ID M3XQA4_MUSPF Unreviewed; 560 AA.
AC M3XQA4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Interferon alpha/beta receptor 1 {ECO:0000256|ARBA:ARBA00016784, ECO:0000256|PIRNR:PIRNR016567};
DE Short=IFN-R-1 {ECO:0000256|PIRNR:PIRNR016567};
DE Short=IFN-alpha/beta receptor 1 {ECO:0000256|PIRNR:PIRNR016567};
DE AltName: Full=Type I interferon receptor 1 {ECO:0000256|ARBA:ARBA00032112, ECO:0000256|PIRNR:PIRNR016567};
GN Name=IFNAR1 {ECO:0000313|Ensembl:ENSMPUP00000001254.1,
GN ECO:0000313|RefSeq:XP_004757568.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000001254.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000001254.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004757568.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004757568.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Together with IFNAR2, forms the heterodimeric receptor for
CC type I interferons (including interferons alpha, beta, epsilon, omega
CC and kappa). Type I interferon binding activates the JAK-STAT signaling
CC cascade. Can also act independently of IFNAR2: form an active IFNB1
CC receptor by itself and activate a signaling cascade that does not
CC involve activation of the JAK-STAT pathway.
CC {ECO:0000256|PIRNR:PIRNR016567}.
CC -!- SUBUNIT: Heterodimer with IFNAR2. {ECO:0000256|PIRNR:PIRNR016567}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR016567};
CC Single-pass type I membrane protein {ECO:0000256|PIRNR:PIRNR016567}.
CC Late endosome {ECO:0000256|ARBA:ARBA00004603,
CC ECO:0000256|PIRNR:PIRNR016567}. Lysosome
CC {ECO:0000256|ARBA:ARBA00004371, ECO:0000256|PIRNR:PIRNR016567}.
CC Endosome {ECO:0000256|ARBA:ARBA00004177}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Note=Interferon binding triggers
CC internalization of the receptor from the cell membrane into endosomes
CC and then into lysosomes. {ECO:0000256|PIRNR:PIRNR016567}.
CC -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC {ECO:0000256|ARBA:ARBA00005399, ECO:0000256|PIRNR:PIRNR016567}.
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DR EMBL; AEYP01043158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004757568.1; XM_004757511.3.
DR STRING; 9669.ENSMPUP00000001254; -.
DR Ensembl; ENSMPUT00000001281.1; ENSMPUP00000001254.1; ENSMPUG00000001265.1.
DR GeneID; 101673686; -.
DR KEGG; mpuf:101673686; -.
DR CTD; 3454; -.
DR eggNOG; ENOG502RISU; Eukaryota.
DR GeneTree; ENSGT00940000158406; -.
DR HOGENOM; CLU_035134_0_0_1; -.
DR OMA; YCINTTV; -.
DR OrthoDB; 5320327at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008269; F:JAK pathway signal transduction adaptor activity; IEA:Ensembl.
DR GO; GO:0019962; F:type I interferon binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004905; F:type I interferon receptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035457; P:cellular response to interferon-alpha; IEA:UniProtKB-UniRule.
DR GO; GO:0035458; P:cellular response to interferon-beta; IEA:Ensembl.
DR GO; GO:1901857; P:positive regulation of cellular respiration; IEA:Ensembl.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR20859:SF54; INTERFERON ALPHA_BETA RECEPTOR 1; 1.
DR PANTHER; PTHR20859; INTERFERON/INTERLEUKIN RECEPTOR; 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; 4.
DR SUPFAM; SSF49265; Fibronectin type III; 4.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR016567};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR016567-50};
KW Endosome {ECO:0000256|ARBA:ARBA00022753, ECO:0000256|PIRNR:PIRNR016567};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Isopeptide bond {ECO:0000256|PIRSR:PIRSR016567-51};
KW Lipoprotein {ECO:0000256|PIRSR:PIRSR016567-52};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228, ECO:0000256|PIRNR:PIRNR016567};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR016567};
KW Palmitate {ECO:0000256|PIRSR:PIRSR016567-52};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR016567};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR016567};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|PIRNR:PIRNR016567};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843,
KW ECO:0000256|PIRSR:PIRSR016567-51}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..560
FT /note="Interferon alpha/beta receptor 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041118311"
FT TRANSMEM 439..462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 231..329
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 516..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 COMPBIAS 546..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 464
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-52"
FT DISULFID 78..86
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-50"
FT DISULFID 200..220
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-50"
FT DISULFID 283..291
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-50"
FT DISULFID 404..427
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-50"
FT CROSSLNK 526
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-51"
FT CROSSLNK 527
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-51"
SQ SEQUENCE 560 AA; 63638 MW; 3154D53CE00C24BF CRC64;
MLALLSATTL VLVAGVPWML PAAAGGTNLK SPQNVEVYII DDTFILRWNR SNPSVRNVTF
SADYQILENG AWLQLPGCQS VASTECNFSS VKLNVYEEIK LRIRAEEGNN TSPWRYVDSF
TLFEKAQIGP PKVHLEAEDK AIIVNISPPG TKDGGMWASD SSGFIYSLDI WKNSSSGERK
TKTVYSRDKI YELSPETTYC LKVRARLLPR KTGAYSPVYC IKTAVENKLP PPENIQVEAK
NQTYILKWDY AQENVTFYAQ WLHAYLKKIP GDNSGKWKQI PNCKNVRTTQ CVFPKNTFHK
GIYLIRVRAS DGNTTSVWSH EEKFDTQLQI TLFPPVITMK PTNNASLRVY ISAPGESENK
PVNHLYPLIY EIVFWENTSN AERKILEKRT DFTFPQLKPL TVYCVKARAL IQDERWNKSS
VFSDIVCEKT KPGNTSKTWL IAGVCAALFS IPVVIYVMKL LFRCISYVFF PSSKPPSTID
EYFSEQPLRN LLLFTSEELT ERCFIIENTN TITAVEETNQ TDGEHKKYSS QTSQDSGNYS
NEDESTGSKF SEEFLHQETE
//
