I12R2_BOVIN
ID I12R2_BOVIN Reviewed; 861 AA.
AC Q9BEG2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Interleukin-12 receptor subunit beta-2;
DE Short=IL-12 receptor subunit beta-2;
DE Short=IL-12R subunit beta-2;
DE Short=IL-12R-beta-2;
DE Short=IL-12RB2;
DE Flags: Precursor;
GN Name=IL12RB2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymph node;
RX PubMed=12036584; DOI=10.1016/s0378-1119(02)00464-x;
RA Waldvogel A.S., Zakher A., Guionaud C.T., Fernandez P., Heussler V.T.;
RT "Regulation of bovine IL-12R beta 2 subunit mRNA expression in bovine lymph
RT node cells.";
RL Gene 289:61-67(2002).
CC -!- FUNCTION: Receptor for interleukin-12. This subunit is the signaling
CC component coupling to the JAK2/STAT4 pathway. On IL12 stimulation,
CC enhances IFN-gamma expression.
CC -!- SUBUNIT: Heterodimer/heterooligomer; disulfide-linked. The functional
CC high affinity IL12 receptor is composed of I12RB1 and IL12RB2. Il12RB2
CC binds JAK2 (via its N-terminal) through a membrane-proximal region of
CC the cytoplasmic domain (By 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 -!- PTM: On IL12 stimulation, phosphorylated on C-terminal tyrosine
CC residues. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ308426; CAC28320.1; -; mRNA.
DR RefSeq; NP_777070.1; NM_174645.3.
DR AlphaFoldDB; Q9BEG2; -.
DR SMR; Q9BEG2; -.
DR STRING; 9913.ENSBTAP00000012441; -.
DR PaxDb; Q9BEG2; -.
DR PRIDE; Q9BEG2; -.
DR GeneID; 282452; -.
DR KEGG; bta:282452; -.
DR CTD; 3595; -.
DR eggNOG; ENOG502QRRE; Eukaryota.
DR InParanoid; Q9BEG2; -.
DR OrthoDB; 144839at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0042022; C:interleukin-12 receptor complex; NAS:UniProtKB.
DR GO; GO:0019972; F:interleukin-12 binding; NAS:UniProtKB.
DR GO; GO:0016517; F:interleukin-12 receptor activity; NAS:UniProtKB.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR010457; IgC2-like_lig-bd.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF06328; Lep_receptor_Ig; 1.
DR SMART; SM00060; FN3; 4.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..861
FT /note="Interleukin-12 receptor subunit beta-2"
FT /id="PRO_0000010919"
FT TOPO_DOM 24..622
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..861
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 126..221
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 226..319
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 320..415
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 423..519
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 521..620
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 722..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..806
FT /note="Required for STAT4 binding"
FT /evidence="ECO:0000250"
FT MOTIF 305..309
FT /note="WSXWS motif"
FT MOTIF 662..670
FT /note="Box 1 motif"
FT COMPBIAS 731..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 800
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99665"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 861 AA; 96208 MW; 4B7B1E5D1E358E5B CRC64;
MAHTVGGCSL ALIFIIMLLL VKAKIDVCKR GDVTVQPSHV ISLGSAVNIS CSLKPKQGCL
PSSSFNKLIL YKFDRRIYVQ HGHSLSSQVK GLPLGTTLFV CKLACSSSDE IRICGAEISV
GVVPEQPRNL SCIQKGERGT VTCTWHRGRD THLYTAYTLQ LNGPKNLTWQ KQCNDHYCDH
LDLGINLTPE SLESSYTVKV TAINSLGSAS SFPFSFTLLD IVRPLPPWDI RIKFVNASVD
RCTLLWRDEG LVLLNRLRYR PINSRSWNMV NVTNAKGRHD LLDLKPFTEY EFQISSKLHL
YKGSWSDWSE SLRTQTPEEE PIGMLNVWYM RQHIDYNRQQ ISLFWKNLSL SEARGKILHY
QVTLQKVAGG EITLQNITEH TSWTWVIPRT GNWAAAVSAA NSKGSSLPTR INITDLCGAE
LLAPQQVLAK SEGMDKLMVT WTPPEKATAA VQEYVVEWRE LHPGAGMQPP LGWLWSPPYR
LSALISENIK PYICYEIRVH ALAGDQGGCN STRGNSQHKA PLSGPHINAI SEEKGSVLIS
WDEIPAREQM GCILHYRIYW KERDSNSQPQ LCEIPYRISP NSHPIDSLQP RVTYVLWMTA
LTAAGESPQG NEREFCLQGK ANWSTFVAPS ICMAVIMVGV LSMRCFRQKV FVLLLALRPQ
WCSKEIPDPA NSTWAKKYPI VEEKTQLALD RLLTEWPTPE EPEPLVINEV LCRVTPVFRP
PHHRSWSEKG QGVQGHYTSE EDTGYSASSP PPPRAPTAET GQGVDLYKVL GSKGPDSKPG
NPASPLTILP VDYLPTHDGY LPSNMDYLPS HEAPITDPLE ELPQHISLSI FPSSSLRPLT
FSCGEKLTLD QLKMGCGSLM L
