I12R1_MOUSE
ID I12R1_MOUSE Reviewed; 738 AA.
AC Q60837; Q3UV59;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Interleukin-12 receptor subunit beta-1;
DE Short=IL-12 receptor subunit beta-1;
DE Short=IL-12R subunit beta-1;
DE Short=IL-12R-beta-1;
DE AltName: Full=IL-12 receptor beta component;
DE AltName: CD_antigen=CD212;
DE Flags: Precursor;
GN Name=Il12rb1; Synonyms=Il12rb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=7594587;
RA Chua A.O., Wilkinson V.L., Presky D.H., Gubler U.;
RT "Cloning and characterization of a mouse IL-12 receptor-beta component.";
RL J. Immunol. 155:4286-4294(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP SUBUNIT.
RX PubMed=8943050; DOI=10.1073/pnas.93.24.14002;
RA Presky D.H., Yang H., Minetti L.J., Chua A.O., Nabavi N., Wu C.-Y.,
RA Gately M.K., Gubler U.;
RT "A functional interleukin 12 receptor complex is composed of two beta-type
RT cytokine receptor subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14002-14007(1996).
CC -!- FUNCTION: Functions as an interleukin receptor which binds interleukin-
CC 12 with low affinity and is involved in IL12 transduction. Associated
CC with IL12RB2 it forms a functional, high affinity receptor for IL12.
CC Associates also with IL23R to form the interleukin-23 receptor which
CC functions in IL23 signal transduction probably through activation of
CC the Jak-Stat signaling cascade.
CC -!- SUBUNIT: Dimer or oligomer; disulfide-linked. Interacts with IL12RB2 to
CC form the high affinity IL12 receptor. Heterodimer with IL23R; in
CC presence of IL23. The heterodimer forms the IL23 receptor (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-surface
CC receptor binding.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; U23922; AAA87457.1; -; mRNA.
DR EMBL; AK137577; BAE23414.1; -; mRNA.
DR CCDS; CCDS22382.1; -.
DR PIR; I49295; I49295.
DR RefSeq; NP_032379.2; NM_008353.2.
DR AlphaFoldDB; Q60837; -.
DR SMR; Q60837; -.
DR BioGRID; 200611; 1.
DR ComplexPortal; CPX-388; Interleukin-12-receptor complex.
DR ComplexPortal; CPX-389; Interleukin-23-receptor complex.
DR IntAct; Q60837; 1.
DR STRING; 10090.ENSMUSP00000000808; -.
DR GlyGen; Q60837; 13 sites.
DR PhosphoSitePlus; Q60837; -.
DR EPD; Q60837; -.
DR PaxDb; Q60837; -.
DR PRIDE; Q60837; -.
DR ProteomicsDB; 273069; -.
DR Antibodypedia; 14966; 483 antibodies from 40 providers.
DR DNASU; 16161; -.
DR Ensembl; ENSMUST00000000808; ENSMUSP00000000808; ENSMUSG00000000791.
DR GeneID; 16161; -.
DR KEGG; mmu:16161; -.
DR UCSC; uc009mbr.2; mouse.
DR CTD; 3594; -.
DR MGI; MGI:104579; Il12rb1.
DR VEuPathDB; HostDB:ENSMUSG00000000791; -.
DR eggNOG; ENOG502S2KP; Eukaryota.
DR GeneTree; ENSGT00390000012431; -.
DR HOGENOM; CLU_031440_0_0_1; -.
DR InParanoid; Q60837; -.
DR OMA; ECSWEYE; -.
DR OrthoDB; 1260765at2759; -.
DR PhylomeDB; Q60837; -.
DR TreeFam; TF338613; -.
DR Reactome; R-MMU-9020591; Interleukin-12 signaling.
DR Reactome; R-MMU-9020933; Interleukin-23 signaling.
DR BioGRID-ORCS; 16161; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Il12rb1; mouse.
DR PRO; PR:Q60837; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q60837; protein.
DR Bgee; ENSMUSG00000000791; Expressed in appendicular skeleton and 47 other tissues.
DR ExpressionAtlas; Q60837; baseline and differential.
DR Genevisible; Q60837; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0042022; C:interleukin-12 receptor complex; ISO:MGI.
DR GO; GO:0072536; C:interleukin-23 receptor complex; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0016517; F:interleukin-12 receptor activity; ISO:MGI.
DR GO; GO:0005143; F:interleukin-12 receptor binding; ISO:MGI.
DR GO; GO:0042019; F:interleukin-23 binding; ISO:MGI.
DR GO; GO:0042020; F:interleukin-23 receptor activity; ISO:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IC:ComplexPortal.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IMP:MGI.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISO:MGI.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; ISO:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:MGI.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IC:ComplexPortal.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; ISO:MGI.
DR GO; GO:0051142; P:positive regulation of NK T cell proliferation; ISO:MGI.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:ComplexPortal.
DR GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; ISO:MGI.
DR GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; IC:ComplexPortal.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00041; fn3; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 2.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..738
FT /note="Interleukin-12 receptor subunit beta-1"
FT /id="PRO_0000010918"
FT TOPO_DOM 20..565
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..738
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 47..152
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 152..258
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 259..359
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 360..465
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 469..565
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT MOTIF 244..248
FT /note="WSXWS motif"
FT MOTIF 598..606
FT /note="Box 1 motif"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..63
FT /evidence="ECO:0000250"
FT CONFLICT 7
FT /note="A -> P (in Ref. 1; AAA87457)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="R -> G (in Ref. 1; AAA87457)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="R -> C (in Ref. 1; AAA87457)"
FT /evidence="ECO:0000305"
SQ 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
