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Interleukin-12 subunit beta (IL-12B) (Cytotoxic lymphocyte maturation factor 40 kDa subunit) (CLMF p40) (IL-12 subunit p40) (NK cell stimulatory factor chain 2) (NKSF2)

 IL12B_HUMAN             Reviewed;         328 AA.
P29460;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
30-AUG-2017, entry version 198.
RecName: Full=Interleukin-12 subunit beta;
Short=IL-12B;
AltName: Full=Cytotoxic lymphocyte maturation factor 40 kDa subunit;
Short=CLMF p40;
AltName: Full=IL-12 subunit p40;
AltName: Full=NK cell stimulatory factor chain 2;
Short=NKSF2;
Flags: Precursor;
Name=IL12B; Synonyms=NKSF2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1674604; DOI=10.1073/pnas.88.10.4143;
Gubler U., Chua A.O., Schoenhaut D.S., Dwyer C.M., McComas W.,
Motyka R., Nabavi N., Wolitzky A.G., Quinn P.M., Familletti P.C.,
Gately M.K.;
"Coexpression of two distinct genes is required to generate secreted
bioactive cytotoxic lymphocyte maturation factor.";
Proc. Natl. Acad. Sci. U.S.A. 88:4143-4147(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1673147;
Wolf S.F., Temple P.A., Kobayashi M., Young D., Dicig M., Lowe L.,
Dzialo R., Fitz L., Ferenz C., Hewick R.M., Kelleher K.,
Herrmann S.H., Clark S.C., Azzoni L., Chan S.H., Trinchieri G.,
Perussia B.;
"Cloning of cDNA for natural killer cell stimulatory factor, a
heterodimeric cytokine with multiple biologic effects on T and natural
killer cells.";
J. Immunol. 146:3074-3081(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11197695; DOI=10.1038/sj.gene.6363720;
Huang D., Cancilla M.R., Morahan G.;
"Complete primary structure, chromosomal localization, and definition
of polymorphisms of the gene encoding the human interleukin 12 p40
subunit.";
Genes Immun. 1:515-520(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Hongyuan J., Meiyun Z.;
"Cloning and sequence analysis of IL-12 cDNA from Chinese.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-33 AND PHE-298.
SeattleSNPs variation discovery resource;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 23-45.
PubMed=2204066; DOI=10.1073/pnas.87.17.6808;
Stern A.S., Podlaski F.J., Hulmes J.D., Pan Y.C.E., Quinn P.M.,
Wolitzky A.G., Familletti P.C., Stremlo D.L., Truitt T.,
Chizzonite R., Gately M.K.;
"Purification to homogeneity and partial characterization of cytotoxic
lymphocyte maturation factor from human B-lymphoblastoid cells.";
Proc. Natl. Acad. Sci. U.S.A. 87:6808-6812(1990).
[8]
SIMILARITY TO IL-6 RECEPTOR.
PubMed=2070420; DOI=10.1016/0092-8674(91)90131-H;
Gearing D.P., Cosman D.;
"Homology of the p40 subunit of natural killer cell stimulatory factor
(NKSF) with the extracellular domain of the interleukin-6 receptor.";
Cell 66:9-10(1991).
[9]
SUBUNIT.
PubMed=7836910; DOI=10.1084/jem.181.2.537;
D'Andrea A., Ma X., Aste-Amezaga M., Paganin C., Trinchieri G.;
"Stimulatory and inhibitory effects of interleukin (IL)-4 and IL-13 on
the production of cytokines by human peripheral blood mononuclear
cells: priming for IL-12 and tumor necrosis factor alpha production.";
J. Exp. Med. 181:537-546(1995).
[10]
GLYCOSYLATION AT TRP-319.
PubMed=10207176; DOI=10.1093/glycob/9.5.435;
Doucey M.A., Hess D., Blommers M.J., Hofsteenge J.;
"Recombinant human interleukin-12 is the second example of a C-
mannosylated protein.";
Glycobiology 9:435-441(1999).
[11]
INVOLVEMENT IN IMD29.
PubMed=9854038; DOI=10.1172/JCI4950;
Altare F., Lammas D., Revy P., Jouanguy E., Doeffinger R.,
Lamhamedi-Cherradi S.-E., Drysdale P., Scheel-Toellner D.,
Girdlestone J., Darbyshire P., Wadhwa M., Dockrell H., Salmon M.,
Fischer A., Durandy A., Casanova J.-L., Kumararatne D.S.;
"Inherited interleukin 12 deficiency in a child with bacille Calmette-
Guerin and Salmonella enteritidis disseminated infection.";
J. Clin. Invest. 102:2035-2040(1998).
[12]
FUNCTION, AND INTERACTION WITH IL23A.
PubMed=11114383; DOI=10.1016/S1074-7613(00)00070-4;
Oppmann B., Lesley R., Blom B., Timans J.C., Xu Y., Hunte B., Vega F.,
Yu N., Wang J., Singh K.P., Zonin F., Vaisberg E., Churakova T.,
Liu M.-R., Gorman D., Wagner J., Zurawski S., Liu Y.-J., Abrams J.S.,
Moore K.W., Rennick D.M., de Waal-Malefyt R., Hannum C., Bazan J.F.,
Kastelein R.A.;
"Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with
biological activities similar as well as distinct from IL-12.";
Immunity 13:715-725(2000).
[13]
INVOLVEMENT IN IMD29.
PubMed=11753820; DOI=10.1086/338625;
Picard C., Fieschi C., Altare F., Al-Jumaah S., Al-Hajjar S.,
Feinberg J., Dupuis S., Soudais C., Al-Mohsen I.Z., Genin E.,
Lammas D., Kumararatne D.S., Leclerc T., Rafii A., Frayha H.,
Murugasu B., Wah L.B., Sinniah R., Loubser M., Okamoto E.,
Al-Ghonaium A., Tufenkeji H., Abel L., Casanova J.-L.;
"Inherited interleukin-12 deficiency: IL12B genotype and clinical
phenotype of 13 patients from six kindreds.";
Am. J. Hum. Genet. 70:336-348(2002).
[14]
ASSOCIATION WITH PSORIASIS.
PubMed=17587057; DOI=10.1007/s00439-007-0397-0;
Capon F., Di Meglio P., Szaub J., Prescott N.J., Dunster C.,
Baumber L., Timms K., Gutin A., Abkevic V., Burden A.D., Lanchbury J.,
Barker J.N., Trembath R.C., Nestle F.O.;
"Sequence variants in the genes for the interleukin-23 receptor
(IL23R) and its ligand (IL12B) confer protection against psoriasis.";
Hum. Genet. 122:201-206(2007).
[15]
ASSOCIATION WITH PSORIASIS.
PubMed=18800148; DOI=10.1038/jid.2008.233;
Huffmeier U., Lascorz J., Bohm B., Lohmann J., Wendler J., Mossner R.,
Reich K., Traupe H., Kurrat W., Burkhardt H., Reis A.;
"Genetic variants of the IL-23R pathway: association with psoriatic
arthritis and psoriasis vulgaris, but no specific risk factor for
arthritis.";
J. Invest. Dermatol. 129:355-358(2009).
[16]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-328 ALONE AND IN COMPLEX
WITH IL12A, GLYCOSYLATION AT ASN-222, AND DISULFIDE BONDS.
PubMed=10899108; DOI=10.1093/emboj/19.14.3530;
Yoon C., Johnston S.C., Tang J., Stahl M., Tobin J.F., Somers W.S.;
"Charged residues dominate a unique interlocking topography in the
heterodimeric cytokine interleukin-12.";
EMBO J. 19:3530-3541(2000).
[17]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 23-328 IN COMPLEX WITH IL23A
AND ANTIBODY.
PubMed=18708069; DOI=10.1016/j.jmb.2008.08.001;
Beyer B.M., Ingram R., Ramanathan L., Reichert P., Le H.V.,
Madison V., Orth P.;
"Crystal structures of the pro-inflammatory cytokine interleukin-23
and its complex with a high-affinity neutralizing antibody.";
J. Mol. Biol. 382:942-955(2008).
[18]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-328 IN COMPLEX WITH IL23A,
AND SUBUNIT.
PubMed=18680750; DOI=10.1016/j.jmb.2008.07.051;
Lupardus P.J., Garcia K.C.;
"The structure of interleukin-23 reveals the molecular basis of p40
subunit sharing with interleukin-12.";
J. Mol. Biol. 382:931-941(2008).
-!- FUNCTION: Cytokine that can act as a growth factor for activated T
and NK cells, enhance the lytic activity of NK/lymphokine-
activated killer cells, and stimulate the production of IFN-gamma
by resting PBMC. {ECO:0000269|PubMed:11114383}.
-!- FUNCTION: Associates with IL23A to form the IL-23 interleukin, a
heterodimeric cytokine which functions in innate and adaptive
immunity. IL-23 may constitute with IL-17 an acute response to
infection in peripheral tissues. IL-23 binds to a heterodimeric
receptor complex composed of IL12RB1 and IL23R, activates the Jak-
Stat signaling cascade, stimulates memory rather than naive T-
cells and promotes production of proinflammatory cytokines. IL-23
induces autoimmune inflammation and thus may be responsible for
autoimmune inflammatory diseases and may be important for
tumorigenesis. {ECO:0000269|PubMed:11114383}.
-!- SUBUNIT: Heterodimer with IL12A; disulfide-linked. The heterodimer
is known as interleukin IL-12. Heterodimer with IL23A; disulfide-
linked. The heterodimer is known as interleukin IL-23. Also
secreted as a monomer. {ECO:0000269|PubMed:10899108,
ECO:0000269|PubMed:18680750, ECO:0000269|PubMed:18708069,
ECO:0000269|PubMed:7836910}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1029614, EBI-1029614;
P29459:IL12A; NbExp=2; IntAct=EBI-1029614, EBI-1029636;
Q9NPF7:IL23A; NbExp=4; IntAct=EBI-1029614, EBI-2481154;
Q9EQ14:Il23a (xeno); NbExp=2; IntAct=EBI-1029614, EBI-2481329;
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: Known to be C-mannosylated in the recombinant protein; it is
not yet known for sure if the wild-type protein is also modified.
-!- DISEASE: Immunodeficiency 29 (IMD29) [MIM:614890]: A form of
Mendelian susceptibility to mycobacterial disease, a rare
condition caused by impairment of interferon-gamma mediated
immunity. It is characterized by predisposition to illness caused
by moderately virulent mycobacterial species, such as Bacillus
Calmette-Guerin (BCG) vaccine, environmental non-tuberculous
mycobacteria, and by the more virulent Mycobacterium tuberculosis.
Other microorganisms rarely cause severe clinical disease in
individuals with susceptibility to mycobacterial infections, with
the exception of Salmonella which infects less than 50% of these
individuals. Clinical outcome severity depends on the degree of
impairment of interferon-gamma mediated immunity. Some patients
die of overwhelming mycobacterial disease with lepromatous-like
lesions in early childhood, whereas others develop, later in life,
disseminated but curable infections with tuberculoid granulomas.
IMD29 is characterized by undetectable IL12B secretion from
leukocytes. Affected individuals generally present with BCG
disease after vaccination in childhood, and at least half also
have Salmonella infection. Disease phenotype is relatively mild,
and patients have a good prognosis. {ECO:0000269|PubMed:11753820,
ECO:0000269|PubMed:9854038}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Psoriasis 11 (PSORS11) [MIM:612599]: A common, chronic
inflammatory disease of the skin with multifactorial etiology. It
is characterized by red, scaly plaques usually found on the scalp,
elbows and knees. These lesions are caused by abnormal
keratinocyte proliferation and infiltration of inflammatory cells
into the dermis and epidermis. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 3
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=IL12Bbase; Note=IL12B mutation db;
URL="http://structure.bmc.lu.se/idbase/IL12Bbase/";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il12b/";
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EMBL; M65272; AAA35695.1; -; mRNA.
EMBL; M65290; AAA59938.1; -; mRNA.
EMBL; AY008847; AAG32620.1; -; Genomic_DNA.
EMBL; AF180563; AAD56386.1; -; mRNA.
EMBL; AF512686; AAM34792.1; -; Genomic_DNA.
EMBL; BC067498; AAH67498.1; -; mRNA.
EMBL; BC067499; AAH67499.1; -; mRNA.
EMBL; BC067500; AAH67500.1; -; mRNA.
EMBL; BC067501; AAH67501.1; -; mRNA.
EMBL; BC067502; AAH67502.1; -; mRNA.
EMBL; BC074723; AAH74723.1; -; mRNA.
CCDS; CCDS4346.1; -.
PIR; A38957; A38957.
RefSeq; NP_002178.2; NM_002187.2.
UniGene; Hs.674; -.
PDB; 1F42; X-ray; 2.50 A; A=23-328.
PDB; 1F45; X-ray; 2.80 A; A=23-328.
PDB; 3D85; X-ray; 1.90 A; D=23-328.
PDB; 3D87; X-ray; 2.90 A; B/D=23-328.
PDB; 3DUH; X-ray; 2.30 A; A/B=23-328.
PDB; 3HMX; X-ray; 3.00 A; A=23-328.
PDB; 3QWR; X-ray; 3.25 A; A=23-328.
PDB; 4GRW; X-ray; 2.55 A; B/D=1-328.
PDB; 5MJ3; X-ray; 1.74 A; A=23-328.
PDB; 5MJ4; X-ray; 3.40 A; A=23-328.
PDBsum; 1F42; -.
PDBsum; 1F45; -.
PDBsum; 3D85; -.
PDBsum; 3D87; -.
PDBsum; 3DUH; -.
PDBsum; 3HMX; -.
PDBsum; 3QWR; -.
PDBsum; 4GRW; -.
PDBsum; 5MJ3; -.
PDBsum; 5MJ4; -.
ProteinModelPortal; P29460; -.
SMR; P29460; -.
BioGrid; 109807; 3.
DIP; DIP-3774N; -.
ELM; P29460; -.
IntAct; P29460; 5.
STRING; 9606.ENSP00000231228; -.
ChEMBL; CHEMBL3580484; -.
DrugBank; DB02763; 5-Mercapto-2-Nitro-Benzoic Acid.
DrugBank; DB05459; Briakinumab.
DrugBank; DB05848; humanized SMART Anti-IL-12 Antibody.
DrugBank; DB05679; Ustekinumab.
iPTMnet; P29460; -.
PhosphoSitePlus; P29460; -.
UniCarbKB; P29460; -.
BioMuta; IL12B; -.
DMDM; 266320; -.
PaxDb; P29460; -.
PRIDE; P29460; -.
DNASU; 3593; -.
Ensembl; ENST00000231228; ENSP00000231228; ENSG00000113302.
GeneID; 3593; -.
KEGG; hsa:3593; -.
UCSC; uc003lxr.2; human.
CTD; 3593; -.
DisGeNET; 3593; -.
GeneCards; IL12B; -.
HGNC; HGNC:5970; IL12B.
HPA; HPA040970; -.
MalaCards; IL12B; -.
MIM; 161561; gene.
MIM; 612599; phenotype.
MIM; 614890; phenotype.
neXtProt; NX_P29460; -.
OpenTargets; ENSG00000113302; -.
Orphanet; 319558; Mendelian susceptibility to mycobacterial diseases due to complete IL12B deficiency.
Orphanet; 3287; Takayasu arteritis.
PharmGKB; PA29785; -.
eggNOG; ENOG410IF5K; Eukaryota.
eggNOG; ENOG410YWXR; LUCA.
GeneTree; ENSGT00390000012630; -.
HOGENOM; HOG000113027; -.
HOVERGEN; HBG052094; -.
InParanoid; P29460; -.
KO; K05425; -.
OMA; WSTPHSY; -.
OrthoDB; EOG091G0EKV; -.
PhylomeDB; P29460; -.
TreeFam; TF334829; -.
Reactome; R-HSA-447115; Interleukin-12 family signaling.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SIGNOR; P29460; -.
EvolutionaryTrace; P29460; -.
GeneWiki; Interleukin-12_subunit_beta; -.
GenomeRNAi; 3593; -.
PMAP-CutDB; P29460; -.
PRO; PR:P29460; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113302; -.
CleanEx; HS_IL12B; -.
Genevisible; P29460; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:UniProtKB.
GO; GO:0043514; C:interleukin-12 complex; IDA:UniProtKB.
GO; GO:0070743; C:interleukin-23 complex; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042164; F:interleukin-12 alpha subunit binding; IPI:AgBase.
GO; GO:0005143; F:interleukin-12 receptor binding; TAS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; IDA:BHF-UCL.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:BHF-UCL.
GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
GO; GO:0042095; P:interferon-gamma biosynthetic process; TAS:UniProtKB.
GO; GO:0030101; P:natural killer cell activation; IDA:UniProtKB.
GO; GO:0002323; P:natural killer cell activation involved in immune response; IEA:Ensembl.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IEA:Ensembl.
GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0032693; P:negative regulation of interleukin-10 production; IMP:BHF-UCL.
GO; GO:0032700; P:negative regulation of interleukin-17 production; IDA:BHF-UCL.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:UniProtKB.
GO; GO:0010536; P:positive regulation of activation of Janus kinase activity; IDA:BHF-UCL.
GO; GO:0045785; P:positive regulation of cell adhesion; IDA:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:BHF-UCL.
GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; IDA:BHF-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0045078; P:positive regulation of interferon-gamma biosynthetic process; TAS:UniProtKB.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:BHF-UCL.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:BHF-UCL.
GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:BHF-UCL.
GO; GO:0050671; P:positive regulation of lymphocyte proliferation; IDA:UniProtKB.
GO; GO:0043382; P:positive regulation of memory T cell differentiation; ISS:BHF-UCL.
GO; GO:0032946; P:positive regulation of mononuclear cell proliferation; IMP:AgBase.
GO; GO:0032816; P:positive regulation of natural killer cell activation; IDA:UniProtKB.
GO; GO:0002860; P:positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IDA:UniProtKB.
GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IDA:BHF-UCL.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; TAS:BHF-UCL.
GO; GO:0051135; P:positive regulation of NK T cell activation; IDA:BHF-UCL.
GO; GO:0051142; P:positive regulation of NK T cell proliferation; IDA:BHF-UCL.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:BHF-UCL.
GO; GO:0034393; P:positive regulation of smooth muscle cell apoptotic process; IDA:BHF-UCL.
GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISS:BHF-UCL.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:BHF-UCL.
GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IDA:BHF-UCL.
GO; GO:2000330; P:positive regulation of T-helper 17 cell lineage commitment; ISS:BHF-UCL.
GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; ISS:BHF-UCL.
GO; GO:0034105; P:positive regulation of tissue remodeling; IC:BHF-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
GO; GO:0042035; P:regulation of cytokine biosynthetic process; TAS:UniProtKB.
GO; GO:0042509; P:regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
GO; GO:0010224; P:response to UV-B; IDA:UniProtKB.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
GO; GO:0019953; P:sexual reproduction; TAS:BHF-UCL.
GO; GO:0042088; P:T-helper 1 type immune response; TAS:UniProtKB.
GO; GO:0042093; P:T-helper cell differentiation; IDA:UniProtKB.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR003961; FN3_dom.
InterPro; IPR003530; Hematopoietin_rcpt_L_F3_CS.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR015528; IL-12_beta.
InterPro; IPR019482; IL-12_beta_cen-dom.
PANTHER; PTHR10078:SF37; PTHR10078:SF37; 1.
Pfam; PF10420; IL12p40_C; 1.
PIRSF; PIRSF038007; IL_12_beta; 1.
PRINTS; PR01928; INTRLEUKN12B.
SMART; SM00408; IGc2; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 1.
PROSITE; PS01354; HEMATOPO_REC_L_F3; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytokine; Direct protein sequencing;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 22 {ECO:0000269|PubMed:2204066}.
CHAIN 23 328 Interleukin-12 subunit beta.
/FTId=PRO_0000010930.
DOMAIN 23 106 Ig-like C2-type.
DOMAIN 237 328 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 222 222 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10899108}.
CARBOHYD 319 319 C-linked (Man) tryptophan.
{ECO:0000269|PubMed:10207176}.
/FTId=CAR_000187.
DISULFID 50 90 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10899108}.
DISULFID 131 142 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10899108}.
DISULFID 170 193 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10899108}.
DISULFID 199 199 Interchain (with C-96 in IL12A).
{ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10899108}.
DISULFID 300 327 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:10899108}.
VARIANT 33 33 V -> I (in dbSNP:rs3213096).
{ECO:0000269|Ref.5}.
/FTId=VAR_020001.
VARIANT 298 298 V -> F (in dbSNP:rs3213119).
{ECO:0000269|Ref.5}.
/FTId=VAR_049170.
CONFLICT 239 239 K -> N (in Ref. 2; AAA59938).
{ECO:0000305}.
STRAND 24 27 {ECO:0000244|PDB:5MJ3}.
STRAND 30 36 {ECO:0000244|PDB:5MJ3}.
STRAND 44 49 {ECO:0000244|PDB:5MJ3}.
STRAND 51 53 {ECO:0000244|PDB:3D85}.
STRAND 59 62 {ECO:0000244|PDB:5MJ3}.
STRAND 70 79 {ECO:0000244|PDB:5MJ3}.
HELIX 82 84 {ECO:0000244|PDB:5MJ3}.
STRAND 86 92 {ECO:0000244|PDB:5MJ3}.
STRAND 95 108 {ECO:0000244|PDB:5MJ3}.
STRAND 116 118 {ECO:0000244|PDB:3D87}.
STRAND 122 126 {ECO:0000244|PDB:5MJ3}.
STRAND 130 147 {ECO:0000244|PDB:5MJ3}.
STRAND 150 160 {ECO:0000244|PDB:5MJ3}.
STRAND 162 164 {ECO:0000244|PDB:5MJ3}.
STRAND 166 170 {ECO:0000244|PDB:5MJ3}.
STRAND 174 181 {ECO:0000244|PDB:5MJ3}.
STRAND 184 197 {ECO:0000244|PDB:5MJ3}.
STRAND 200 202 {ECO:0000244|PDB:3D87}.
STRAND 208 216 {ECO:0000244|PDB:5MJ3}.
STRAND 219 227 {ECO:0000244|PDB:5MJ3}.
HELIX 229 232 {ECO:0000244|PDB:5MJ3}.
STRAND 239 245 {ECO:0000244|PDB:5MJ3}.
STRAND 249 257 {ECO:0000244|PDB:5MJ3}.
STRAND 260 262 {ECO:0000244|PDB:3HMX}.
TURN 266 268 {ECO:0000244|PDB:5MJ3}.
STRAND 271 278 {ECO:0000244|PDB:5MJ3}.
STRAND 287 299 {ECO:0000244|PDB:5MJ3}.
STRAND 302 304 {ECO:0000244|PDB:5MJ4}.
STRAND 305 315 {ECO:0000244|PDB:5MJ3}.
STRAND 323 326 {ECO:0000244|PDB:5MJ3}.
SEQUENCE 328 AA; 37169 MW; 118FA801B8F5BB2F CRC64;
MCHQQLVISW FSLVFLASPL VAIWELKKDV YVVELDWYPD APGEMVVLTC DTPEEDGITW
TLDQSSEVLG SGKTLTIQVK EFGDAGQYTC HKGGEVLSHS LLLLHKKEDG IWSTDILKDQ
KEPKNKTFLR CEAKNYSGRF TCWWLTTIST DLTFSVKSSR GSSDPQGVTC GAATLSAERV
RGDNKEYEYS VECQEDSACP AAEESLPIEV MVDAVHKLKY ENYTSSFFIR DIIKPDPPKN
LQLKPLKNSR QVEVSWEYPD TWSTPHSYFS LTFCVQVQGK SKREKKDRVF TDKTSATVIC
RKNASISVRA QDRYYSSSWS EWASVPCS


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