IL17_HUMAN
ID IL17_HUMAN Reviewed; 155 AA.
AC Q16552; Q5T2P0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Interleukin-17A;
DE Short=IL-17;
DE Short=IL-17A;
DE AltName: Full=Cytotoxic T-lymphocyte-associated antigen 8;
DE Short=CTLA-8;
DE Flags: Precursor;
GN Name=IL17A; Synonyms=CTLA8, IL17;
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], FUNCTION, SUBCELLULAR LOCATION, AND PTM.
RX PubMed=8676080; DOI=10.1084/jem.183.6.2593;
RA Fossiez F., Djossou O., Chomarat P., Flores-Romo L., Ait-Yahia S., Maat C.,
RA Pin J.-J., Garrone P., Garcia E., Saeland S., Blanchard D., Gaillard C.,
RA Das Mahapatra B., Rouvier E., Golstein P., Banchereau J., Lebecque S.;
RT "T cell interleukin-17 induces stromal cells to produce proinflammatory and
RT hematopoietic cytokines.";
RL J. Exp. Med. 183:2593-2603(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=T-cell;
RX PubMed=7499828;
RA Yao Z., Painter S.L., Fanslow W.C., Ulrich D., Macduff B.M., Spriggs M.K.,
RA Armitage R.J.;
RT "Human IL-17: a novel cytokine derived from T cells.";
RL J. Immunol. 155:5483-5486(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
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 [6]
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 [7]
RP PROTEIN SEQUENCE OF 24-38.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY IL23A-IL12B.
RX PubMed=17763419; DOI=10.1002/art.22866;
RA Chen Z., Tato C.M., Muul L., Laurence A., O'Shea J.J.;
RT "Distinct regulation of interleukin-17 in human T helper lymphocytes.";
RL Arthritis Rheum. 56:2936-2946(2007).
RN [9]
RP SUBUNIT.
RX PubMed=17355969; DOI=10.1074/jbc.m700499200;
RA Wright J.F., Guo Y., Quazi A., Luxenberg D.P., Bennett F., Ross J.F.,
RA Qiu Y., Whitters M.J., Tomkinson K.N., Dunussi-Joannopoulos K.,
RA Carreno B.M., Collins M., Wolfman N.M.;
RT "Identification of an interleukin 17F/17A heterodimer in activated human
RT CD4+ T cells.";
RL J. Biol. Chem. 282:13447-13455(2007).
RN [10]
RP FUNCTION.
RX PubMed=17911633; DOI=10.4049/jimmunol.179.8.5462;
RA Kuestner R.E., Taft D.W., Haran A., Brandt C.S., Brender T., Lum K.,
RA Harder B., Okada S., Ostrander C.D., Kreindler J.L., Aujla S.J.,
RA Reardon B., Moore M., Shea P., Schreckhise R., Bukowski T.R., Presnell S.,
RA Guerra-Lewis P., Parrish-Novak J., Ellsworth J.L., Jaspers S., Lewis K.E.,
RA Appleby M., Kolls J.K., Rixon M., West J.W., Gao Z., Levin S.D.;
RT "Identification of the IL-17 receptor related molecule IL-17RC as the
RT receptor for IL-17F.";
RL J. Immunol. 179:5462-5473(2007).
RN [11]
RP FUNCTION.
RX PubMed=18684971; DOI=10.4049/jimmunol.181.4.2799;
RA Wright J.F., Bennett F., Li B., Brooks J., Luxenberg D.P., Whitters M.J.,
RA Tomkinson K.N., Fitz L.J., Wolfman N.M., Collins M.,
RA Dunussi-Joannopoulos K., Chatterjee-Kishore M., Carreno B.M.;
RT "The human IL-17F/IL-17A heterodimeric cytokine signals through the IL-
RT 17RA/IL-17RC receptor complex.";
RL J. Immunol. 181:2799-2805(2008).
RN [12]
RP FUNCTION.
RX PubMed=19825828; DOI=10.1126/scisignal.2000382;
RA Liu C., Qian W., Qian Y., Giltiay N.V., Lu Y., Swaidani S., Misra S.,
RA Deng L., Chen Z.J., Li X.;
RT "Act1, a U-box E3 ubiquitin ligase for IL-17 signaling.";
RL Sci. Signal. 2:ra63-ra63(2009).
RN [13]
RP FUNCTION.
RX PubMed=21350122; DOI=10.1126/science.1200439;
RA Puel A., Cypowyj S., Bustamante J., Wright J.F., Liu L., Lim H.K.,
RA Migaud M., Israel L., Chrabieh M., Audry M., Gumbleton M., Toulon A.,
RA Bodemer C., El-Baghdadi J., Whitters M., Paradis T., Brooks J., Collins M.,
RA Wolfman N.M., Al-Muhsen S., Galicchio M., Abel L., Picard C.,
RA Casanova J.L.;
RT "Chronic mucocutaneous candidiasis in humans with inborn errors of
RT interleukin-17 immunity.";
RL Science 332:65-68(2011).
RN [14]
RP FUNCTION.
RX PubMed=24120361; DOI=10.1016/j.immuni.2013.09.002;
RA Boisson B., Wang C., Pedergnana V., Wu L., Cypowyj S., Rybojad M.,
RA Belkadi A., Picard C., Abel L., Fieschi C., Puel A., Li X., Casanova J.L.;
RT "An ACT1 mutation selectively abolishes interleukin-17 responses in humans
RT with chronic mucocutaneous candidiasis.";
RL Immunity 39:676-686(2013).
RN [15]
RP INDUCTION.
RX PubMed=27795421; DOI=10.1128/jvi.01529-16;
RA Acharya D., Wang P., Paul A.M., Dai J., Gate D., Lowery J.E., Stokic D.S.,
RA Leis A.A., Flavell R.A., Town T., Fikrig E., Bai F.;
RT "Interleukin-17A Promotes CD8+ T Cell Cytotoxicity To Facilitate West Nile
RT Virus Clearance.";
RL J. Virol. 91:0-0(2017).
RN [16]
RP INTERACTION WITH IL17F; IL17RA AND IL17RC.
RX PubMed=32187518; DOI=10.1016/j.immuni.2020.02.004;
RA Goepfert A., Lehmann S., Blank J., Kolbinger F., Rondeau J.M.;
RT "Structural Analysis Reveals that the Cytokine IL-17F Forms a Homodimeric
RT Complex with Receptor IL-17RC to Drive IL-17RA-Independent Signaling.";
RL Immunity 52:499-512.e5(2020).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 20-155 IN COMPLEX WITH ANTIBODY,
RP DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=19835883; DOI=10.1016/j.jmb.2009.10.008;
RA Gerhardt S., Abbott W.M., Hargreaves D., Pauptit R.A., Davies R.A.,
RA Needham M.R., Langham C., Barker W., Aziz A., Snow M.J., Dawson S.,
RA Welsh F., Wilkinson T., Vaugan T., Beste G., Bishop S., Popovic B.,
RA Rees G., Sleeman M., Tuske S.J., Coales S.J., Hamuro Y., Russell C.;
RT "Structure of IL-17A in complex with a potent, fully human neutralizing
RT antibody.";
RL J. Mol. Biol. 394:905-921(2009).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 34-155 IN COMPLEX WITH IL17RA,
RP DISULFIDE BONDS, SUBUNIT, AND MUTAGENESIS OF ARG-78; TRP-90; TYR-108 AND
RP HIS-109.
RX PubMed=23695682; DOI=10.1038/ncomms2880;
RA Liu S., Song X., Chrunyk B.A., Shanker S., Hoth L.R., Marr E.S.,
RA Griffor M.C.;
RT "Crystal structures of interleukin 17A and its complex with IL-17 receptor
RT A.";
RL Nat. Commun. 4:1888-1888(2013).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 24-155 IN COMPLEX WITH IL17F;
RP IL17RA AND IL17RC, SUBUNIT, AND MUTAGENESIS OF ARG-69.
RX PubMed=28827714; DOI=10.1038/s41598-017-08360-9;
RA Goepfert A., Lehmann S., Wirth E., Rondeau J.M.;
RT "The human IL-17A/F heterodimer: a two-faced cytokine with unique receptor
RT recognition properties.";
RL Sci. Rep. 7:8906-8906(2017).
CC -!- FUNCTION: Effector cytokine of innate and adaptive immune system
CC involved in antimicrobial host defense and maintenance of tissue
CC integrity (PubMed:24120361). Signals via IL17RA-IL17RC heterodimeric
CC receptor complex, triggering homotypic interaction of IL17RA and IL17RC
CC chains with TRAF3IP2 adapter. This leads to downstream TRAF6-mediated
CC activation of NF-kappa-B and MAPkinase pathways ultimately resulting in
CC transcriptional activation of cytokines, chemokines, antimicrobial
CC peptides and matrix metalloproteinases, with potential strong immune
CC inflammation (PubMed:19825828, PubMed:21350122, PubMed:17911633,
CC PubMed:18684971, PubMed:8676080, PubMed:24120361). Plays an important
CC role in connecting T cell-mediated adaptive immunity and acute
CC inflammatory response to destroy extracellular bacteria and fungi. As a
CC signature effector cytokine of T-helper 17 cells (Th17), primarily
CC induces neutrophil activation and recruitment at infection and
CC inflammatory sites (By similarity). In airway epithelium, mediates
CC neutrophil chemotaxis via induction of CXCL1 and CXCL5 chemokines (By
CC similarity). In secondary lymphoid organs, contributes to germinal
CC center formation by regulating the chemotactic response of B cells to
CC CXCL12 and CXCL13, enhancing retention of B cells within the germinal
CC centers, B cell somatic hypermutation rate and selection toward plasma
CC cells (By similarity). Effector cytokine of a subset of gamma-delta T
CC cells that functions as part of an inflammatory circuit downstream
CC IL1B, TLR2 and IL23A-IL12B to promote neutrophil recruitment for
CC efficient bacterial clearance (By similarity). Effector cytokine of
CC innate immune cells including invariant natural killer cell (iNKT) and
CC group 3 innate lymphoid cells that mediate initial neutrophilic
CC inflammation (By similarity). Involved in the maintenance of the
CC integrity of epithelial barriers during homeostasis and pathogen
CC infection (PubMed:21350122). Upon acute injury, has a direct role in
CC epithelial barrier formation by regulating OCLN localization and tight
CC junction biogenesis (By similarity). As part of the mucosal immune
CC response induced by commensal bacteria, enhances host's ability to
CC resist pathogenic bacterial and fungal infections by promoting
CC neutrophil recruitment and antimicrobial peptides release (By
CC similarity). In synergy with IL17F, mediates the production of
CC antimicrobial beta-defensins DEFB1, DEFB103A, and DEFB104A by mucosal
CC epithelial cells, limiting the entry of microbes through the epithelial
CC barriers (By similarity). Involved in antiviral host defense through
CC various mechanisms (By similarity). Enhances immunity against West Nile
CC virus by promoting T cell cytotoxicity (By similarity). May play a
CC beneficial role in influenza A virus (H5N1) infection by enhancing B
CC cell recruitment and immune response in the lung (By similarity).
CC Contributes to influenza A virus (H1N1) clearance by driving the
CC differentiation of B-1a B cells, providing for production of virus-
CC specific IgM antibodies at first line of host defense (By similarity).
CC {ECO:0000250|UniProtKB:Q62386, ECO:0000269|PubMed:17911633,
CC ECO:0000269|PubMed:18684971, ECO:0000269|PubMed:19825828,
CC ECO:0000269|PubMed:21350122, ECO:0000269|PubMed:24120361,
CC ECO:0000269|PubMed:8676080}.
CC -!- SUBUNIT: Homodimer (PubMed:19835883). Forms complexes with IL17RA and
CC IL17RC receptors with 2:1 binding stoichiometry: two receptor chains
CC for one interleukin molecule (PubMed:32187518). IL17A homodimer
CC preferentially drives the formation of IL17RA-IL17RC heterodimeric
CC receptor complex (PubMed:32187518). IL17A homodimer adopts an
CC asymmetrical ternary structure with one IL17RA molecule, allowing for
CC high affinity interactions of one IL17A monomer with one IL17RA
CC molecule (via D1 and D2 domains), while disfavoring binding of a second
CC IL17RA molecule on the other IL17A monomer (PubMed:23695682).
CC Heterodimer with IL17F (PubMed:17355969). IL17A-IL17F forms complexes
CC with IL17RA-IL17RC, but with lower affinity when compared to IL17A
CC homodimer (PubMed:32187518). IL17RA and IL17RC chains cannot
CC distinguish between IL17A and IL17F molecules, potentially enabling the
CC formation of topologically distinct complexes (PubMed:17355969,
CC PubMed:28827714). {ECO:0000269|PubMed:17355969,
CC ECO:0000269|PubMed:19835883, ECO:0000269|PubMed:23695682,
CC ECO:0000269|PubMed:28827714, ECO:0000269|PubMed:32187518}.
CC -!- INTERACTION:
CC Q16552; Q9BQC3: DPH2; NbExp=3; IntAct=EBI-10237926, EBI-10237931;
CC Q16552; Q6PIL6: KCNIP4; NbExp=3; IntAct=EBI-10237926, EBI-1051469;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17763419,
CC ECO:0000269|PubMed:8676080}.
CC -!- TISSUE SPECIFICITY: Expressed in memory Th17 cells (at protein level).
CC {ECO:0000269|PubMed:17763419}.
CC -!- INDUCTION: Induced upon differentiation of CD4-positive T cells. Up-
CC regulated by IL23A-IL12B (PubMed:17763419). Up-regulated in peripheral
CC blood mononuclear cells upon West Nile virus infection
CC (PubMed:27795421). {ECO:0000269|PubMed:17763419,
CC ECO:0000269|PubMed:27795421}.
CC -!- PTM: N-glycosylated. Found both in glycosylated and nonglycosylated
CC forms. {ECO:0000269|PubMed:8676080}.
CC -!- SIMILARITY: Belongs to the IL-17 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-17 entry;
CC URL="https://en.wikipedia.org/wiki/Interleukin_17";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il17/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/IL17AID40945ch6p12.html";
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DR EMBL; Z58820; CAA91233.1; -; mRNA.
DR EMBL; U32659; AAC50341.1; -; mRNA.
DR EMBL; AY460616; AAR23263.1; -; Genomic_DNA.
DR EMBL; AL391221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04362.1; -; Genomic_DNA.
DR EMBL; BC066251; AAH66251.1; -; mRNA.
DR EMBL; BC066252; AAH66252.1; -; mRNA.
DR EMBL; BC067503; AAH67503.1; -; mRNA.
DR EMBL; BC067504; AAH67504.1; -; mRNA.
DR EMBL; BC067505; AAH67505.1; -; mRNA.
DR CCDS; CCDS4937.1; -.
DR RefSeq; NP_002181.1; NM_002190.2.
DR PDB; 2VXS; X-ray; 2.63 A; A/B/C/D=20-155.
DR PDB; 4HR9; X-ray; 2.48 A; A/B=34-155.
DR PDB; 4HSA; X-ray; 3.15 A; A/B/D/E=34-155.
DR PDB; 4QHU; X-ray; 2.20 A; C/D=24-154.
DR PDB; 5HHV; X-ray; 2.20 A; A/B=34-155.
DR PDB; 5HHX; X-ray; 3.00 A; A/B=20-155.
DR PDB; 5HI3; X-ray; 2.15 A; A/B=24-155.
DR PDB; 5HI4; X-ray; 1.80 A; A/B=24-155.
DR PDB; 5HI5; X-ray; 1.80 A; A/B=24-155.
DR PDB; 5N7W; X-ray; 1.96 A; X/Y=1-155.
DR PDB; 5N92; X-ray; 2.30 A; A=24-155.
DR PDB; 5NAN; X-ray; 3.30 A; A/D=24-155.
DR PDB; 5VB9; X-ray; 1.70 A; A/B=38-155.
DR PDB; 6WIO; X-ray; 2.17 A; C=1-155.
DR PDB; 6WIR; X-ray; 2.96 A; C=1-155.
DR PDB; 7WKX; X-ray; 2.81 A; E/F=20-155.
DR PDBsum; 2VXS; -.
DR PDBsum; 4HR9; -.
DR PDBsum; 4HSA; -.
DR PDBsum; 4QHU; -.
DR PDBsum; 5HHV; -.
DR PDBsum; 5HHX; -.
DR PDBsum; 5HI3; -.
DR PDBsum; 5HI4; -.
DR PDBsum; 5HI5; -.
DR PDBsum; 5N7W; -.
DR PDBsum; 5N92; -.
DR PDBsum; 5NAN; -.
DR PDBsum; 5VB9; -.
DR PDBsum; 6WIO; -.
DR PDBsum; 6WIR; -.
DR PDBsum; 7WKX; -.
DR AlphaFoldDB; Q16552; -.
DR SMR; Q16552; -.
DR BioGRID; 109818; 11.
DR DIP; DIP-6014N; -.
DR IntAct; Q16552; 7.
DR STRING; 9606.ENSP00000344192; -.
DR BindingDB; Q16552; -.
DR ChEMBL; CHEMBL3390822; -.
DR DrugBank; DB11569; Ixekizumab.
DR DrugBank; DB09029; Secukinumab.
DR DrugCentral; Q16552; -.
DR GlyGen; Q16552; 1 site.
DR iPTMnet; Q16552; -.
DR PhosphoSitePlus; Q16552; -.
DR BioMuta; IL17A; -.
DR DMDM; 2498481; -.
DR PaxDb; Q16552; -.
DR PeptideAtlas; Q16552; -.
DR PRIDE; Q16552; -.
DR ProteomicsDB; 60910; -.
DR ABCD; Q16552; 183 sequenced antibodies.
DR Antibodypedia; 17132; 1912 antibodies from 50 providers.
DR DNASU; 3605; -.
DR Ensembl; ENST00000648244.1; ENSP00000497968.1; ENSG00000112115.7.
DR GeneID; 3605; -.
DR KEGG; hsa:3605; -.
DR MANE-Select; ENST00000648244.1; ENSP00000497968.1; NM_002190.3; NP_002181.1.
DR UCSC; uc003pak.1; human.
DR CTD; 3605; -.
DR DisGeNET; 3605; -.
DR GeneCards; IL17A; -.
DR HGNC; HGNC:5981; IL17A.
DR HPA; ENSG00000112115; Tissue enhanced (lymphoid).
DR MIM; 603149; gene.
DR neXtProt; NX_Q16552; -.
DR OpenTargets; ENSG00000112115; -.
DR PharmGKB; PA29794; -.
DR VEuPathDB; HostDB:ENSG00000112115; -.
DR eggNOG; ENOG502S5A0; Eukaryota.
DR GeneTree; ENSGT00940000161882; -.
DR HOGENOM; CLU_118641_0_0_1; -.
DR InParanoid; Q16552; -.
DR OMA; HHMNSVP; -.
DR OrthoDB; 1469254at2759; -.
DR PhylomeDB; Q16552; -.
DR TreeFam; TF314701; -.
DR PathwayCommons; Q16552; -.
DR Reactome; R-HSA-448424; Interleukin-17 signaling.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; Q16552; -.
DR SIGNOR; Q16552; -.
DR BioGRID-ORCS; 3605; 9 hits in 1061 CRISPR screens.
DR EvolutionaryTrace; Q16552; -.
DR GeneWiki; IL17A; -.
DR GenomeRNAi; 3605; -.
DR Pharos; Q16552; Tclin.
DR PRO; PR:Q16552; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q16552; protein.
DR Bgee; ENSG00000112115; Expressed in vermiform appendix and 24 other tissues.
DR Genevisible; Q16552; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005125; F:cytokine activity; TAS:ProtInc.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0008219; P:cell death; TAS:ProtInc.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0050832; P:defense response to fungus; IEA:Ensembl.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:Ensembl.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR GO; GO:0072537; P:fibroblast activation; IDA:BHF-UCL.
DR GO; GO:0097530; P:granulocyte migration; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0097400; P:interleukin-17-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0060729; P:intestinal epithelial structure maintenance; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0002225; P:positive regulation of antimicrobial peptide production; IEA:Ensembl.
DR GO; GO:1903348; P:positive regulation of bicellular tight junction assembly; IEA:Ensembl.
DR GO; GO:2000340; P:positive regulation of chemokine (C-X-C motif) ligand 1 production; IDA:UniProtKB.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IDA:ARUK-UCL.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:ARUK-UCL.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:ARUK-UCL.
DR GO; GO:0032739; P:positive regulation of interleukin-16 production; IDA:ARUK-UCL.
DR GO; GO:0032747; P:positive regulation of interleukin-23 production; IDA:BHF-UCL.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:ARUK-UCL.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR020440; IL-17_chr.
DR InterPro; IPR010345; IL-17_fam.
DR Pfam; PF06083; IL17; 1.
DR PRINTS; PR01932; INTRLEUKIN17.
DR SUPFAM; SSF57501; SSF57501; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cytokine; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunity; Inflammatory response;
KW Innate immunity; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 24..155
FT /note="Interleukin-17A"
FT /id="PRO_0000015423"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..144
FT /evidence="ECO:0000269|PubMed:19835883,
FT ECO:0000269|PubMed:23695682"
FT DISULFID 99..146
FT /evidence="ECO:0000269|PubMed:19835883,
FT ECO:0000269|PubMed:23695682"
FT MUTAGEN 69
FT /note="R->A: Impairs binding to IL17RA and IL17RC."
FT /evidence="ECO:0000269|PubMed:28827714"
FT MUTAGEN 78
FT /note="R->V: Decreases the affinity for IL17RA by 5-fold."
FT /evidence="ECO:0000269|PubMed:23695682"
FT MUTAGEN 90
FT /note="W->V: Has no effect on the affinity for IL17RA."
FT /evidence="ECO:0000269|PubMed:23695682"
FT MUTAGEN 108
FT /note="Y->I: Decreases the affinity for IL17RA."
FT /evidence="ECO:0000269|PubMed:23695682"
FT MUTAGEN 109
FT /note="H->S: Decreases the affinity for IL17RA."
FT /evidence="ECO:0000269|PubMed:23695682"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:4QHU"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:5N7W"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:5HI5"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:5HI5"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:5VB9"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5VB9"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:5VB9"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:5VB9"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:5VB9"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:5VB9"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:5VB9"
FT STRAND 110..126
FT /evidence="ECO:0007829|PDB:5VB9"
FT STRAND 133..147
FT /evidence="ECO:0007829|PDB:5VB9"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:4HSA"
SQ SEQUENCE 155 AA; 17504 MW; 2BCAE9CB2F4886D1 CRC64;
MTPGKTSLVS LLLLLSLEAI VKAGITIPRN PGCPNSEDKN FPRTVMVNLN IHNRNTNTNP
KRSSDYYNRS TSPWNLHRNE DPERYPSVIW EAKCRHLGCI NADGNVDYHM NSVPIQQEIL
VLRREPPHCP NSFRLEKILV SVGCTCVTPI VHHVA
