IL12B_HORSE
ID IL12B_HORSE Reviewed; 329 AA.
AC Q9XSQ5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 122.
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 Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10541814; DOI=10.1007/s002510050693;
RA Nicolson L., Penha-Goncalves M.N., Keanie J.L., Logan N.A., Argyle D.J.,
RA Onions D.E.;
RT "Cloning and sequencing of horse interleukin-12 and interleukin-18 cDNAs.";
RL Immunogenetics 50:94-97(1999).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y11129; CAA72011.1; -; mRNA.
DR RefSeq; NP_001075985.1; NM_001082516.1.
DR AlphaFoldDB; Q9XSQ5; -.
DR SMR; Q9XSQ5; -.
DR STRING; 9796.ENSECAP00000010803; -.
DR PaxDb; Q9XSQ5; -.
DR GeneID; 100034222; -.
DR KEGG; ecb:100034222; -.
DR CTD; 3593; -.
DR InParanoid; Q9XSQ5; -.
DR OrthoDB; 1179405at2759; -.
DR Proteomes; UP000002281; 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 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;
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_0000010929"
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 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 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; 37442 MW; 7104BB0DFF8FA73C CRC64;
MCHQWLVLSW FSLVLLASPL MAIWELEKDV YVVELDWYPD APGEMVVLTC NTPEEEGITW
TSAQSNEVLG SGKTLTIQVK EFGDAGWYTC HKGGEVLSHS HLLLHKKEDG IWSTDILKDQ
KESKNKTFLK CEAKNYSGRF TCWWLTAIST DLKFSVKSSR GSSDPRGVTC GAATLSAERV
SVDDREYKKY TVECQEGSAC PAAEESLPIE IVVDAVHKLK YENYTSGFFI RDIIKPDPPK
NLQLKPLKNS RQVEVSWEYP ETWSTPHSYF SLTFSIQVQG KNKKERKDRL FMDETSATVT
CHKDGQIRVQ ARDRYYSSSW SEWASVSCS