INAR2_BOVIN
ID INAR2_BOVIN Reviewed; 530 AA.
AC Q95141;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Interferon alpha/beta receptor 2;
DE Short=IFN-R-2;
DE Short=IFN-alpha/beta receptor 2;
DE AltName: Full=Type I interferon receptor 2;
DE Flags: Precursor;
GN Name=IFNAR2; Synonyms=IFNARB;
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=Endometrium;
RX PubMed=9348203; DOI=10.1210/endo.138.11.5530;
RA Han C.-S., Mathialagan N., Klemann S.W., Roberts R.M.;
RT "Molecular cloning of ovine and bovine type I interferon receptor subunits
RT from uteri, and endometrial expression of messenger ribonucleic acid for
RT ovine receptors during the estrous cycle and pregnancy.";
RL Endocrinology 138:4757-4767(1997).
CC -!- FUNCTION: Associates with IFNAR1 to form the plasma membrane receptor
CC in the type I interferon signaling pathway. Directly involved in signal
CC transduction through its association with the TYR kinase JAK1. Involved
CC in interferon-mediated STAT1, STAT2 and STAT3 activation.
CC {ECO:0000250|UniProtKB:P48551}.
CC -!- SUBUNIT: Heterodimer with IFNAR1. Interacts with the transcriptional
CC factors STAT1 and STAT2. Interacts with JAK1. Interacts with USP18;
CC indirectly via STAT2, it negatively regulates the assembly of the
CC ternary interferon-IFNAR1-IFNAR2 complex and therefore type I
CC interferon signaling. {ECO:0000250|UniProtKB:P48551}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48551};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P48551}.
CC -!- PTM: Phosphorylated on tyrosine residues upon interferon binding.
CC Phosphorylation at Tyr-340 or Tyr-519 are sufficient to mediate
CC interferon dependent activation of STAT1, STAT2 and STAT3 leading to
CC antiproliferative effects on many different cell types (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC {ECO:0000305}.
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DR EMBL; U75304; AAB84233.1; -; mRNA.
DR RefSeq; NP_776978.1; NM_174553.2.
DR AlphaFoldDB; Q95141; -.
DR SMR; Q95141; -.
DR STRING; 9913.ENSBTAP00000020239; -.
DR PaxDb; Q95141; -.
DR PRIDE; Q95141; -.
DR GeneID; 282258; -.
DR KEGG; bta:282258; -.
DR CTD; 3455; -.
DR eggNOG; ENOG502S60E; Eukaryota.
DR InParanoid; Q95141; -.
DR OrthoDB; 680035at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0004905; F:type I interferon receptor activity; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0035455; P:response to interferon-alpha; ISS:UniProtKB.
DR GO; GO:0035456; P:response to interferon-beta; ISS:UniProtKB.
DR GO; GO:0060337; P:type I interferon signaling pathway; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015373; Interferon/interleukin_rcp_dom.
DR Pfam; PF09294; Interfer-bind; 1.
DR Pfam; PF01108; Tissue_fac; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..530
FT /note="Interferon alpha/beta receptor 2"
FT /id="PRO_0000011005"
FT TOPO_DOM 27..246
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 358..362
FT /note="1"
FT REPEAT 363..367
FT /note="2"
FT REGION 356..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..367
FT /note="2 X 5 AA tandem repeats of S-L-E-D-C"
FT REGION 427..451
FT /note="Mediates interaction with STAT2 (and required for
FT the recruitment of USP18)"
FT /evidence="ECO:0000250|UniProtKB:P48551"
FT REGION 462..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 340
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P48551"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35664"
FT MOD_RES 519
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P48551"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..122
FT /evidence="ECO:0000250|UniProtKB:P48551"
FT DISULFID 85..93
FT /evidence="ECO:0000250|UniProtKB:P48551"
FT DISULFID 210..230
FT /evidence="ECO:0000250|UniProtKB:P48551"
SQ SEQUENCE 530 AA; 59584 MW; 66A2C6D896B4DAD6 CRC64;
MLLSQNVSAI GPLNLYPMVH ISLVFGISYV APVLSDEHCT LKMRFRNFQS VLSWELKNHS
IVPTHYTLWY TIMSKREDMK VVKDCINVTR SFCDLTDVWV NTTDMYIPQV VGFRENAKLV
ICMGSFFLVP DKPLDPPEFE IVGFTNHISV NVKFQFDSPG ILSEELQFYL AFIEEHAGNS
VKRHQPQITG NITKNFNYVI DKLIPNTNYC ISVYFEPKDP RKINRSPLKC TLFRPRRESE
SSESATIGGI ITLFLITAVF ISTVMILKRI GYICLRNDFP KVLNFYKLSV WVFAELPPLE
KVATVEVIHV NRKKKVWNYN YDDENDIENE AAPHLISGGY TKHGLTGKLC PTSTTSPSLE
DCSLEDCSEP SAEEPYLPEP KGDAETPMAP GPGLWQSEGT SGGYQTRGTL WQDPTSEEDS
DSTEGSEGRI VFNVNLNSVC VRALEDDKDS EVTLMSPSCP EETVELEDLN ETESSVLVAS
EEGTQLPFTN PSTECPRPQD APSDKSDTSD PDVDMGDGYI VRQVNLKKFN
