ID   IL12B_PAPAN             Reviewed;         328 AA.
AC   Q865Y3;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Interleukin-12 subunit beta;
DE            Short=IL-12B;
DE   AltName: Full=Cytotoxic lymphocyte maturation factor 40 kDa subunit;
DE            Short=CLMF p40;
DE   AltName: Full=IL-12 subunit p40;
DE   Flags: Precursor;
GN   Name=IL12B;
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Villinger F.J.;
RT   "Nonhuman primate cytokines.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cytokine that can act as a growth factor for activated T and
CC       NK cells, enhance the lytic activity of NK/lymphokine-activated killer
CC       cells, and stimulate the production of IFN-gamma by resting PBMC.
CC       {ECO:0000250}.
CC   -!- FUNCTION: Associates with IL23A to form the IL-23 interleukin, a
CC       heterodimeric cytokine which functions in innate and adaptive immunity.
CC       IL-23 may constitute with IL-17 an acute response to infection in
CC       peripheral tissues. IL-23 binds to a heterodimeric receptor complex
CC       composed of IL12RB1 and IL23R, activates the Jak-Stat signaling
CC       cascade, stimulates memory rather than naive T-cells and promotes
CC       production of pro-inflammatory cytokines. IL-23 induces autoimmune
CC       inflammation and thus may be responsible for autoimmune inflammatory
CC       diseases and may be important for tumorigenesis (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with IL12A; disulfide-linked. The heterodimer is
CC       known as interleukin IL-12. Heterodimer with IL23A; disulfide-linked.
CC       The heterodimer is known as interleukin IL-23. Also secreted as a
CC       monomer (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the IL-12B family. {ECO:0000305}.
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DR   EMBL; AY234218; AAO85331.1; -; mRNA.
DR   RefSeq; NP_001106105.1; NM_001112635.1.
DR   AlphaFoldDB; Q865Y3; -.
DR   SMR; Q865Y3; -.
DR   STRING; 9555.ENSPANP00000003288; -.
DR   GeneID; 100126717; -.
DR   KEGG; panu:100126717; -.
DR   CTD; 3593; -.
DR   eggNOG; ENOG502RZMA; Eukaryota.
DR   OrthoDB; 1179405at2759; -.
DR   Proteomes; UP000028761; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR003530; Hematopoietin_rcpt_L_F3_CS.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR015528; IL-12_beta.
DR   InterPro; IPR019482; IL-12_beta_cen-dom.
DR   PANTHER; PTHR23036:SF156; PTHR23036:SF156; 1.
DR   Pfam; PF10420; IL12p40_C; 1.
DR   PIRSF; PIRSF038007; IL_12_beta; 1.
DR   PRINTS; PR01928; INTRLEUKN12B.
DR   SMART; SM00408; IGc2; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS01354; HEMATOPO_REC_L_F3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Cytokine; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..328
FT                   /note="Interleukin-12 subunit beta"
FT                   /id="PRO_0000010934"
FT   DOMAIN          29..106
FT                   /note="Ig-like C2-type"
FT   DOMAIN          237..328
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..90
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        199
FT                   /note="Interchain (with C-96 in IL12A and C-73 in IL23A)"
FT                   /evidence="ECO:0000250|UniProtKB:P29460,
FT                   ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   328 AA;  37245 MW;  6B86C8AAD44BFF79 CRC64;
     MCHQQLVISW FSLVFLASPL MAIWELKKDV YVVELDWYPD APGEMVVLTC DTPEEDGITW
     TLDQSGEVLG SGKTLTIQVK EFGDAGQYTC HKGGEALSHS LLLLHKKEDG IWSTDVLKDQ
     KEPKNKTFLR CEAKNYSGRF TCWWLTTIST DLTFSVKSSR GSSNPQGVTC GAVTLSAERV
     RGDNKEYEYS VECQEDSACP AAEERLPIEV MVDAIHKLKY ENYTSSFFIR DIIKPDPPKN
     LQLKPLKNSR QAEVSWEYPD TWSTPHSYFS LTFCIQVQGK SKREKKDRIF TDKTSATVIC
     RKNASFSVQA QDRYYSSSWS EWASVPCS