IFNA8_HUMAN
ID IFNA8_HUMAN Reviewed; 189 AA.
AC P32881; P01565; P09236; Q5VWV7; Q5VYQ3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Interferon alpha-8;
DE Short=IFN-alpha-8;
DE AltName: Full=Interferon alpha-B;
DE Short=LeIF B;
DE AltName: Full=Interferon alpha-B2;
DE Flags: Precursor;
GN Name=IFNA8;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6325303; DOI=10.1016/0378-1119(84)90241-5;
RA Bowden D.W., Mao J., Gill T., Hsiao K., Lillquist J.S., Testa D.,
RA Vovis G.F.;
RT "Cloning of eukaryotic genes in single-strand phage vectors: the human
RT interferon genes.";
RL Gene 27:87-99(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6164048; DOI=10.1093/nar/9.3.731;
RA Yelverton E., Leung D., Weck P., Gray P.W., Goeddel D.V.;
RT "Bacterial synthesis of a novel human leukocyte interferon.";
RL Nucleic Acids Res. 9:731-741(1981).
RN [4]
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 [5]
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 [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
RP PROTEIN SEQUENCE OF 24-53.
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 [9]
RP ABSENCE OF POLYMORPHISM.
RX PubMed=8836918; DOI=10.1089/jir.1996.16.523;
RA Hussain M., Gill D.S., Liao M.-J., Testa D.;
RT "Interferon-alpha 8b is the only variant of interferon-alpha 8 identified
RT in a large human population.";
RL J. Interferon Cytokine Res. 16:523-529(1996).
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 -!- INTERACTION:
CC P32881; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-18211524, EBI-13345167;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the alpha/beta interferon family. {ECO:0000305}.
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DR EMBL; X03125; CAA26903.1; -; Genomic_DNA.
DR EMBL; K01900; AAA52716.1; -; mRNA.
DR EMBL; V00545; CAA23806.1; -; mRNA.
DR EMBL; V00550; CAA23811.1; -; mRNA.
DR EMBL; AL353732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58610.1; -; Genomic_DNA.
DR EMBL; BC104828; AAI04829.1; -; mRNA.
DR EMBL; BC104830; AAI04831.1; -; mRNA.
DR CCDS; CCDS6507.1; -.
DR PIR; A93747; IVHUA4.
DR PIR; B61413; B61413.
DR PIR; D23753; IVHUI8.
DR RefSeq; NP_002161.2; NM_002170.3.
DR PDB; 6JHD; NMR; -; A=24-189.
DR PDBsum; 6JHD; -.
DR AlphaFoldDB; P32881; -.
DR SMR; P32881; -.
DR BioGRID; 109668; 16.
DR ComplexPortal; CPX-6001; Interferon alpha receptor-ligand complex, IFNA8 variant.
DR DIP; DIP-6017N; -.
DR IntAct; P32881; 9.
DR STRING; 9606.ENSP00000369553; -.
DR ChEMBL; CHEMBL3856161; -.
DR BioMuta; IFNA8; -.
DR DMDM; 417188; -.
DR jPOST; P32881; -.
DR MassIVE; P32881; -.
DR PaxDb; P32881; -.
DR PeptideAtlas; P32881; -.
DR PRIDE; P32881; -.
DR ProteomicsDB; 54886; -.
DR ABCD; P32881; 3 sequenced antibodies.
DR Antibodypedia; 24879; 128 antibodies from 21 providers.
DR DNASU; 3445; -.
DR Ensembl; ENST00000380205.2; ENSP00000369553.1; ENSG00000120242.4.
DR GeneID; 3445; -.
DR KEGG; hsa:3445; -.
DR MANE-Select; ENST00000380205.2; ENSP00000369553.1; NM_002170.4; NP_002161.2.
DR UCSC; uc003zpc.1; human.
DR CTD; 3445; -.
DR DisGeNET; 3445; -.
DR GeneCards; IFNA8; -.
DR HGNC; HGNC:5429; IFNA8.
DR HPA; ENSG00000120242; Not detected.
DR MIM; 147568; gene.
DR neXtProt; NX_P32881; -.
DR OpenTargets; ENSG00000120242; -.
DR PharmGKB; PA29668; -.
DR PharmGKB; PA88; -.
DR VEuPathDB; HostDB:ENSG00000120242; -.
DR eggNOG; ENOG502SQAC; Eukaryota.
DR GeneTree; ENSGT01000000214430; -.
DR HOGENOM; CLU_109427_0_0_1; -.
DR InParanoid; P32881; -.
DR OMA; TETHLMY; -.
DR OrthoDB; 1358010at2759; -.
DR PhylomeDB; P32881; -.
DR TreeFam; TF336177; -.
DR PathwayCommons; P32881; -.
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; P32881; -.
DR BioGRID-ORCS; 3445; 9 hits in 992 CRISPR screens.
DR ChiTaRS; IFNA8; human.
DR GeneWiki; IFNA8; -.
DR GenomeRNAi; 3445; -.
DR Pharos; P32881; Tbio.
DR PRO; PR:P32881; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P32881; protein.
DR Bgee; ENSG00000120242; Expressed in cerebellar cortex and 4 other tissues.
DR Genevisible; P32881; 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:0005126; F:cytokine receptor binding; TAS:ProtInc.
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:9425112"
FT CHAIN 24..189
FT /note="Interferon alpha-8"
FT /id="PRO_0000016365"
FT DISULFID 24..122
FT /evidence="ECO:0000250"
FT DISULFID 52..162
FT /evidence="ECO:0000250"
FT VARIANT 137
FT /note="E -> K (in dbSNP:rs3739630)"
FT /id="VAR_021975"
FT CONFLICT 8
FT /note="L -> M (in Ref. 3; CAA23806 and 4; CAA23811)"
FT /evidence="ECO:0000305"
FT CONFLICT 121..124
FT /note="SCVM -> VLCD (in Ref. 3; CAA23806 and 4; CAA23811)"
FT /evidence="ECO:0000305"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:6JHD"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:6JHD"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:6JHD"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:6JHD"
FT HELIX 73..92
FT /evidence="ECO:0007829|PDB:6JHD"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6JHD"
FT HELIX 102..125
FT /evidence="ECO:0007829|PDB:6JHD"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:6JHD"
FT HELIX 133..157
FT /evidence="ECO:0007829|PDB:6JHD"
FT HELIX 162..178
FT /evidence="ECO:0007829|PDB:6JHD"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:6JHD"
SQ SEQUENCE 189 AA; 21989 MW; 83128DA2B6DBB2C1 CRC64;
MALTFYLLVA LVVLSYKSFS SLGCDLPQTH SLGNRRALIL LAQMRRISPF SCLKDRHDFE
FPQEEFDDKQ FQKAQAISVL HEMIQQTFNL FSTKDSSAAL DETLLDEFYI ELDQQLNDLE
SCVMQEVGVI ESPLMYEDSI LAVRKYFQRI TLYLTEKKYS SCAWEVVRAE IMRSFSLSIN
LQKRLKSKE
