ID   ENV_QRFVE               Reviewed;         511 AA.
AC   D0QX25;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   23-FEB-2022, entry version 22.
DE   RecName: Full=Envelope glycoprotein;
DE   Flags: Precursor;
GN   OrderedLocusNames=Segment 5;
OS   Quaranfil virus (isolate QrfV/Tick/Afghanistan/EG_T_377/1968) (QRFV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Quaranjavirus.
OX   NCBI_TaxID=1559362;
OH   NCBI_TaxID=6939; Ixodidae (hardbacked ticks).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=19726499; DOI=10.1128/jvi.00677-09;
RA   Presti R.M., Zhao G., Beatty W.L., Mihindukulasuriya K.A., da Rosa A.P.,
RA   Popov V.L., Tesh R.B., Virgin H.W., Wang D.;
RT   "Quaranfil, Johnston Atoll, and Lake Chad viruses are novel members of the
RT   family Orthomyxoviridae.";
RL   J. Virol. 83:11599-11606(2009).
CC   -!- FUNCTION: Attaches the virus to host cellular receptor and later
CC       induces fusion of virion with host membrane. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255}; Single-pass
CC       membrane protein {ECO:0000255}.
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DR   EMBL; FJ861694; ACY56281.1; -; Genomic_RNA.
DR   SMR; D0QX25; -.
DR   Proteomes; UP000029941; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:InterPro.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019048; P:modulation by virus of host process; IEA:InterPro.
DR   InterPro; IPR004955; Baculovirus_Gp64.
DR   Pfam; PF03273; Baculo_gp64; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Virion.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..511
FT                   /note="Envelope glycoprotein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000443067"
FT   TOPO_DOM        17..487
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        488..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        506..511
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        422
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   511 AA;  57282 MW;  673A802778B5E1A9 CRC64;
     MFMVALSLLL LRLSTASPCT SEACSGPYRI SKYKMPTIDV SNHKTHVTVW KGPKEVTGIL
     GYRSRYTAYC YEGGVLDGNT GCTKWHVMFP PSAAELQKWA IDGKCYYGVE CNKGGDCWGS
     WADRCHDDRV DLNSAQEKEY NGNNDEWRMF AHHTCISTWR CGFSKSSYPI HFTNVKKGRG
     DGDITYTLAT YDQHGSILSL DKPSVKIDQE TTLSFELPRS LVSRSSTEID CFFGNDQTPV
     CQLNEHFEDL EGQFVTFNGD YTATYGNYLL ALNDKKAING SVGAKKFGNK AWVEKQLGKA
     ASLEDVRNIL SIQMWSHQES GYNLVQLYKV VGEMMNTLTT VINSVGKLDD ELIGRLIGVE
     GKSKWFNSEL FHMCPCFQLG SFGDSNCASG YIFSEGRVKV DKDGSKCTSF GGSITPLYLF
     DNVSYKFAVL HTPPAQGVAQ DWEGWSWLAA EKQRLIETMT FQDSVSGGNN VLSQLYKETL
     DSFNIWKWFE RFSTLAAWGA LAISVINMMR K