IL10_PAPHA
ID IL10_PAPHA Reviewed; 178 AA.
AC Q5Q0V6;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Interleukin-10;
DE Short=IL-10;
DE AltName: Full=Cytokine synthesis inhibitory factor;
DE Short=CSIF;
DE Flags: Precursor;
GN Name=IL10;
OS Papio hamadryas (Hamadryas baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9557;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=15652450; DOI=10.1016/j.cyto.2004.10.011;
RA Orange S., Rasko J.E.J., Thompson J.F., Vaughan J., Olive E., Pedler M.,
RA Horvath J.S., Hennessy A.;
RT "Interleukin-10 regulates arterial pressure in early primate pregnancy.";
RL Cytokine 29:176-185(2005).
CC -!- FUNCTION: Major immune regulatory cytokine that acts on many cells of
CC the immune system where it has profound anti-inflammatory functions,
CC limiting excessive tissue disruption caused by inflammation.
CC Mechanistically, IL10 binds to its heterotetrameric receptor comprising
CC IL10RA and IL10RB leading to JAK1 and STAT2-mediated phosphorylation of
CC STAT3. In turn, STAT3 translocates to the nucleus where it drives
CC expression of anti-inflammatory mediators. Targets antigen-presenting
CC cells (APCs) such as macrophages and monocytes and inhibits their
CC release of pro-inflammatory cytokines including granulocyte-macrophage
CC colony-stimulating factor /GM-CSF, granulocyte colony-stimulating
CC factor/G-CSF, IL-1 alpha, IL-1 beta, IL-6, IL-8 and TNF-alpha.
CC Interferes also with antigen presentation by reducing the expression of
CC MHC-class II and co-stimulatory molecules, thereby inhibiting their
CC ability to induce T cell activation (By similarity). In addition,
CC controls the inflammatory response of macrophages by reprogramming
CC essential metabolic pathways including mTOR signaling (By similarity).
CC {ECO:0000250|UniProtKB:P18893, ECO:0000250|UniProtKB:P22301}.
CC -!- SUBUNIT: Homodimer. Interacts with IL10RA and IL10RB.
CC {ECO:0000250|UniProtKB:P22301}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P22301}.
CC -!- SIMILARITY: Belongs to the IL-10 family. {ECO:0000305}.
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DR EMBL; AY796417; AAV85009.1; -; mRNA.
DR AlphaFoldDB; Q5Q0V6; -.
DR SMR; Q5Q0V6; -.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; ISS:UniProtKB.
DR GO; GO:0002719; P:negative regulation of cytokine production involved in immune response; ISS:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; ISS:UniProtKB.
DR GO; GO:0002904; P:positive regulation of B cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0051384; P:response to glucocorticoid; ISS:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; ISS:UniProtKB.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR000098; IL-10.
DR InterPro; IPR020443; IL-10/19/20/22/24/26_fam.
DR InterPro; IPR020423; IL-10_CS.
DR Pfam; PF00726; IL10; 1.
DR PRINTS; PR01294; INTRLEUKIN10.
DR SMART; SM00188; IL10; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00520; INTERLEUKIN_10; 1.
PE 2: Evidence at transcript level;
KW Cytokine; Disulfide bond; Glycoprotein; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..178
FT /note="Interleukin-10"
FT /id="PRO_0000015369"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..126
FT /evidence="ECO:0000250"
FT DISULFID 80..132
FT /evidence="ECO:0000250"
SQ SEQUENCE 178 AA; 20543 MW; D05E9E4AAE845D49 CRC64;
MHSSALLCCL VVLTGVRASP GQGTQSENSC TRFPGNLPHM LRDLRDAFSR VKTFFQMKDQ
LDNILLKESL LEDFKGYLGC QALSEMIQFY LEEVMPQAEN HDPDIKEHVN SLGENLKTLR
LRLRRCHRFL PCENKSKAVE QVKNAFSKLQ EKGVYKAMSE FDIFINYIEA YMTMKIQN