IFNA3_ONCMY
ID IFNA3_ONCMY Reviewed; 175 AA.
AC P0DMS7; A8E0J5; B6UQB2; T2K1L7;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Interferon a3 {ECO:0000303|PubMed:25080482};
DE AltName: Full=Type I interferon 1 {ECO:0000303|PubMed:17785823};
DE Short=rtIFN1 {ECO:0000303|PubMed:17785823};
DE AltName: Full=Type I interferon a3 {ECO:0000303|PubMed:25080482};
DE Short=IFN1-a3;
DE Flags: Precursor;
GN Name=ifna3 {ECO:0000303|PubMed:25080482};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17785823; DOI=10.4049/jimmunol.179.6.3859;
RA Zou J., Tafalla C., Truckle J., Secombes C.J.;
RT "Identification of a second group of type I IFNs in fish sheds light on IFN
RT evolution in vertebrates.";
RL J. Immunol. 179:3859-3871(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP INDUCTION BY POLY(I:C) AND IHNV.
RX PubMed=19070666; DOI=10.1016/j.fsi.2008.11.012;
RA Purcell M.K., Laing K.J., Woodson J.C., Thorgaard G.H., Hansen J.D.;
RT "Characterization of the interferon genes in homozygous rainbow trout
RT reveals two novel genes, alternate splicing and differential regulation of
RT duplicated genes.";
RL Fish Shellfish Immunol. 26:293-304(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERFERON NOMENCLATURE.
RX PubMed=25080482; DOI=10.4049/jimmunol.1301796;
RA Zou J., Gorgoglione B., Taylor N.G., Summathed T., Lee P.T., Panigrahi A.,
RA Genet C., Chen Y.M., Chen T.Y., Ul Hassan M., Mughal S.M., Boudinot P.,
RA Secombes C.J.;
RT "Salmonids have an extraordinary complex type I IFN system:
RT characterization of the IFN locus in rainbow trout oncorhynchus mykiss
RT reveals two novel IFN subgroups.";
RL J. Immunol. 193:2273-2286(2014).
RN [4]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), INDUCTION BY
RP POLY(I:C) AND VHSV, AND SUBCELLULAR LOCATION (ISOFORMS 1; 2 AND 3).
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: Key player in antiviral response. Induces expression of TLRs,
CC including that of TLR3, TLR9 and TLR8a1, and that of cytosolic pattern
CC recognition receptors, including DDX58/RIG-1, IFIH1/MDA5 and
CC DHX58/LGP2. Also induces MX1 and its own expression. In the presence of
CC intracellular IFNAR2 (iIFNAR2) and IFNAR1B, intracellular isoform 3 may
CC mediate STAT1 and STAT2 phosphorylation and induction of EIF2AK2, MX1
CC and RSAD2. {ECO:0000269|PubMed:24244163}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted
CC {ECO:0000305|PubMed:24244163}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:24244163}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:24244163}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Secreted IFN1, sIFN1, IFN1 short
CC {ECO:0000303|PubMed:19070666, ECO:0000303|PubMed:24244163};
CC IsoId=P0DMS7-1; Sequence=Displayed;
CC Name=2; Synonyms=Intracellular IFN1a, iIFN1a, IFN1 long
CC {ECO:0000303|PubMed:19070666, ECO:0000303|PubMed:24244163};
CC IsoId=P0DMS7-2; Sequence=VSP_057532;
CC Name=3; Synonyms=Intracellular IFN1b, iIFN1b
CC {ECO:0000303|PubMed:24244163};
CC IsoId=P0DMS7-3; Sequence=VSP_057533;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in several
CC tissues, including gill, spleen, intestine, kidney and skin.
CC {ECO:0000269|PubMed:19070666}.
CC -!- INDUCTION: In the RTG-2 fibroblastic cell line, isoform 1 is highly
CC induced by polyinosine-polycytidylic acid (poly(I:C)), a synthetic
CC analog of dsRNA, that binds TLR3. Isoforms 2 and 3 are also up-
CC regulated by poly(I:C), but to a lesser extent. In vivo, all 3 isoforms
CC are induced by poly(I:C) (in anterior kidney leukocytes) and by viral
CC infection, such as that of viral hemorrhagic septicemia virus (VHSV)
CC (isoform 1>isoform 3>>isoform 2) and infectious hematopoietic necrosis
CC virus (IHNV). However, induction kinetics is isoform-specific. Also up-
CC regulated in vivo by a DNA vaccine based on the IHNV glycoprotein.
CC {ECO:0000269|PubMed:19070666, ECO:0000269|PubMed:24244163}.
CC -!- MISCELLANEOUS: Salmonid type I IFNs are classified into 2 groups with 2
CC (group I) or 4 (group II) cysteines in the mature peptide. These groups
CC can be further divided into 3 subgroups (group I IFN1-a, IFN1-d and
CC IFN1-e and group II IFN1-b, IFN1-c and IFN1-f). Each subgroup can be
CC represented by several genes (up to at least 7 for IFN1-e).
CC {ECO:0000305|PubMed:25080482}.
CC -!- SIMILARITY: Belongs to the alpha/beta interferon family.
CC {ECO:0000255|RuleBase:RU000436}.
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DR EMBL; AM489415; CAM28538.1; -; Genomic_DNA.
DR EMBL; FJ184370; ACJ03566.1; -; mRNA.
DR EMBL; FJ184371; ACJ03567.1; -; mRNA.
DR EMBL; HF931021; CCV17397.1; -; Genomic_DNA.
DR AlphaFoldDB; P0DMS7; -.
DR SMR; P0DMS7; -.
DR OrthoDB; 1358010at2759; -.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0005132; F:type I interferon receptor binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IDA:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:AgBase.
DR GO; GO:0060337; P:type I interferon signaling pathway; IMP:AgBase.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR000471; Interferon_alpha/beta/delta.
DR InterPro; IPR015588; Interferon_beta.
DR PANTHER; PTHR11691; PTHR11691; 1.
DR PANTHER; PTHR11691:SF68; PTHR11691:SF68; 1.
DR Pfam; PF00143; Interferon; 1.
DR SMART; SM00076; IFabd; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Antiviral defense; Cytokine; Cytoplasm;
KW Disulfide bond; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..175
FT /note="Interferon a3"
FT /id="PRO_0000432615"
FT DISULFID 24..120
FT /evidence="ECO:0000305|PubMed:25080482"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305|PubMed:24244163"
FT /id="VSP_057532"
FT VAR_SEQ 1..16
FT /note="MYTMQSWSCIFLIICS -> MRRGRHGIPSATCASPENESPRLR (in
FT isoform 3)"
FT /evidence="ECO:0000305|PubMed:24244163"
FT /id="VSP_057533"
FT CONFLICT 160
FT /note="I -> M (in Ref. 1; ACJ03566/ACJ03567 and 2;
FT CAM28538)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 175 AA; 20847 MW; 056A211C5BFFDF66 CRC64;
MYTMQSWSCI FLIICSMQSV CHCCDWIRHH YGHLSAEYLS LLDQMGGDIT KQNAPVLFPT
SLYRHIDDAE FEDKVIFLKE TIYQITKLFD GNMKSVTWDK KNLDDFLNIL ERQLENLNSC
VSPAMKPERR LKRYFKKLNS KVLRKMNYSA QAWELIRKEI KRHLQRLDIL AAQMY
