IL17_BOVIN
ID IL17_BOVIN Reviewed; 153 AA.
AC Q687Y7; Q95L56;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Interleukin-17A;
DE Short=IL-17;
DE Short=IL-17A;
DE Flags: Precursor;
GN Name=IL17A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Riollet C., Rainard P.;
RT "Neutrophil recruitment in the bovine mammary gland.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-153.
RA Lee I.-K., Mwangi S.M., Olsen S., Kehrli M. Jr.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Effector cytokine of innate and adaptive immune system
CC involved in antimicrobial host defense and maintenance of tissue
CC integrity. Signals via IL17RA-IL17RC heterodimeric receptor complex,
CC triggering homotypic interaction of IL17RA and IL17RC chains with
CC TRAF3IP2 adapter. This leads to downstream TRAF6-mediated activation of
CC NF-kappa-B and MAPkinase pathways ultimately resulting in
CC transcriptional activation of cytokines, chemokines, antimicrobial
CC peptides and matrix metalloproteinases, with potential strong immune
CC inflammation. Plays an important role in connecting T cell-mediated
CC adaptive immunity and acute inflammatory response to destroy
CC extracellular bacteria and fungi. As a signature effector cytokine of
CC T-helper 17 cells (Th17), primarily induces neutrophil activation and
CC recruitment at infection and inflammatory sites. In airway epithelium,
CC mediates neutrophil chemotaxis via induction of CXCL1 and CXCL5
CC chemokines. In secondary lymphoid organs, contributes to germinal
CC center formation by regulating the chemotactic response of B cells to
CC CXCL12 and CXCL13, enhancing retention of B cells within the germinal
CC centers, B cell somatic hypermutation rate and selection toward plasma
CC cells. Effector cytokine of a subset of gamma-delta T cells that
CC functions as part of an inflammatory circuit downstream IL1B, TLR2 and
CC IL23A-IL12B to promote neutrophil recruitment for efficient bacterial
CC clearance. Effector cytokine of innate immune cells including invariant
CC natural killer cell (iNKT) and group 3 innate lymphoid cells that
CC mediate initial neutrophilic inflammation. Involved in the maintenance
CC of the integrity of epithelial barriers during homeostasis and pathogen
CC infection. Upon acute injury, has a direct role in epithelial barrier
CC formation by regulating OCLN localization and tight junction
CC biogenesis. As part of the mucosal immune response induced by commensal
CC bacteria, enhances host's ability to resist pathogenic bacterial and
CC fungal infections by promoting neutrophil recruitment and antimicrobial
CC peptides release. In synergy with IL17F, mediates 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. Involved in antiviral host defense through various
CC mechanisms. Enhances immunity against West Nile virus by promoting T
CC cell cytotoxicity. May play a beneficial role in influenza A virus
CC (H5N1) infection by enhancing B cell recruitment and immune response in
CC the lung. Contributes to influenza A virus (H1N1) clearance by driving
CC the differentiation of B-1a B cells, providing for production of virus-
CC specific IgM antibodies at first line of host defense.
CC {ECO:0000250|UniProtKB:Q62386}.
CC -!- SUBUNIT: Homodimer. Forms complexes with IL17RA and IL17RC receptors
CC with 2:1 binding stoichiometry: two receptor chains for one interleukin
CC molecule. IL17A homodimer preferentially drives the formation of
CC IL17RA-IL17RC heterodimeric receptor complex. IL17A homodimer adopts an
CC asymmetrical ternary structure with one IL17RA molecule, allowing for
CC high affinity interactions of one IL17A monomer with one IL17RA
CC molecule (via D1 and D2 domains), while disfavoring binding of a second
CC IL17RA molecule on the other IL17A monomer. Heterodimer with IL17F.
CC IL17A-IL17F forms complexes with IL17RA-IL17RC, but with lower affinity
CC when compared to IL17A homodimer. IL17RA and IL17RC chains cannot
CC distinguish between IL17A and IL17F molecules, potentially enabling the
CC formation of topologically distinct complexes.
CC {ECO:0000250|UniProtKB:Q16552}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q62386}.
CC -!- SIMILARITY: Belongs to the IL-17 family. {ECO:0000305}.
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DR EMBL; AF412040; AAQ03220.1; -; mRNA.
DR EMBL; AF416586; AAL08013.1; -; mRNA.
DR RefSeq; NP_001008412.1; NM_001008412.2.
DR AlphaFoldDB; Q687Y7; -.
DR SMR; Q687Y7; -.
DR STRING; 9913.ENSBTAP00000002786; -.
DR PaxDb; Q687Y7; -.
DR Ensembl; ENSBTAT00000002786; ENSBTAP00000002786; ENSBTAG00000002150.
DR GeneID; 282863; -.
DR KEGG; bta:282863; -.
DR CTD; 3605; -.
DR VEuPathDB; HostDB:ENSBTAG00000002150; -.
DR VGNC; VGNC:30117; IL17A.
DR eggNOG; ENOG502S5A0; Eukaryota.
DR GeneTree; ENSGT00940000161882; -.
DR HOGENOM; CLU_118641_0_0_1; -.
DR InParanoid; Q687Y7; -.
DR OMA; HHMNSVP; -.
DR OrthoDB; 1469254at2759; -.
DR TreeFam; TF314701; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000002150; Expressed in pharyngeal tonsil and 16 other tissues.
DR ExpressionAtlas; Q687Y7; baseline.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0050832; P:defense response to fungus; IEA:Ensembl.
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:0072537; P:fibroblast activation; IEA:Ensembl.
DR GO; GO:0097530; P:granulocyte migration; 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; IEA:Ensembl.
DR GO; GO:0060729; P:intestinal epithelial structure maintenance; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0002225; P:positive regulation of antimicrobial peptide production; IEA:Ensembl.
DR GO; GO:1903348; P:positive regulation of bicellular tight junction assembly; IEA:Ensembl.
DR GO; GO:2000340; P:positive regulation of chemokine (C-X-C motif) ligand 1 production; IEA:Ensembl.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IEA:Ensembl.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IEA:Ensembl.
DR GO; GO:0032739; P:positive regulation of interleukin-16 production; IEA:Ensembl.
DR GO; GO:0032747; P:positive regulation of interleukin-23 production; IEA:Ensembl.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR Gene3D; 2.10.90.10; -; 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; SSF57501; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Cytokine; Disulfide bond; Glycoprotein; Immunity;
KW Inflammatory response; Innate immunity; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..153
FT /note="Interleukin-17A"
FT /id="PRO_0000227500"
FT REGION 56..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 92..142
FT /evidence="ECO:0000250"
FT DISULFID 97..144
FT /evidence="ECO:0000250"
SQ SEQUENCE 153 AA; 17242 MW; 658D88BE75EE381B CRC64;
MASMRTSSMS LLLLLSLVAL VKAGVIIPQS PGCPPTEDKN FPQHVRVNLN IVNRSTNSRR
PTDYHKRSTS PWTLHRNEDP ERYPSVIWEA KCSHSGCINA EGKVDHHMNS VTIQQEILVL
RRESQHCPHS FRLEKMLVAV GCTCVTPIVR HLA
