ID   IRA1A_ONCMY             Reviewed;         405 AA.
AC   K7NA32;
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 1a;
DE   AltName: Full=Membrane-associated type I interferon receptor {ECO:0000312|EMBL:ADU04482.1};
DE            Short=mIFNAR1 {ECO:0000303|PubMed:24244163};
DE   AltName: Full=Type I interferon receptor 1a;
DE   Flags: Precursor;
GN   Name=ifnar1a {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:ADU04482.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY POLY(I:C).
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. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with IFNAR2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
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; GU319961; ADU04482.1; -; mRNA.
DR   RefSeq; NP_001268239.1; NM_001281310.1.
DR   AlphaFoldDB; K7NA32; -.
DR   SMR; K7NA32; -.
DR   GeneID; 101867533; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0060337; P:type I interferon signaling pathway; 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.
DR   PROSITE; PS50853; FN3; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Membrane; Receptor; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..405
FT                   /note="Interferon alpha/beta receptor 1a"
FT                   /id="PRO_0000432616"
FT   TOPO_DOM        21..233
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..405
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          22..123
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          126..228
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          325..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        75..83
FT                   /evidence="ECO:0000255"
FT   DISULFID        201..222
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   405 AA;  46095 MW;  2F465EE50E86A0E0 CRC64;
     MKVGFALVLL WSLPITNVLA ELPQPQNLTL LTLNTQYVLT WDWDQTTTGN SVSFTVEYMA
     KYKMKMKKKN WSRVCERTTR TRCDLTGSDL HYLGMYVLRV RASADGVNSD WVNKDFCPDI
     DASLGPPSRV ELAPVGNLLD VTISDPLTST QHSMKEHVLF LYYRILYWSR SDDPQGLKPK
     VLDSSNNLVT LPELEAWTWY CVMIQSRYDY YNKTSSYTEP QCMQTEGDTP YGQIFLYFLV
     SMMVCFLLVL LSSYAFFRFY RGLKNTFYPS IQLPAHIQEY LCDSSPGSDM PRLITADSEA
     ELCCDKLTIC PEVVLLEIHV PPPLTAPPSE LEQDSGRRIR QDSGDSGIYS TEGGSAQQGR
     SGGEPIRRDQ EVDSWQTLEQ VKMEEMGREL ADERDLDEGV VDICV