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Interferon alpha-1/13 (IFN-alpha-1/13) (Interferon alpha-D) (LeIF D)

 IFNA1_HUMAN             Reviewed;         189 AA.
P01562; D4Q9M8; Q14605; Q2M1L8; Q52LB8; Q5VYQ2; Q7M4Q1; Q8WZ68;
Q9UMJ3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
20-JUN-2018, entry version 183.
RecName: Full=Interferon alpha-1/13;
Short=IFN-alpha-1/13;
AltName: Full=Interferon alpha-D;
Short=LeIF D;
Flags: Precursor;
Name=IFNA1;
and
Name=IFNA13;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6157600; DOI=10.1016/0378-1119(80)90137-7;
Mantei N., Schwarzstein M., Streuli M., Panem S., Nagata S.,
Weissmann C.;
"The nucleotide sequence of a cloned human leukocyte interferon
cDNA.";
Gene 10:1-10(1980).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6157095; DOI=10.1038/285547a0;
Taniguchi T., Mantei N., Schwarzstein M., Nagata S., Muramatsu M.,
Weissmann C.;
"Human leukocyte and fibroblast interferons are structurally
related.";
Nature 285:547-549(1980).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6163083; DOI=10.1038/290020a0;
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6479148;
Todokoro K., Kioussis D., Weissmann C.;
"Two non-allelic human interferon alpha genes with identical coding
regions.";
EMBO J. 3:1809-1812(1984).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=4057246; DOI=10.1016/0022-2836(85)90401-2;
Henco K., Brosius J., Fujisawa A., Fujisawa J., Haynes J.R.,
Hochstadt J., Kovacic T., Pasek M., Schamboeck A., Schmid J.,
Todokoro K., Waelchli M., Nagata S., Weissmann C.;
"Structural relationship of human interferon alpha genes and
pseudogenes.";
J. Mol. Biol. 185:227-260(1985).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2985969; DOI=10.1128/MCB.5.4.768;
Capon D.J., Shepard H.M., Goeddel D.V.;
"Two distinct families of human and bovine interferon-alpha genes are
coordinately expressed and encode functional polypeptides.";
Mol. Cell. Biol. 5:768-779(1985).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=20857263; DOI=10.1007/s00795-010-0492-5;
Kimura T., Hashimoto I., Nishizawa M., Ito S., Yamada H.;
"Novel cis-active structures in the coding region mediate CRM1-
dependent nuclear export of IFN-alpha 1 mRNA.";
Med. Mol. Morphol. 43:145-157(2010).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-10.
Rostoks N.;
Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-10; VAL-137 AND
GLY-163.
NIEHS SNPs program;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-10.
TISSUE=Cerebellum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-189.
PubMed=6310510; DOI=10.1093/nar/11.16.5661;
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).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-189.
TISSUE=Leukocyte;
Chen H.H., Yu X.B.;
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[15]
PROTEIN SEQUENCE OF 24-59, AND FUNCTION.
PubMed=1634550;
Zoon K.C., Miller D., Bekisz J., zur Nedden D., Enterline J.C.,
Nguyen N.Y., Hu R.-Q.;
"Purification and characterization of multiple components of human
lymphoblastoid interferon-alpha.";
J. Biol. Chem. 267:15210-15216(1992).
[16]
PROTEIN SEQUENCE OF 24-58.
PubMed=9425112; DOI=10.1042/bj3290295;
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).
[17]
POLYMORPHISM.
PubMed=11032395; DOI=10.1089/10799900050151021;
Hussain M., Ni D., Gill D., Liao M.-J.;
"IFN-alpha-1a gene is the major variant in the North American
population.";
J. Interferon Cytokine Res. 20:763-768(2000).
[18]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 24-189 IN COMPLEX WITH
ANTIBODY, AND DISULFIDE BOND.
PubMed=22307521; DOI=10.1007/s00109-012-0866-3;
Ouyang S., Gong B., Li J.Z., Zhao L.X., Wu W., Zhang F.S., Sun L.,
Wang S.J., Pan M., Li C., Liang W., Shaw N., Zheng J., Zhao G.P.,
Wang Y., Liu Z.J., Liang M.;
"Structural insights into a human anti-IFN antibody exerting
therapeutic potential for systemic lupus erythematosus.";
J. Mol. Med. 90:837-846(2012).
-!- FUNCTION: Produced by macrophages, IFN-alpha have antiviral
activities. Interferon stimulates the production of two enzymes: a
protein kinase and an oligoadenylate synthetase.
{ECO:0000269|PubMed:1634550}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- POLYMORPHISM: Two forms exist; alpha-1a (shown here) and alpha-1b
(PubMed:11032395). {ECO:0000269|PubMed:11032395}.
-!- MISCELLANEOUS: Interferons alpha-1 and alpha-13 have identical
protein sequences.
-!- SIMILARITY: Belongs to the alpha/beta interferon family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ifna1/";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; V00537; CAA23798.1; -; mRNA.
EMBL; J00210; AAB59403.1; -; Genomic_DNA.
EMBL; V00538; CAA23799.1; -; mRNA.
EMBL; X00803; CAA25381.1; -; Genomic_DNA.
EMBL; X75934; CAA53538.1; -; Genomic_DNA.
EMBL; AB445100; BAI99735.1; -; Genomic_DNA.
EMBL; DQ185447; ABA03167.1; -; Genomic_DNA.
EMBL; AL353732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471071; EAW58609.1; -; Genomic_DNA.
EMBL; BC069427; AAH69427.1; -; mRNA.
EMBL; BC074928; AAH74928.1; -; mRNA.
EMBL; BC074929; AAH74929.1; -; mRNA.
EMBL; BC093988; AAH93988.1; -; mRNA.
EMBL; BC112002; AAI12003.1; -; mRNA.
EMBL; BC112300; AAI12301.1; -; mRNA.
EMBL; BC112302; AAI12303.1; -; mRNA.
EMBL; M29884; AAA52714.1; -; Genomic_DNA.
EMBL; AF439447; AAL35223.1; -; Genomic_DNA.
CCDS; CCDS6508.1; -.
PIR; C23285; IVHUA1.
PIR; F42753; F42753.
PIR; H42753; H42753.
RefSeq; NP_008831.3; NM_006900.3.
RefSeq; NP_076918.1; NM_024013.2.
UniGene; Hs.37026; -.
UniGene; Hs.533471; -.
PDB; 3UX9; X-ray; 2.80 A; A/C=24-189.
PDBsum; 3UX9; -.
ProteinModelPortal; P01562; -.
SMR; P01562; -.
BioGrid; 109662; 8.
BioGrid; 109670; 7.
DIP; DIP-6020N; -.
IntAct; P01562; 1.
MINT; P01562; -.
STRING; 9606.ENSP00000276927; -.
iPTMnet; P01562; -.
PhosphoSitePlus; P01562; -.
BioMuta; IFNA1; -.
DMDM; 124455; -.
MaxQB; P01562; -.
PaxDb; P01562; -.
PeptideAtlas; P01562; -.
PRIDE; P01562; -.
ProteomicsDB; 51380; -.
DNASU; 3439; -.
DNASU; 3447; -.
Ensembl; ENST00000276927; ENSP00000276927; ENSG00000197919.
Ensembl; ENST00000449498; ENSP00000394494; ENSG00000233816.
GeneID; 3439; -.
GeneID; 3447; -.
KEGG; hsa:3439; -.
KEGG; hsa:3447; -.
UCSC; uc003zpd.2; human.
CTD; 3439; -.
CTD; 3447; -.
DisGeNET; 3439; -.
DisGeNET; 3447; -.
EuPathDB; HostDB:ENSG00000197919.4; -.
EuPathDB; HostDB:ENSG00000233816.3; -.
GeneCards; IFNA1; -.
GeneCards; IFNA13; -.
HGNC; HGNC:5417; IFNA1.
HGNC; HGNC:5419; IFNA13.
HPA; HPA047557; -.
MIM; 147578; gene.
MIM; 147660; gene.
neXtProt; NX_P01562; -.
OpenTargets; ENSG00000197919; -.
PharmGKB; PA29658; -.
eggNOG; ENOG410IR8X; Eukaryota.
eggNOG; ENOG4110Q1A; LUCA.
GeneTree; ENSGT00760000119150; -.
HOVERGEN; HBG052086; -.
InParanoid; P01562; -.
KO; K05414; -.
OMA; VEEMALV; -.
PhylomeDB; P01562; -.
TreeFam; TF336177; -.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
Reactome; R-HSA-912694; Regulation of IFNA signaling.
Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SignaLink; P01562; -.
SIGNOR; P01562; -.
GeneWiki; IFNA13; -.
GeneWiki; Interferon,_alpha_1; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000197919; -.
CleanEx; HS_IFNA1; -.
CleanEx; HS_IFNA13; -.
ExpressionAtlas; P01562; baseline and differential.
Genevisible; P01562; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0005132; F:type I interferon receptor binding; IBA:GO_Central.
GO; GO:0002250; P:adaptive immune response; IBA:GO_Central.
GO; GO:0030183; P:B cell differentiation; IBA:GO_Central.
GO; GO:0042100; P:B cell proliferation; IBA:GO_Central.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0006959; P:humoral immune response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0002323; P:natural killer cell activation involved in immune response; IBA:GO_Central.
GO; GO:0033141; P:positive regulation of peptidyl-serine phosphorylation of STAT protein; IBA:GO_Central.
GO; GO:0043330; P:response to exogenous dsRNA; IBA:GO_Central.
GO; GO:0002286; P:T cell activation involved in immune response; IBA:GO_Central.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
CDD; cd00095; IFab; 1.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR000471; Interferon_alpha/beta/delta.
PANTHER; PTHR11691; PTHR11691; 1.
Pfam; PF00143; Interferon; 1.
PRINTS; PR00266; INTERFERONAB.
SMART; SM00076; IFabd; 1.
SUPFAM; SSF47266; SSF47266; 1.
PROSITE; PS00252; INTERFERON_A_B_D; 1.
1: Evidence at protein level;
3D-structure; Antiviral defense; Complete proteome; Cytokine;
Direct protein sequencing; Disulfide bond; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 23 {ECO:0000269|PubMed:1634550,
ECO:0000269|PubMed:9425112}.
CHAIN 24 189 Interferon alpha-1/13.
/FTId=PRO_0000016359.
DISULFID 24 122 {ECO:0000250}.
DISULFID 52 162 {ECO:0000269|PubMed:22307521}.
VARIANT 10 10 V -> A (in dbSNP:rs1758567).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.8, ECO:0000269|Ref.9}.
/FTId=VAR_024508.
VARIANT 137 137 A -> V (in alpha-1B; dbSNP:rs2230050).
{ECO:0000269|Ref.9}.
/FTId=VAR_013000.
VARIANT 163 163 A -> G (in dbSNP:rs28383794).
{ECO:0000269|Ref.9}.
/FTId=VAR_025173.
CONFLICT 116 116 L -> P (in Ref. 14; AAL35223).
{ECO:0000305}.
CONFLICT 172 172 M -> V (in Ref. 14; AAL35223).
{ECO:0000305}.
HELIX 35 43 {ECO:0000244|PDB:3UX9}.
HELIX 49 51 {ECO:0000244|PDB:3UX9}.
TURN 53 55 {ECO:0000244|PDB:3UX9}.
HELIX 63 66 {ECO:0000244|PDB:3UX9}.
HELIX 77 91 {ECO:0000244|PDB:3UX9}.
HELIX 94 99 {ECO:0000244|PDB:3UX9}.
HELIX 102 122 {ECO:0000244|PDB:3UX9}.
HELIX 137 156 {ECO:0000244|PDB:3UX9}.
TURN 157 159 {ECO:0000244|PDB:3UX9}.
HELIX 161 178 {ECO:0000244|PDB:3UX9}.
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


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