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UniProtKB/Swiss-Prot entry P01563


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IFNA2_HUMAN
Primary accession number P01563
Secondary accession numbers P01564 Q14606 Q96KI6
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    October 14, 2008 (Entry version 93)
Name and origin of the protein
Protein name Interferon alpha-2 [Precursor]
Synonyms Interferon alpha-A
LeIF A
Gene name
Name: IFNA2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
DOI=10.1038/287411a0; PubMed=6159538 [NCBI, ExPASy, EBI, Israel, Japan]
Goeddel D.V., Yelverton E., Ullrich A., Heyneker H.L., Miozzari G., Holmes W., Seeburg P.H., Dull T.J., May L., Stebbing N., Crea R., Maeda S., McCandliss R., Sloma A., Tabor J.M., Gross M., Familletti P.C., Pestka S.;
"Human leukocyte interferon produced by E. coli is biologically active.";
Nature 287:411-416(1980).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
DOI=10.1038/290020a0; PubMed=6163083 [NCBI, ExPASy, EBI, Israel, Japan]
Goeddel D.V., Leung D.W., Dull T.J., Gross M., Lawn R.M., McCandliss R., Seeburg P.H., Ullrich A., Yelverton E., Gray P.W.;
"The structure of eight distinct cloned human leukocyte interferon cDNAs.";
Nature 290:20-26(1981).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=6170983 [NCBI, ExPASy, EBI, Israel, Japan]
Lawn R.M., Gross M., Houck C.M., Franke A.E., Gray P.V., Goeddel D.V.;
"DNA sequence of a major human leukocyte interferon gene.";
Proc. Natl. Acad. Sci. U.S.A. 78:5435-5439(1981).
[4]
NUCLEOTIDE SEQUENCE.
TISSUE=Bone marrow tumor;
PubMed=3906813 [NCBI, ExPASy, EBI, Israel, Japan]
Oliver G., Balbas P., Valle F., Soberon X., Bolivar F.;
"Cloning of human leukocyte interferon cDNA and a strategy for its production in E. coli.";
Rev. Latinoam. Microbiol. 27:141-150(1985).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=9694076 [NCBI, ExPASy, EBI, Israel, Japan]
Austruy E., Bagnis C., Carbuccia N., Maroc C., Birg F., Dubreuil P., Mannoni P., Chabannon C.;
"A defective retroviral vector encoding human interferon alpha 2 can transduce human leukemic cell lines.";
Cancer Gene Ther. 5:247-256(1998).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 7-188.
PubMed=6158094 [NCBI, ExPASy, EBI, Israel, Japan]
Streuli M., Nagata S., Weissmann C.;
"At least three human type alpha interferons: structure of alpha 2.";
Science 209:1343-1347(1980).
[7]
NUCLEOTIDE SEQUENCE OF 24-188.
DOI=10.1093/nar/11.16.5661; PubMed=6310510 [NCBI, ExPASy, EBI, Israel, Japan]
Weber H., Weissmann C.;
"Formation of genes coding for hybrid proteins by recombination between related, cloned genes in E. coli.";
Nucleic Acids Res. 11:5661-5669(1983).
[8]
PROTEIN SEQUENCE OF 24-112 AND 136-188.
DOI=10.1038/287408a0; PubMed=6159537 [NCBI, ExPASy, EBI, Israel, Japan]
Allen G., Fantes K.H.;
"A family of structural genes for human lymphoblastoid (leukocyte-type) interferon.";
Nature 287:408-411(1980).
[9]
PROTEIN SEQUENCE OF 24-58.
PubMed=9425112 [NCBI, ExPASy, EBI, Israel, Japan]
Nyman T.A., Toeloe H., Parkkinen J., Kalkkinen N.;
"Identification of nine interferon-alpha subtypes produced by Sendai virus-induced human peripheral blood leucocytes.";
Biochem. J. 329:295-302(1998).
[10]
DISULFIDE BONDS.
DOI=10.1038/289606a0; PubMed=6162107 [NCBI, ExPASy, EBI, Israel, Japan]
Wetzel R.;
"Assignment of the disulphide bonds of leukocyte interferon.";
Nature 289:606-607(1981).
[11]
GLYCOSYLATION AT THR-129, AND VARIANTS ALPHA-2B AND ALPHA-2C.
PubMed=2049076 [NCBI, ExPASy, EBI, Israel, Japan]
Adolf G.R., Kalsner I., Ahorn H., Maurer-Fogy I., Cantell K.;
"Natural human interferon-alpha 2 is O-glycosylated.";
Biochem. J. 276:511-518(1991).
[12]
POLYMORPHISM.
PubMed=7627809 [NCBI, ExPASy, EBI, Israel, Japan]
Lee N., Ni D., Brissette R., Chou M., Hussain M., Gill D.S., Liao M.-J., Testa D.;
"Interferon-alpha 2 variants in the human genome.";
J. Interferon Cytokine Res. 15:341-349(1995).
[13]
3D-STRUCTURE MODELING.
DOI=10.1002/prot.340170109; PubMed=8234245 [NCBI, ExPASy, EBI, Israel, Japan]
Murgolo N.J., Windsor W.T., Hruza A., Reichert P., Tsarbopoulos A., Baldwin S., Huang E., Pramanik B., Ealick S., Trotta P.P.;
"A homology model of human interferon alpha-2.";
Proteins 17:62-74(1993).
[14]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
DOI=10.1016/S0969-2126(96)00152-9; PubMed=8994971 [NCBI, ExPASy, EBI, Israel, Japan]
Radhakrishnan R., Walter L.J., Hruza A., Reichert P., Trotta P.P., Nagabhushan T.L., Walter M.R.;
"Zinc mediated dimer of human interferon-alpha 2b revealed by X-ray crystallography.";
Structure 4:1453-1463(1996).
[15]
STRUCTURE BY NMR.
DOI=10.1006/jmbi.1997.1396; PubMed=9417943 [NCBI, ExPASy, EBI, Israel, Japan]
Klaus W., Gsell B., Labhardt A.M., Wipf B., Senn H.;
"The three-dimensional high resolution structure of human interferon alpha-2a determined by heteronuclear NMR spectroscopy in solution.";
J. Mol. Biol. 274:661-675(1997).
[16]
VARIANT [LARGE SCALE ANALYSIS] LEU-177.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
  • FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
  • SUBCELLULAR LOCATION: Secreted.
  • POLYMORPHISM: Three forms exist; alpha-2a (shown here), alpha-2b and alpha-2c.
  • PHARMACEUTICAL: Available under the names Roferon-A (Roche) or Intron-A (Schering-Plough). Used as an anticancer drug for its antiproliferative activity.
  • SIMILARITY: Belongs to the alpha/beta interferon family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J00207; AAB59402.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V00544; CAA23805.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V00548; CAA23809.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V00549; CAA23810.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11834; CAA72532.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M54886; AAA59181.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29883; AAA52715.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
A04970; CAA00410.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A93234; IVHUA2.
I78570; I78570.
UniGene Hs.211575
3D structure databases
PDB
1ITF; NMR; -; A=24-188.[ExPASy / RCSB / EBI]
1RH2; X-ray; 2.90 A; A/B/C/D/E/F=24-188.[ExPASy / RCSB / EBI]
2HIE; Model; -; A=24-188.[ExPASy / RCSB / EBI]
2HYM; NMR; -; B=24-188.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ITF; -.
1RH2; -.
2HIE; -.
2HYM; -.
ModBase P01563.
Protein-protein interaction databases
DIP DIP:3784N; -.
DIP:481N; -.
PTM databases
GlycoSuiteDB P01563; -.
Organism-specific databases
H-InvDB HIX0034810; -.
HGNC HGNC:5423; IFNA2.
GenAtlas IFNA2.
MIM 147562; gene. [NCBI / EBI]
PharmGKB PA29662; -.
GeneCards P01563.
Gene expression databases
ArrayExpress P01563; -.
CleanEx HS_IFNA2; -.
GermOnline ENSG00000188379; Homo sapiens.
Ontologies
GO
GO:0005132; Molecular function: interferon-alpha/beta receptor binding (traceable author statement from ProtInc).
GO:0007166; Biological process: cell surface receptor linked signal transduction (traceable author statement from ProtInc).
GO:0007267; Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0006917; Biological process: induction of apoptosis (traceable author statement from ProtInc).
GO:0006954; Biological process: inflammatory response (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR012351; 4_helix_cytokine_core.
IPR015589; IFNa.
IPR000471; Interferon_abd.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1250.10; 4_helix_cytokine_core; 1.
PANTHER PTHR11691:SF9; IFNa; 1.
PTHR11691; Interferon_abd; 1.
Pfam PF00143; Interferon; 1.
Pfam graphical view of domain structure.
PRINTS PR00266; INTERFERONAB.
ProDom PD000550; Interferon_abd; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00076; IFabd; 1.
SMART graphical view of domain structure.
PROSITE PS00252; INTERFERON_A_B_D; 1.
BLOCKS P01563.
ProtoNet P01563.
Genome annotation databases
Ensembl ENSG00000188379; Homo sapiens. [Contig view]
Phylogenomic databases
HOGENOM P01563; -.
HOVERGEN P01563; -.
Other
DrugBank DB00034; Interferon Alfa-2a, Recombinant.
DB00105; Interferon Alfa-2b, Recombinant.
DB00011; Interferon alfa-n1.
DB00008; Peginterferon alfa-2a.
DB00022; Peginterferon alfa-2b.
LinkHub P01563; -.
SOURCE IFNA2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Antiviral defense; Cytokine; Direct protein sequencing; Glycoprotein; Pharmaceutical; Polymorphism; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    23  23      
CHAIN   24   188  165     Interferon alpha-2. PRO_0000016360
CARBOHYD   129   129        O-linked (GalNAc...) [GlycoSuiteDB]. CAR_000049
DISULFID   24   121         
DISULFID   52   161         
VARIANT   46    46  1     K -> R (in alpha-2B and alpha-2C). VAR_004012 
VARIANT   57    57  1     H -> R (in alpha-2C). VAR_013001 
VARIANT   177   177  1     S -> L (in a breast cancer sample; somatic mutation). VAR_036329 
HELIX   33    44  12      
TURN   49    54  6      
HELIX   63    66  4      
STRAND   67    69  3      
STRAND   71    75  5      
HELIX   76    91  16      
HELIX   93    98  6      
HELIX   101   123  23      
HELIX   134   155  22      
HELIX   160   178  19      
TURN   179   182  4      
Sequence information
Length: 188 AA [This is the length of the unprocessed precursor] Molecular weight: 21550 Da [This is the MW of the unprocessed precursor] CRC64: 101DD21D394CBF97 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MALTFALLVA LLVLSCKSSC SVGCDLPQTH SLGSRRTLML LAQMRKISLF SCLKDRHDFG 

        70         80         90        100        110        120 
FPQEEFGNQF QKAETIPVLH EMIQQIFNLF STKDSSAAWD ETLLDKFYTE LYQQLNDLEA 

       130        140        150        160        170        180 
CVIQGVGVTE TPLMKEDSIL AVRKYFQRIT LYLKEKKYSP CAWEVVRAEI MRSFSLSTNL 


QESLRSKE 

P01563 in FASTA format

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