POLG_LIVK
ID POLG_LIVK Reviewed; 496 AA.
AC P35765;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 07-OCT-2020, entry version 102.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Envelope protein E;
DE Flags: Fragment;
OS Louping ill virus (strain K) (Li).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Flavivirus.
OX NCBI_TaxID=36387;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH NCBI_TaxID=34878; Cervinae.
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=34613; Ixodes ricinus (Common tick) (Acarus ricinus).
OH NCBI_TaxID=9940; Ovis aries (Sheep).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8380831; DOI=10.1099/0022-1317-74-1-109;
RA Gao G.F., Jiang W.R., Hussain M.H., Venugopal K., Gritsun T.S., Reid H.W.,
RA Gould E.A.;
RT "Sequencing and antigenic studies of a Norwegian virus isolated from
RT encephalomyelitic sheep confirm the existence of louping ill virus outside
RT Great Britain and Ireland.";
RL J. Gen. Virol. 74:109-114(1993).
CC -!- FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and
CC mediates fusion between viral and cellular membranes. Envelope protein
CC is synthesized in the endoplasmic reticulum in the form of heterodimer
CC with protein prM. They play a role in virion budding in the ER, and the
CC newly formed immature particle is covered with 60 spikes composed of
CC heterodimer between precursor prM and envelope protein E. The virion is
CC transported to the Golgi apparatus where the low pH causes dissociation
CC of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is
CC ineficient, and many virions are only partially matured. These
CC uncleaved prM would play a role in immune evasion.
CC {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBUNIT: [Envelope protein E]: Homodimer; in the endoplasmic reticulum
CC and Golgi. {ECO:0000250|UniProtKB:P17763}.
CC -!- SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane
CC {ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein
CC {ECO:0000255}. Note=ER membrane retention is mediated by the
CC transmembrane domains. {ECO:0000250|UniProtKB:P03314}.
CC -!- PTM: [Envelope protein E]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P17763}.
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DR EMBL; D12935; BAA02311.1; -; Genomic_RNA.
DR PIR; JQ1883; JQ1883.
DR SMR; P35765; -.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd12149; Flavi_E_C; 1.
DR Gene3D; 1.20.1280.260; -; 1.
DR Gene3D; 2.60.40.350; -; 1.
DR Gene3D; 2.60.98.10; -; 1.
DR Gene3D; 3.30.387.10; -; 1.
DR Gene3D; 3.30.67.10; -; 1.
DR InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
DR InterPro; IPR027287; Flavi_E_Ig-like.
DR InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
DR InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR InterPro; IPR011998; Glycoprot_cen/dimer.
DR InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR InterPro; IPR013756; GlyE_cen_dom_subdom2.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF02832; Flavi_glycop_C; 1.
DR Pfam; PF00869; Flavi_glycoprot; 1.
DR SUPFAM; SSF56983; SSF56983; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PE 3: Inferred from homology;
KW Clathrin-mediated endocytosis of virus by host;
KW Cleavage on pair of basic residues; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host endoplasmic reticulum; Host membrane; Host-virus interaction;
KW Membrane; Suppressor of RNA silencing; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell; Zinc.
FT CHAIN <1..>496
FT /note="Genome polyprotein"
FT /id="PRO_0000405184"
FT CHAIN 1..496
FT /note="Envelope protein E"
FT /evidence="ECO:0000250|UniProtKB:P06935"
FT /id="PRO_0000037832"
FT TOPO_DOM <1..447
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..>496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 98..111
FT /note="Fusion peptide"
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 3..30
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT DISULFID 60..121
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 60..116
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT DISULFID 74..105
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT DISULFID 92..121
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT DISULFID 92..116
FT /evidence="ECO:0000250|UniProtKB:P17763"
FT DISULFID 186..290
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT DISULFID 307..338
FT /evidence="ECO:0000250|UniProtKB:P14336"
FT NON_TER 1
FT NON_TER 496
SQ SEQUENCE 496 AA; 53632 MW; 0652418F831E392F CRC64;
SRCTHLENRD FVTGTQGTTR VTLVLELGGC VTITAEGKPS MDVWLDAIYQ ESPAKTREYC
LHAKLSETKV AARCPTMGPA VLTEERQIGT VCKRDQSDRG WGNHCGLFGK GSIVACVKAA
CEAKKKATGY VYDANKIVYT VKVEPHTGDY VAANETHKGR KTATFTVSSE KTILTLGEYG
DVSLLCRVAS GVDLAQTIIL ELDKTAEHLP TAWQVHRDWF NDLALPWKHD GNPHWNNAER
LVEFGAPHAV KMDVYNLGDQ TGVLLKALAG VPVAHIEGNK YHLKSGHVTC EVGLEKLKMK
GLTYTMCDKS KFAWKRTPTD SGHDTVVMEV TFSGSKPCRI PVRAVAHGSP DVNVAMLITP
NPTIENDGGG FIEMQLPPGD NIIYVGELSH QWFQTGSSIG RVFQTTRKGI ERLTVIGEHA
WDFGSAGGFF SSIGKAVHTV LGGAFNSIFG GVGFLPKLLM GVALAWLGLN TRNPTMSMSF
LLAGGLVLAM TLGVGA
