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Interferon alpha-14 (IFN-alpha-14) (Interferon alpha-H) (LeIF H) (Interferon lambda-2-H)

 IFN14_HUMAN             Reviewed;         189 AA.
P01570; Q5VZ56; Q7M4S1;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 3.
12-SEP-2018, entry version 177.
RecName: Full=Interferon alpha-14;
Short=IFN-alpha-14;
AltName: Full=Interferon alpha-H;
Short=LeIF H;
AltName: Full=Interferon lambda-2-H;
Flags: Precursor;
Name=IFNA14;
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=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).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6165082; DOI=10.1126/science.6165082;
Lawn R.M., Adelman J., Dull T.J., Gross M., Goeddel D.V., Ullrich A.;
"DNA sequence of two closely linked human leukocyte interferon
genes.";
Science 212:1159-1162(1981).
[3]
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).
[4]
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).
[5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[7]
PROTEIN SEQUENCE OF 24-55, 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).
[8]
PROTEIN SEQUENCE OF 24-53, AND GLYCOSYLATION AT ASN-95.
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).
[9]
PROTEIN SEQUENCE OF 24-43.
PubMed=7765487; DOI=10.1271/bbb.58.1714;
Shirono H., Koga J., Uemura H., Matsuo A.;
"Identification of glycosylated subtypes of interferon-alpha produced
by human leukocytes.";
Biosci. Biotechnol. Biochem. 58:1714-1715(1994).
[10]
ABSENCE OF POLYMORPHISM.
PubMed=8910771; DOI=10.1089/jir.1996.16.853;
Hussain M., Gill D.S., Liao M.-J.;
"Identification of interferon-alpha 7, -alpha 14, and -alpha 21
variants in the genome of a large human population.";
J. Interferon Cytokine Res. 16:853-859(1996).
-!- 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.
-!- SIMILARITY: Belongs to the alpha/beta interferon family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; V00542; CAA23803.1; -; mRNA.
EMBL; V00533; CAA23794.1; -; Genomic_DNA.
EMBL; X02959; CAA26705.1; -; Genomic_DNA.
EMBL; AL162420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471071; EAW58616.1; -; Genomic_DNA.
EMBL; BC074956; AAH74956.1; -; mRNA.
EMBL; BC104159; AAI04160.1; -; mRNA.
EMBL; BC104160; AAI04161.1; -; mRNA.
CCDS; CCDS6501.1; -.
PIR; A42753; A42753.
PIR; A92916; IVHU14.
RefSeq; NP_002163.2; NM_002172.2.
UniGene; Hs.93907; -.
ProteinModelPortal; P01570; -.
SMR; P01570; -.
BioGrid; 109671; 9.
IntAct; P01570; 1.
STRING; 9606.ENSP00000369571; -.
ChEMBL; CHEMBL3856161; -.
GlyConnect; 288; -.
iPTMnet; P01570; -.
PhosphoSitePlus; P01570; -.
UniCarbKB; P01570; -.
BioMuta; IFNA14; -.
DMDM; 20178265; -.
REPRODUCTION-2DPAGE; P01570; -.
PaxDb; P01570; -.
PeptideAtlas; P01570; -.
PRIDE; P01570; -.
ProteomicsDB; 51386; -.
Ensembl; ENST00000380222; ENSP00000369571; ENSG00000228083.
GeneID; 3448; -.
KEGG; hsa:3448; -.
UCSC; uc010mis.4; human.
CTD; 3448; -.
DisGeNET; 3448; -.
EuPathDB; HostDB:ENSG00000228083.2; -.
GeneCards; IFNA14; -.
HGNC; HGNC:5420; IFNA14.
HPA; HPA047557; -.
MIM; 147579; gene.
neXtProt; NX_P01570; -.
OpenTargets; ENSG00000228083; -.
PharmGKB; PA29659; -.
eggNOG; ENOG410J735; Eukaryota.
eggNOG; ENOG410ZH91; LUCA.
GeneTree; ENSGT00760000119150; -.
HOGENOM; HOG000230500; -.
HOVERGEN; HBG052086; -.
InParanoid; P01570; -.
KO; K05414; -.
OMA; NNRRTLM; -.
OrthoDB; EOG091G0MJ6; -.
PhylomeDB; P01570; -.
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.
GeneWiki; IFNA14; -.
GenomeRNAi; 3448; -.
PRO; PR:P01570; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000228083; Expressed in 2 organ(s), highest expression level in cortex of kidney.
CleanEx; HS_IFNA14; -.
Genevisible; P01570; 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:0005126; F:cytokine receptor binding; TAS:ProtInc.
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;
Antiviral defense; Complete proteome; Cytokine;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Reference proteome; Secreted; Signal.
SIGNAL 1 23 {ECO:0000269|PubMed:1634550,
ECO:0000269|PubMed:7765487,
ECO:0000269|PubMed:9425112}.
CHAIN 24 189 Interferon alpha-14.
/FTId=PRO_0000016367.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9425112}.
DISULFID 24 122 {ECO:0000250}.
DISULFID 52 162 {ECO:0000250}.
CONFLICT 175 175 L -> F (in Ref. 1; CAA23803).
{ECO:0000305}.
SEQUENCE 189 AA; 22063 MW; B6B71E2F0D644FE7 CRC64;
MALPFALMMA LVVLSCKSSC SLGCNLSQTH SLNNRRTLML MAQMRRISPF SCLKDRHDFE
FPQEEFDGNQ FQKAQAISVL HEMMQQTFNL FSTKNSSAAW DETLLEKFYI ELFQQMNDLE
ACVIQEVGVE ETPLMNEDSI LAVKKYFQRI TLYLMEKKYS PCAWEVVRAE IMRSLSFSTN
LQKRLRRKD


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