ID   IL17_PIG                Reviewed;         153 AA.
AC   Q60I29;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Interleukin-17A;
DE            Short=IL-17;
DE            Short=IL-17A;
DE   Flags: Precursor;
GN   Name=IL17A; Synonyms=IL17;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Thymus;
RX   PubMed=15450131; DOI=10.1089/jir.2004.24.553;
RA   Katoh S., Kitazawa H., Shimosato T., Tohno M., Kawai Y., Saito T.;
RT   "Cloning and characterization of swine interleukin-17, preferentially
RT   expressed in the intestines.";
RL   J. Interferon Cytokine Res. 24:553-559(2004).
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   -!- TISSUE SPECIFICITY: Highly expressed in adult heart, skin, and
CC       intestinal tissues, such as jejunum and ileum.
CC       {ECO:0000269|PubMed:15450131}.
CC   -!- SIMILARITY: Belongs to the IL-17 family. {ECO:0000305}.
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DR   EMBL; AB102693; BAD52431.1; -; mRNA.
DR   RefSeq; NP_001005729.1; NM_001005729.1.
DR   AlphaFoldDB; Q60I29; -.
DR   SMR; Q60I29; -.
DR   STRING; 9823.ENSSSCP00000001905; -.
DR   PaxDb; Q60I29; -.
DR   GeneID; 449530; -.
DR   KEGG; ssc:449530; -.
DR   CTD; 3605; -.
DR   eggNOG; ENOG502S5A0; Eukaryota.
DR   InParanoid; Q60I29; -.
DR   OrthoDB; 1469254at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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_0000227501"
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;  17312 MW;  1C7D32185E31E67E CRC64;
     MTPVRSSSLS LLLLLSLVAL VKAGIMIPQS PGCPKTEDKN FPQHVRVNLN ILNRSTPARR
     PSDYSKRFTS PWTLQRNEDP ERYSSVIWEA KCSHSGCINA EGKEDHHMNS VPIQQEILVL
     RREPRHCPNS FRLEKVMVTV GCTCVTPIVR HIS