IFNA1_HUMAN
ID IFNA1_HUMAN Reviewed; 189 AA.
AC P01562; D4Q9M8; Q14605; Q2M1L8; Q52LB8; Q5VYQ2; Q7M4Q1; Q8WZ68; Q9UMJ3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Interferon alpha-1/13;
DE Short=IFN-alpha-1/13;
DE AltName: Full=Interferon alpha-D;
DE Short=LeIF D;
DE Flags: Precursor;
GN Name=IFNA1;
GN and
GN Name=IFNA13;
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 [MRNA].
RX PubMed=6157600; DOI=10.1016/0378-1119(80)90137-7;
RA Mantei N., Schwarzstein M., Streuli M., Panem S., Nagata S., Weissmann C.;
RT "The nucleotide sequence of a cloned human leukocyte interferon cDNA.";
RL Gene 10:1-10(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6157095; DOI=10.1038/285547a0;
RA Taniguchi T., Mantei N., Schwarzstein M., Nagata S., Muramatsu M.,
RA Weissmann C.;
RT "Human leukocyte and fibroblast interferons are structurally related.";
RL Nature 285:547-549(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6479148; DOI=10.1002/j.1460-2075.1984.tb02050.x;
RA Todokoro K., Kioussis D., Weissmann C.;
RT "Two non-allelic human interferon alpha genes with identical coding
RT regions.";
RL EMBO J. 3:1809-1812(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=4057246; DOI=10.1016/0022-2836(85)90401-2;
RA Henco K., Brosius J., Fujisawa A., Fujisawa J., Haynes J.R., Hochstadt J.,
RA Kovacic T., Pasek M., Schamboeck A., Schmid J., Todokoro K., Waelchli M.,
RA Nagata S., Weissmann C.;
RT "Structural relationship of human interferon alpha genes and pseudogenes.";
RL J. Mol. Biol. 185:227-260(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2985969; DOI=10.1128/mcb.5.4.768-779.1985;
RA Capon D.J., Shepard H.M., Goeddel D.V.;
RT "Two distinct families of human and bovine interferon-alpha genes are
RT coordinately expressed and encode functional polypeptides.";
RL Mol. Cell. Biol. 5:768-779(1985).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=20857263; DOI=10.1007/s00795-010-0492-5;
RA Kimura T., Hashimoto I., Nishizawa M., Ito S., Yamada H.;
RT "Novel cis-active structures in the coding region mediate CRM1-dependent
RT nuclear export of IFN-alpha 1 mRNA.";
RL Med. Mol. Morphol. 43:145-157(2010).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-10.
RA Rostoks N.;
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-10; VAL-137 AND
RP GLY-163.
RG NIEHS SNPs program;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-10.
RC TISSUE=Cerebellum;
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 [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-189.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-189.
RC TISSUE=Leukocyte;
RA Chen H.H., Yu X.B.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP PROTEIN SEQUENCE OF 24-59, AND FUNCTION.
RX PubMed=1634550; DOI=10.1016/s0021-9258(18)42167-9;
RA Zoon K.C., Miller D., Bekisz J., zur Nedden D., Enterline J.C.,
RA Nguyen N.Y., Hu R.-Q.;
RT "Purification and characterization of multiple components of human
RT lymphoblastoid interferon-alpha.";
RL J. Biol. Chem. 267:15210-15216(1992).
RN [16]
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 [17]
RP POLYMORPHISM.
RX PubMed=11032395; DOI=10.1089/10799900050151021;
RA Hussain M., Ni D., Gill D., Liao M.-J.;
RT "IFN-alpha-1a gene is the major variant in the North American population.";
RL J. Interferon Cytokine Res. 20:763-768(2000).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 24-189 IN COMPLEX WITH ANTIBODY,
RP AND DISULFIDE BOND.
RX PubMed=22307521; DOI=10.1007/s00109-012-0866-3;
RA Ouyang S., Gong B., Li J.Z., Zhao L.X., Wu W., Zhang F.S., Sun L.,
RA Wang S.J., Pan M., Li C., Liang W., Shaw N., Zheng J., Zhao G.P., Wang Y.,
RA Liu Z.J., Liang M.;
RT "Structural insights into a human anti-IFN antibody exerting therapeutic
RT potential for systemic lupus erythematosus.";
RL J. Mol. Med. 90:837-846(2012).
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. {ECO:0000269|PubMed:1634550}.
CC -!- INTERACTION:
CC P01562; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-11478589, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- POLYMORPHISM: Two forms exist; alpha-1a (shown here) and alpha-1b
CC (PubMed:11032395). {ECO:0000269|PubMed:11032395}.
CC -!- MISCELLANEOUS: Interferons alpha-1 and alpha-13 have identical protein
CC sequences.
CC -!- SIMILARITY: Belongs to the alpha/beta interferon family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ifna1/";
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; V00537; CAA23798.1; -; mRNA.
DR EMBL; J00210; AAB59403.1; -; Genomic_DNA.
DR EMBL; V00538; CAA23799.1; -; mRNA.
DR EMBL; X00803; CAA25381.1; -; Genomic_DNA.
DR EMBL; X75934; CAA53538.1; -; Genomic_DNA.
DR EMBL; AB445100; BAI99735.1; -; Genomic_DNA.
DR EMBL; DQ185447; ABA03167.1; -; Genomic_DNA.
DR EMBL; AL353732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58609.1; -; Genomic_DNA.
DR EMBL; BC069427; AAH69427.1; -; mRNA.
DR EMBL; BC074928; AAH74928.1; -; mRNA.
DR EMBL; BC074929; AAH74929.1; -; mRNA.
DR EMBL; BC093988; AAH93988.1; -; mRNA.
DR EMBL; BC112002; AAI12003.1; -; mRNA.
DR EMBL; BC112300; AAI12301.1; -; mRNA.
DR EMBL; BC112302; AAI12303.1; -; mRNA.
DR EMBL; M29884; AAA52714.1; -; Genomic_DNA.
DR EMBL; AF439447; AAL35223.1; -; Genomic_DNA.
DR CCDS; CCDS6508.1; -.
DR PIR; C23285; IVHUA1.
DR PIR; F42753; F42753.
DR PIR; H42753; H42753.
DR RefSeq; NP_008831.3; NM_006900.3.
DR RefSeq; NP_076918.1; NM_024013.2.
DR PDB; 3UX9; X-ray; 2.80 A; A/C=24-189.
DR PDBsum; 3UX9; -.
DR AlphaFoldDB; P01562; -.
DR SMR; P01562; -.
DR BioGRID; 109662; 12.
DR BioGRID; 109670; 10.
DR ComplexPortal; CPX-5996; Interferon alpha receptor-ligand complex, IFNA1 variant.
DR DIP; DIP-6020N; -.
DR IntAct; P01562; 13.
DR MINT; P01562; -.
DR STRING; 9606.ENSP00000276927; -.
DR ChEMBL; CHEMBL3713007; -.
DR iPTMnet; P01562; -.
DR PhosphoSitePlus; P01562; -.
DR BioMuta; IFNA1; -.
DR DMDM; 124455; -.
DR MassIVE; P01562; -.
DR MaxQB; P01562; -.
DR PaxDb; P01562; -.
DR PeptideAtlas; P01562; -.
DR PRIDE; P01562; -.
DR ABCD; P01562; 7 sequenced antibodies.
DR Antibodypedia; 10448; 844 antibodies from 36 providers.
DR Antibodypedia; 24875; 57 antibodies from 13 providers.
DR DNASU; 3439; -.
DR Ensembl; ENST00000276927.3; ENSP00000276927.1; ENSG00000197919.6.
DR Ensembl; ENST00000449498.2; ENSP00000394494.2; ENSG00000233816.3.
DR GeneID; 3439; -.
DR GeneID; 3447; -.
DR KEGG; hsa:3439; -.
DR KEGG; hsa:3447; -.
DR MANE-Select; ENST00000276927.3; ENSP00000276927.1; NM_024013.3; NP_076918.1.
DR UCSC; uc003zpd.2; human.
DR CTD; 3439; -.
DR CTD; 3447; -.
DR DisGeNET; 3439; -.
DR DisGeNET; 3447; -.
DR GeneCards; IFNA1; -.
DR GeneCards; IFNA13; -.
DR HGNC; HGNC:5417; IFNA1.
DR HGNC; HGNC:5419; IFNA13.
DR HPA; ENSG00000197919; Not detected.
DR HPA; ENSG00000233816; Tissue enhanced (brain).
DR MIM; 147578; gene.
DR MIM; 147660; gene.
DR neXtProt; NX_P01562; -.
DR OpenTargets; ENSG00000197919; -.
DR PharmGKB; PA29658; -.
DR VEuPathDB; HostDB:ENSG00000197919; -.
DR VEuPathDB; HostDB:ENSG00000233816; -.
DR eggNOG; ENOG502SQAC; Eukaryota.
DR GeneTree; ENSGT01000000214430; -.
DR HOGENOM; CLU_109427_0_0_1; -.
DR InParanoid; P01562; -.
DR OMA; RTEVWRT; -.
DR OrthoDB; 1358010at2759; -.
DR PhylomeDB; P01562; -.
DR TreeFam; TF336177; -.
DR PathwayCommons; P01562; -.
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; P01562; -.
DR SIGNOR; P01562; -.
DR BioGRID-ORCS; 3439; 38 hits in 937 CRISPR screens.
DR BioGRID-ORCS; 3447; 24 hits in 964 CRISPR screens.
DR GeneWiki; IFNA13; -.
DR GeneWiki; Interferon,_alpha_1; -.
DR Pharos; P01562; Tbio.
DR PRO; PR:P01562; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P01562; protein.
DR Bgee; ENSG00000197919; Expressed in cerebellum and 24 other tissues.
DR ExpressionAtlas; P01562; baseline and differential.
DR Genevisible; P01562; HS.
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:0030183; P:B cell differentiation; IBA:GO_Central.
DR GO; GO:0042100; P:B cell proliferation; IBA:GO_Central.
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; 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 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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:1634550,
FT ECO:0000269|PubMed:9425112"
FT CHAIN 24..189
FT /note="Interferon alpha-1/13"
FT /id="PRO_0000016359"
FT DISULFID 24..122
FT /evidence="ECO:0000250"
FT DISULFID 52..162
FT /evidence="ECO:0000269|PubMed:22307521"
FT VARIANT 10
FT /note="V -> A (in dbSNP:rs1758567)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.8,
FT ECO:0000269|Ref.9"
FT /id="VAR_024508"
FT VARIANT 137
FT /note="A -> V (in alpha-1B; dbSNP:rs2230050)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_013000"
FT VARIANT 163
FT /note="A -> G (in dbSNP:rs28383794)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_025173"
FT CONFLICT 116
FT /note="L -> P (in Ref. 14; AAL35223)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="M -> V (in Ref. 14; AAL35223)"
FT /evidence="ECO:0000305"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:3UX9"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3UX9"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:3UX9"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:3UX9"
FT HELIX 77..91
FT /evidence="ECO:0007829|PDB:3UX9"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:3UX9"
FT HELIX 102..122
FT /evidence="ECO:0007829|PDB:3UX9"
FT HELIX 137..156
FT /evidence="ECO:0007829|PDB:3UX9"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:3UX9"
FT HELIX 161..178
FT /evidence="ECO:0007829|PDB:3UX9"
SQ SEQUENCE 189 AA; 21725 MW; F32F9CB969606B69 CRC64;
MASPFALLMV LVVLSCKSSC SLGCDLPETH SLDNRRTLML LAQMSRISPS SCLMDRHDFG
FPQEEFDGNQ FQKAPAISVL HELIQQIFNL FTTKDSSAAW DEDLLDKFCT ELYQQLNDLE
ACVMQEERVG ETPLMNADSI LAVKKYFRRI TLYLTEKKYS PCAWEVVRAE IMRSLSLSTN
LQERLRRKE