ID IL17F_HUMAN Reviewed; 163 AA.
AC Q96PD4; Q6NSI0; Q7Z6P4; Q96PI8; Q9NUE6;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 24-JAN-2024, entry version 176.
DE RecName: Full=Interleukin-17F;
DE Short=IL-17F;
DE AltName: Full=Cytokine ML-1;
DE Flags: Precursor;
GN Name=IL17F;
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], AND FUNCTION.
RX PubMed=11591732; DOI=10.4049/jimmunol.167.8.4137;
RA Starnes T., Robertson M.J., Sledge G., Kelich S., Nakshatri H.,
RA Broxmeyer H.E., Hromas R.;
RT "IL-17F, a novel cytokine selectively expressed in activated T cells and
RT monocytes, regulates angiogenesis and endothelial cell cytokine
RT production.";
RL J. Immunol. 167:4137-4140(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-161.
RC TISSUE=Blood;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-163, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11591768; DOI=10.4049/jimmunol.167.8.4430;
RA Kawaguchi M., Onuchic L.F., Li X.-D., Essayan D.M., Schroeder J.,
RA Xiao H.-Q., Liu M.C., Krishnaswamy G., Germino G., Huang S.-K.;
RT "Identification of a novel cytokine, ML-1, and its expression in subjects
RT with asthma.";
RL J. Immunol. 167:4430-4435(2001).
RN [5]
RP PROTEIN SEQUENCE OF 31-45.
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 SUBUNIT.
RX PubMed=17355969; DOI=10.1074/jbc.m700499200;
RA Wright J.F., Guo Y., Quazi A., Luxenberg D.P., Bennett F., Ross J.F.,
RA Qiu Y., Whitters M.J., Tomkinson K.N., Dunussi-Joannopoulos K.,
RA Carreno B.M., Collins M., Wolfman N.M.;
RT "Identification of an interleukin 17F/17A heterodimer in activated human
RT CD4+ T cells.";
RL J. Biol. Chem. 282:13447-13455(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH IL17RC.
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 [8]
RP FUNCTION, AND INTERACTION WITH IL17RA AND IL17RC.
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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS), AND FUNCTION.
RX PubMed=11574464; DOI=10.1093/emboj/20.19.5332;
RA Hymowitz S.G., Filvaroff E.H., Yin J.P., Lee J., Cai L., Risser P.,
RA Maruoka M., Mao W., Foster J., Kelley R.F., Pan G., Gurney A.L.,
RA de Vos A.M., Starovasnik M.A.;
RT "IL-17s adopt a cystine knot fold: structure and activity of a novel
RT cytokine, IL-17F, and implications for receptor binding.";
RL EMBO J. 20:5332-5341(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 31-163 IN COMPLEX WITH IL17R,
RP GLYCOSYLATION AT ASN-83, SUBUNIT, AND 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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 31-163 IN COMPLEX WITH IL17A;
RP INTERACTION WITH IL17RA AND IL17RC, FUNCTION, AND MUTAGENESIS OF ARG-77.
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 [12]
RP X-RAY CRYSTALLOGRAPHY (3.32 ANGSTROMS) OF 31-163 IN COMPLEX WITH IL17RC,
RP DISULFIDE BOND, INTERACTION WITH IL17A; IL17RC AND IL17RA, 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 [13]
RP VARIANT CANDF6 LEU-95, 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: Effector cytokine of innate and adaptive immune system
CC involved in antimicrobial host defense and maintenance of tissue
CC integrity (PubMed:21350122). IL17A-IL17F signals via IL17RA-IL17RC
CC heterodimeric receptor complex, triggering homotypic interaction of
CC IL17RA and IL17RC chains with TRAF3IP2 adapter through SEFIR domains.
CC This 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:21350122, PubMed:11591732, PubMed:11591768,
CC PubMed:17911633, PubMed:11574464, PubMed:28827714). IL17A-IL17F is
CC primarily involved in host defense against extracellular bacteria and
CC fungi by inducing neutrophilic inflammation (By similarity). As
CC signature effector cytokine of T-helper 17 cells (Th17), primarily
CC induces neutrophil activation and recruitment at infection and
CC inflammatory sites (By similarity). 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). IL17F homodimer can signal via IL17RC
CC homodimeric receptor complex, triggering downstream activation of TRAF6
CC and NF-kappa-B signaling pathway (PubMed:32187518). Via IL17RC induces
CC transcriptional activation of IL33, a potent cytokine that stimulates
CC group 2 innate lymphoid cells and adaptive T-helper 2 cells involved in
CC pulmonary allergic response to fungi. Likely via IL17RC, promotes
CC sympathetic innervation of peripheral organs by coordinating the
CC communication between gamma-delta T cells and parenchymal cells.
CC Stimulates sympathetic innervation of thermogenic adipose tissue by
CC driving TGFB1 expression (By similarity). Regulates the composition of
CC intestinal microbiota and immune tolerance by inducing antimicrobial
CC proteins that specifically control the growth of commensal Firmicutes
CC and Bacteroidetes (By similarity). {ECO:0000250|UniProtKB:Q7TNI7,
CC ECO:0000269|PubMed:11574464, ECO:0000269|PubMed:11591732,
CC ECO:0000269|PubMed:11591768, ECO:0000269|PubMed:17911633,
CC ECO:0000269|PubMed:18684971, ECO:0000269|PubMed:21350122,
CC ECO:0000269|PubMed:28827714, ECO:0000269|PubMed:32187518}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:19838198,
CC PubMed:32187518). Heterodimer with IL17A (IL17A-IL17F)
CC (PubMed:17355969). Forms complexes with IL17RA and IL17RC receptors
CC with 2:1 binding stoichiometry: two receptor chains for one interleukin
CC molecule. IL17F homodimer forms predominantly complexes with IL17RC
CC homodimer, whereas IL17A-IL17F favors complexes with IL17RA-IL17RC
CC (PubMed:32187518, PubMed:28827714, PubMed:17911633, PubMed:18684971).
CC IL17RA and IL17RC chains cannot distinguish between IL17A and IL17F
CC molecules, potentially enabling the formation of topologically distinct
CC complexes (PubMed:28827714). {ECO:0000269|PubMed:17355969,
CC ECO:0000269|PubMed:17911633, ECO:0000269|PubMed:18684971,
CC ECO:0000269|PubMed:19838198, ECO:0000269|PubMed:28827714,
CC ECO:0000269|PubMed:32187518}.
CC -!- INTERACTION:
CC Q96PD4; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-10292310, EBI-10172181;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q7TNI7}.
CC -!- TISSUE SPECIFICITY: Expressed in T-helper 1 and T-helper 2 cells,
CC basophils and mast cells. {ECO:0000269|PubMed:11591768}.
CC -!- DISEASE: Candidiasis, familial, 6 (CANDF6) [MIM:613956]: 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 -!- SIMILARITY: Belongs to the IL-17 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL14427.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-17 entry;
CC URL="https://en.wikipedia.org/wiki/Interleukin_17";
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DR EMBL; AF384857; AAK83350.1; -; mRNA.
DR EMBL; AL034343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC070124; AAH70124.1; -; mRNA.
DR EMBL; AF332389; AAL14427.1; ALT_SEQ; mRNA.
DR CCDS; CCDS4938.1; -.
DR RefSeq; NP_443104.1; NM_052872.3.
DR RefSeq; XP_011512578.1; XM_011514276.1.
DR PDB; 1JPY; X-ray; 2.85 A; A/B/X/Y=31-163.
DR PDB; 3JVF; X-ray; 3.30 A; A/B=31-163.
DR PDB; 5N92; X-ray; 2.30 A; F=31-163.
DR PDB; 5NAN; X-ray; 3.30 A; E/F=31-163.
DR PDB; 6HG4; X-ray; 3.32 A; A=31-163.
DR PDB; 6HG9; X-ray; 3.62 A; A=31-163.
DR PDB; 6HGO; X-ray; 2.10 A; A/B/C/D=31-163.
DR PDB; 6PPG; X-ray; 2.75 A; F/G=31-163.
DR PDBsum; 1JPY; -.
DR PDBsum; 3JVF; -.
DR PDBsum; 5N92; -.
DR PDBsum; 5NAN; -.
DR PDBsum; 6HG4; -.
DR PDBsum; 6HG9; -.
DR PDBsum; 6HGO; -.
DR PDBsum; 6PPG; -.
DR AlphaFoldDB; Q96PD4; -.
DR SMR; Q96PD4; -.
DR BioGRID; 125201; 32.
DR IntAct; Q96PD4; 1.
DR STRING; 9606.ENSP00000337432; -.
DR BindingDB; Q96PD4; -.
DR ChEMBL; CHEMBL4630880; -.
DR DrugBank; DB12917; Bimekizumab.
DR GlyCosmos; Q96PD4; 1 site, No reported glycans.
DR GlyGen; Q96PD4; 1 site.
DR iPTMnet; Q96PD4; -.
DR PhosphoSitePlus; Q96PD4; -.
DR BioMuta; IL17F; -.
DR DMDM; 239938888; -.
DR MassIVE; Q96PD4; -.
DR PaxDb; 9606-ENSP00000337432; -.
DR PeptideAtlas; Q96PD4; -.
DR ProteomicsDB; 77668; -.
DR ABCD; Q96PD4; 54 sequenced antibodies.
DR Antibodypedia; 30885; 962 antibodies from 41 providers.
DR DNASU; 112744; -.
DR Ensembl; ENST00000336123.5; ENSP00000337432.4; ENSG00000112116.11.
DR Ensembl; ENST00000699946.1; ENSP00000514702.1; ENSG00000112116.11.
DR GeneID; 112744; -.
DR KEGG; hsa:112744; -.
DR MANE-Select; ENST00000336123.5; ENSP00000337432.4; NM_052872.4; NP_443104.1.
DR UCSC; uc003pam.2; human.
DR AGR; HGNC:16404; -.
DR CTD; 112744; -.
DR DisGeNET; 112744; -.
DR GeneCards; IL17F; -.
DR HGNC; HGNC:16404; IL17F.
DR HPA; ENSG00000112116; Tissue enhanced (lymphoid).
DR MalaCards; IL17F; -.
DR MIM; 606496; gene.
DR MIM; 613956; phenotype.
DR neXtProt; NX_Q96PD4; -.
DR OpenTargets; ENSG00000112116; -.
DR Orphanet; 1334; Chronic mucocutaneous candidiasis.
DR PharmGKB; PA29800; -.
DR VEuPathDB; HostDB:ENSG00000112116; -.
DR eggNOG; ENOG502S5A0; Eukaryota.
DR GeneTree; ENSGT00940000156618; -.
DR HOGENOM; CLU_118641_0_0_1; -.
DR InParanoid; Q96PD4; -.
DR OMA; SPWDYNV; -.
DR OrthoDB; 5400717at2759; -.
DR PhylomeDB; Q96PD4; -.
DR TreeFam; TF314701; -.
DR PathwayCommons; Q96PD4; -.
DR Reactome; R-HSA-448424; Interleukin-17 signaling.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; Q96PD4; -.
DR BioGRID-ORCS; 112744; 13 hits in 1134 CRISPR screens.
DR EvolutionaryTrace; Q96PD4; -.
DR GenomeRNAi; 112744; -.
DR Pharos; Q96PD4; Tclin.
DR PRO; PR:Q96PD4; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q96PD4; Protein.
DR Bgee; ENSG00000112116; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 36 other cell types or tissues.
DR Genevisible; Q96PD4; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IDA:UniProtKB.
DR GO; GO:0019955; F:cytokine binding; IDA:UniProtKB.
DR GO; GO:0005126; F:cytokine receptor binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0051216; P:cartilage development; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:Ensembl.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; 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:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0002225; P:positive regulation of antimicrobial peptide production; IEA:Ensembl.
DR GO; GO:2000340; P:positive regulation of chemokine (C-X-C motif) ligand 1 production; IDA:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0032761; P:positive regulation of lymphotoxin A production; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032645; P:regulation of granulocyte macrophage colony-stimulating factor production; IDA:UniProtKB.
DR GO; GO:0032663; P:regulation of interleukin-2 production; IDA:UniProtKB.
DR GO; GO:0032675; P:regulation of interleukin-6 production; IDA:UniProtKB.
DR GO; GO:0032677; P:regulation of interleukin-8 production; IDA:UniProtKB.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR020440; IL-17_chr.
DR InterPro; IPR010345; IL-17_fam.
DR Pfam; PF06083; IL17; 1.
DR PRINTS; PR01932; INTRLEUKIN17.
DR SUPFAM; SSF57501; Cystine-knot cytokines; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cytokine; Direct protein sequencing;
KW Disease variant; Disulfide bond; Glycoprotein; Immunity;
KW Inflammatory response; Innate immunity; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 31..163
FT /note="Interleukin-17F"
FT /id="PRO_0000015432"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19838198"
FT DISULFID 47
FT /note="Interchain (with C-137)"
FT /evidence="ECO:0000269|PubMed:19838198"
FT DISULFID 102..152
FT /evidence="ECO:0000269|PubMed:19838198,
FT ECO:0000269|PubMed:32187518"
FT DISULFID 107..154
FT /evidence="ECO:0000269|PubMed:19838198,
FT ECO:0000269|PubMed:32187518"
FT DISULFID 137
FT /note="Interchain (with C-47)"
FT /evidence="ECO:0000269|PubMed:19838198"
FT VARIANT 95
FT /note="S -> L (in CANDF6; dbSNP:rs748486078)"
FT /evidence="ECO:0000269|PubMed:21350122"
FT /id="VAR_065813"
FT VARIANT 126
FT /note="E -> G (in dbSNP:rs2397084)"
FT /id="VAR_058287"
FT VARIANT 155
FT /note="V -> I (in dbSNP:rs11465553)"
FT /id="VAR_058288"
FT VARIANT 161
FT /note="H -> R (in dbSNP:rs763780)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_058289"
FT MUTAGEN 77
FT /note="R->A: Significantly decreases the affinity for
FT IL17RA and IL17RC by nearly 5-fold and 200-fold,
FT respectively."
FT /evidence="ECO:0000269|PubMed:28827714"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1JPY"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:6HGO"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:6HGO"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:5N92"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:6HGO"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6HGO"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:6HGO"
FT STRAND 92..103
FT /evidence="ECO:0007829|PDB:6HGO"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:6HGO"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:5N92"
FT STRAND 118..134
FT /evidence="ECO:0007829|PDB:6HGO"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:6HGO"
FT STRAND 140..155
FT /evidence="ECO:0007829|PDB:6HGO"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:3JVF"
SQ SEQUENCE 163 AA; 18045 MW; E5287737C9E7BD46 CRC64;
MTVKTLHGPA MVKYLLLSIL GLAFLSEAAA RKIPKVGHTF FQKPESCPPV PGGSMKLDIG
IINENQRVSM SRNIESRSTS PWNYTVTWDP NRYPSEVVQA QCRNLGCINA QGKEDISMNS
VPIQQETLVV RRKHQGCSVS FQLEKVLVTV GCTCVTPVIH HVQ
//
