ID I17RA_HUMAN Reviewed; 866 AA.
AC Q96F46; O43844; Q20WK1;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 28-JUN-2023, entry version 184.
DE RecName: Full=Interleukin-17 receptor A {ECO:0000305};
DE Short=IL-17 receptor A;
DE Short=IL-17RA;
DE AltName: Full=CDw217;
DE AltName: CD_antigen=CD217;
DE Flags: Precursor;
GN Name=IL17RA {ECO:0000312|HGNC:HGNC:5985}; Synonyms=IL17R;
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] (ISOFORM 1), AND FUNCTION.
RC TISSUE=T-cell;
RX PubMed=9367539; DOI=10.1006/cyto.1997.0240;
RA Yao Z., Spriggs M.K., Derry J.M.J., Strockbine L., Park L.S.,
RA Vanden Bos T., Zappone J., Painter S.L., Armitage R.J.;
RT "Molecular characterization of the human interleukin (Il)-17 receptor.";
RL Cytokine 9:794-800(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-367
RP AND HIS-580.
RC TISSUE=Uterus;
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 [5]
RP PROTEIN SEQUENCE OF 33-47.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 237-431 (ISOFORM 2).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16785495; DOI=10.4049/jimmunol.177.1.36;
RA Toy D., Kugler D., Wolfson M., Vanden Bos T., Gurgel J., Derry J.,
RA Tocker J., Peschon J.;
RT "Interleukin 17 signals through a heteromeric receptor complex.";
RL J. Immunol. 177:36-39(2006).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [9]
RP FUNCTION, AND SUBUNIT.
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 [10]
RP FUNCTION, IDENTIFICATION AS IL17C CORECEPTOR, INTERACTION WITH IL17RE, AND
RP TISSUE SPECIFICITY.
RX PubMed=21993848; DOI=10.1038/ni.2156;
RA Ramirez-Carrozzi V., Sambandam A., Luis E., Lin Z., Jeet S., Lesch J.,
RA Hackney J., Kim J., Zhou M., Lai J., Modrusan Z., Sai T., Lee W., Xu M.,
RA Caplazi P., Diehl L., de Voss J., Balazs M., Gonzalez L. Jr., Singh H.,
RA Ouyang W., Pappu R.;
RT "IL-17C regulates the innate immune function of epithelial cells in an
RT autocrine manner.";
RL Nat. Immunol. 12:1159-1166(2011).
RN [11]
RP ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION.
RX PubMed=24084331; DOI=10.1016/j.cyto.2013.09.012;
RA Sohda M., Misumi Y., Tashiro K., Yamazaki M., Saku T., Oda K.;
RT "Identification of a soluble isoform of human IL-17RA generated by
RT alternative splicing.";
RL Cytokine 64:642-645(2013).
RN [12]
RP FUNCTION, AND INTERACTION WITH TRAF3IP2.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-708, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP INTERACTION WITH IL17RC; IL17A AND IL17F.
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 [15]
RP INTERACTION WITH SARS-COV-2 VIRUS PROTEIN ORF8 (MICROBIAL INFECTION).
RX PubMed=33060197; DOI=10.1126/science.abe9403;
RG QCRG Structural Biology Consortium;
RG Zoonomia Consortium;
RA Gordon D.E., Hiatt J., Bouhaddou M., Rezelj V.V., Ulferts S., Braberg H.,
RA Jureka A.S., Obernier K., Guo J.Z., Batra J., Kaake R.M., Weckstein A.R.,
RA Owens T.W., Gupta M., Pourmal S., Titus E.W., Cakir M., Soucheray M.,
RA McGregor M., Cakir Z., Jang G., O'Meara M.J., Tummino T.A., Zhang Z.,
RA Foussard H., Rojc A., Zhou Y., Kuchenov D., Huettenhain R., Xu J.,
RA Eckhardt M., Swaney D.L., Fabius J.M., Ummadi M., Tutuncuoglu B.,
RA Rathore U., Modak M., Haas P., Haas K.M., Naing Z.Z.C., Pulido E.H.,
RA Shi Y., Barrio-Hernandez I., Memon D., Petsalaki E., Dunham A.,
RA Marrero M.C., Burke D., Koh C., Vallet T., Silvas J.A., Azumaya C.M.,
RA Billesboelle C., Brilot A.F., Campbell M.G., Diallo A., Dickinson M.S.,
RA Diwanji D., Herrera N., Hoppe N., Kratochvil H.T., Liu Y., Merz G.E.,
RA Moritz M., Nguyen H.C., Nowotny C., Puchades C., Rizo A.N.,
RA Schulze-Gahmen U., Smith A.M., Sun M., Young I.D., Zhao J., Asarnow D.,
RA Biel J., Bowen A., Braxton J.R., Chen J., Chio C.M., Chio U.S.,
RA Deshpande I., Doan L., Faust B., Flores S., Jin M., Kim K., Lam V.L.,
RA Li F., Li J., Li Y.L., Li Y., Liu X., Lo M., Lopez K.E., Melo A.A.,
RA Moss F.R. III, Nguyen P., Paulino J., Pawar K.I., Peters J.K.,
RA Pospiech T.H. Jr., Safari M., Sangwan S., Schaefer K., Thomas P.V.,
RA Thwin A.C., Trenker R., Tse E., Tsui T.K.M., Wang F., Whitis N., Yu Z.,
RA Zhang K., Zhang Y., Zhou F., Saltzberg D., Hodder A.J., Shun-Shion A.S.,
RA Williams D.M., White K.M., Rosales R., Kehrer T., Miorin L., Moreno E.,
RA Patel A.H., Rihn S., Khalid M.M., Vallejo-Gracia A., Fozouni P.,
RA Simoneau C.R., Roth T.L., Wu D., Karim M.A., Ghoussaini M., Dunham I.,
RA Berardi F., Weigang S., Chazal M., Park J., Logue J., McGrath M.,
RA Weston S., Haupt R., Hastie C.J., Elliott M., Brown F., Burness K.A.,
RA Reid E., Dorward M., Johnson C., Wilkinson S.G., Geyer A., Giesel D.M.,
RA Baillie C., Raggett S., Leech H., Toth R., Goodman N., Keough K.C.,
RA Lind A.L., Klesh R.J., Hemphill K.R., Carlson-Stevermer J., Oki J.,
RA Holden K., Maures T., Pollard K.S., Sali A., Agard D.A., Cheng Y.,
RA Fraser J.S., Frost A., Jura N., Kortemme T., Manglik A., Southworth D.R.,
RA Stroud R.M., Alessi D.R., Davies P., Frieman M.B., Ideker T., Abate C.,
RA Jouvenet N., Kochs G., Shoichet B., Ott M., Palmarini M., Shokat K.M.,
RA Garcia-Sastre A., Rassen J.A., Grosse R., Rosenberg O.S., Verba K.A.,
RA Basler C.F., Vignuzzi M., Peden A.A., Beltrao P., Krogan N.J.;
RT "Comparative host-coronavirus protein interaction networks reveal pan-viral
RT disease mechanisms.";
RL Science 0:0-0(2020).
RN [16]
RP INTERACTION WITH SARS-COV-2 VIRUS PROTEIN ORF8 (MICROBIAL INFECTION), AND
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=33723527; DOI=10.1016/j.isci.2021.102293;
RA Lin X., Fu B., Yin S., Li Z., Liu H., Zhang H., Xing N., Wang Y., Xue W.,
RA Xiong Y., Zhang S., Zhao Q., Xu S., Zhang J., Wang P., Nian W., Wang X.,
RA Wu H.;
RT "Title: ORF8 contributes to cytokine storm during SARS-CoV-2 infection by
RT activating IL-17 pathway.";
RL IScience 1:102293-102293(2021).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 32-317 IN COMPLEX WITH IL17F,
RP GLYCOSYLATION AT ASN-49; ASN-54; ASN-67; ASN-225 AND ASN-265, FUNCTION, AND
RP DISULFIDE BONDS.
RX PubMed=19838198; DOI=10.1038/ni.1813;
RA Ely L.K., Fischer S., Garcia K.C.;
RT "Structural basis of receptor sharing by interleukin 17 cytokines.";
RL Nat. Immunol. 10:1245-1251(2009).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 32-317 IN COMPLEX WITH IL17A,
RP DISULFIDE BONDS, SUBUNIT, AND GLYCOSYLATION AT ASN-49; ASN-54 AND ASN-225.
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 (3.30 ANGSTROMS) OF 33-320 IN COMPLEX WITH IL17A AND
RP IL17F, AND SUBUNIT.
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).
RN [20]
RP INVOLVEMENT IN IMD51, VARIANT IMD51 284-GLN--ALA-866 DEL, AND 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).
CC -!- FUNCTION: Receptor for IL17A and IL17F, major effector cytokines of
CC innate and adaptive immune system involved in antimicrobial host
CC defense and maintenance of tissue integrity. Receptor for IL17A
CC (PubMed:17911633, PubMed:9367539). Receptor for IL17F (PubMed:19838198,
CC PubMed:17911633). Binds to IL17A with higher affinity than to IL17F
CC (PubMed:17911633). Binds IL17A and IL17F homodimers as part of a
CC heterodimeric complex with IL17RC (PubMed:16785495). Also binds
CC heterodimers formed by IL17A and IL17F as part of a heterodimeric
CC complex with IL17RC (PubMed:18684971). Cytokine binding triggers
CC homotypic interaction of IL17RA and IL17RC chains with TRAF3IP2
CC adapter, leading to TRAF6-mediated activation of NF-kappa-B and
CC MAPkinase pathways, ultimately resulting in transcriptional activation
CC of cytokines, chemokines, antimicrobial peptides and matrix
CC metalloproteinases, with potential strong immune inflammation
CC (PubMed:16785495, PubMed:24120361, PubMed:17911633, PubMed:18684971,
CC PubMed:21350122). Involved in antimicrobial host defense primarily
CC promoting neutrophil activation and recruitment at infection sites to
CC destroy extracellular bacteria and fungi (By similarity). In secondary
CC lymphoid organs, contributes to germinal center formation by regulating
CC the chemotactic response of B cells to CXCL12 and CXCL13, enhancing
CC retention of B cells within the germinal centers, B cell somatic
CC hypermutation rate and selection toward plasma cells (By similarity).
CC Plays a role in the maintenance of the integrity of epithelial barriers
CC during homeostasis and pathogen infection. Stimulates 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. Enhances immunity against West Nile virus by
CC promoting T cell cytotoxicity. Contributes to Influenza virus clearance
CC by driving the differentiation of B-1a B cells, providing for
CC production of virus-specific IgM antibodies at first line of host
CC defense (By similarity). Receptor for IL17C as part of a heterodimeric
CC complex with IL17RE (PubMed:21993848). {ECO:0000250|UniProtKB:Q60943,
CC ECO:0000269|PubMed:16785495, ECO:0000269|PubMed:17911633,
CC ECO:0000269|PubMed:18684971, ECO:0000269|PubMed:19838198,
CC ECO:0000269|PubMed:21350122, ECO:0000269|PubMed:21993848,
CC ECO:0000269|PubMed:24120361, ECO:0000269|PubMed:9367539}.
CC -!- FUNCTION: (Microbial infection) Receptor for SARS coronavirus-2/SARS-
CC CoV-2 virus protein ORF8, leading to IL17 pathway activation and an
CC increased secretion of pro-inflammatory factors through activating NF-
CC kappa-B signaling pathway. {ECO:0000269|PubMed:33723527}.
CC -!- SUBUNIT: Forms heterodimers with IL17RC; the heterodimer binds IL17A
CC and IL17F homodimers as well as the heterodimer formed by IL17A and
CC IL17F (PubMed:16785495, PubMed:18684971, PubMed:32187518). Forms
CC complexes with 2:1 binding stoichiometry: two receptor chains for one
CC interleukin molecule (PubMed:32187518). IL17A homodimer preferentially
CC drives the formation of IL17RA-IL17RC heterodimeric receptor complex,
CC whereas IL17F homodimer forms predominantly complexes with IL17RC
CC homodimer (PubMed:32187518). IL17A homodimer adopts an asymmetrical
CC ternary structure with one IL17RA molecule, allowing for high affinity
CC interactions of one IL17A monomer with one IL17RA molecule (via D1 and
CC D2 domains), while disfavoring binding of a second IL17RA molecule on
CC the other IL17A monomer (PubMed:23695682). IL17A-IL17F forms complexes
CC with IL17RA-IL17RC, but with lower affinity when compared to IL17A
CC homodimer (PubMed:32187518). IL17RA chain cannot distinguish between
CC IL17A and IL17F molecules, potentially enabling the formation of
CC topologically distinct complexes (PubMed:28827714). Interacts with
CC TRAF3IP2 (PubMed:24120361). Forms heterodimers with IL17RE; the
CC heterodimer binds IL17C (PubMed:21993848, PubMed:16785495,
CC PubMed:18684971). {ECO:0000269|PubMed:16785495,
CC ECO:0000269|PubMed:18684971, ECO:0000269|PubMed:21993848,
CC ECO:0000269|PubMed:23695682, ECO:0000269|PubMed:24120361,
CC ECO:0000269|PubMed:28827714, ECO:0000269|PubMed:32187518}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus-2/SARS-
CC CoV-2 virus protein ORF8. {ECO:0000269|PubMed:33060197,
CC ECO:0000269|PubMed:33723527}.
CC -!- INTERACTION:
CC Q96F46; Q8NFR9: IL17RE; NbExp=2; IntAct=EBI-5591258, EBI-5591275;
CC Q96F46; P0DTC8: 8; Xeno; NbExp=3; IntAct=EBI-5591258, EBI-25475900;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:17911633}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000269|PubMed:24084331}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96F46-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96F46-2; Sequence=VSP_053496;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:21993848}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:19838198}.
CC -!- DISEASE: Immunodeficiency 51 (IMD51) [MIM:613953]: A primary
CC immunodeficiency disorder with altered immune responses and impaired
CC clearance of fungal infections, selective against Candida. It is
CC characterized by persistent and/or recurrent infections of the skin,
CC nails and mucous membranes caused by organisms of the genus Candida,
CC mainly Candida albicans. {ECO:0000269|PubMed:21350122}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Soluble isoform lacking the transmembrane
CC segment. {ECO:0000305}.
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DR EMBL; U58917; AAB99730.1; -; mRNA.
DR EMBL; CT841520; CAJ86450.1; -; mRNA.
DR EMBL; CH471193; EAW57739.1; -; Genomic_DNA.
DR EMBL; BC011624; AAH11624.1; -; mRNA.
DR EMBL; BX368715; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS13739.1; -. [Q96F46-1]
DR CCDS; CCDS77645.1; -. [Q96F46-2]
DR RefSeq; NP_001276834.1; NM_001289905.1. [Q96F46-2]
DR RefSeq; NP_055154.3; NM_014339.6. [Q96F46-1]
DR PDB; 3JVF; X-ray; 3.30 A; C=32-317.
DR PDB; 4HSA; X-ray; 3.15 A; C/F=32-317.
DR PDB; 4NUX; X-ray; 2.30 A; A=376-591.
DR PDB; 5N9B; X-ray; 1.90 A; A=33-318.
DR PDB; 5NAN; X-ray; 3.30 A; B/C=33-320.
DR PDB; 7UWL; EM; 3.70 A; E/F=33-317.
DR PDB; 7UWM; EM; 2.50 A; C/F=33-304.
DR PDB; 7UWN; EM; 3.01 A; C/F=33-317.
DR PDB; 7ZAN; X-ray; 5.06 A; C=33-320.
DR PDBsum; 3JVF; -.
DR PDBsum; 4HSA; -.
DR PDBsum; 4NUX; -.
DR PDBsum; 5N9B; -.
DR PDBsum; 5NAN; -.
DR PDBsum; 7UWL; -.
DR PDBsum; 7UWM; -.
DR PDBsum; 7UWN; -.
DR PDBsum; 7ZAN; -.
DR AlphaFoldDB; Q96F46; -.
DR SMR; Q96F46; -.
DR BioGRID; 117265; 216.
DR IntAct; Q96F46; 67.
DR STRING; 9606.ENSP00000320936; -.
DR BindingDB; Q96F46; -.
DR ChEMBL; CHEMBL3580485; -.
DR DrugCentral; Q96F46; -.
DR GuidetoPHARMACOLOGY; 1738; -.
DR GlyCosmos; Q96F46; 7 sites, No reported glycans.
DR GlyGen; Q96F46; 8 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q96F46; -.
DR PhosphoSitePlus; Q96F46; -.
DR BioMuta; IL17RA; -.
DR DMDM; 116242517; -.
DR EPD; Q96F46; -.
DR jPOST; Q96F46; -.
DR MassIVE; Q96F46; -.
DR MaxQB; Q96F46; -.
DR PaxDb; Q96F46; -.
DR PeptideAtlas; Q96F46; -.
DR ProteomicsDB; 76496; -. [Q96F46-1]
DR ABCD; Q96F46; 25 sequenced antibodies.
DR Antibodypedia; 22632; 828 antibodies from 43 providers.
DR DNASU; 23765; -.
DR Ensembl; ENST00000319363.11; ENSP00000320936.6; ENSG00000177663.15. [Q96F46-1]
DR Ensembl; ENST00000612619.2; ENSP00000479970.1; ENSG00000177663.15. [Q96F46-2]
DR GeneID; 23765; -.
DR KEGG; hsa:23765; -.
DR MANE-Select; ENST00000319363.11; ENSP00000320936.6; NM_014339.7; NP_055154.3.
DR UCSC; uc002zly.5; human. [Q96F46-1]
DR AGR; HGNC:5985; -.
DR CTD; 23765; -.
DR DisGeNET; 23765; -.
DR GeneCards; IL17RA; -.
DR HGNC; HGNC:5985; IL17RA.
DR HPA; ENSG00000177663; Tissue enhanced (bone).
DR MalaCards; IL17RA; -.
DR MIM; 605461; gene.
DR MIM; 613953; phenotype.
DR neXtProt; NX_Q96F46; -.
DR OpenTargets; ENSG00000177663; -.
DR Orphanet; 1334; Chronic mucocutaneous candidiasis.
DR PharmGKB; PA29801; -.
DR VEuPathDB; HostDB:ENSG00000177663; -.
DR eggNOG; ENOG502QV5J; Eukaryota.
DR GeneTree; ENSGT00940000159018; -.
DR HOGENOM; CLU_018087_0_0_1; -.
DR InParanoid; Q96F46; -.
DR OMA; EPGRIHQ; -.
DR OrthoDB; 4613833at2759; -.
DR PhylomeDB; Q96F46; -.
DR TreeFam; TF329644; -.
DR PathwayCommons; Q96F46; -.
DR Reactome; R-HSA-448424; Interleukin-17 signaling.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; Q96F46; -.
DR SIGNOR; Q96F46; -.
DR BioGRID-ORCS; 23765; 13 hits in 1179 CRISPR screens.
DR ChiTaRS; IL17RA; human.
DR EvolutionaryTrace; Q96F46; -.
DR GeneWiki; IL17RA; -.
DR GenomeRNAi; 23765; -.
DR Pharos; Q96F46; Tclin.
DR PRO; PR:Q96F46; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q96F46; protein.
DR Bgee; ENSG00000177663; Expressed in blood and 189 other tissues.
DR Genevisible; Q96F46; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030368; F:interleukin-17 receptor activity; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IEA:Ensembl.
DR GO; GO:0072537; P:fibroblast activation; IDA:BHF-UCL.
DR GO; GO:0071621; P:granulocyte chemotaxis; IEA:Ensembl.
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:0038173; P:interleukin-17A-mediated signaling pathway; IDA:UniProt.
DR GO; GO:2000340; P:positive regulation of chemokine (C-X-C motif) ligand 1 production; IMP:UniProtKB.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IDA:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:0032736; P:positive regulation of interleukin-13 production; IEA:Ensembl.
DR GO; GO:0032747; P:positive regulation of interleukin-23 production; IDA:BHF-UCL.
DR GO; GO:0032754; P:positive regulation of interleukin-5 production; IEA:Ensembl.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR GO; GO:0072538; P:T-helper 17 type immune response; IEA:Ensembl.
DR Gene3D; 3.40.50.11530; -; 1.
DR Gene3D; 2.60.40.2160; Interleukin-17 receptor A/B, fibronectin-III-like domain 1; 1.
DR Gene3D; 2.60.40.2150; Interleukin-17 receptor A/B, fibronectin-III-like domain 2; 1.
DR InterPro; IPR039465; IL-17_rcpt-like.
DR InterPro; IPR032356; IL17R_fnIII_D1.
DR InterPro; IPR038683; IL17RA/B_FnIII-like_1_sf.
DR InterPro; IPR043046; IL17RA/B_FnIII-like_2_sf.
DR InterPro; IPR013568; SEFIR_dom.
DR PANTHER; PTHR15583; INTERLEUKIN-17 RECEPTOR; 1.
DR PANTHER; PTHR15583:SF13; INTERLEUKIN-17 RECEPTOR A; 1.
DR Pfam; PF16556; IL17R_fnIII_D1; 1.
DR Pfam; PF16578; IL17R_fnIII_D2; 1.
DR Pfam; PF08357; SEFIR; 1.
DR PROSITE; PS51534; SEFIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Immunity; Inflammatory response; Innate immunity;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 33..866
FT /note="Interleukin-17 receptor A"
FT /id="PRO_0000011030"
FT TOPO_DOM 33..320
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..866
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 377..534
FT /note="SEFIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00867"
FT REGION 717..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60943"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19838198,
FT ECO:0000269|PubMed:23695682"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19838198,
FT ECO:0000269|PubMed:23695682"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19838198"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19838198,
FT ECO:0000269|PubMed:23695682"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19838198"
FT DISULFID 43..50
FT /evidence="ECO:0000269|PubMed:19838198,
FT ECO:0000269|PubMed:23695682"
FT DISULFID 57..126
FT /evidence="ECO:0000269|PubMed:19838198,
FT ECO:0000269|PubMed:23695682"
FT DISULFID 185..196
FT /evidence="ECO:0000269|PubMed:19838198,
FT ECO:0000269|PubMed:23695682"
FT DISULFID 245..276
FT /evidence="ECO:0000269|PubMed:19838198,
FT ECO:0000269|PubMed:23695682"
FT DISULFID 277..303
FT /evidence="ECO:0000269|PubMed:23695682"
FT DISULFID 290..294
FT /evidence="ECO:0000269|PubMed:19838198,
FT ECO:0000269|PubMed:23695682"
FT VAR_SEQ 315..348
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_053496"
FT VARIANT 284..866
FT /note="Missing (in IMD51; results in complete loss of
FT expression and loss-of-function)"
FT /evidence="ECO:0000269|PubMed:21350122"
FT /id="VAR_083722"
FT VARIANT 367
FT /note="A -> V (in dbSNP:rs879577)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027966"
FT VARIANT 562
FT /note="P -> Q (in dbSNP:rs12484684)"
FT /id="VAR_049176"
FT VARIANT 580
FT /note="R -> H (in dbSNP:rs17850765)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027967"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5N9B"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:5N9B"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:7UWM"
FT STRAND 74..84
FT /evidence="ECO:0007829|PDB:5N9B"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4HSA"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:5N9B"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:7UWM"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:5N9B"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:5N9B"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:5N9B"
FT STRAND 141..150
FT /evidence="ECO:0007829|PDB:5N9B"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:5N9B"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:5N9B"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:5N9B"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:5N9B"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:5N9B"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:5N9B"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:5N9B"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:5N9B"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:5N9B"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:5N9B"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:7UWN"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:5N9B"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:5N9B"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:5N9B"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:5N9B"
FT TURN 288..292
FT /evidence="ECO:0007829|PDB:5N9B"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:5N9B"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:4NUX"
FT HELIX 389..406
FT /evidence="ECO:0007829|PDB:4NUX"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:4NUX"
FT HELIX 413..416
FT /evidence="ECO:0007829|PDB:4NUX"
FT HELIX 417..422
FT /evidence="ECO:0007829|PDB:4NUX"
FT HELIX 425..438
FT /evidence="ECO:0007829|PDB:4NUX"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:4NUX"
FT HELIX 449..458
FT /evidence="ECO:0007829|PDB:4NUX"
FT HELIX 478..486
FT /evidence="ECO:0007829|PDB:4NUX"
FT HELIX 487..491
FT /evidence="ECO:0007829|PDB:4NUX"
FT HELIX 493..498
FT /evidence="ECO:0007829|PDB:4NUX"
FT STRAND 499..504
FT /evidence="ECO:0007829|PDB:4NUX"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:4NUX"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:4NUX"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:4NUX"
FT TURN 526..528
FT /evidence="ECO:0007829|PDB:4NUX"
FT HELIX 529..537
FT /evidence="ECO:0007829|PDB:4NUX"
FT HELIX 557..560
FT /evidence="ECO:0007829|PDB:4NUX"
FT HELIX 564..580
FT /evidence="ECO:0007829|PDB:4NUX"
FT HELIX 584..588
FT /evidence="ECO:0007829|PDB:4NUX"
SQ SEQUENCE 866 AA; 96122 MW; 88AF626A83F3FF70 CRC64;
MGAARSPPSA VPGPLLGLLL LLLGVLAPGG ASLRLLDHRA LVCSQPGLNC TVKNSTCLDD
SWIHPRNLTP SSPKDLQIQL HFAHTQQGDL FPVAHIEWTL QTDASILYLE GAELSVLQLN
TNERLCVRFE FLSKLRHHHR RWRFTFSHFV VDPDQEYEVT VHHLPKPIPD GDPNHQSKNF
LVPDCEHARM KVTTPCMSSG SLWDPNITVE TLEAHQLRVS FTLWNESTHY QILLTSFPHM
ENHSCFEHMH HIPAPRPEEF HQRSNVTLTL RNLKGCCRHQ VQIQPFFSSC LNDCLRHSAT
VSCPEMPDTP EPIPDYMPLW VYWFITGISI LLVGSVILLI VCMTWRLAGP GSEKYSDDTK
YTDGLPAADL IPPPLKPRKV WIIYSADHPL YVDVVLKFAQ FLLTACGTEV ALDLLEEQAI
SEAGVMTWVG RQKQEMVESN SKIIVLCSRG TRAKWQALLG RGAPVRLRCD HGKPVGDLFT
AAMNMILPDF KRPACFGTYV VCYFSEVSCD GDVPDLFGAA PRYPLMDRFE EVYFRIQDLE
MFQPGRMHRV GELSGDNYLR SPGGRQLRAA LDRFRDWQVR CPDWFECENL YSADDQDAPS
LDEEVFEEPL LPPGTGIVKR APLVREPGSQ ACLAIDPLVG EEGGAAVAKL EPHLQPRGQP
APQPLHTLVL AAEEGALVAA VEPGPLADGA AVRLALAGEG EACPLLGSPG AGRNSVLFLP
VDPEDSPLGS STPMASPDLL PEDVREHLEG LMLSLFEQSL SCQAQGGCSR PAMVLTDPHT
PYEEEQRQSV QSDQGYISRS SPQPPEGLTE MEEEEEEEQD PGKPALPLSP EDLESLRSLQ
RQLLFRQLQK NSGWDTMGSE SEGPSA
//