IRA1B_ONCMY
ID IRA1B_ONCMY Reviewed; 388 AA.
AC K7NAJ3;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Interferon alpha/beta receptor 1b;
DE AltName: Full=Intracellular type I interferon receptor {ECO:0000312|EMBL:ADU04483.1};
DE Short=iIFNAR1 {ECO:0000303|PubMed:24244163};
GN Name=ifnar1b {ECO:0000303|PubMed:24244163};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000312|EMBL:ADU04483.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY POLY(I:C), AND
RP SUBCELLULAR LOCATION.
RX PubMed=24244163; DOI=10.1371/journal.ppat.1003736;
RA Chang M.X., Zou J., Nie P., Huang B., Yu Z., Collet B., Secombes C.J.;
RT "Intracellular interferons in fish: a unique means to combat viral
RT infection.";
RL PLoS Pathog. 9:E1003736-E1003736(2013).
CC -!- FUNCTION: Involved in antiviral response. Associates with IFNAR2 to
CC form the type I interferon receptor. In the presence of intracellular
CC IFNAR1 (IFNAR1B) and IFNA1 (iIFN1b isoform), may mediate STAT1 and
CC STAT2 phosphorylation and induction of EIF2AK2, MX1 and RSAD2.
CC {ECO:0000269|PubMed:24244163}.
CC -!- SUBUNIT: Heterodimer with IFNAR2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:24244163}. Note=Mainly detected in perinuclear
CC regions, when overexpressed in RTG-2 cell line.
CC {ECO:0000269|PubMed:24244163}.
CC -!- INDUCTION: In the fibroblastic RTG-2 cell line, induced by polyinosine-
CC polycytidylic acid (poly(I:C)), a synthetic analog of dsRNA, that binds
CC TLR3. {ECO:0000269|PubMed:24244163}.
CC -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC {ECO:0000305}.
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DR EMBL; GU319962; ADU04483.1; -; mRNA.
DR RefSeq; NP_001268321.1; NM_001281392.1.
DR AlphaFoldDB; K7NAJ3; -.
DR SMR; K7NAJ3; -.
DR GeneID; 101268957; -.
DR KEGG; omy:101268957; -.
DR OrthoDB; 892736at2759; -.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
DR GO; GO:0004905; F:type I interferon receptor activity; IMP:AgBase.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:AgBase.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015373; Interferon/interleukin_rcp_dom.
DR Pfam; PF09294; Interfer-bind; 1.
DR Pfam; PF01108; Tissue_fac; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; Receptor; Repeat.
FT CHAIN 1..388
FT /note="Interferon alpha/beta receptor 1b"
FT /id="PRO_0000432617"
FT DOMAIN 5..102
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 109..211
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 308..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 388 AA; 44137 MW; C8332A17FDF79511 CRC64;
MLAELPQPQN LTLLTLNTQY VLTWDWDQTT TGNSVSFTVE YMAKYKMKMK KKNWSRVCER
TTRTRCDLTG SDLHYLGMYV LRVRASADGV DSDWVNKDFC PDIDASLGPP SRAELAPVGN
LLDVTISDPL TSTQHSMKEH VLFLYYRILY WSRSDDPQGL KPKVLDSSNN LVTPPELEAW
AWYCVMIQSR YDYYNKTSSY TEPQCMQTEG DTPYGQIFLY FLVSMMVCFL LVLLSSYAFF
RFYRGLKNTF YPSIQLPAHI QEYLCDSSPG SDMPRLITAD SEAELCCDKL TICPEVVLLE
IHVPPPLTAP PSELEQDSGR HIRQDSGDSG IYSTEGGSAQ QGRSGGEPIR RDQEVDSWQT
LEQVKMEEMG RELADERDLD EGVVDVCV