ID A0A2K6LNY3_RHIBE Unreviewed; 553 AA.
AC A0A2K6LNY3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 34.
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:ENSRBIP00000025179.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000025179.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000025179.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000025179.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_017739414.1; XM_017883925.1.
DR AlphaFoldDB; A0A2K6LNY3; -.
DR STRING; 61621.ENSRBIP00000025179; -.
DR Ensembl; ENSRBIT00000049087.1; ENSRBIP00000025179.1; ENSRBIG00000036473.1.
DR GeneID; 108536856; -.
DR KEGG; rbb:108536856; -.
DR CTD; 3454; -.
DR GeneTree; ENSGT00940000158406; -.
DR OrthoDB; 5320327at2759; -.
DR Proteomes; UP000233180; 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|PIRNR:PIRNR016567};
KW Reference proteome {ECO:0000313|Proteomes:UP000233180};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..553
FT /note="Interferon alpha/beta receptor 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014374270"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 327..428
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 512..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 459
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-52"
FT DISULFID 79..87
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-50"
FT DISULFID 200..221
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-50"
FT DISULFID 279..287
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-50"
FT DISULFID 399..422
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-50"
FT CROSSLNK 497
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-51"
FT CROSSLNK 521
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-51"
FT CROSSLNK 522
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-51"
SQ SEQUENCE 553 AA; 63232 MW; 31B76782DE0591E6 CRC64;
MMVTLLGATT LVLVTLAPWV LSAAAGGKNL KSPQKVEVDI IDDTFILRWN RSDESVGNVT
FSFDYQKPGM DNWIKLPGCQ NITSTKCNFS SLKLNIYEEI KLRIRAEKEN TSSWYEVDSF
TPFRKAQIGP PEVHLEAEDK AIVIHISPPG TKDSVMWALD GLSFTYSLVI WKNSSSVEER
IENIYSRHKI YKLSPETTYC LKVKAALLTS RKIGVYSPVH CIKTTVENEL PPPENIEVIV
QNQNYVLKWD YTYANMTFQV QWLQNPGNHL YKWKQIRECE NVKATQCVFP QNIFQKGIYL
LRVQASDGKN TSFWSEEIKF DTEIQASLLP PVFNVRSLSD SLCISIGAPQ RSENKPVIQD
YPLIYEILFW ENTSKAERKI IEKKTDVTIP NLKPLTVYCV KARAHSMDEK LNKSSVFSDV
VCEETKSGNT SKIWLIIGIF TVLLALPFVI YAVKVLLRCI NYVFFPSLKP SSNIEEYFSE
QPLKNLLLLT SEEQIEKCFI IENISTIATV EETNQTDEDH KKYSSQTSQD SGNYSNEDES
ENKTSEELQQ DFI
//