IL2RB_PANTR
ID IL2RB_PANTR Reviewed; 551 AA.
AC Q38J84;
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
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}.
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DR EMBL; DQ223725; ABB03909.1; -; mRNA.
DR RefSeq; NP_001030599.1; NM_001035522.1.
DR AlphaFoldDB; Q38J84; -.
DR SMR; Q38J84; -.
DR STRING; 9598.ENSPTRP00000024676; -.
DR GeneID; 470203; -.
DR KEGG; ptr:470203; -.
DR CTD; 3560; -.
DR InParanoid; Q38J84; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0004911; F:interleukin-2 receptor activity; ISS:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
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; IBA:GO_Central.
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_0000045410"
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 393..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..476
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 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; 61126 MW; 5C4B1ECB17BEF52B CRC64;
MAAPALSWRL PLLILLLPLA TPWASATVNG TSQFTCFYNS RANISCVWSQ DGALQDTSCQ
VHAWPDRRRW NQTCELLPVS QASWACNLIL GAPDSQKLTT VDIVTLRVLC REGVRWRVMA
IQDFKPFENL RLMAPISLQV VHVETHRCNI SWEISQASHY FERHLEFEAR TLSPGHTWEE
APLLTLKQKQ EWICLETLTP DTQYEFQVRV KPLQGEFTTW SPWSQPLAFR TKPASLGKDT
IPWLGHLLVG LSGAFGFIIL VYLLINCRNT GPWLKKVLKC HTPDPSKFFS QLSSEHGGDV
QKWLSSPFPS SSFSPGGLAP EISPLEVLER DKVTQLLLQQ DKVPEPASLS SNHSLTSCFT
NQGYFFFHLP DALEIEACQV YFTYDPYAEE DADEGVAGAP TGSSPQPLQP LSGEDDTYCT
FPSRDGLLLF SPSLLGGPSP PSTAPGGSGA GEERMPPSLQ ERVPRDWDPQ PLGPPTPGVP
DLVDFQPPPE LVLREAGEEV PDAGPREGVS FPWSRPPGQG EFRALNARLP LNTDAYLSLQ
ELQGQDPTHL V
