ID   IL6_SPAAU               Reviewed;         225 AA.
AC   B6CKP4;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Interleukin-6;
DE            Short=IL-6;
DE            Short=sbIL-6;
DE   Flags: Precursor;
GN   Name=il6;
OS   Sparus aurata (Gilthead sea bream).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Sparus.
OX   NCBI_TaxID=8175;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=18513800; DOI=10.1016/j.molimm.2008.04.012;
RA   Castellana B., Iliev D.B., Sepulcre M.P., MacKenzie S., Goetz F.W.,
RA   Mulero V., Planas J.V.;
RT   "Molecular characterization of interleukin-6 in the gilthead seabream
RT   (Sparus aurata).";
RL   Mol. Immunol. 45:3363-3370(2008).
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 white muscle, skin, spleen, anterior
CC       intestine and stomach. Not expressed in brain, gill, head kidney,
CC       posterior intestine and adipose tissue. {ECO:0000269|PubMed:18513800}.
CC   -!- INDUCTION: By LPS or Vibrio anguillarum infection.
CC       {ECO:0000269|PubMed:18513800}.
CC   -!- SIMILARITY: Belongs to the IL-6 superfamily. {ECO:0000305}.
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DR   EMBL; EU244588; ABY76175.1; -; mRNA.
DR   AlphaFoldDB; B6CKP4; -.
DR   SMR; B6CKP4; -.
DR   PRIDE; B6CKP4; -.
DR   Ensembl; ENSSAUT00010039692; ENSSAUP00010037684; ENSSAUG00010015916.
DR   GeneTree; ENSGT00390000000878; -.
DR   Proteomes; UP000472265; Unplaced.
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   SUPFAM; SSF47266; SSF47266; 1.
PE   2: Evidence at transcript level;
KW   Acute phase; Cytokine; Glycoprotein; Growth factor; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..225
FT                   /note="Interleukin-6"
FT                   /id="PRO_0000387951"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   225 AA;  25598 MW;  B2F8779C99D723DA CRC64;
     MPSRLNVFWL CAAALAALLR CAPAAPVDGA FTDNPAGDTS GEEWETERPA DPLIALLKVV
     LEVIKTHRQE FEAEFHIRYD VLAQYNIPSL PADCPSTNFS MEALLHRLLQ GLPVYTALLK
     YVEKEEPKSQ IPSRFRQNSE LLKQRITGKM RHAVQVTPLT SSQEQQLLRD LDSSDTFHRK
     MTAHSILYQL RSFLVDCKNA INKKEKLRES RANRAMTPVT LYYQS