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Database: UniProt
Entry: A0A2K6LNY3_RHIBE
LinkDB: A0A2K6LNY3_RHIBE
Original site: A0A2K6LNY3_RHIBE 
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
//
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