INAR1_BOVIN
ID INAR1_BOVIN Reviewed; 560 AA.
AC Q04790;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Interferon alpha/beta receptor 1;
DE Short=IFN-R-1;
DE Short=IFN-alpha/beta receptor 1;
DE AltName: Full=Type I interferon receptor 1;
DE Flags: Precursor;
GN Name=IFNAR1; Synonyms=IFNAR;
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=Lung;
RX PubMed=1446745; DOI=10.1016/0014-5793(92)81204-y;
RA Mouchel-Vielh E., Lutfalla G., Mogensen K.E., Uze G.;
RT "Specific antiviral activities of the human alpha interferons are
RT determined at the level of receptor (IFNAR) structure.";
RL FEBS Lett. 313:255-259(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8318540; DOI=10.1016/0167-4781(93)90129-2;
RA Lim J.-K., Langer J.A.;
RT "Cloning and characterization of a bovine alpha interferon receptor.";
RL Biochim. Biophys. Acta 1173:314-319(1993).
CC -!- FUNCTION: Component of the receptor for type I interferons, including
CC interferons alpha, IFNB1 and IFNW1 (PubMed:8318540). Functions in
CC general as heterodimer with IFNAR2. Type I interferon binding activates
CC the JAK-STAT signaling cascade, and triggers tyrosine phosphorylation
CC of a number of proteins including JAKs, TYK2, STAT proteins and the
CC IFNR alpha- and beta-subunits themselves (By similarity). Can form an
CC active IFNB1 receptor by itself and activate a signaling cascade that
CC does not involve activation of the JAK-STAT pathway (By similarity).
CC {ECO:0000250|UniProtKB:P17181, ECO:0000250|UniProtKB:P33896,
CC ECO:0000269|PubMed:8318540}.
CC -!- SUBUNIT: Heterodimer with IFNAR2. Interacts with STAT1 and STAT2; the
CC interaction requires its phosphorylation at Tyr-467. Interacts with
CC TYK2. Interacts (serine-phosphorylated form) with FBXW11, the substrate
CC recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-
CC protein ligase complex. Interacts with SHMT2; this promotes interaction
CC with ABRAXAS2 and the BRISC complex. Interacts with TRIM10; this
CC interaction prevents association between IFNAR1 and TYK2.
CC {ECO:0000250|UniProtKB:P17181}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8318540};
CC Single-pass type I membrane protein {ECO:0000305}. Late endosome
CC {ECO:0000250|UniProtKB:P17181}. Lysosome
CC {ECO:0000250|UniProtKB:P17181}. Note=Interferon binding triggers
CC internalization of the receptor from the cell membrane into endosomes
CC and then into lysosomes. {ECO:0000250|UniProtKB:P17181}.
CC -!- PTM: Ubiquitinated, leading to its internalization and lysosomal
CC degradation. The 'Lys-63'-linked ubiquitin chains are cleaved off by
CC the BRISC complex; this prevents receptor internalization and
CC degradation. Probable ubiquitination sites have been identified in
CC human, but are poorly conserved across species.
CC {ECO:0000250|UniProtKB:P17181}.
CC -!- PTM: Phosphorylated on serine residues in response to interferon
CC binding; this promotes interaction with FBXW11 and ubiquitination.
CC Phosphorylated on tyrosine residues by TYK2 tyrosine kinase.
CC {ECO:0000250|UniProtKB:P17181}.
CC -!- PTM: Palmitoylation at Cys-464 is required for the activation of STAT1
CC and STAT2. {ECO:0000250|UniProtKB:P17181}.
CC -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC {ECO:0000305}.
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DR EMBL; X68443; CAA48484.1; -; mRNA.
DR EMBL; L06320; AAA02571.1; -; mRNA.
DR PIR; S27387; S27387.
DR RefSeq; NP_776977.1; NM_174552.2.
DR AlphaFoldDB; Q04790; -.
DR SMR; Q04790; -.
DR STRING; 9913.ENSBTAP00000029080; -.
DR PaxDb; Q04790; -.
DR PRIDE; Q04790; -.
DR Ensembl; ENSBTAT00000029080; ENSBTAP00000029080; ENSBTAG00000021819.
DR GeneID; 282257; -.
DR KEGG; bta:282257; -.
DR CTD; 3454; -.
DR VEuPathDB; HostDB:ENSBTAG00000021819; -.
DR VGNC; VGNC:30054; IFNAR1.
DR eggNOG; ENOG502RISU; Eukaryota.
DR GeneTree; ENSGT00940000158406; -.
DR HOGENOM; CLU_035134_0_0_1; -.
DR InParanoid; Q04790; -.
DR OMA; YCINTTV; -.
DR OrthoDB; 941128at2759; -.
DR Reactome; R-BTA-909733; Interferon alpha/beta signaling.
DR Reactome; R-BTA-912694; Regulation of IFNA/IFNB signaling.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000021819; Expressed in neutrophil and 105 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019962; F:type I interferon binding; ISS:UniProtKB.
DR GO; GO:0004905; F:type I interferon receptor activity; ISS:UniProtKB.
DR GO; GO:0035457; P:cellular response to interferon-alpha; ISS:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:1901857; P:positive regulation of cellular respiration; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0060337; P:type I interferon signaling pathway; ISS:UniProtKB.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015373; Interferon/interleukin_rcp_dom.
DR InterPro; IPR016669; Interferon_alpha/beta_rcpt-1.
DR Pfam; PF09294; Interfer-bind; 2.
DR Pfam; PF01108; Tissue_fac; 1.
DR PIRSF; PIRSF016567; IFN_alpha/beta_recept-1; 1.
DR SMART; SM00060; FN3; 3.
DR SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 3.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Endosome; Glycoprotein; Isopeptide bond;
KW Lipoprotein; Lysosome; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..560
FT /note="Interferon alpha/beta receptor 1"
FT /id="PRO_0000011000"
FT TOPO_DOM 25..437
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 126..226
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 231..329
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 333..433
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 492..501
FT /note="Important for interaction with TYK2"
FT /evidence="ECO:0000250|UniProtKB:P17181"
FT REGION 522..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 467
FT /note="Phosphotyrosine; by TYK2"
FT /evidence="ECO:0000250|UniProtKB:P17181"
FT MOD_RES 482
FT /note="Phosphotyrosine; by TYK2"
FT /evidence="ECO:0000250|UniProtKB:P17181"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17181"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17181"
FT LIPID 464
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P17181"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 76..84
FT /evidence="ECO:0000250|UniProtKB:P17181"
FT DISULFID 199..220
FT /evidence="ECO:0000250|UniProtKB:P17181"
FT DISULFID 283..291
FT /evidence="ECO:0000250|UniProtKB:P17181"
FT DISULFID 404..427
FT /evidence="ECO:0000250|UniProtKB:P33896"
FT CROSSLNK 526
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P17181"
FT CROSSLNK 527
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P17181"
FT CONFLICT 422
FT /note="F -> V (in Ref. 2; AAA02571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 560 AA; 63819 MW; 66D76B72861E1D11 CRC64;
MLALLGATTL MLVAGRWVLP AASGEANLKP ENVEIHIIDD NFFLKWNSSS ESVKNVTFSA
DYQILGTDNW KKLSGCQHIT STKCNFSSVE LENVFEKIEL RIRAEEGNNT STWYEVEPFV
PFLEAQIGPP DVHLEAEDKA IILSISPPGT KDSIMWAMDR SSFRYSVVIW KNSSSLEERT
ETVYPEDKIY KLSPEITYCL KVKAELRLQS RVGCYSPVYC INTTERHKVP SPENIQINAD
NQIYVLKWDY PYENATFQAQ WLRAFFKKIP GNHSDKWKQI PNCENVTSTH CVFPREVSSR
GIYYVRVRAS NGNGTSFWSE EKEFNTEMKT IIFPPVISVK SVTDDSLHVS VGASEESENM
SVNQLYPLIY EVIFWENTSN AERKVLEKRT NFIFPDLKPL TVYCVKARAL IENDRRNKGS
SFSDTVCEKT KPGNTSKTWL IVGTCTALFS IPVVIYVVSV FLRCVKYVFF PSSKPPSSVD
EYFSDQPLRN LLLSTSEEQT ERCFIIENAS IITEIEETDE IDEVHKKYSS QTSQDSGNYS
NEDENSGSKI SEEFPQQDSV
