /id="PRO_0000016360"
FT CARBOHYD 129
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:2049076"
FT /id="CAR_000049"
FT DISULFID 24..121
FT /evidence="ECO:0000269|PubMed:6162107"
FT DISULFID 52..161
FT /evidence="ECO:0000269|PubMed:6162107"
FT VARIANT 6
FT /note="A -> D (in dbSNP:rs35971916)"
FT /id="VAR_055972"
FT VARIANT 46
FT /note="R -> K (in allele alpha-2A; dbSNP:rs1061959)"
FT /evidence="ECO:0000269|PubMed:3906813,
FT ECO:0000269|PubMed:6159538, ECO:0000269|PubMed:6163083,
FT ECO:0000269|PubMed:7627809"
FT /id="VAR_004012"
FT VARIANT 57
FT /note="H -> R (in allele alpha-2C; dbSNP:rs73420190)"
FT /evidence="ECO:0000269|PubMed:7627809"
FT /id="VAR_013001"
FT VARIANT 177
FT /note="S -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036329"
FT CONFLICT 85
FT /note="Q -> L (in Ref. 6; AEX60803)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="K -> M (in Ref. 6; AEX60802)"
FT /evidence="ECO:0000305"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:4YPG"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:3S9D"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:3S9D"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3S9D"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:4Z5R"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4YPG"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:3S9D"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:3S9D"
FT HELIX 101..120
FT /evidence="ECO:0007829|PDB:3S9D"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:2HYM"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:4YPG"
FT HELIX 138..155
FT /evidence="ECO:0007829|PDB:3S9D"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:3S9D"
FT HELIX 160..177
FT /evidence="ECO:0007829|PDB:3S9D"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:4Z5R"
SQ SEQUENCE 188 AA; 21578 MW; 9BAA221D2BFB421D CRC64;
MALTFALLVA LLVLSCKSSC SVGCDLPQTH SLGSRRTLML LAQMRRISLF SCLKDRHDFG
FPQEEFGNQF QKAETIPVLH EMIQQIFNLF STKDSSAAWD ETLLDKFYTE LYQQLNDLEA
CVIQGVGVTE TPLMKEDSIL AVRKYFQRIT LYLKEKKYSP CAWEVVRAEI MRSFSLSTNL
QESLRSKE
