INAR2_SHEEP
ID INAR2_SHEEP Reviewed; 536 AA.
AC Q95207;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 25-MAY-2022, entry version 104.
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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 -!- TISSUE SPECIFICITY: Expressed in the endometrium. Expressed in all
CC tissues examined except conceptus at day 15 of pregnancy.
CC {ECO:0000269|PubMed:9348203}.
CC -!- PTM: Phosphorylated on tyrosine residues upon interferon binding.
CC Phosphorylation at Tyr-340 or Tyr-525 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; U65979; AAB84232.1; -; mRNA.
DR RefSeq; NP_001009342.1; NM_001009342.1.
DR AlphaFoldDB; Q95207; -.
DR SMR; Q95207; -.
DR STRING; 9940.ENSOARP00000014268; -.
DR GeneID; 443363; -.
DR KEGG; oas:443363; -.
DR CTD; 3455; -.
DR eggNOG; ENOG502S60E; Eukaryota.
DR OrthoDB; 680035at2759; -.
DR Proteomes; UP000002356; 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..536
FT /note="Interferon alpha/beta receptor 2"
FT /id="PRO_0000011008"
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..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 358..362
FT /note="1"
FT REPEAT 363..367
FT /note="2"
FT REPEAT 368..372
FT /note="3"
FT REGION 358..372
FT /note="3 X 5 AA tandem repeats of S-L-E-D-C"
FT REGION 369..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..456
FT /note="Mediates interaction with STAT2 (and required for
FT the recruitment of USP18)"
FT /evidence="ECO:0000250|UniProtKB:P48551"
FT REGION 487..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..421
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 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35664"
FT MOD_RES 525
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 147
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 536 AA; 60261 MW; 1055F27D80545150 CRC64;
MLLSQNVSAI GPLNLYPMVH ISLVFGISYV VPDLSDESCT LKMRFRNFQS ILSWELKNRS
IVPTHYTLWY TIMSKPEDMK VVKDCINITR SFCDLTDVWV NRTDMYISQV VGYRENAVVV
SCMGSFFLAS DKPLDPPKFE IVDFTNNISV NVKFRLDSPR IPSEELQFYL AFIEEHAGNS
VKRHQPQITG NITENFNYVI DKLIPNTNYC ISVYFEPKDP RKINRSPLKC ILFRPRRESE
SSEPATIGGI LILFLLAAVC ISTVMILKRI GYICLRNDFP EALNFYKLSV WVFPELPPLE
KMATVEVIHI TRKKKEWNYN YDDESDIENE VAPRVNSGGY TKHGLTGRLC PTSTTAASLE
DCSLEDCSLE DCSDPSAEEP YLPEPKRDAE TPAAPGPGPW QSEGTGGGYQ TRGTLWQDPT
SEEDSDSTEG SEGRIVFNVN LNSVCVRALE DDKDSEVTLM SPSPPEETAV LEEDLSETES
SLLVASEEGT QLPFTDPSME CLRPQDALSD KSDTSESDVD IGDGYIVRQV NLKNFN
