POLS_RRV2
ID POLS_RRV2 Reviewed; 422 AA.
AC P17517;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 29-SEP-2021, entry version 80.
DE RecName: Full=Structural polyprotein;
DE Contains:
DE RecName: Full=Spike glycoprotein E2;
DE AltName: Full=E2 envelope glycoprotein;
DE Flags: Fragment;
OS Ross river virus (strain 213970) (RRV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus.
OX NCBI_TaxID=11030;
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=162997; Culex annulirostris (Common banded mosquito).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9322; Macropus sp. (kangaroo).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2849242;
RA Burness A.T.H., Pardoe I., Faragher S.G., Vrati S., Dalgarno L.;
RT "Genetic stability of Ross River virus during epidemic spread in nonimmune
RT humans.";
RL Virology 167:639-643(1988).
CC -!- FUNCTION: Spike glycoprotein E2: Plays a role in viral attachment to
CC target host cell, by binding to the cell receptor. Synthesized as a p62
CC precursor which is processed by furin at the cell membrane just before
CC virion budding, giving rise to E2-E1 heterodimer. The p62-E1
CC heterodimer is stable, whereas E2-E1 is unstable and dissociate at low
CC pH. p62 is processed at the last step, presumably to avoid E1 fusion
CC activation before its final export to cell surface. E2 C-terminus
CC contains a transitory transmembrane that would be disrupted by
CC palmitoylation, resulting in reorientation of the C-terminal tail from
CC lumenal to cytoplasmic side. This step is critical since E2 C-terminus
CC is involved in budding by interacting with capsid proteins. This
CC release of E2 C-terminus in cytoplasm occurs lately in protein export,
CC and precludes premature assembly of particles at the endoplasmic
CC reticulum membrane. {ECO:0000250|UniProtKB:P03315}.
CC -!- SUBUNIT: Spike glycoprotein E2: Processing of the precursor of protein
CC E3/E2 into E2 and E3 results in a heterodimer of the spike
CC glycoproteins E2 and E1. Spike glycoprotein E2: Spike at virion surface
CC are constituted of three E2-E1 heterodimers. Spike glycoprotein E2:
CC Interacts with 6K protein. {ECO:0000250|UniProtKB:P03315,
CC ECO:0000250|UniProtKB:P03316}.
CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane
CC {ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein
CC {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:P03316};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8JUX5}.
CC -!- DOMAIN: Structural polyprotein: As soon as the capsid protein has been
CC autocleaved, an internal uncleaved signal peptide directs the remaining
CC polyprotein to the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield
CC mature proteins. Capsid protein is auto-cleaved during polyprotein
CC translation, unmasking a signal peptide at the N-terminus of the
CC precursor of E3/E2. The remaining polyprotein is then targeted to the
CC host endoplasmic reticulum, where host signal peptidase cleaves it into
CC pE2, 6K and E1 proteins. pE2 is further processed to mature E3 and E2
CC by host furin in trans-Golgi vesicle. {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: Spike glycoprotein E2: Palmitoylated via thioester bonds. These
CC palmitoylations may induce disruption of the C-terminus transmembrane.
CC This would result in the reorientation of E2 C-terminus from lumenal to
CC cytoplasmic side. {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: Spike glycoprotein E2: N-glycosylated.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- MISCELLANEOUS: Structural polyprotein: Translated from a subgenomic RNA
CC synthesized during togavirus replication.
CC {ECO:0000250|UniProtKB:Q86925}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M23709; AAA47406.1; -; Genomic_RNA.
DR PIR; B31833; VHWV70.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.2400; -; 1.
DR Gene3D; 2.60.40.3200; -; 1.
DR Gene3D; 2.60.40.4310; -; 1.
DR InterPro; IPR000936; Alpha_E2_glycop.
DR InterPro; IPR042304; Alphavir_E2_A.
DR InterPro; IPR042305; Alphavir_E2_B.
DR InterPro; IPR042306; Alphavir_E2_C.
DR Pfam; PF00943; Alpha_E2_glycop; 1.
PE 3: Inferred from homology;
KW Capsid protein; Glycoprotein; Host cell membrane; Host membrane;
KW Host-virus interaction; Lipoprotein; Membrane; Palmitate; RNA-binding;
KW T=4 icosahedral capsid protein; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Virion; Virus entry into host cell.
FT CHAIN 1..422
FT /note="Spike glycoprotein E2"
FT /id="PRO_0000041296"
FT TOPO_DOM 1..359
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 395..415
FT /note="Transient transmembrane before p62-6K protein
FT processing"
FT /evidence="ECO:0000255"
FT LIPID 385
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255"
FT LIPID 395
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT LIPID 416
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 422
SQ SEQUENCE 422 AA; 46660 MW; A70785E2A903B297 CRC64;
SVTEHFNVYK ATRPYXXXCA DCGDGYFCYS PVAIEKIRDE ASDGMLKIQV SAQIGLDKAG
THAHTKLRYM AGHDVQESKR DSLRVYTSAA CSIHGTMGHF IVAHCPPGDY LKVSFEDADS
HVKACKVQYK HNPLPVGREK FVVRPHFGVE LPCTSYQLTT APTDEEIDMH TPPDIPDRTL
LSQTAGNVKI TAGGRTIRYN CTWGRDNVGT TSTDKTINAC KIDQCHAAVT SHDKWQFTSP
FVPRADQTAR KGKVHVPFPL TNVTCRVPLA RAPDVTYGKK EVTLRLHPDH PTLFSYRSLG
AEPHPYEEWV DKFSERIIPV TEEGXEYQWG NNPPVRLWAX LTTEGKPHGW PHEIIQYYYG
LYPAATIAAV SGXSLMALLT LAATCCMLAT ARRKCLTPYA LTPGAVVPLT LGLXXCAPRA
NA
