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Database: UniProt
Entry: P17517
LinkDB: P17517
Original site: P17517 
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   25-APR-2018, entry version 75.
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; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
OC   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
RT   nonimmune humans.";
RL   Virology 167:639-643(1988).
CC   -!- FUNCTION: Spike glycoprotein E2: Plays a role in viral attachment
CC       to target host cell, by binding to the cell receptor. Synthesized
CC       as a p62 precursor which is processed by furin at the cell
CC       membrane just before virion budding, giving rise to E2-E1
CC       heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is
CC       unstable and dissociate at low pH. p62 is processed at the last
CC       step, presumably to avoid E1 fusion activation before its final
CC       export to cell surface. E2 C-terminus contains a transitory
CC       transmembrane that would be disrupted by palmitoylation, resulting
CC       in reorientation of the C-terminal tail from lumenal to
CC       cytoplasmic side. This step is critical since E2 C-terminus is
CC       involved in budding by interacting with capsid proteins. This
CC       release of E2 C-terminus in cytoplasm occurs lately in protein
CC       export, and precludes premature assembly of particles at the
CC       endoplasmic reticulum membrane. {ECO:0000250|UniProtKB:P03315}.
CC   -!- SUBUNIT: Spike glycoprotein E2: Processing of the precursor of
CC       protein E3/E2 into E2 and E3 results in a heterodimer of the spike
CC       glycoproteins E2 and E1. Spike glycoprotein E2: Spike at virion
CC       surface are constituted of three E2-E1 heterodimers. Spike
CC       glycoprotein E2: Interacts with 6K protein.
CC       {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:P03316}.
CC   -!- SUBCELLULAR LOCATION: Spike glycoprotein E2: Virion membrane
CC       {ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane
CC       protein {ECO:0000255}. Host cell membrane
CC       {ECO:0000250|UniProtKB:P03316}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:Q8JUX5}.
CC   -!- DOMAIN: Structural polyprotein: As soon as the capsid protein has
CC       been autocleaved, an internal uncleaved signal peptide directs the
CC       remaining polyprotein to the endoplasmic reticulum.
CC       {ECO:0000250|UniProtKB:P03315}.
CC   -!- PTM: Structural polyprotein: Specific enzymatic cleavages in vivo
CC       yield mature proteins. Capsid protein is auto-cleaved during
CC       polyprotein translation, unmasking a signal peptide at the N-
CC       terminus of the precursor of E3/E2. The remaining polyprotein is
CC       then targeted to the host endoplasmic reticulum, where host signal
CC       peptidase cleaves it into pE2, 6K and E1 proteins. pE2 is further
CC       processed to mature E3 and E2 by host furin in trans-Golgi
CC       vesicle. {ECO:0000250|UniProtKB:P03315}.
CC   -!- PTM: Spike glycoprotein E2: Palmitoylated via thioester bonds.
CC       These palmitoylations may induce disruption of the C-terminus
CC       transmembrane. This would result in the reorientation of E2 C-
CC       terminus from lumenal to cytoplasmic side.
CC       {ECO:0000250|UniProtKB:P03315}.
CC   -!- PTM: Spike glycoprotein E2: N-glycosylated.
CC       {ECO:0000250|UniProtKB:P03315}.
CC   -!- MISCELLANEOUS: Structural polyprotein: Translated from a
CC       subgenomic RNA synthesized during togavirus replication.
CC       {ECO:0000250|UniProtKB:Q86925}.
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:0019028; C:viral capsid; IEA:InterPro.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
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   InterPro; IPR000936; Alpha_E2_glycop.
DR   Pfam; PF00943; Alpha_E2_glycop; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Host cell membrane; Host membrane;
KW   Host-virus interaction; Lipoprotein; Membrane; Palmitate;
KW   Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW   Virion; Virus entry into host cell.
FT   CHAIN         1    422       Spike glycoprotein E2.
FT                                /FTId=PRO_0000041296.
FT   TOPO_DOM      1    359       Extracellular. {ECO:0000255}.
FT   TRANSMEM    360    382       Helical. {ECO:0000255}.
FT   TOPO_DOM    383    422       Cytoplasmic. {ECO:0000255}.
FT   REGION      395    415       Transient transmembrane before p62-6K
FT                                protein processing. {ECO:0000255}.
FT   LIPID       385    385       S-palmitoyl cysteine; by host.
FT                                {ECO:0000255}.
FT   LIPID       395    395       S-palmitoyl cysteine; by host.
FT                                {ECO:0000250}.
FT   LIPID       416    416       S-palmitoyl cysteine; by host.
FT                                {ECO:0000250}.
FT   CARBOHYD    200    200       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   CARBOHYD    262    262       N-linked (GlcNAc...) asparagine; by host.
FT                                {ECO:0000255}.
FT   NON_TER       1      1
FT   NON_TER     422    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
//
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