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Interleukin-12 subunit alpha (IL-12A) (Cytotoxic lymphocyte maturation factor 35 kDa subunit) (CLMF p35) (IL-12 subunit p35) (NK cell stimulatory factor chain 1) (NKSF1)

 IL12A_HUMAN             Reviewed;         219 AA.
P29459; Q96QZ1;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2002, sequence version 2.
25-OCT-2017, entry version 164.
RecName: Full=Interleukin-12 subunit alpha;
Short=IL-12A;
AltName: Full=Cytotoxic lymphocyte maturation factor 35 kDa subunit;
Short=CLMF p35;
AltName: Full=IL-12 subunit p35;
AltName: Full=NK cell stimulatory factor chain 1;
Short=NKSF1;
Flags: Precursor;
Name=IL12A; Synonyms=NKSF1;
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=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).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
PROTEIN SEQUENCE OF 23-48.
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).
[6]
SIMILARITY TO IL-6.
PubMed=1374259; DOI=10.1016/0167-5699(92)90140-3;
Merberg D.M., Wolf S.F., Clark S.C.;
"Sequence similarity between NKSF and the IL-6/G-CSF family.";
Immunol. Today 13:77-78(1992).
[7]
INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
Leong W.F., Chow V.T.;
"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells
reveal differential cellular gene expression in response to
enterovirus 71 infection.";
Cell. Microbiol. 8:565-580(2006).
[8]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-219, 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).
-!- 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.
-!- SUBUNIT: Heterodimer with IL12B; disulfide-linked. The heterodimer
is known as interleukin IL-12. {ECO:0000269|PubMed:10899108}.
-!- INTERACTION:
P29460:IL12B; NbExp=2; IntAct=EBI-1029636, EBI-1029614;
-!- SUBCELLULAR LOCATION: Secreted.
-!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71)
infection. {ECO:0000269|PubMed:16548883}.
-!- SIMILARITY: Belongs to the IL-6 superfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA59937.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-12 entry;
URL="https://en.wikipedia.org/wiki/Interleukin_12";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il12a/";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M65291; AAA59937.1; ALT_INIT; mRNA.
EMBL; M65271; AAA35694.1; -; mRNA.
EMBL; AF404773; AAK84425.1; -; Genomic_DNA.
EMBL; AC010370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_000873.2; NM_000882.3.
UniGene; Hs.673; -.
PDB; 1F45; X-ray; 2.80 A; B=23-219.
PDB; 3HMX; X-ray; 3.00 A; B=23-219.
PDBsum; 1F45; -.
PDBsum; 3HMX; -.
ProteinModelPortal; P29459; -.
SMR; P29459; -.
BioGrid; 109806; 7.
CORUM; P29459; -.
DIP; DIP-3772N; -.
IntAct; P29459; 3.
STRING; 9606.ENSP00000303231; -.
ChEMBL; CHEMBL2364153; -.
iPTMnet; P29459; -.
PhosphoSitePlus; P29459; -.
BioMuta; IL12A; -.
DMDM; 20141534; -.
PaxDb; P29459; -.
PRIDE; P29459; -.
Ensembl; ENST00000305579; ENSP00000303231; ENSG00000168811.
GeneID; 3592; -.
KEGG; hsa:3592; -.
UCSC; uc003fcx.4; human.
CTD; 3592; -.
DisGeNET; 3592; -.
EuPathDB; HostDB:ENSG00000168811.6; -.
GeneCards; IL12A; -.
HGNC; HGNC:5969; IL12A.
HPA; HPA001886; -.
MalaCards; IL12A; -.
MIM; 161560; gene.
neXtProt; NX_P29459; -.
Orphanet; 186; Primary biliary cirrhosis.
PharmGKB; PA29784; -.
eggNOG; ENOG410IVIR; Eukaryota.
eggNOG; ENOG410ZGHJ; LUCA.
HOVERGEN; HBG063691; -.
InParanoid; P29459; -.
KO; K05406; -.
OrthoDB; EOG091G13SK; -.
PhylomeDB; P29459; -.
TreeFam; TF330814; -.
Reactome; R-HSA-447115; Interleukin-12 family signaling.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-8984722; Interleukin-35 Signalling.
SignaLink; P29459; -.
SIGNOR; P29459; -.
EvolutionaryTrace; P29459; -.
GeneWiki; IL12A; -.
GenomeRNAi; 3592; -.
PRO; PR:P29459; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000168811; -.
CleanEx; HS_IL12A; -.
ExpressionAtlas; P29459; baseline and differential.
Genevisible; P29459; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0043514; C:interleukin-12 complex; IDA:UniProtKB.
GO; GO:0031906; C:late endosome lumen; TAS:Reactome.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0042163; F:interleukin-12 beta subunit binding; IPI:AgBase.
GO; GO:0005143; F:interleukin-12 receptor binding; NAS:UniProtKB.
GO; GO:0045513; F:interleukin-27 binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; IDA:BHF-UCL.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0098586; P:cellular response to virus; IMP:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IEP:UniProtKB.
GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0006955; P:immune response; TAS:UniProtKB.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
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:0045785; P:positive regulation of cell adhesion; IDA:UniProtKB.
GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; IMP:UniProtKB.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:0050671; P:positive regulation of lymphocyte proliferation; IDA:UniProtKB.
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:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IDA:UniProtKB.
GO; GO:0002860; P:positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IDA:UniProtKB.
GO; GO:0051135; P:positive regulation of NK T cell activation; IDA:BHF-UCL.
GO; GO:0034393; P:positive regulation of smooth muscle cell apoptotic process; IDA:BHF-UCL.
GO; GO:0045582; P:positive regulation of T cell differentiation; IEA:Ensembl.
GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0010224; P:response to UV-B; IDA:UniProtKB.
GO; GO:0009615; P:response to virus; IEP:UniProtKB.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR004281; IL-12_alpha.
Pfam; PF03039; IL12; 1.
SUPFAM; SSF47266; SSF47266; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytokine; Direct protein sequencing;
Disulfide bond; Glycoprotein; Growth factor; Reference proteome;
Secreted; Signal.
SIGNAL 1 22 {ECO:0000269|PubMed:2204066}.
CHAIN 23 219 Interleukin-12 subunit alpha.
/FTId=PRO_0000015604.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 64 196 {ECO:0000269|PubMed:10899108}.
DISULFID 85 123 {ECO:0000269|PubMed:10899108}.
DISULFID 96 96 Interchain (with C-199 in IL12B).
{ECO:0000269|PubMed:10899108}.
CONFLICT 213 213 M -> T (in Ref. 2; AAA35694).
{ECO:0000305}.
HELIX 43 58 {ECO:0000244|PDB:1F45}.
HELIX 59 61 {ECO:0000244|PDB:1F45}.
TURN 74 78 {ECO:0000244|PDB:3HMX}.
HELIX 81 84 {ECO:0000244|PDB:1F45}.
HELIX 88 92 {ECO:0000244|PDB:1F45}.
STRAND 107 109 {ECO:0000244|PDB:3HMX}.
TURN 114 116 {ECO:0000244|PDB:3HMX}.
HELIX 118 145 {ECO:0000244|PDB:1F45}.
HELIX 155 169 {ECO:0000244|PDB:1F45}.
HELIX 190 217 {ECO:0000244|PDB:1F45}.
SEQUENCE 219 AA; 24874 MW; 7C658AB7716112B2 CRC64;
MCPARSLLLV ATLVLLDHLS LARNLPVATP DPGMFPCLHH SQNLLRAVSN MLQKARQTLE
FYPCTSEEID HEDITKDKTS TVEACLPLEL TKNESCLNSR ETSFITNGSC LASRKTSFMM
ALCLSSIYED LKMYQVEFKT MNAKLLMDPK RQIFLDQNML AVIDELMQAL NFNSETVPQK
SSLEEPDFYK TKIKLCILLH AFRIRAVTID RVMSYLNAS


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