ID   INRA2_ONCMY             Reviewed;         268 AA.
AC   V5JFY4; V5JFP7;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Interferon alpha/beta receptor 2;
DE   AltName: Full=Type I interferon receptor 2;
DE   Flags: Precursor;
GN   Name=ifnar2 {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:AGO14284.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INDUCTION BY POLY(I:C),
RP   FUNCTION, AND 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: Associates with IFNAR1 to form the plasma membrane receptor
CC       in the type I interferon signaling pathway. In the presence of
CC       intracellular IFNAR2 (iIFNAR2) and IFNA1 (iIFN1b isoform), may mediate
CC       STAT1 and STAT2 phosphorylation and induction of EIF2AK2, MX1 and
CC       RSAD2. {ECO:0000269|PubMed:24244163}.
CC   -!- SUBUNIT: Heterodimer with IFNAR1. {ECO:0000250|UniProtKB:P48551}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC       {ECO:0000305|PubMed:24244163}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC       {ECO:0000305|PubMed:24244163}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Membrane-associated interferon receptor 2, mIFNAR2
CC       {ECO:0000303|PubMed:24244163};
CC         IsoId=V5JFY4-1; Sequence=Displayed;
CC       Name=2; Synonyms=Intracellular interferon receptor 2, iIFNAR2
CC       {ECO:0000303|PubMed:24244163};
CC         IsoId=V5JFY4-2; Sequence=VSP_057534;
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; JX532086; AGO14284.1; -; mRNA.
DR   EMBL; JX532087; AGO14285.1; -; mRNA.
DR   AlphaFoldDB; V5JFY4; -.
DR   SMR; V5JFY4; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IC:AgBase.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004905; F:type I interferon receptor activity; IMP:AgBase.
DR   GO; GO:0060337; P:type I interferon signaling pathway; IMP:AgBase.
DR   Gene3D; 2.60.40.10; -; 1.
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   Alternative splicing; Cell membrane; Cytoplasm; Disulfide bond; Membrane;
KW   Receptor; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..268
FT                   /note="Interferon alpha/beta receptor 2"
FT                   /id="PRO_0000432618"
FT   TOPO_DOM        17..223
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        245..268
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          18..114
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          115..217
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DISULFID        65..74
FT                   /evidence="ECO:0000250|UniProtKB:P48551"
FT   DISULFID        191..211
FT                   /evidence="ECO:0000250|UniProtKB:P48551"
FT   VAR_SEQ         1..105
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305|PubMed:24244163"
FT                   /id="VSP_057534"
FT   CONFLICT        130
FT                   /note="P -> L (in Ref. 1; AGO14285)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   268 AA;  29459 MW;  ECB67D7A8D533924 CRC64;
     MGPWTLLLLH LPLVVSMLPA PTNVSIVSFN LEHTLTWLPG PETPDNTHFT VQSLRKNSWQ
     LVKGCARLKT RQSCDLTNTF KDPFYHYKAR VQAITTTQKS NRSLSMLFYP LTDTLLGPPV
     VSVSGCGNCP LLQVTPPTSR GLQRSLSPTQ LYYRQFTCKV RRTRDGSQFS MWVTSTEKTV
     IGYLEPGAEY CVTVTPSTSF NPHSVPSEPH CAFTSPTAAN TVPVVLSVLC AFSLLVVLLC
     GIVVYSGRLL CMHKPLPKTL SSVPLCGG