ID I17RC_HUMAN Reviewed; 791 AA. AC Q8NAC3; A8BWC1; A8BWC9; A8BWD5; E9PHG1; E9PHJ6; Q6UVY3; Q6UWD4; Q8NFS1; AC Q9BR97; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 2. DT 24-JAN-2024, entry version 164. DE RecName: Full=Interleukin-17 receptor C; DE Short=IL-17 receptor C; DE Short=IL-17RC; DE AltName: Full=Interleukin-17 receptor homolog; DE Short=IL17Rhom; DE AltName: Full=Interleukin-17 receptor-like protein; DE Short=IL-17RL; DE AltName: Full=ZcytoR14; DE Flags: Precursor; GN Name=IL17RC; ORFNames=UNQ6118/PRO20040/PRO38901; 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] (ISOFORMS 5; 6 AND 7), FUNCTION, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING. 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8). RA Presnell S.R., Burkhead S.K., Pownder S.L.; RL Patent number JP2003504058, 04-FEB-2003. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT LEU-182. RA Gilbert J.M., Gorman D.M.; RT "Identification of novel IL-17 related receptors."; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-182. RC TISSUE=Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). 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 [8] RP PROTEIN SEQUENCE OF 21-35. 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 [9] RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RX PubMed=11706037; DOI=10.1074/jbc.m109372200; RA Haudenschild D., Moseley T., Rose L., Reddi A.H.; RT "Soluble and transmembrane isoforms of novel interleukin-17 receptor-like RT protein by RNA splicing and expression in prostate cancer."; RL J. Biol. Chem. 277:4309-4316(2002). RN [10] RP INDUCTION BY HGF AND VEGF. RX PubMed=14504135; DOI=10.1038/sj.bjp.0705494; RA Gerritsen M.E., Tomlinson J.E., Zlot C., Ziman M., Hwang S.; RT "Using gene expression profiling to identify the molecular basis of the RT synergistic actions of hepatocyte growth factor and vascular endothelial RT growth factor in human endothelial cells."; RL Br. J. Pharmacol. 140:595-610(2003). RN [11] 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 [12] 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 [13] RP 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 [14] RP INTERACTION WITH IL17A AND IL17F. 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 [15] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 279-538 IN COMPLEX WITH IL17F, RP DISULFIDE BOND, INTERACTION WITH IL17RA; IL17F AND IL17A, AND FUNCTION. 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 [16] RP INVOLVEMENT IN CANDF9. RX PubMed=25918342; DOI=10.1084/jem.20141065; RA Ling Y., Cypowyj S., Aytekin C., Galicchio M., Camcioglu Y., Nepesov S., RA Ikinciogullari A., Dogu F., Belkadi A., Levy R., Migaud M., Boisson B., RA Bolze A., Itan Y., Goudin N., Cottineau J., Picard C., Abel L., RA Bustamante J., Casanova J.L., Puel A.; RT "Inherited IL-17RC deficiency in patients with chronic mucocutaneous RT candidiasis."; RL J. Exp. Med. 212:619-631(2015). 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 (By similarity). Receptor CC for IL17A and IL17F, major effector cytokines of innate and adaptive CC immune system involved in antimicrobial host defense and maintenance of CC tissue integrity. Receptor for IL17A and IL17F homodimers as part of a CC heterodimeric complex with IL17RA (PubMed:16785495). Receptor for the CC heterodimer formed by IL17A and IL17B as part of a heterodimeric CC complex with IL17RA (PubMed:18684971). Has also been shown to be the CC cognate receptor for IL17F and to bind IL17A with high affinity without CC the need for IL17RA (PubMed:17911633). Upon binding of IL17F homodimer CC triggers downstream activation of TRAF6 and NF-kappa-B signaling CC pathway (PubMed:16785495, PubMed:32187518). Induces transcriptional CC activation of IL33, a potent cytokine that stimulates group 2 innate CC lymphoid cells and adaptive T-helper 2 cells involved in pulmonary CC allergic response to fungi (By similarity). Promotes sympathetic CC innervation of peripheral organs by coordinating the communication CC between gamma-delta T cells and parenchymal cells. Stimulates CC sympathetic innervation of thermogenic adipose tissue by driving TGFB1 CC expression (By similarity). Binding of IL17A-IL17F to IL17RA-IL17RC CC heterodimeric receptor complex triggers homotypic interaction of IL17RA CC and IL17RC chains with TRAF3IP2 adapter through SEFIR domains. This CC leads to downstream 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:18684971, PubMed:17911633). Primarily induces neutrophil CC activation and recruitment at infection and inflammatory sites (By CC similarity). Stimulates the production of antimicrobial beta-defensins CC DEFB1, DEFB103A, and DEFB104A by mucosal epithelial cells, limiting the CC entry of microbes through the epithelial barriers (By similarity). CC {ECO:0000250|UniProtKB:Q8K4C2, ECO:0000269|PubMed:16785495, CC ECO:0000269|PubMed:17911633, ECO:0000269|PubMed:18684971, CC ECO:0000269|PubMed:32187518}. CC -!- FUNCTION: [Isoform 5]: Receptor for both IL17A and IL17F. CC {ECO:0000269|PubMed:16785495}. CC -!- FUNCTION: [Isoform 6]: Does not bind IL17A or IL17F. CC {ECO:0000269|PubMed:16785495}. CC -!- FUNCTION: [Isoform 7]: Does not bind IL17A or IL17F. CC {ECO:0000269|PubMed:16785495}. CC -!- FUNCTION: [Isoform 8]: Receptor for both IL17A and IL17F. CC {ECO:0000269|PubMed:16785495}. CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:32187518). Heterodimer CC with IL17RA (PubMed:16785495, PubMed:18684971). Heterodimerization with CC IL17RA is independent of the cytoplasmic tail (By similarity). CC Associates with non-glycosylated IL17RA constitutively (By similarity). CC Binding of IL17A and IL17F induces association with glycosylated IL17RA CC (By similarity). Forms complexes with 2:1 binding stoichiometry: two CC receptor chains for one interleukin molecule (PubMed:32187518, CC PubMed:28827714). IL17A homodimer preferentially drives the formation CC of IL17RA-IL17RC heterodimeric receptor complex, whereas IL17F CC homodimer forms predominantly complexes with IL17RC homodimer CC (PubMed:32187518). IL17A-IL17F forms complexes with IL17RA-IL17RC, but CC with lower affinity when compared to IL17A homodimer (PubMed:32187518). CC IL17RC chain cannot distinguish between IL17A and IL17F molecules, CC potentially enabling the formation of topologically distinct complexes CC (PubMed:28827714). Interacts (through SEFIR domain and extended CC downstream region) with TRAF3IP2/ACT1 (phosphorylated) CC (PubMed:24120361). {ECO:0000250|UniProtKB:Q8K4C2, CC ECO:0000269|PubMed:16785495, ECO:0000269|PubMed:18684971, CC ECO:0000269|PubMed:24120361, ECO:0000269|PubMed:28827714, CC ECO:0000269|PubMed:32187518}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17911633}; CC Single-pass type I membrane protein {ECO:0000255}. Note=Soluble CC isoforms may be produced. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=Q8NAC3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8NAC3-2; Sequence=VSP_014138; CC Name=3; CC IsoId=Q8NAC3-3; Sequence=VSP_014138, VSP_014139; CC Name=4; CC IsoId=Q8NAC3-4; Sequence=VSP_014138, VSP_014139, VSP_014140, CC VSP_014141; CC Name=5; Synonyms=IL17RC {ECO:0000303|PubMed:17911633}; CC IsoId=Q8NAC3-5; Sequence=VSP_014138, VSP_047292; CC Name=6; Synonyms=IL17RC-delta7,12 {ECO:0000303|PubMed:17911633}; CC IsoId=Q8NAC3-6; Sequence=VSP_014138, VSP_014139, VSP_047291; CC Name=7; Synonyms=IL17RC-delta12 {ECO:0000303|PubMed:17911633}; CC IsoId=Q8NAC3-7; Sequence=VSP_014138, VSP_047291, VSP_047292; CC Name=8; Synonyms=IL17RC-delta7 {ECO:0000303|PubMed:17911633}; CC IsoId=Q8NAC3-8; Sequence=VSP_014138, VSP_014139, VSP_047292; CC -!- TISSUE SPECIFICITY: Expressed in prostate, skeletal muscle, kidney and CC placenta (at protein level) (PubMed:11706037). Expressed in brain, CC cartilage, colon, heart, intestine, kidney, liver, lung, muscle, CC placenta, and prostate (PubMed:11706037). Also detected in thyroid, CC trachea and adrenal gland (PubMed:17911633). Low expression in thymus CC and leukocytes (PubMed:11706037). {ECO:0000269|PubMed:11706037, CC ECO:0000269|PubMed:17911633}. CC -!- INDUCTION: By HGF and VEGF. {ECO:0000269|PubMed:14504135}. CC -!- DISEASE: Candidiasis, familial, 9 (CANDF9) [MIM:616445]: A disorder CC characterized by altered immune responses and impaired clearance of CC fungal infections, selective against Candida. It is characterized by CC persistent and/or recurrent infections of the skin, nails and mucous CC membranes caused by organisms of the genus Candida, mainly Candida CC albicans. {ECO:0000269|PubMed:25918342}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EF676032; ABV44615.1; -; mRNA. DR EMBL; EF676033; ABV44616.1; -; mRNA. DR EMBL; EF676034; ABV44617.1; -; mRNA. DR EMBL; BD292072; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AF458065; AAM77569.1; -; mRNA. DR EMBL; AY358840; AAQ89199.1; -; mRNA. DR EMBL; AY359098; AAQ89456.1; -; mRNA. DR EMBL; AK092907; BAC04001.1; -; mRNA. DR EMBL; AC018809; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC006411; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS2590.1; -. [Q8NAC3-1] DR CCDS; CCDS2591.2; -. [Q8NAC3-3] DR CCDS; CCDS46746.1; -. [Q8NAC3-2] DR CCDS; CCDS56240.1; -. [Q8NAC3-5] DR CCDS; CCDS56241.1; -. [Q8NAC3-6] DR CCDS; CCDS74898.1; -. [Q8NAC3-7] DR CCDS; CCDS93202.1; -. [Q8NAC3-8] DR RefSeq; NP_001190192.1; NM_001203263.1. [Q8NAC3-5] DR RefSeq; NP_001190193.1; NM_001203264.1. [Q8NAC3-7] DR RefSeq; NP_001190194.1; NM_001203265.1. [Q8NAC3-6] DR RefSeq; NP_116121.2; NM_032732.5. [Q8NAC3-3] DR RefSeq; NP_703190.1; NM_153460.3. [Q8NAC3-2] DR RefSeq; NP_703191.1; NM_153461.3. [Q8NAC3-1] DR RefSeq; XP_016862835.1; XM_017007346.1. DR PDB; 6HG4; X-ray; 3.32 A; B=95-538. DR PDB; 6HG9; X-ray; 3.62 A; B=95-538. DR PDB; 6HGA; X-ray; 2.60 A; B=279-538. DR PDB; 7UWN; EM; 3.01 A; G=95-536. DR PDB; 7ZAN; X-ray; 5.06 A; D=95-538. DR PDBsum; 6HG4; -. DR PDBsum; 6HG9; -. DR PDBsum; 6HGA; -. DR PDBsum; 7UWN; -. DR PDBsum; 7ZAN; -. DR AlphaFoldDB; Q8NAC3; -. DR EMDB; EMD-26837; -. DR SMR; Q8NAC3; -. DR BioGRID; 124278; 53. DR IntAct; Q8NAC3; 45. DR STRING; 9606.ENSP00000295981; -. DR DrugCentral; Q8NAC3; -. DR GlyCosmos; Q8NAC3; 9 sites, No reported glycans. DR GlyGen; Q8NAC3; 9 sites. DR iPTMnet; Q8NAC3; -. DR PhosphoSitePlus; Q8NAC3; -. DR BioMuta; IL17RC; -. DR DMDM; 229462881; -. DR jPOST; Q8NAC3; -. DR MassIVE; Q8NAC3; -. DR PaxDb; 9606-ENSP00000295981; -. DR PeptideAtlas; Q8NAC3; -. DR ProteomicsDB; 20526; -. DR ProteomicsDB; 20554; -. DR ProteomicsDB; 72669; -. [Q8NAC3-1] DR ProteomicsDB; 72670; -. [Q8NAC3-2] DR ProteomicsDB; 72671; -. [Q8NAC3-3] DR ProteomicsDB; 72672; -. [Q8NAC3-4] DR Antibodypedia; 10412; 376 antibodies from 34 providers. DR DNASU; 84818; -. DR Ensembl; ENST00000295981.7; ENSP00000295981.3; ENSG00000163702.21. [Q8NAC3-1] DR Ensembl; ENST00000383812.9; ENSP00000373323.4; ENSG00000163702.21. [Q8NAC3-3] DR Ensembl; ENST00000403601.8; ENSP00000384969.3; ENSG00000163702.21. [Q8NAC3-2] DR Ensembl; ENST00000413608.2; ENSP00000396064.1; ENSG00000163702.21. [Q8NAC3-5] DR Ensembl; ENST00000416074.6; ENSP00000395315.3; ENSG00000163702.21. [Q8NAC3-7] DR Ensembl; ENST00000455057.5; ENSP00000407894.1; ENSG00000163702.21. [Q8NAC3-6] DR Ensembl; ENST00000483582.5; ENSP00000512844.1; ENSG00000163702.21. [Q8NAC3-4] DR Ensembl; ENST00000696816.1; ENSP00000512897.1; ENSG00000163702.21. [Q8NAC3-8] DR GeneID; 84818; -. DR KEGG; hsa:84818; -. DR MANE-Select; ENST00000403601.8; ENSP00000384969.3; NM_153460.4; NP_703190.2. [Q8NAC3-2] DR UCSC; uc003btz.4; human. [Q8NAC3-1] DR AGR; HGNC:18358; -. DR CTD; 84818; -. DR DisGeNET; 84818; -. DR GeneCards; IL17RC; -. DR HGNC; HGNC:18358; IL17RC. DR HPA; ENSG00000163702; Low tissue specificity. DR MalaCards; IL17RC; -. DR MIM; 610925; gene. DR MIM; 616445; phenotype. DR neXtProt; NX_Q8NAC3; -. DR OpenTargets; ENSG00000163702; -. DR Orphanet; 1334; Chronic mucocutaneous candidiasis. DR PharmGKB; PA134986616; -. DR VEuPathDB; HostDB:ENSG00000163702; -. DR eggNOG; ENOG502RYE0; Eukaryota. DR GeneTree; ENSGT00730000111286; -. DR HOGENOM; CLU_026893_1_0_1; -. DR InParanoid; Q8NAC3; -. DR OMA; GHPNICV; -. DR OrthoDB; 5309006at2759; -. DR PhylomeDB; Q8NAC3; -. DR TreeFam; TF335852; -. DR PathwayCommons; Q8NAC3; -. 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; Q8NAC3; -. DR SIGNOR; Q8NAC3; -. DR BioGRID-ORCS; 84818; 14 hits in 1156 CRISPR screens. DR ChiTaRS; IL17RC; human. DR GeneWiki; IL17RC; -. DR GenomeRNAi; 84818; -. DR Pharos; Q8NAC3; Tclin. DR PRO; PR:Q8NAC3; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q8NAC3; Protein. DR Bgee; ENSG00000163702; Expressed in adenohypophysis and 168 other cell types or tissues. DR ExpressionAtlas; Q8NAC3; baseline and differential. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0015026; F:coreceptor activity; IDA:UniProt. DR GO; GO:0030368; F:interleukin-17 receptor activity; IDA:MGI. DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl. DR GO; GO:0050832; P:defense response to fungus; IEA:Ensembl. DR GO; GO:0071621; P:granulocyte chemotaxis; IEA:Ensembl. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0038173; P:interleukin-17A-mediated signaling pathway; IDA:UniProt. DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IEA:Ensembl. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl. DR Gene3D; 3.40.50.11530; -; 1. DR InterPro; IPR039465; IL-17_rcpt-like. DR InterPro; IPR027841; IL-17_rcpt_C/E_N. DR InterPro; IPR013568; SEFIR_dom. DR PANTHER; PTHR15583; INTERLEUKIN-17 RECEPTOR; 1. DR PANTHER; PTHR15583:SF12; INTERLEUKIN-17 RECEPTOR C; 1. DR Pfam; PF15037; IL17_R_N; 1. DR Pfam; PF08357; SEFIR; 1. DR PROSITE; PS51534; SEFIR; 1. DR Genevisible; Q8NAC3; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Inflammatory response; Membrane; Receptor; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..20 FT /evidence="ECO:0000269|PubMed:15340161" FT CHAIN 21..791 FT /note="Interleukin-17 receptor C" FT /id="PRO_0000011034" FT TOPO_DOM 21..538 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 539..559 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 560..791 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 583..735 FT /note="SEFIR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00867" FT REGION 762..791 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 189 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 257 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 284 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 297 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 324 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 334 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 420 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 443 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 477 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 265..277 FT /evidence="ECO:0000269|PubMed:32187518, FT ECO:0007744|PDB:6HG4" FT DISULFID 341..391 FT /evidence="ECO:0000269|PubMed:32187518, FT ECO:0007744|PDB:6HG4" FT DISULFID 343..359 FT /evidence="ECO:0000269|PubMed:32187518, FT ECO:0007744|PDB:6HG4" FT DISULFID 400..409 FT /evidence="ECO:0000269|PubMed:32187518, FT ECO:0007744|PDB:6HG4" FT DISULFID 439..453 FT /evidence="ECO:0000269|PubMed:32187518, FT ECO:0007744|PDB:6HG4" FT DISULFID 481..488 FT /evidence="ECO:0000269|PubMed:32187518, FT ECO:0007744|PDB:6HG4" FT DISULFID 515..529 FT /evidence="ECO:0000269|PubMed:32187518, FT ECO:0007744|PDB:6HG4" FT VAR_SEQ 36..106 FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform FT 5, isoform 6, isoform 7 and isoform 8)" FT /evidence="ECO:0000269|PubMed:17911633, FT ECO:0000303|PubMed:12975309, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17911633" FT /id="VSP_014138" FT VAR_SEQ 264..278 FT /note="Missing (in isoform 3, isoform 4, isoform 6 and FT isoform 8)" FT /evidence="ECO:0000269|PubMed:17911633, FT ECO:0000303|PubMed:12975309, ECO:0000303|PubMed:15489334" FT /id="VSP_014139" FT VAR_SEQ 425..441 FT /note="Missing (in isoform 6 and isoform 7)" FT /evidence="ECO:0000269|PubMed:17911633, ECO:0000305" FT /id="VSP_047291" FT VAR_SEQ 566..578 FT /note="Missing (in isoform 5, isoform 7 and isoform 8)" FT /evidence="ECO:0000269|PubMed:17911633, ECO:0000305" FT /id="VSP_047292" FT VAR_SEQ 579..624 FT /note="AAARGRAALLLYSADDSGFERLVGALASALCQLPLRVAVDLWSRRE -> GE FT WEQALGGGPPPGSQACASSPLPSPSVFSGSGRQGPRGSAPLLSR (in isoform FT 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014140" FT VAR_SEQ 625..791 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014141" FT VARIANT 182 FT /note="S -> L (in dbSNP:rs708567)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:17911633" FT /id="VAR_022680" FT CONFLICT 241 FT /note="E -> G (in Ref. 4; AAQ89199)" FT CONFLICT 378 FT /note="Q -> R (in Ref. 1; ABV44615/ABV44616/ABV44617, 2; FT BD292072, 3; AAM77569, 4; AAQ89199/AAQ89456 and 5; FT BAC04001)" FT /evidence="ECO:0000305" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:7UWN" FT STRAND 106..112 FT /evidence="ECO:0007829|PDB:7UWN" FT STRAND 115..117 FT /evidence="ECO:0007829|PDB:6HG4" FT STRAND 131..144 FT /evidence="ECO:0007829|PDB:7UWN" FT STRAND 152..164 FT /evidence="ECO:0007829|PDB:7UWN" FT STRAND 194..198 FT /evidence="ECO:0007829|PDB:7UWN" FT STRAND 209..214 FT /evidence="ECO:0007829|PDB:7UWN" FT HELIX 217..219 FT /evidence="ECO:0007829|PDB:6HG4" FT STRAND 222..235 FT /evidence="ECO:0007829|PDB:7UWN" FT STRAND 241..250 FT /evidence="ECO:0007829|PDB:7UWN" FT STRAND 256..261 FT /evidence="ECO:0007829|PDB:7UWN" FT HELIX 270..273 FT /evidence="ECO:0007829|PDB:7UWN" FT HELIX 275..278 FT /evidence="ECO:0007829|PDB:7UWN" FT STRAND 283..286 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 289..296 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 303..312 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 313..315 FT /evidence="ECO:0007829|PDB:6HG4" FT STRAND 321..333 FT /evidence="ECO:0007829|PDB:6HGA" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 342..350 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 356..358 FT /evidence="ECO:0007829|PDB:6HGA" FT TURN 360..363 FT /evidence="ECO:0007829|PDB:6HGA" FT HELIX 365..373 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 376..381 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 384..388 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 395..401 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 409..411 FT /evidence="ECO:0007829|PDB:7UWN" FT TURN 413..415 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 419..421 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 425..427 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 438..444 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 447..452 FT /evidence="ECO:0007829|PDB:6HGA" FT TURN 454..458 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 465..473 FT /evidence="ECO:0007829|PDB:6HGA" FT TURN 474..476 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 477..479 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 481..483 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 485..492 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 495..497 FT /evidence="ECO:0007829|PDB:6HGA" FT HELIX 498..501 FT /evidence="ECO:0007829|PDB:6HGA" FT HELIX 503..511 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 515..521 FT /evidence="ECO:0007829|PDB:6HGA" FT STRAND 524..530 FT /evidence="ECO:0007829|PDB:6HGA" FT HELIX 532..534 FT /evidence="ECO:0007829|PDB:6HGA" SQ SEQUENCE 791 AA; 86240 MW; E9A4032C17ECD4AF CRC64; MPVPWFLLSL ALGRSPVVLS LERLVGPQDA THCSPVSLEP WGDEERLRVQ FLAQQSLSLA PVTAATARTA LSGLSGADGR REERGRGKSW VCLSLGGSGN TEPQKKGLSC RLWDSDILCL PGDIVPAPGP VLAPTHLQTE LVLRCQKETD CDLCLRVAVH LAVHGHWEEP EDEEKFGGAA DSGVEEPRNA SLQAQVVLSF QAYPTARCVL LEVQVPAALV QFGQSVGSVV YDCFEAALGS EVRIWSYTQP RYEKELNHTQ QLPDCRGLEV WNSIPSCWAL PWLNVSADGD NVHLVLNVSE EQHFGLSLYW NQVQGPPKPR WHKNLTGPQI ITLNHTDLVP CLCIQVWPLE PDSVRTNICP FREDPRAHQN LWQAARLQLL TLQSWLLDAP CSLPAEAALC WRAPGGDPCQ PLVPPLSWEN VTVDKVLEFP LLKGHPNLCV QVNSSEKLQL QECLWADSLG PLKDDVLLLE TRGPQDNRSL CALEPSGCTS LPSKASTRAA RLGEYLLQDL QSGQCLQLWD DDLGALWACP MDKYIHKRWA LVWLACLLFA AALSLILLLK KDHAKGWLRL LKQDVRSGAA ARGRAALLLY SADDSGFERL VGALASALCQ LPLRVAVDLW SRRELSAQGP VAWFHAQRRQ TLQEGGVVVL LFSPGAVALC SEWLQDGVSG PGAHGPHDAF RASLSCVLPD FLQGRAPGSY VGACFDRLLH PDAVPALFRT VPVFTLPSQL PDFLGALQQP RAPRSGRLQE RAEQVSRALQ PALDSYFHPP GTPAPGRGVG PGAGPGAGDG T //