IL2RB_RAT
ID IL2RB_RAT Reviewed; 537 AA.
AC P26896;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 131.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1889461; DOI=10.1002/eji.1830210922;
RA Page T.H., Dallman M.J.;
RT "Molecular cloning of cDNAs for the rat interleukin 2 receptor alpha and
RT beta chain genes: differentially regulated gene activity in response to
RT mitogenic stimulation.";
RL Eur. J. Immunol. 21:2133-2138(1991).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M55050; AAA41429.1; -; mRNA.
DR PIR; B46535; B46535.
DR RefSeq; NP_037327.1; NM_013195.1.
DR AlphaFoldDB; P26896; -.
DR SMR; P26896; -.
DR STRING; 10116.ENSRNOP00000064699; -.
DR GlyGen; P26896; 4 sites.
DR PaxDb; P26896; -.
DR GeneID; 25746; -.
DR KEGG; rno:25746; -.
DR CTD; 3560; -.
DR RGD; 2896; Il2rb.
DR eggNOG; ENOG502S0MR; Eukaryota.
DR InParanoid; P26896; -.
DR PhylomeDB; P26896; -.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-8983432; Interleukin-15 signaling.
DR Reactome; R-RNO-9020558; Interleukin-2 signaling.
DR Reactome; R-RNO-912526; Interleukin receptor SHC signaling.
DR PRO; PR:P26896; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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; IMP:RGD.
DR GO; GO:0004911; F:interleukin-2 receptor activity; IMP:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IEP:RGD.
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; IMP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..537
FT /note="Interleukin-2 receptor subunit beta"
FT /id="PRO_0000010880"
FT TOPO_DOM 27..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..537
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 442..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 221..225
FT /note="WSXWS motif"
FT MOTIF 280..288
FT /note="Box 1 motif"
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 DISULFID 36..46
FT /evidence="ECO:0000250"
FT DISULFID 74..86
FT /evidence="ECO:0000250"
SQ SEQUENCE 537 AA; 60657 MW; 9C744A24F3361968 CRC64;
MATVDLSWRL PLYILLLLLA TTWVSAAVND CSHLKCFYNS RANVSCMWSP EEALNVTSCH
IHAKSDMRHW NKTCELTPVR QASWACNLIL GPLPDSQSLT SVDLLSLSVV CWEEKGWRRV
KTCTFHPFDN LRLIAPHSLQ VLHIETRRCN ISWEVSQVSH YVNPYLEFEA RRRLLDRSWE
DASVFSLKQR QQWIFLETLT PDTSYELQVR VIAQRGKTRT WSPWSQPMAF RTRPADPKEI
FPLPWLRCLL LVLGCFFGFL SCVCVLVKCR YLGPWLKTLL KCHIPDPSEF FSQLSSQHGG
DLQKWLSSPV PQSFFSPTGS APEISPLEVL DRDSKTMQML LFQKEKASSP SPSGHSQASC
FTNQGYFFFH LSNALEIESC QVYFTYDPCM EEDVEEDGPR LPEESPLPPL LPFTGEQDDY
CAFPPRDDLL LFSPSMSTPN TAYGNSITPE ERPPLSLQEG LPSLASPDLM GLQHPLELEL
GDDGEGMSTN SSGQQASVPE AALMGTTKTE ARPVLTLNTD AYLSLQELQA QDSAHLI
