FUS_ISAV8
ID FUS_ISAV8 Reviewed; 444 AA.
AC Q8V3T9;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 02-DEC-2020, entry version 43.
DE RecName: Full=Fusion glycoprotein F0;
DE AltName: Full=Protein 3;
DE Short=P3;
DE Contains:
DE RecName: Full=Fusion glycoprotein F1;
DE Contains:
DE RecName: Full=Fusion glycoprotein F2;
DE Flags: Precursor;
GN Name=Segment-5 {ECO:0000303|PubMed:20979983};
OS Infectious salmon anemia virus (isolate Atlantic salmon/Norway/810/9/99)
OS (ISAV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Isavirus.
OX NCBI_TaxID=652965;
OH NCBI_TaxID=8049; Gadus morhua (Atlantic cod).
OH NCBI_TaxID=8019; Oncorhynchus kisutch (Coho salmon) (Salmo kisutch).
OH NCBI_TaxID=8022; Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OH NCBI_TaxID=8060; Pollachius virens (Saithe) (Gadus virens).
OH NCBI_TaxID=8030; Salmo salar (Atlantic salmon).
OH NCBI_TaxID=8032; Salmo trutta (Brown trout).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11807235; DOI=10.1099/0022-1317-83-2-421;
RA Clouthier S.C., Rector T., Brown N.E., Anderson E.D.;
RT "Genomic organization of infectious salmon anaemia virus.";
RL J. Gen. Virol. 83:421-428(2002).
RN [2]
RP FUNCTION.
RX PubMed=16160182; DOI=10.1128/jvi.79.19.12544-12553.2005;
RA Aspehaug V., Mikalsen A.B., Snow M., Biering E., Villoing S.;
RT "Characterization of the infectious salmon anemia virus fusion protein.";
RL J. Virol. 79:12544-12553(2005).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=14990725; DOI=10.1128/jvi.78.6.3063-3071.2004;
RA Falk K., Aspehaug V., Vlasak R., Endresen C.;
RT "Identification and characterization of viral structural proteins of
RT infectious salmon anemia virus.";
RL J. Virol. 78:3063-3071(2004).
RN [4]
RP REVIEW.
RX PubMed=20979983; DOI=10.1016/j.virusres.2010.10.021;
RA Cottet L., Rivas-Aravena A., Cortez-San Martin M., Sandino A.M.,
RA Spencer E.;
RT "Infectious salmon anemia virus--genetics and pathogenesis.";
RL Virus Res. 155:10-19(2011).
RN [5]
RP INTERACTION WITH HEMAGGLUTININ ESTERASE.
RX PubMed=24486627; DOI=10.1099/vir.0.061648-0;
RA Fourrier M., Lester K., Thoen E., Mikalsen A., Evensen O., Falk K.,
RA Collet B., McBeath A.;
RT "Deletions in the highly polymorphic region (HPR) of infectious salmon
RT anaemia virus HPR0 haemagglutinin-esterase enhance viral fusion and
RT influence the interaction with the fusion protein.";
RL J. Gen. Virol. 95:1015-1024(2014).
RN [6]
RP FUNCTION.
RX PubMed=26082488; DOI=10.1074/jbc.m115.644781;
RA Cook J.D., Soto-Montoya H., Korpela M.K., Lee J.E.;
RT "Electrostatic architecture of the infectious salmon anemia virus (ISAV)
RT core fusion protein illustrates a carboxyl-carboxylate pH sensor.";
RL J. Biol. Chem. 290:18495-18504(2015).
CC -!- FUNCTION: Class I viral fusion protein. Under the current model, the
CC protein has at least 3 conformational states: pre-fusion native state,
CC pre-hairpin intermediate state, and post-fusion hairpin state. During
CC viral and target cell membrane fusion, the heptad repeat (HR) regions
CC assume a trimer-of-hairpins structure, positioning the fusion peptide
CC in close proximity to the C-terminal region of the ectodomain. The
CC formation of this structure appears to drive apposition and subsequent
CC fusion of viral and target cell membranes. Directs fusion of viral and
CC cellular membranes leading to delivery of the nucleocapsid into the
CC cytoplasm. The trimer of F1-F2 (F protein) probably interacts with HE
CC at the virion surface. Upon HE binding to its cellular receptor, the
CC hydrophobic fusion peptide is unmasked and interacts with the cellular
CC membrane, inducing the fusion between cell and virion membranes.
CC {ECO:0000269|PubMed:16160182, ECO:0000269|PubMed:26082488}.
CC -!- SUBUNIT: Homotrimer of disulfide-linked F1-F2 (PubMed:16160182).
CC Interacts with Hemagglutinin esterase (PubMed:24486627).
CC {ECO:0000269|PubMed:16160182, ECO:0000269|PubMed:24486627}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:14990725}.
CC Host membrane {ECO:0000305}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- PTM: The inactive precursor F0 is glycosylated and proteolytically
CC cleaved into F1 and F2 to be functionally active. The cleavage is
CC mediated by cellular proteases during the transport and maturation of
CC the polypeptide. {ECO:0000269|PubMed:16160182}.
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DR EMBL; AF404343; AAL67959.1; -; Viral_cRNA.
DR RefSeq; YP_145801.1; NC_006500.2.
DR SMR; Q8V3T9; -.
DR GeneID; 3170815; -.
DR KEGG; vg:3170815; -.
DR Proteomes; UP000008772; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR025167; Fusion_F0_Isavirus.
DR Pfam; PF13044; Fusion_F0; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Host membrane; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Virion.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..444
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000403919"
FT CHAIN 18..276
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000403920"
FT CHAIN 277..444
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000403921"
FT TOPO_DOM 18..413
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 277..292
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT SITE 276..277
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 444 AA; 48773 MW; 388C3090B65C8D41 CRC64;
MAFLTILVLF LFKEVLCEPC ICENPTCLGI TIPQAGFVRS APGGVLLTET ITERPQLTEW
TTSRPKLEET LWLDGETKNG KVSQTLFEAI QGTQMENCAV KAVLDTTFVN LTKQDIVLGK
IKVSEFGGDS DISKCGRKGL KVFICGGTVG YVTRGCPPEE CKGKKGRMMA LEPTTDCGVE
KGLTTDRIKT GMLDITSCCT QHGCTKGIRV EVPSPVLVSS KCQEVTFRVV PFHSVPDKLG
FARTSSFTLK ANFVNKHGWS KYNFNLRGFP GEEFIKCCGF TLGVGGAWFQ AYLNGMVQGD
GAASADDVKE KLNGIIDQIN KANTLLEGEI EAVRRIAYMN QASSLQNQVE IGLIGEYLNI
SSWLETTTLT KTEEGLMKNG WCQSNTHCWC PPKPTIVPTI GYVDSIKEVT GTSWWMVMIH
YIIVGLIVIV VVVFGLKLWG CLRR
