ID   IL12B_MARMO             Reviewed;         327 AA.
AC   Q61729;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 98.
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   Marmota monax (Woodchuck).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Marmota.
OX   NCBI_TaxID=9995;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Peripheral blood;
RA   Laxton C.D., Foster G.R., Shanmuganathan S., Mills J.S., Ackrill A.M.;
RL   Submitted (APR-1996) 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; X97019; CAA65747.1; -; mRNA.
DR   AlphaFoldDB; Q61729; -.
DR   SMR; Q61729; -.
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_0000010932"
FT   DOMAIN          23..106
FT                   /note="Ig-like C2-type"
FT   DOMAIN          237..327
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
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-98 in IL12A)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   327 AA;  37172 MW;  9A15445915AB90E6 CRC64;
     MCLQQLVISW VSLVWLASPL LAIWELEKNV YVVELDWHPD TPGEKVVLTC DTPEEDGITW
     TSEQSSEVLG SGKTLTILVK EFEDAGHYTC RRGGEVLSQM LLLLHKNEDG IWSTDILKKK
     EPENKNLVTC EAKNYSGRFT CWWLTAISTD VNFSVKSHRG SSDPQGVTCG EATLSAERVK
     IEQREYKKYS VQCQEDNACP TAEETLPITV VVDAVHKLKY ENYISSFFIR DIIKPDPPKN
     LKMKPSKTPQ QVEVTWEYPD SWSTPHSYFS LTFSVQVQGK KKKRSNTLHV DKTSVTVTCQ
     KGAKVSVQAR DRYYNSSWSE WATMSCP