ID   IL6_PAROL               Reviewed;         230 AA.
AC   A0S0B0;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Interleukin-6;
DE            Short=IL-6;
DE   Flags: Precursor;
GN   Name=il6;
OS   Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Paralichthyidae;
OC   Paralichthys.
OX   NCBI_TaxID=8255;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP   INDUCTION.
RX   PubMed=17097890; DOI=10.1016/j.fsi.2006.10.001;
RA   Nam B.-H., Byon J.-Y., Kim Y.-O., Park E.-M., Cho Y.-C., Cheong J.;
RT   "Molecular cloning and characterisation of the flounder (Paralichthys
RT   olivaceus) interleukin-6 gene.";
RL   Fish Shellfish Immunol. 23:231-236(2007).
CC   -!- FUNCTION: Cytokine with a wide variety of biological functions in
CC       immunity, tissue regeneration, and metabolism. Binds to IL6R, then the
CC       complex associates to the signaling subunit IL6ST/gp130 to trigger the
CC       intracellular IL6-signaling pathway. The interaction with the membrane-
CC       bound IL6R and IL6ST stimulates 'classic signaling', whereas the
CC       binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'.
CC       Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R
CC       complexes on transmitter cells activate IL6ST receptors on neighboring
CC       receiver cells. {ECO:0000250|UniProtKB:P05231}.
CC   -!- SUBUNIT: Component of a hexamer of two molecules each of IL6, IL6R and
CC       IL6ST; first binds to IL6R to associate with the signaling subunit
CC       IL6ST. {ECO:0000250|UniProtKB:P05231}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P05231}.
CC   -!- TISSUE SPECIFICITY: Expressed in kidney and spleen. Low expression in
CC       liver and gills. {ECO:0000269|PubMed:17097890}.
CC   -!- INDUCTION: By LPS. {ECO:0000269|PubMed:17097890}.
CC   -!- SIMILARITY: Belongs to the IL-6 superfamily. {ECO:0000305}.
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DR   EMBL; DQ267937; ABB90401.1; -; mRNA.
DR   EMBL; DQ884914; ABJ53333.1; -; Genomic_DNA.
DR   RefSeq; XP_019946148.1; XM_020090589.1.
DR   AlphaFoldDB; A0S0B0; -.
DR   SMR; A0S0B0; -.
DR   GeneID; 109631714; -.
DR   KEGG; pov:109631714; -.
DR   OrthoDB; 1144279at2759; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005138; F:interleukin-6 receptor binding; IEA:InterPro.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR   GO; GO:0072574; P:hepatocyte proliferation; ISS:UniProtKB.
DR   GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0097421; P:liver regeneration; ISS:UniProtKB.
DR   GO; GO:1904894; P:positive regulation of receptor signaling pathway via STAT; ISS:UniProtKB.
DR   GO; GO:0070092; P:regulation of glucagon secretion; ISS:UniProtKB.
DR   GO; GO:0050796; P:regulation of insulin secretion; ISS:UniProtKB.
DR   GO; GO:0014823; P:response to activity; ISS:UniProtKB.
DR   GO; GO:0072540; P:T-helper 17 cell lineage commitment; IEA:InterPro.
DR   GO; GO:0010573; P:vascular endothelial growth factor production; ISS:UniProtKB.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR003574; IL-6.
DR   InterPro; IPR030474; IL-6/GCSF/MGF.
DR   PANTHER; PTHR10511; PTHR10511; 1.
DR   PANTHER; PTHR10511:SF3; PTHR10511:SF3; 1.
DR   Pfam; PF00489; IL6; 1.
DR   PRINTS; PR00433; IL6GCSFMGF.
DR   SMART; SM00126; IL6; 1.
DR   SUPFAM; SSF47266; SSF47266; 1.
PE   2: Evidence at transcript level;
KW   Acute phase; Cytokine; Disulfide bond; Glycoprotein; Growth factor;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..230
FT                   /note="Interleukin-6"
FT                   /id="PRO_0000387950"
FT   REGION          206..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..220
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        96..106
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   230 AA;  26043 MW;  9436DFE12471350A CRC64;
     MASKHNADLS SAAMLAALLL CALGAPVEYE PTDSPAGDFS GEEQEVTPDL LSASPVWDLI
     IGVTAHHQKE FEDEFQQEVK YRFLNHYKLS SLPADCPSAN FSKEACLQRL AEGLHTYMVL
     FKHVEKEYPS SSILLHARYH SGALIGLIKE KMRNPGQVTV PTSRQEQQLL QDMDNPSTFH
     RKMTAHNILR QLHNFLRNGK VAIRKREMPK QKRRKDDGII PPIHPSYQMT