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   24-JAN-2024, entry version 187.
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   EMDB; EMD-26835; -.
DR   EMDB; EMD-26836; -.
DR   EMDB; EMD-26837; -.
DR   SMR; Q96F46; -.
DR   BioGRID; 117265; 217.
DR   IntAct; Q96F46; 68.
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; 9606-ENSP00000320936; -.
DR   PeptideAtlas; Q96F46; -.
DR   ProteomicsDB; 76496; -. [Q96F46-1]
DR   Pumba; Q96F46; -.
DR   ABCD; Q96F46; 25 sequenced antibodies.
DR   Antibodypedia; 22632; 843 antibodies from 44 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 191 other cell types or 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
//