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 27-MAR-2024, entry version 23.
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: Together with IFNAR1, forms the heterodimeric receptor for
CC type I interferons (including interferons alpha, beta, epsilon, omega
CC and kappa) (PubMed:24244163). Type I interferon binding activates the
CC JAK-STAT signaling cascade, resulting in transcriptional activation or
CC repression of interferon-regulated genes that encode the effectors of
CC the interferon response. Mechanistically, type I interferon-binding
CC brings the IFNAR1 and IFNAR2 subunits into close proximity with one
CC another, driving their associated Janus kinases (JAKs) (TYK2 bound to
CC IFNAR1 and JAK1 bound to IFNAR2) to cross-phosphorylate one another.
CC The activated kinases phosphorylate specific tyrosine residues on the
CC intracellular domains of IFNAR1 and IFNAR2, forming docking sites for
CC the STAT transcription factors (STAT1, STAT2 and STAT). STAT proteins
CC are then phosphorylated by the JAKs, promoting their translocation into
CC the nucleus to regulate expression of interferon-regulated genes (By
CC similarity). {ECO:0000250|UniProtKB:P48551,
CC ECO:0000269|PubMed:24244163}.
CC -!- SUBUNIT: Heterodimer with IFNAR1; forming the receptor for type I
CC interferon. {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 Proteomes; UP000694395; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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-mediated signaling pathway; IMP:AgBase.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR20859:SF53; CYTOKINE RECEPTOR FAMILY MEMBER B6-RELATED; 1.
DR PANTHER; PTHR20859; INTERFERON/INTERLEUKIN RECEPTOR; 1.
DR Pfam; PF09294; Interfer-bind; 1.
DR Pfam; PF01108; Tissue_fac; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 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
//
