ID   IL12B_SIGHI             Reviewed;         327 AA.
AC   Q91ZK7;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 76.
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   Sigmodon hispidus (Hispid cotton rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Sigmodontinae; Sigmodon.
OX   NCBI_TaxID=42415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=14980081; DOI=10.1089/107999004772719873;
RA   Blanco J.C., Pletneva L.M., Boukhvalova M., Richardson J.Y., Harris K.A.,
RA   Prince G.A.;
RT   "The cotton rat: an underutilized animal model for human infectious
RT   diseases can now be exploited using specific reagents to cytokines,
RT   chemokines, and interferons.";
RL   J. Interferon Cytokine Res. 24:21-28(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; AF421395; AAL16936.1; -; mRNA.
DR   AlphaFoldDB; Q91ZK7; -.
DR   SMR; Q91ZK7; -.
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..327
FT                   /note="Interleukin-12 subunit beta"
FT                   /id="PRO_0000045048"
FT   DOMAIN          23..106
FT                   /note="Ig-like C2-type"
FT   DOMAIN          238..327
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        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..90
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        200
FT                   /note="Interchain (with C-92 in IL12A)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   327 AA;  37119 MW;  F096702CC950FD56 CRC64;
     MCHQKLTISW FAMVLLVSPL MAIWELEKDV YVVEVDWSPG APGERVVLTC DTSEEDDIIW
     TSDQSSEVVG SGKTLIVQVK EFSDAGQYTC HKGGETLSHS RLLLHKKEDG IWSTDILKDQ
     KDPKNKTFLK CEAANYSGRF TCWWLTAVST DLKFSLKSSS SSSDSRSVTC GAASLSTEKV
     TVDQRDYNKY SVACQEDITC PTAEETLPIE LVMEAQHKYK YENYSTGFFI RDIIKPDPPK
     NLQLKPLKSS QVEVSWEYPD SWSTPHSYFS LKFFVQVYRK KEKKGESLLV DKPSAKIRCS
     KGGEVRVRAQ DHYYNSSWSE WASVSCN