IFN_ANAPL
ID IFN_ANAPL Reviewed; 191 AA.
AC P51526;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Interferon;
DE Flags: Precursor;
GN Name=IFN;
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Embryo;
RX PubMed=7571434; DOI=10.1006/viro.1995.1522;
RA Schultz U., Koeck J., Schlicht H.J., Staeheli P.;
RT "Recombinant duck interferon: a new reagent for studying the mode of
RT interferon action against hepatitis B virus.";
RL Virology 212:641-649(1995).
CC -!- FUNCTION: Has antiviral activities.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: By viral infection.
CC -!- SIMILARITY: Belongs to the alpha/beta interferon family. {ECO:0000305}.
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DR EMBL; X84764; CAA59235.1; -; Genomic_DNA.
DR PIR; S57642; S57642.
DR AlphaFoldDB; P51526; -.
DR SMR; P51526; -.
DR Ensembl; ENSAPLT00020028982; ENSAPLP00020026913; ENSAPLG00020018289.
DR Ensembl; ENSAPLT00020028985; ENSAPLP00020026916; ENSAPLG00020018290.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR CDD; cd00095; IFab; 1.
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.
DR PROSITE; PS00252; INTERFERON_A_B_D; 1.
PE 2: Evidence at transcript level;
KW Antiviral defense; Cytokine; Disulfide bond; Glycoprotein; Secreted;
KW Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..191
FT /note="Interferon"
FT /id="PRO_0000016427"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..128
FT /evidence="ECO:0000250"
FT DISULFID 60..154
FT /evidence="ECO:0000255"
FT DISULFID 67..167
FT /evidence="ECO:0000250"
SQ SEQUENCE 191 AA; 21652 MW; 54D197AC899BB82F CRC64;
MPGPSAPPPP AIYSALALLL LLTPPANAFS CSPLRLHDSA FAWDSLQLLR NMAPSPTQPC
PQQHAPCSFP DTLLDTNDTQ QAAHTALHLL QHLFDTLSSP STPAHWLHTA RHDLLNQLQH
HIHHLERCFP ADAARLHRRG PRNLHLSINK YFGCIQHFLQ NHTYSPCAWD HVRLEAHACF
QRIHRLTRTM R