ID A0A2Y9F6W6_PHYMC Unreviewed; 562 AA.
AC A0A2Y9F6W6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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|RefSeq:XP_007115989.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007115989.1};
RN [1] {ECO:0000313|RefSeq:XP_007115989.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007115989.1};
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 RefSeq; XP_007115989.1; XM_007115927.4.
DR AlphaFoldDB; A0A2Y9F6W6; -.
DR STRING; 9755.ENSPCTP00005004820; -.
DR GeneID; 102991034; -.
DR KEGG; pcad:102991034; -.
DR CTD; 3454; -.
DR InParanoid; A0A2Y9F6W6; -.
DR OrthoDB; 5320327at2759; -.
DR Proteomes; UP000248484; Chromosome 8.
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: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:0032496; P:response to lipopolysaccharide; IEA:UniProtKB-UniRule.
DR CDD; cd00063; FN3; 1.
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; 3.
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:UP000248484};
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..562
FT /note="Interferon alpha/beta receptor 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016008347"
FT TRANSMEM 441..464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 335..435
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 525..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 466
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 201..222
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-50"
FT DISULFID 285..293
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-50"
FT DISULFID 406..429
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-50"
FT CROSSLNK 528
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-51"
FT CROSSLNK 529
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000256|PIRSR:PIRSR016567-51"
SQ SEQUENCE 562 AA; 63710 MW; 6AE6C2FC7B92F212 CRC64;
MLALLGATTL MLVAGAPWVL PAASGGTNLK SPENGSVCII DDNFTLKWNS SSESVRNVTF
SAEYKIPGMD NWKKLPGCQH ITSTECNFSS VKLKNVYEKI ELRIRAEKGN NTSQWHEVKP
FIPFQKAQIG PPDVHLEAED KAIIINMSPP GTKDSIMWAM DHSSFTYSLV IWKNSSSLEE
RTETVYSRDK IYKLSPETTY CLKVKAELRS PRRVGVYSPV YCINTTEKHK VPSPENIQID
AENQVYVLKW DYAYENTTFR AQWSHEFLKR IPGGHSDKWK QIPNCEDVET THCVIPQNVF
PEGIHRIRVQ ASNGNNTSFW SEEKMFNTEM KTIIFPPVIS MKSVNDDSLH VSIGAPKESE
NKSVNQLYPL IYEVIFRENT SNAERKVVEK RTDFTFPNLK SLTVYCVKAR ALTENDKWNK
SSVFSDTVCE KTKPGNTSKT WLIAGICTAL FSIIVVIYVV KVLLRCINYV FFPSSKPPST
VDEYFSEQPV RNLLLSTSEE QTERCSIIEN ANSITVIEET NPIYEDPKKY NSQTSQDSGN
YSNEDENSGS KIGEELLPQE TV
//
