IL12A_PIG
ID IL12A_PIG Reviewed; 222 AA.
AC Q29053;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Interleukin-12 subunit alpha;
DE Short=IL-12A;
DE AltName: Full=Cytotoxic lymphocyte maturation factor 35 kDa subunit;
DE Short=CLMF p35;
DE AltName: Full=IL-12 subunit p35;
DE Flags: Precursor;
GN Name=IL12A;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peripheral blood;
RX PubMed=9239844; DOI=10.1016/s0165-2427(96)05773-x;
RA Foss D.L., Murtaugh M.P.;
RT "Molecular cloning and mRNA expression of porcine interleukin-12.";
RL Vet. Immunol. Immunopathol. 57:121-134(1997).
CC -!- FUNCTION: Heterodimerizes with IL12B to form the IL-12 cytokine or with
CC EBI3/IL27B to form the IL-35 cytokine. IL-12 is primarily produced by
CC professional antigen-presenting cells (APCs) such as B-cells and
CC dendritic cells (DCs) as well as macrophages and granulocytes and
CC regulates T-cell and natural killer-cell responses, induces the
CC production of interferon-gamma (IFN-gamma), favors the differentiation
CC of T-helper 1 (Th1) cells and is an important link between innate
CC resistance and adaptive immunity. Mechanistically, exerts its
CC biological effects through a receptor composed of IL12R1 and IL12R2
CC subunits. Binding to the receptor results in the rapid tyrosine
CC phosphorylation of a number of cellular substrates including the JAK
CC family kinases TYK2 and JAK2. In turn, recruited STAT4 gets
CC phosphorylated and translocates to the nucleus where it regulates
CC cytokine/growth factor responsive genes (By similarity). As part of IL-
CC 35, plays essential roles in maintaining the immune homeostasis of the
CC liver microenvironment and functions also as an immune-suppressive
CC cytokine (By similarity). Mediates biological events through
CC unconventional receptors composed of IL12RB2 and gp130/IL6ST
CC heterodimers or homodimers. Signaling requires the transcription
CC factors STAT1 and STAT4, which form a unique heterodimer that binds to
CC distinct DNA sites (By similarity). {ECO:0000250|UniProtKB:P29459,
CC ECO:0000250|UniProtKB:P43431}.
CC -!- SUBUNIT: Heterodimer with IL12B; disulfide-linked. This heterodimer is
CC known as interleukin IL-12. Heterodimer with EBI3/IL27B; not disulfide-
CC linked. This heterodimer is known as interleukin IL-35.
CC {ECO:0000250|UniProtKB:P29459}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P29459}.
CC -!- SIMILARITY: Belongs to the IL-6 superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA73897.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L35765; AAA73897.1; ALT_INIT; mRNA.
DR RefSeq; NP_999158.1; NM_213993.1.
DR AlphaFoldDB; Q29053; -.
DR SMR; Q29053; -.
DR STRING; 9823.ENSSSCP00000012500; -.
DR PaxDb; Q29053; -.
DR GeneID; 397053; -.
DR KEGG; ssc:397053; -.
DR CTD; 3592; -.
DR eggNOG; ENOG502S8JN; Eukaryota.
DR InParanoid; Q29053; -.
DR OMA; MNESCLA; -.
DR OrthoDB; 1409826at2759; -.
DR TreeFam; TF330814; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q29053; SS.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005143; F:interleukin-12 receptor binding; IEA:InterPro.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR004281; IL-12_alpha.
DR Pfam; PF03039; IL12; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
PE 2: Evidence at transcript level;
KW Cytokine; Disulfide bond; Glycoprotein; Growth factor; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..222
FT /note="Interleukin-12 subunit alpha"
FT /id="PRO_0000015610"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..199
FT /evidence="ECO:0000250"
FT DISULFID 88..126
FT /evidence="ECO:0000250"
FT DISULFID 99
FT /note="Interchain (with C-195 in IL12B)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 222 AA; 24945 MW; 027D04411333AC94 CRC64;
MCPLRNLLLV ATLVLLNHLD HLSLGRSLPA TTAGPGMFKC LNHSQNLLKA VSNTLQKAKQ
TLEFYSCTSE EIDHEDITKD KTSTVEACLP LELATNESCL AARETSLITN GNCLTSGKTS
FMTTLCLSSI YEDLKMYHVE FQAMNAKLLM DPKRQIFLDQ NMLTAITELM QALNFNSETV
PQKPSLEELD FYKTKIKLCI LLHAFRIRAV TIDRMMSYLN SS