INAR1_PIG
ID INAR1_PIG Reviewed; 560 AA.
AC Q764M8;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
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;
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 [LARGE SCALE MRNA].
RX PubMed=14681463; DOI=10.1093/nar/gkh037;
RA Uenishi H., Eguchi T., Suzuki K., Sawazaki T., Toki D., Shinkai H.,
RA Okumura N., Hamasima N., Awata T.;
RT "PEDE (Pig EST Data Explorer): construction of a database for ESTs derived
RT from porcine full-length cDNA libraries.";
RL Nucleic Acids Res. 32:D484-D488(2004).
CC -!- FUNCTION: Component of the receptor for type I interferons, including
CC interferons alpha, IFNB1 and IFNW1. Functions in general as heterodimer
CC with IFNAR2. Type I interferon binding activates the JAK-STAT signaling
CC cascade, and triggers tyrosine phosphorylation of a number of proteins
CC including JAKs, TYK2, STAT proteins and the IFNR alpha- and beta-
CC subunits themselves (By similarity). Can form an active IFNB1 receptor
CC by itself and activate a signaling cascade that does not involve
CC activation of the JAK-STAT pathway (By similarity).
CC {ECO:0000250|UniProtKB:P17181, ECO:0000250|UniProtKB:P33896}.
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:0000250|UniProtKB:P17181};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P17181}.
CC Late endosome {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; AB116561; BAD06315.1; -; mRNA.
DR RefSeq; NP_998937.1; NM_213772.1.
DR AlphaFoldDB; Q764M8; -.
DR SMR; Q764M8; -.
DR PRIDE; Q764M8; -.
DR GeneID; 396658; -.
DR KEGG; ssc:396658; -.
DR CTD; 3454; -.
DR InParanoid; Q764M8; -.
DR OrthoDB; 941128at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0060337; P:type I interferon signaling pathway; ISS:UniProtKB.
DR CDD; cd00063; FN3; 1.
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 SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 3.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Endosome; Glycoprotein; Lipoprotein;
KW 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_0000011003"
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 29..125
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 133..224
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 231..329
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 333..433
FT /note="Fibronectin type-III 4"
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 520..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..545
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 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 108
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 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
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 417
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"
SQ SEQUENCE 560 AA; 63221 MW; DC193651033DFBDB CRC64;
MLGLLGATTL MLVAGAPWVL PAGGADLRSP ENVVVSIIDD NFILKWKSSS ESVSNVTFSA
DYQITGMDNW IKLPGCQYVT STECNFSSIK LKSVYEKTKL RIRAETGNST SPWYEVEPFI
PFQEAQIGPP DVHLEAEDKA IIINLSPPGT KNSVMWAMDS SSFVYSLVIW KNSSSLEERT
KTVYARDKIH QLSPETTYCL KVKAGLRSPR KVGVYSPVYC INTTVKHHLP SPENLEINAE
NRVYVLKWNY TYENVTFQAQ WLHAFLKKIP EDHSDKWKQI PNCENVKTTH CVFPQNVFTK
GIFFIRVQAS NGNSTSLWSE EKRFNTEMQT ILFPPVINMK PINDASLRVG IGAPKESEDK
SVNQLYPLIY EVIFRENTSD TERDVLEKRT DFTFSNLKPL TVYCVKARAL IENDRWNRSS
VFSDTVCEKT KPGSTSQAWL IAGILSAILL FPAVFYGVKV VSRCINYVFF PSSKPPSTID
EYFAEQPLKN LLLSTSEEQT EICFIVENTN TITTIEETDQ IDDNHSRCSS QTNRDSGVYS
NEDENSGSKI GEEILRQAAV
