IL12B_MACMU
ID IL12B_MACMU Reviewed; 328 AA.
AC P48095;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
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 Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=7561102;
RA Villinger F.J., Brar S.S., Mayne A.E., Chikkala N., Ansari A.A.;
RT "Comparative sequence analysis of cytokine genes from human and nonhuman
RT primates.";
RL J. Immunol. 155:3946-3954(1995).
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; U19841; AAB60397.1; -; mRNA.
DR RefSeq; NP_001038190.1; NM_001044725.1.
DR RefSeq; XP_014996758.1; XM_015141272.1.
DR AlphaFoldDB; P48095; -.
DR SMR; P48095; -.
DR STRING; 9544.ENSMMUP00000028574; -.
DR GeneID; 694747; -.
DR KEGG; mcc:694747; -.
DR CTD; 3593; -.
DR eggNOG; ENOG502RZMA; Eukaryota.
DR HOGENOM; CLU_071206_1_0_1; -.
DR InParanoid; P48095; -.
DR OMA; VAIWELK; -.
DR OrthoDB; 1179405at2759; -.
DR TreeFam; TF334829; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0043514; C:interleukin-12 complex; IBA:GO_Central.
DR GO; GO:0070743; C:interleukin-23 complex; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0042164; F:interleukin-12 alpha subunit binding; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
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..328
FT /note="Interleukin-12 subunit beta"
FT /id="PRO_0000010931"
FT DOMAIN 29..106
FT /note="Ig-like C2-type"
FT DOMAIN 237..328
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 222
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-96 in IL12A and C-72 in IL23A)"
FT /evidence="ECO:0000250|UniProtKB:P29460,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 106
FT /note="K -> I"
FT VARIANT 206
FT /note="L -> P"
FT VARIANT 218
FT /note="L -> P"
FT VARIANT 289
FT /note="I -> T"
FT VARIANT 295
FT /note="S -> P"
SQ SEQUENCE 328 AA; 37273 MW; A46198AAC6D2746B CRC64;
MCHQQLVISW FSLVFLASPL MAIWELKKDV YVVELDWYPD APGEMVVLTC DTPEEDGITW
TLDQSGEVLG SGKTLTIQVK EFGDAGQYTC HKGGEALSHS LLLLHKKEDG IWSTDVLKDQ
KEPKNKTFLR CEAKNYSGRF TCWWLTTIST DLTFSVKSSR GSSNPQGVTC GAVTLSAERV
RGDNKEYEYS VECQEDSACP AAEERLPIEV MVDAIHKLKY ENYTSSFFIR DIIKPDPPKN
LQLKPLKNSR QVEVSWEYPD TWSTPHSYFS LTFCIQVQGK SKREKKDRIF TDKTSATVIC
RKNASFSVQA QDRYYSSSWS EWASVPCS
