ID   IL12B_LAMGL             Reviewed;         330 AA.
AC   Q865W9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 74.
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   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].
RX   PubMed=15570698; DOI=10.1016/j.vetimm.2004.06.001;
RA   Odbileg R., Lee S.-I., Yoshida R., Chang K.-S., Ohashi K., Sugimoto C.,
RA   Onuma M.;
RT   "Cloning and sequence analysis of llama cytokines related to cell-mediated
RT   immunity.";
RL   Vet. Immunol. Immunopathol. 102:93-102(2004).
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.
CC   -!- SIMILARITY: Belongs to the IL-12B family. {ECO:0000305}.
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DR   EMBL; AB107654; BAC75391.1; -; mRNA.
DR   AlphaFoldDB; Q865W9; -.
DR   SMR; Q865W9; -.
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; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..330
FT                   /note="Interleukin-12 subunit beta"
FT                   /id="PRO_0000045046"
FT   DOMAIN          23..106
FT                   /note="Ig-like C2-type"
FT   DOMAIN          239..330
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..90
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        201
FT                   /note="Interchain (with C-99 in IL12A and C-74 in IL23A)"
FT                   /evidence="ECO:0000250|UniProtKB:P29460,
FT                   ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   330 AA;  37295 MW;  CE5E105C6D2F43CE CRC64;
     MHPQQLVVSW FSLVLLASPI MAIWELEKNV YVVELDWYPD APGETVVLTC DTPEEDGITW
     TSDHSSEVLG SGKTLTIQVK EFGDAGQYTC HKGGEVLSHS LLLLHKKEDG VWSTDILKKD
     QKEPKSKTFL KCEAKNYSGH FTCWWLTAVS TDLKFSVKSS RGSSDPRGVT CGAATLSAER
     VGVEHRDSWK YTVECQEGSS CPAAEESLPI ELVVEAVHKL KYENYSSSFF IRDIIRPDPP
     KNLQLKPLKN SRHVEVSWEY PDTWSTPHSY FSLTFCVQVQ GKHKREKKDK LFVDQTSAKV
     TCPKDASIRV QARDRYYSSS WSEWASVSCS