ID   IL10_LAMGL              Reviewed;         178 AA.
AC   Q865X4;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 73.
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   Lama glama (Llama).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Lama.
OX   NCBI_TaxID=9844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Raadan O., Lee S., Yoshida R., Chang K., Ohashi K., Sugimoto C., Onuma M.;
RT   "Cloning and sequence analysis of cytokine cDNAs of llama and camel.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
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; AB107649; BAC75386.1; -; mRNA.
DR   AlphaFoldDB; Q865X4; -.
DR   SMR; Q865X4; -.
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_0000015361"
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;  20471 MW;  CB25D68CAEF88333 CRC64;
     MPRSALLCCL ILLAGVAASR DQGTQSENSC AHFPASLPHM LRELRAAFGR VKTFFQMKDQ
     LDNMLLTRSL LEDFKGYLGC QALSEMIQFY LEEVMPQAEN HGPDIKEHVN SLGEKLKTLR
     LRLRRCHRFL PCENKSKAVE QVRGVFSKLQ EKGVYKAMSE FDIFINYIEA YMTMKMKN