I12R2_PIG
ID I12R2_PIG Reviewed; 861 AA.
AC Q8MJS1; Q8WN24;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, 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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peripheral blood monocyte;
RX PubMed=12543551; DOI=10.1016/s0165-2427(02)00288-x;
RA Kokuho T., Inumaru S., Watanabe S., Kubota T.;
RT "Cloning of porcine interleukin (IL)-12 receptor beta2 (IL-12Rbeta2) gene
RT and its application to a rapid biological assay for human/porcine IL-12.";
RL Vet. Immunol. Immunopathol. 91:155-160(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-859.
RC TISSUE=Lymphoblast;
RX PubMed=12383645; DOI=10.1016/s0165-2427(02)00205-2;
RA Solano-Aguilar G.I., Zarlenga D., Beshah E., Vengroski K., Gasbarre L.,
RA Junker D.E., Cochran M.D., Weston C.Q., Valencia D.M., Chiang C.,
RA Dawson H.D., Urban J.F. Jr., Lunney J.K.;
RT "Limited effect of recombinant porcine interleukin-12 on porcine
RT lymphocytes due to a low level of IL-12 beta2 receptor.";
RL Vet. Immunol. Immunopathol. 89:133-148(2002).
RN [3]
RP ERRATUM OF PUBMED:12383645.
RA Solano-Aguilar G.I., Zarlenga D., Beshah E., Vengroski K., Gasbarre L.,
RA Junker D.E., Cochran M.D., Weston C.Q., Valencia D.M., Chiang C.,
RA Dawson H.D., Urban J.F. Jr., Lunney J.K.;
RL Vet. Immunol. Immunopathol. 95:183-183(2003).
CC -!- FUNCTION: Receptor for interleukin-12. This subunit is the signaling
CC component coupling to the JAK2/STAT4 pathway.
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; AF330213; AAM47543.1; -; mRNA.
DR EMBL; AF448143; AAL60218.1; -; mRNA.
DR RefSeq; NP_999262.1; NM_214097.2.
DR AlphaFoldDB; Q8MJS1; -.
DR SMR; Q8MJS1; -.
DR STRING; 9823.ENSSSCP00000004110; -.
DR PaxDb; Q8MJS1; -.
DR PRIDE; Q8MJS1; -.
DR GeneID; 397178; -.
DR KEGG; ssc:397178; -.
DR CTD; 3595; -.
DR eggNOG; ENOG502QRRE; Eukaryota.
DR InParanoid; Q8MJS1; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
DR CDD; cd00063; FN3; 3.
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; 1.
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_0000010922"
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..224
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 226..317
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 318..415
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 423..520
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 718..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 305..309
FT /note="WSXWS motif"
FT MOTIF 662..670
FT /note="Box 1 motif"
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"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 212..214
FT /note="LPS -> FPC (in Ref. 2; AAL60218)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="F -> L (in Ref. 2; AAL60218)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="V -> M (in Ref. 2; AAL60218)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="G -> S (in Ref. 2; AAL60218)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="L -> P (in Ref. 2; AAL60218)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="C -> R (in Ref. 2; AAL60218)"
FT /evidence="ECO:0000305"
FT CONFLICT 736
FT /note="R -> H (in Ref. 2; AAL60218)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="M -> I (in Ref. 2; AAL60218)"
FT /evidence="ECO:0000305"
FT CONFLICT 848
FT /note="A -> T (in Ref. 2; AAL60218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 861 AA; 96056 MW; 2AB663E3C5F42534 CRC64;
MARTVCGCSW ALIFIIMSLL VKAKIDVCKR GDVTVQPSHV ISLGSAVNIS CSLKPRQGCL
QVSSLNKLIL YRFHRRIHFQ RGHSLSSQVT GLPLGTTLFV CKLACSSKEE IRICGAEISV
GVVPEQPQNV SCMQKGERGT VACSWDRGRD THLYTAYTLQ LNGPKNLTWQ KQCSDYYCDS
LDLGINLPPE SPESSYTAQV TAINSLGTAS SLPSTFTFLD VVRPLPPWDI RIKCVNASVS
TCTLQWRDEG LVLLNRLRYR PVYSRSWNMV NATNAKGRHD LVDLKPFTEY EFQISSKPHL
QKGRWSDWSE SLRTQTPEKE PTGMLDVWYM KQHIDYKRQQ ISLFWKNLSL SEARGKILHY
QVTLQEVAEG NATLQNITER NSWTWTIPRT GIWAAAVSAA NSKGSSLPTR INIADLCGAG
LLAPQQVSAN PEGSDNLLVK WTSPGEGATA VQEYVVEWRE LHLRGGMQPP LSWLRSPPYN
TSTLISDNIK PYICYEIRVH ALSGDQGGCS SIRGDLKHKA PLSGPHINAI SEEKGSILIS
WDEIPAQEQM GCILHYRIYW KERDSDSQPQ LCEIPYRVSP KSHPINSLQP RVTYVLWMTA
LTAAGESPQG NEREFCLQGK ANWSTFVAPS ICIAVITVGV FSMRCFRQKV FVLLLALRPQ
WCSREIPDPA NSTWAKKYPI VEEKKQLSLD RLLADWPTPE EPEPLVINEV LPQVTPVFRR
PHHPNWPGKG QRLQGRHASE EDTGSSASSP PPPRALTAET GPAVDLYKVL GSRRPDSKPG
NPVSHLTVLP VDYLPTHEGY LPSNMDYLPS HEAPITDSLE ELPQHISLSV FPSNSLHPLT
FSCGEKLALD QLKMGCGSLM L
