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Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12 receptor beta component) (CD antigen CD212)

 I12R1_MOUSE             Reviewed;         738 AA.
Q60837; Q3UV59;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
08-MAY-2019, entry version 149.
RecName: Full=Interleukin-12 receptor subunit beta-1;
Short=IL-12 receptor subunit beta-1;
Short=IL-12R subunit beta-1;
Short=IL-12R-beta-1;
AltName: Full=IL-12 receptor beta component;
AltName: CD_antigen=CD212;
Flags: Precursor;
Name=Il12rb1; Synonyms=Il12rb;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=7594587;
Chua A.O., Wilkinson V.L., Presky D.H., Gubler U.;
"Cloning and characterization of a mouse IL-12 receptor-beta
component.";
J. Immunol. 155:4286-4294(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
SUBUNIT.
PubMed=8943050; DOI=10.1073/pnas.93.24.14002;
Presky D.H., Yang H., Minetti L.J., Chua A.O., Nabavi N., Wu C.-Y.,
Gately M.K., Gubler U.;
"A functional interleukin 12 receptor complex is composed of two beta-
type cytokine receptor subunits.";
Proc. Natl. Acad. Sci. U.S.A. 93:14002-14007(1996).
-!- FUNCTION: Functions as an interleukin receptor which binds
interleukin-12 with low affinity and is involved in IL12
transduction. Associated with IL12RB2 it forms a functional, high
affinity receptor for IL12. Associates also with IL23R to form the
interleukin-23 receptor which functions in IL23 signal
transduction probably through activation of the Jak-Stat signaling
cascade.
-!- SUBUNIT: Dimer or oligomer; disulfide-linked. Interacts with
IL12RB2 to form the high affinity IL12 receptor. Heterodimer with
IL23R; in presence of IL23. The heterodimer forms the IL23
receptor (By similarity). {ECO:0000250}.
-!- INTERACTION:
P97378:Il12rb2; NbExp=2; IntAct=EBI-2481455, EBI-6253448;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-
surface receptor binding.
-!- DOMAIN: The box 1 motif is required for JAK interaction and/or
activation.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U23922; AAA87457.1; -; mRNA.
EMBL; AK137577; BAE23414.1; -; mRNA.
CCDS; CCDS22382.1; -.
PIR; I49295; I49295.
RefSeq; NP_032379.2; NM_008353.2.
BioGrid; 200611; 1.
ComplexPortal; CPX-388; Interleukin-12-receptor complex.
ComplexPortal; CPX-389; Interleukin-23-receptor complex.
IntAct; Q60837; 1.
STRING; 10090.ENSMUSP00000000808; -.
PhosphoSitePlus; Q60837; -.
EPD; Q60837; -.
PaxDb; Q60837; -.
PRIDE; Q60837; -.
Ensembl; ENSMUST00000000808; ENSMUSP00000000808; ENSMUSG00000000791.
Ensembl; ENSMUST00000217569; ENSMUSP00000149385; ENSMUSG00000111872.
GeneID; 16161; -.
KEGG; mmu:16161; -.
UCSC; uc009mbr.2; mouse.
CTD; 3594; -.
MGI; MGI:104579; Il12rb1.
eggNOG; ENOG410IJY4; Eukaryota.
eggNOG; ENOG410YV8S; LUCA.
GeneTree; ENSGT00390000012431; -.
HOGENOM; HOG000082476; -.
InParanoid; Q60837; -.
KO; K05063; -.
OMA; GMATYSW; -.
OrthoDB; 1260765at2759; -.
TreeFam; TF338613; -.
Reactome; R-MMU-9020591; Interleukin-12 signaling.
Reactome; R-MMU-9020933; Interleukin-23 signaling.
PRO; PR:Q60837; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000000791; Expressed in 40 organ(s), highest expression level in thymus.
ExpressionAtlas; Q60837; baseline and differential.
Genevisible; Q60837; MM.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0042022; C:interleukin-12 receptor complex; ISO:MGI.
GO; GO:0072536; C:interleukin-23 receptor complex; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
GO; GO:0071346; P:cellular response to interferon-gamma; ISO:MGI.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; IEA:GOC.
GO; GO:0038155; P:interleukin-23-mediated signaling pathway; IEA:GOC.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IMP:MGI.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISO:MGI.
GO; GO:0002230; P:positive regulation of defense response to virus by host; ISO:MGI.
GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:MGI.
GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; ISO:MGI.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
Pfam; PF00041; fn3; 1.
SMART; SM00060; FN3; 1.
SUPFAM; SSF49265; SSF49265; 1.
PROSITE; PS50853; FN3; 2.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Membrane; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 738 Interleukin-12 receptor subunit beta-1.
/FTId=PRO_0000010918.
TOPO_DOM 20 565 Extracellular. {ECO:0000255}.
TRANSMEM 566 591 Helical. {ECO:0000255}.
TOPO_DOM 592 738 Cytoplasmic. {ECO:0000255}.
DOMAIN 47 152 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 152 258 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 259 359 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 360 465 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 469 565 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 244 248 WSXWS motif.
MOTIF 598 606 Box 1 motif.
COMPBIAS 230 234 Poly-Arg.
CARBOHYD 50 50 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 169 169 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 188 188 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 374 374 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 401 401 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 463 463 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 477 477 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 53 63 {ECO:0000250}.
CONFLICT 7 7 A -> P (in Ref. 1; AAA87457).
{ECO:0000305}.
CONFLICT 162 162 R -> G (in Ref. 1; AAA87457).
{ECO:0000305}.
CONFLICT 209 209 R -> C (in Ref. 1; AAA87457).
{ECO:0000305}.
SEQUENCE 738 AA; 81788 MW; 595CF60E8B5C74F1 CRC64;
MDMMGLAGTS KHITFLLLCQ LGASGPGDGC CVEKTSFPEG ASGSPLGPRN LSCYRVSKTD
YECSWQYDGP EDNVSHVLWC CFVPPNHTHT GQERCRYFSS GPDRTVQFWE QDGIPVLSKV
NFWVESRLGN RTMKSQKISQ YLYNWTKTTP PLGHIKVSQS HRQLRMDWNV SEEAGAEVQF
RRRMPTTNWT LGDCGPQVNS GSGVLGDIRG SMSESCLCPS ENMAQEIQIR RRRRLSSGAP
GGPWSDWSMP VCVPPEVLPQ AKIKFLVEPL NQGGRRRLTM QGQSPQLAVP EGCRGRPGAQ
VKKHLVLVRM LSCRCQAQTS KTVPLGKKLN LSGATYDLNV LAKTRFGRST IQKWHLPAQE
LTETRALNVS VGGNMTSMQW AAQAPGTTYC LEWQPWFQHR NHTHCTLIVP EEEDPAKMVT
HSWSSKPTLE QEECYRITVF ASKNPKNPML WATVLSSYYF GGNASRAGTP RHVSVRNQTG
DSVSVEWTAS QLSTCPGVLT QYVVRCEAED GAWESEWLVP PTKTQVTLDG LRSRVMYKVQ
VRADTARLPG AWSHPQRFSF EVQISRLSII FASLGSFASV LLVGSLGYIG LNRAAWHLCP
PLPTPCGSTA VEFPGSQGKQ AWQWCNPEDF PEVLYPRDAL VVEMPGDRGD GTESPQAAPE
CALDTRRPLE TQRQRQVQAL SEARRLGLAR EDCPRGDLAH VTLPLLLGGV TQGASVLDDL
WRTHKTAEPG PPTLGQEA


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Bibliography :