IL12A_FELCA
ID IL12A_FELCA Reviewed; 222 AA.
AC O02743; O46672;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
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 Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peripheral blood;
RX PubMed=9089110; DOI=10.1007/s002510050234;
RA Schijns V.E.C.J., Wierda C.M.H., Vahlenkamp T.W., Horzinek M.C.;
RT "Molecular cloning of cat interleukin-12.";
RL Immunogenetics 45:462-463(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9522125; DOI=10.3109/10425179709020889;
RA Fehr D., Dean G.A., Huder J., Fan Z., Huettner S., Higgins J.W.,
RA Pedersen N.C., Lutz H.;
RT "Nucleotide and predicted peptide sequence of feline interleukin-12 (IL-
RT 12).";
RL DNA Seq. 8:77-82(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}.
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DR EMBL; Y07761; CAA69067.1; -; mRNA.
DR EMBL; U83185; AAB93836.1; -; mRNA.
DR RefSeq; NP_001009833.1; NM_001009833.1.
DR AlphaFoldDB; O02743; -.
DR SMR; O02743; -.
DR STRING; 9685.ENSFCAP00000010340; -.
DR GeneID; 493741; -.
DR KEGG; fca:493741; -.
DR CTD; 3592; -.
DR eggNOG; ENOG502S8JN; Eukaryota.
DR InParanoid; O02743; -.
DR OrthoDB; 1409826at2759; -.
DR TreeFam; TF330814; -.
DR Proteomes; UP000011712; Unplaced.
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:0000250"
FT CHAIN 26..222
FT /note="Interleukin-12 subunit alpha"
FT /id="PRO_0000015602"
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 CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
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-200 in IL12B)"
FT /evidence="ECO:0000250"
FT CONFLICT 66
FT /note="S -> P (in Ref. 2; AAB93836)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="A -> S (in Ref. 2; AAB93836)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 25076 MW; 223CF8FE0D30BF17 CRC64;
MCPPRGLLLV TILVLLNHLD HLSLARNLPT PTPSPGMFQC LNHSQTLLRA ISNTLQKARQ
TLEFYSCTSE EIDHEDITKD KTSTVEACLP LELTMNESCL ASREISLITN GSCLASRKTS
FMTTLCLSSI YEDLKMYQVE FKAMNAKLLM DPKRQIFLDQ NMLTAIDELL QALNVNSVTV
PQNSSLEEPD FYKTKIKLCI LLHAFRIRAV TINRMMSYLN AS
