IL2RB_MACFA
ID IL2RB_MACFA Reviewed; 551 AA.
AC Q38J85;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 73.
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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen S., Yu L.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation. {ECO:0000250}.
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; DQ223724; ABB03908.1; -; mRNA.
DR RefSeq; NP_001274237.1; NM_001287308.1.
DR RefSeq; XP_005567439.1; XM_005567382.2.
DR AlphaFoldDB; Q38J85; -.
DR SMR; Q38J85; -.
DR STRING; 9541.XP_005567439.1; -.
DR GeneID; 102138714; -.
DR KEGG; mcf:102138714; -.
DR CTD; 3560; -.
DR VEuPathDB; HostDB:ENSMFAG00000002576; -.
DR eggNOG; ENOG502S0MR; Eukaryota.
DR OMA; QTSCFTN; -.
DR OrthoDB; 1322475at2759; -.
DR Proteomes; UP000233100; Chromosome 10.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042010; F:interleukin-15 receptor activity; ISS:UniProtKB.
DR GO; GO:0019976; F:interleukin-2 binding; ISS:UniProtKB.
DR GO; GO:0004911; F:interleukin-2 receptor activity; ISS:UniProtKB.
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: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 SMART; SM00060; FN3; 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:0000250"
FT CHAIN 27..551
FT /note="Interleukin-2 receptor subunit beta"
FT /id="PRO_0000045409"
FT TOPO_DOM 27..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..551
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 134..234
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 389..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 220..224
FT /note="WSXWS motif"
FT MOTIF 278..286
FT /note="Box 1 motif"
FT COMPBIAS 468..482
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 29
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 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
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 551 AA; 61224 MW; 5CEAEC1A802A1D50 CRC64;
MATLALSWCL PLLILLLPLA TSSASAAVNG TSRFTCFYNS RANISCVWSQ DGALQDTSCQ
VHAWPDRRRW NQTCELLPVS QASWACNLIL GTPDSQKLTA VDIVTLRVMC REGVRWRMMA
IQDFKPFENL RLMAPISLQV VHVETHRCNI SWKISQASHY FERHLEFEAR TLSPGHTWEE
APLMTLKQKQ EWICLETLTP DTQYEFQVRV KPLQGEFTTW SPWSQPLAFR TKPAALGKDT
IPWLGHLLVG LSGAFGFIIL VYLLINCRNT GPWLKKVLKC HTPDPSKFFS QLTSEHGGDV
QKWLSSPFPS SSFSPGGLAP EISPLEVLER DKVTQLLLQQ DKVPEPSSLS SNRSLTSCFT
NQGYFFFHLP DALEIEACQV YFTYDPCAEE EPDEGGADAP TGSSPQPLRP LSAEDDAYCT
FPSGDDLLLF SPSLLGGPSP PSTAPGGSGA GEERLPPSLQ ERVPRDWDPQ PLGPPTPGVP
DLVDFQPRPE LVLREAGEQV PDPGPREPFS FPWARPPGQG EVRALNARLP LNTDAYLSLQ
ELQDQDPTHL V
