IL12B_SHEEP
ID IL12B_SHEEP Reviewed; 327 AA.
AC P68220; O02815; O18989; Q9TT18;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 86.
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RC TISSUE=Peripheral blood;
RX PubMed=11023671; DOI=10.1006/cyto.2000.0755;
RA Swinburne S.J., Russ G.R., Krishnan R.;
RT "Ovine interleukin 12 has biological activity on ovine and human activated
RT peripheral blood mononuclear cells.";
RL Cytokine 12:1546-1552(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Merino; TISSUE=Peripheral blood;
RX PubMed=10888112; DOI=10.1089/10799900050044750;
RA De Rose R., Scheerlinck J.-P.Y., Casey G., Wood P.R., Tennent J.M.,
RA Chaplin P.J.;
RT "Ovine interleukin-12: analysis of biologic function and species
RT comparison.";
RL J. Interferon Cytokine Res. 20:557-564(2000).
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; AF004024; AAB61368.2; -; mRNA.
DR EMBL; AF209435; AAF20151.1; -; mRNA.
DR RefSeq; NP_001009438.1; NM_001009438.1.
DR AlphaFoldDB; P68220; -.
DR SMR; P68220; -.
DR STRING; 9940.ENSOARP00000014084; -.
DR GeneID; 443472; -.
DR KEGG; oas:443472; -.
DR CTD; 3593; -.
DR eggNOG; ENOG502RZMA; Eukaryota.
DR OrthoDB; 1179405at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0043514; C:interleukin-12 complex; IDA:AgBase.
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:0042164; F:interleukin-12 alpha subunit binding; IPI:AgBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:AgBase.
DR GO; GO:0032609; P:interferon-gamma production; IDA:AgBase.
DR GO; GO:0032946; P:positive regulation of mononuclear cell proliferation; IMP:AgBase.
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 1: Evidence at protein level;
KW Cytokine; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..327
FT /note="Interleukin-12 subunit beta"
FT /id="PRO_0000010936"
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 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-98 in IL12A and C-76 in IL23A)"
FT /evidence="ECO:0000250|UniProtKB:P29460,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 290
FT /note="T -> A (in Ref. 2; AAF20151)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 36937 MW; DDCD983A10143A96 CRC64;
MHPQQLVVSW FSLVLLASPI VAIWELEKNV YVVELDWYPN APGETVVLTC DTPEEDGITW
TSDQSSEVLG SGKTLTIQVK EFGDAGQYTC HKGGEVLSRS LLLLHKKEDG IWSTDILKDQ
KEPKAKSFLK CEAKDYSGHF TCSWLTAIST NLKFSVKSSR GSSDPRGVTC GAASLSAEKV
SMDHREYNKY TVECQEGSAC PAAEESLPIE VVMEAVHKLK YENYTSSFFI RDIIKPDPPK
NLQLRPLKNS RQVEVSWEYP DTWSTPHSYF SLTFCVQVQG KNKREKKLFT DQTSAKVTCH
KDANIRVQAR DRYYSSFWSE WASVSCS
