ID IL12B_CANLF Reviewed; 329 AA.
AC Q28268;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 136.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9617567; DOI=10.1006/cyto.1997.0284;
RA Buettner M., Belke-Louis G.F., Rziha H.J., McInnes C., Kaaden O.R.;
RT "Detection, cDNA cloning and sequencing of canine interleukin 12.";
RL Cytokine 10:241-248(1998).
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. Interacts with NBR1; this interaction promotes IL-12 secretion
CC (By similarity). {ECO:0000250|UniProtKB:P29460,
CC ECO:0000250|UniProtKB:P43432}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the IL-12B family. {ECO:0000305}.
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DR EMBL; U49100; AAA92059.1; -; mRNA.
DR RefSeq; NP_001003292.1; NM_001003292.1.
DR AlphaFoldDB; Q28268; -.
DR SMR; Q28268; -.
DR STRING; 9615.ENSCAFP00000025465; -.
DR GlyCosmos; Q28268; 2 sites, No reported glycans.
DR PaxDb; 9612-ENSCAFP00000025465; -.
DR GeneID; 403976; -.
DR KEGG; cfa:403976; -.
DR CTD; 3593; -.
DR eggNOG; ENOG502RZMA; Eukaryota.
DR InParanoid; Q28268; -.
DR OrthoDB; 4006511at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR Proteomes; UP000694429; Unplaced.
DR Proteomes; UP000694542; Unplaced.
DR Proteomes; UP000805418; 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 GO; GO:0030101; P:natural killer cell activation; ISS:UniProtKB.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISS:UniProtKB.
DR GO; GO:0042093; P:T-helper cell differentiation; ISS:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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; PTHR48397:SF1; INTERLEUKIN-12 SUBUNIT BETA; 1.
DR PANTHER; PTHR48397; INTERLEUKIN-12 SUBUNIT BETA-RELATED; 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; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
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..329
FT /note="Interleukin-12 subunit beta"
FT /id="PRO_0000010924"
FT DOMAIN 29..106
FT /note="Ig-like C2-type"
FT DOMAIN 238..329
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
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 DISULFID 50..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 200
FT /note="Interchain (with C-99 in IL12A and C-76 in IL23A)"
FT /evidence="ECO:0000250|UniProtKB:P29460,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 329 AA; 37410 MW; 79F83ED02B5DA93C CRC64;
MHPQQLVISW FSLVLLASSL MTIWELEKDV YVVELDWHPD APGEMVVLTC HTPEEDDITW
TSAQSSEVLG SGKTLTIQVK EFGDAGQYTC HKGGKVLSRS LLLIHKKEDG IWSTDILKEQ
KESKNKIFLK CEAKNYSGRF TCWWLTAIST DLKFSVKSSR GFSDPQGVTC GAVTLSAERV
RVDNRDYKKY TVECQEGSAC PSAEESLPIE VVVDAIHKLK YENYTSSFFI RDIIKPDPPT
NLQLKPLKNS RHVEVSWEYP DTWSTPHSYF SLTFCVQAQG KNNREKKDRL CVDKTSAKVV
CHKDAKIRVQ ARDRYYSSSW SDWASVSCS
//
