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   29-MAY-2024, entry version 165.
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:17911633, PubMed:18684971). 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:28827714,
CC       PubMed:32187518). 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.
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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.
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
//