IL2RB_MOUSE
ID IL2RB_MOUSE Reviewed; 539 AA.
AC P16297; Q3TZT2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Interleukin-2 receptor subunit beta;
DE Short=IL-2 receptor subunit beta;
DE Short=IL-2R subunit beta;
DE Short=IL-2RB;
DE AltName: Full=High affinity IL-2 receptor subunit beta;
DE AltName: Full=p70-75;
DE AltName: CD_antigen=CD122;
DE Flags: Precursor;
GN Name=Il2rb;
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].
RX PubMed=2155425; DOI=10.1073/pnas.87.5.1806;
RA Kono T., Doi T., Yamada G., Hatakeyama M., Minamoto S., Tsudo M.,
RA Miyasaka M., Miyata T., Taniguchi T.;
RT "Murine interleukin 2 receptor beta chain: dysregulated gene expression in
RT lymphoma line EL-4 caused by a promoter insertion.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:1806-1810(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Spleen;
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).
CC -!- FUNCTION: Receptor for interleukin-2. This beta subunit is involved in
CC receptor mediated endocytosis and transduces the mitogenic signals of
CC IL2. Probably in association with IL15RA, involved in the stimulation
CC of neutrophil phagocytosis by IL15 (By similarity).
CC {ECO:0000250|UniProtKB:P14784}.
CC -!- SUBUNIT: Non-covalent dimer of an alpha and a beta subunit. IL2R exists
CC in 3 different forms: a high affinity dimer, an intermediate affinity
CC monomer (beta subunit), and a low affinity monomer (alpha subunit). The
CC high and intermediate affinity forms also associate with a gamma
CC subunit. Interacts with SHB upon interleukin stimulation (By
CC similarity). {ECO:0000250|UniProtKB:P14784}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P14784};
CC Single-pass type I membrane protein {ECO:0000255}. Cell surface
CC {ECO:0000250|UniProtKB:P14784}.
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 4
CC subfamily. {ECO:0000305}.
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DR EMBL; M28052; AAA39283.1; -; mRNA.
DR EMBL; AK017288; BAB30674.1; -; mRNA.
DR EMBL; AK157572; BAE34125.1; -; mRNA.
DR CCDS; CCDS27616.1; -.
DR PIR; A35052; A35052.
DR RefSeq; NP_032394.1; NM_008368.4.
DR RefSeq; XP_006520540.1; XM_006520477.3.
DR RefSeq; XP_006520541.1; XM_006520478.3.
DR RefSeq; XP_006520542.1; XM_006520479.2.
DR RefSeq; XP_006520543.1; XM_006520480.3.
DR RefSeq; XP_006520544.1; XM_006520481.2.
DR PDB; 6DG5; X-ray; 2.52 A; B=27-235.
DR PDBsum; 6DG5; -.
DR AlphaFoldDB; P16297; -.
DR SMR; P16297; -.
DR IntAct; P16297; 1.
DR STRING; 10090.ENSMUSP00000086820; -.
DR GlyGen; P16297; 6 sites.
DR iPTMnet; P16297; -.
DR PhosphoSitePlus; P16297; -.
DR EPD; P16297; -.
DR PaxDb; P16297; -.
DR PRIDE; P16297; -.
DR ProteomicsDB; 269474; -.
DR Antibodypedia; 11905; 952 antibodies from 43 providers.
DR DNASU; 16185; -.
DR Ensembl; ENSMUST00000089398; ENSMUSP00000086820; ENSMUSG00000068227.
DR Ensembl; ENSMUST00000163494; ENSMUSP00000127006; ENSMUSG00000068227.
DR GeneID; 16185; -.
DR KEGG; mmu:16185; -.
DR UCSC; uc007wpk.2; mouse.
DR CTD; 3560; -.
DR MGI; MGI:96550; Il2rb.
DR VEuPathDB; HostDB:ENSMUSG00000068227; -.
DR eggNOG; ENOG502S0MR; Eukaryota.
DR GeneTree; ENSGT00510000049239; -.
DR HOGENOM; CLU_035782_1_0_1; -.
DR InParanoid; P16297; -.
DR OMA; QTSCFTN; -.
DR OrthoDB; 1322475at2759; -.
DR PhylomeDB; P16297; -.
DR TreeFam; TF337874; -.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-8983432; Interleukin-15 signaling.
DR Reactome; R-MMU-9020558; Interleukin-2 signaling.
DR Reactome; R-MMU-912526; Interleukin receptor SHC signaling.
DR BioGRID-ORCS; 16185; 6 hits in 72 CRISPR screens.
DR PRO; PR:P16297; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P16297; protein.
DR Bgee; ENSMUSG00000068227; Expressed in peripheral lymph node and 56 other tissues.
DR Genevisible; P16297; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0042010; F:interleukin-15 receptor activity; ISS:UniProtKB.
DR GO; GO:0019976; F:interleukin-2 binding; IPI:MGI.
DR GO; GO:0004911; F:interleukin-2 receptor activity; ISS:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0038110; P:interleukin-2-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0030101; P:natural killer cell activation; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR040951; IL2RB_N1.
DR Pfam; PF18707; IL2RB_N1; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT CHAIN 27..539
FT /note="Interleukin-2 receptor subunit beta"
FT /id="PRO_0000010879"
FT TOPO_DOM 27..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..539
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 135..235
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 395..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 221..225
FT /note="WSXWS motif"
FT MOTIF 281..289
FT /note="Box 1 motif"
FT COMPBIAS 489..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..46
FT /evidence="ECO:0000250"
FT DISULFID 74..86
FT /evidence="ECO:0000250"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 114..125
FT /evidence="ECO:0007829|PDB:6DG5"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:6DG5"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:6DG5"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:6DG5"
SQ SEQUENCE 539 AA; 60539 MW; 365C9D206E86FE14 CRC64;
MATIALPWSL SLYVFLLLLA TPWASAAVKN CSHLECFYNS RANVSCMWSH EEALNVTTCH
VHAKSNLRHW NKTCELTLVR QASWACNLIL GSFPESQSLT SVDLLDINVV CWEEKGWRRV
KTCDFHPFDN LRLVAPHSLQ VLHIDTQRCN ISWKVSQVSH YIEPYLEFEA RRRLLGHSWE
DASVLSLKQR QQWLFLEMLI PSTSYEVQVR VKAQRNNTGT WSPWSQPLTF RTRPADPMKE
ILPMSWLRYL LLVLGCFSGF FSCVYILVKC RYLGPWLKTV LKCHIPDPSE FFSQLSSQHG
GDLQKWLSSP VPLSFFSPSG PAPEISPLEV LDGDSKAVQL LLLQKDSAPL PSPSGHSQAS
CFTNQGYFFF HLPNALEIES CQVYFTYDPC VEEEVEEDGS RLPEGSPHPP LLPLAGEQDD
YCAFPPRDDL LLFSPSLSTP NTAYGGSRAP EERSPLSLHE GLPSLASRDL MGLQRPLERM
PEGDGEGLSA NSSGEQASVP EGNLHGQDQD RGQGPILTLN TDAYLSLQEL QAQDSVHLI
