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.
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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 Genevisible; Q8NAC3; HS.
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
//