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Structural polyprotein (p110) [Cleaved into: Capsid protein (Coat protein) (C); Spike glycoprotein E2 (E2 envelope glycoprotein); Spike glycoprotein E1 (E1 envelope glycoprotein)]

 POLS_RUBVT              Reviewed;        1063 AA.
P07566;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
28-MAR-2018, entry version 100.
RecName: Full=Structural polyprotein;
AltName: Full=p110;
Contains:
RecName: Full=Capsid protein;
AltName: Full=Coat protein;
Short=C;
Contains:
RecName: Full=Spike glycoprotein E2;
AltName: Full=E2 envelope glycoprotein;
Contains:
RecName: Full=Spike glycoprotein E1;
AltName: Full=E1 envelope glycoprotein;
Rubella virus (strain Therien) (RUBV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Togaviridae; Rubivirus.
NCBI_TaxID=11045;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2353453; DOI=10.1016/0042-6822(90)90476-8;
Dominguez G., Wang C.Y., Frey T.K.;
"Sequence of the genome RNA of rubella virus: evidence for genetic
rearrangement during togavirus evolution.";
Virology 177:225-238(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-621.
PubMed=2836271; DOI=10.1016/0378-1119(88)90582-3;
Frey T.K., Marr L.D.;
"Sequence of the region coding for virion proteins C and E2 and the
carboxy terminus of the nonstructural proteins of rubella virus:
comparison with alphaviruses.";
Gene 62:85-99(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 551-1063.
PubMed=3755848; DOI=10.1016/0042-6822(86)90446-0;
Frey T.K., Marr L.D., Hemphill M.L., Dominguez G.;
"Molecular cloning and sequencing of the region of the rubella virus
genome coding for glycoprotein E1.";
Virology 154:228-232(1986).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-319.
PubMed=3351478; DOI=10.1099/0022-1317-69-3-603;
Takkinen K., Vidgren G., Ekstrand J., Hellman U., Kalkkinen N.,
Wernstedt C., Pettersson R.F.;
"Nucleotide sequence of the rubella virus capsid protein gene reveals
an unusually high G/C content.";
J. Gen. Virol. 69:603-612(1988).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 278-1063.
PubMed=3655744; DOI=10.1099/0022-1317-68-9-2347;
Vidgren G., Takkinen K., Kalkkinen N., Kaeaeriaeinen L.,
Pettersson R.F.;
"Nucleotide sequence of the genes coding for the membrane
glycoproteins E1 and E2 of rubella virus.";
J. Gen. Virol. 68:2347-2357(1987).
[6]
OLIGOMERIZATION.
PubMed=1962452; DOI=10.1016/0042-6822(91)90552-M;
Baron M.D., Forsell K.;
"Oligomerization of the structural proteins of rubella virus.";
Virology 185:811-819(1991).
[7]
DISULFIDE BOND.
PubMed=9143273; DOI=10.1006/viro.1997.8462;
Gros C., Linder M., Wengler G., Wengler G.;
"Analyses of disulfides present in the rubella virus E1
glycoprotein.";
Virology 230:179-186(1997).
[8]
FUNCTION.
PubMed=15557740; DOI=10.1111/j.1348-0421.2004.tb03614.x;
Kee S.H., Cho E.J., Song J.W., Park K.S., Baek L.J., Song K.J.;
"Effects of endocytosis inhibitory drugs on rubella virus entry into
VeroE6 cells.";
Microbiol. Immunol. 48:823-829(2004).
-!- FUNCTION: Capsid protein: Capsid protein interacts with genomic
RNA and assembles into icosahedric core particles. The resulting
nucleocapsid eventually associates with the cytoplasmic domain of
E2 at the cell membrane, leading to budding and formation of
mature virions. Phosphorylation negatively regulates RNA-binding
activity, possibly delaying virion assembly during the viral
replication phase. Capsid protein dimerizes and becomes disulfide-
linked in the virion, but this interaction seems not to be
important for its biological function. Modulates genomic RNA
replication. Modulates subgenomic RNA synthesis by interacting
with human C1QBP/SF2P32. Induces both perinuclear clustering of
mitochondria and the formation of electron-dense
intermitochondrial plaques, both hallmarks of rubella virus
infected cells. Induces apoptosis when expressed in transfected
cells. {ECO:0000250|UniProtKB:P08563}.
-!- FUNCTION: Spike glycoprotein E2: Responsible for viral attachment
to target host cell, by binding to the cell receptor. Its
transport to the plasma membrane depends on interaction with E1
protein. {ECO:0000250|UniProtKB:P08563}.
-!- FUNCTION: Spike glycoprotein E1: Class II viral fusion protein.
Fusion activity is inactive as long as E1 is bound to E2 in mature
virion. After virus attachment to target cell and clathrin-
mediated endocytosis, acidification of the endosome would induce
dissociation of E1/E2 heterodimer and concomitant trimerization of
the E1 subunits. This E1 homotrimer is fusion active, and promotes
release of viral nucleocapsid in cytoplasm after endosome and
viral membrane fusion (By similarity). E1 cytoplasmic tail
modulates virus release, and the tyrosines residues are critical
for this function. {ECO:0000250|UniProtKB:P08563}.
-!- SUBUNIT: Capsid protein: Homooligomer. Forms a dimer shortly after
synthesis, this dimer become disulfide-linked in the virion.
Interacts with human C1QBP. Spike glycoprotein E1: Heterodimer
with spike glycoprotein E2. Spike glycoprotein E2: Heterodimer
with spike glycoprotein E1. {ECO:0000250|UniProtKB:P08563}.
-!- SUBCELLULAR LOCATION: Capsid protein: Virion {ECO:0000250}. Host
cytoplasm {ECO:0000250}. Host mitochondrion {ECO:0000250}.
Note=The capsid protein is concentrated around Golgi region.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Spike glycoprotein E2: Virion membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Host Golgi apparatus membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}. Note=E1 and E2 form heterodimer in
the endoplasmic reticulum before they are transported to and
retained in the Golgi complex, where virus assembly occurs. E1
possesses an endoplasmic reticulum retention signal, and
unassembled E2 and E1 subunits are retained in the endoplasmic
reticulum. Presumably, assembly of E2 and E1 would mask the
signal, thereby allowing transport of the heterodimer to the Golgi
complex (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Spike glycoprotein E1: Virion membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Host Golgi apparatus membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}. Note=E1 and E2 form heterodimer in
the endoplasmic reticulum before they are transported to and
retained in the Golgi complex, where virus assembly occurs. E1
possesses an endoplasmic reticulum retention signal, and
unassembled E2 and E1 subunits are retained in the endoplasmic
reticulum. Presumably, assembly of E2 and E1 would mask the
signal, thereby allowing transport of the heterodimer to the Golgi
complex (By similarity). {ECO:0000250}.
-!- DOMAIN: Structural polyprotein: Contains two internal signal
peptides that are necessary for directing translocation of the
glycoproteins into the lumen of the endoplasmic reticulum.
{ECO:0000250|UniProtKB:P08563}.
-!- PTM: Structural polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. Two signal peptidase-mediated cleavages
within the polyprotein produce the structural proteins capsid, E2,
and E1. The E2 signal peptide remains attached to the C-terminus
of the capsid protein after cleavage by the signal peptidase.
Another signal peptide at E2 C-terminus directs E1 to the ER, with
a similar mechanism. {ECO:0000250|UniProtKB:P08563}.
-!- MISCELLANEOUS: Structural polyprotein: Translated from a
subgenomic RNA synthesized during togaviruses replication.
{ECO:0000250|UniProtKB:Q6X2U3}.
-----------------------------------------------------------------------
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EMBL; M15240; AAA88529.1; -; Genomic_RNA.
EMBL; D00242; BAA00172.1; -; Genomic_RNA.
EMBL; D00156; BAA28178.1; -; Genomic_RNA.
PIR; A24309; A24309.
PIR; A29822; GNWVR4.
RefSeq; NP_062884.1; NC_001545.2.
PDB; 5KHE; EM; 35.00 A; A/B=9-277.
PDB; 5KHF; EM; 35.00 A; A/B=9-277.
PDBsum; 5KHE; -.
PDBsum; 5KHF; -.
SMR; P07566; -.
IntAct; P07566; 2.
GeneID; 1502162; -.
KEGG; vg:1502162; -.
OrthoDB; VOG0900007P; -.
Proteomes; UP000000571; Genome.
GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0019013; C:viral nucleocapsid; IEA:InterPro.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR008819; Rubella_Capsid.
InterPro; IPR008820; Rubella_E1.
InterPro; IPR008821; Rubella_E2.
Pfam; PF05750; Rubella_Capsid; 1.
Pfam; PF05748; Rubella_E1; 1.
Pfam; PF05749; Rubella_E2; 1.
1: Evidence at protein level;
3D-structure; Capsid protein;
Clathrin-mediated endocytosis of virus by host; Complete proteome;
Disulfide bond; Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cytoplasm; Host Golgi apparatus; Host membrane;
Host mitochondrion; Host-virus interaction; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Reference proteome; RNA-binding;
T=4 icosahedral capsid protein; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral envelope protein;
Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 300 Capsid protein.
/FTId=PRO_0000041308.
CHAIN 301 582 Spike glycoprotein E2.
/FTId=PRO_0000041309.
CHAIN 583 1063 Spike glycoprotein E1.
/FTId=PRO_0000041310.
TOPO_DOM 301 534 Extracellular. {ECO:0000255}.
TRANSMEM 535 555 Helical; Note=Golgi retention signal.
{ECO:0000255}.
TOPO_DOM 556 582 Cytoplasmic. {ECO:0000255}.
TOPO_DOM 583 1028 Extracellular. {ECO:0000255}.
TRANSMEM 1029 1049 Helical; Note=Endoplasmic reticulum
retention signal. {ECO:0000255}.
TOPO_DOM 1050 1063 Extracellular. {ECO:0000255}.
REGION 30 69 Human C1QBP/SF2P32-binding.
{ECO:0000250}.
REGION 279 300 Functions as E2 signal peptide.
{ECO:0000250|UniProtKB:P08563}.
REGION 563 582 Functions as E1 signal peptide.
{ECO:0000250|UniProtKB:P08563}.
SITE 300 301 Cleavage; by host signal peptidase.
{ECO:0000255}.
SITE 582 583 Cleavage; by host signal peptidase.
{ECO:0000255}.
MOD_RES 46 46 Phosphoserine; by host. {ECO:0000250}.
CARBOHYD 353 353 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 371 371 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 429 429 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 658 658 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 759 759 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 791 791 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 590 595 {ECO:0000269|PubMed:9143273}.
DISULFID 619 824 {ECO:0000269|PubMed:9143273}.
DISULFID 641 653 {ECO:0000269|PubMed:9143273}.
DISULFID 699 712 {ECO:0000269|PubMed:9143273}.
DISULFID 758 767 {ECO:0000269|PubMed:9143273}.
DISULFID 807 817 {ECO:0000269|PubMed:9143273}.
DISULFID 931 934 {ECO:0000269|PubMed:9143273}.
DISULFID 950 983 {ECO:0000269|PubMed:9143273}.
VARIANT 87 87 T -> S.
VARIANT 163 163 E -> Q.
VARIANT 319 319 C -> R.
VARIANT 395 395 D -> A.
VARIANT 545 545 L -> S.
VARIANT 613 613 K -> R.
VARIANT 825 825 S -> A.
VARIANT 959 959 L -> V.
VARIANT 991 991 T -> S.
VARIANT 1037 1037 I -> T.
SEQUENCE 1063 AA; 114679 MW; F39B475ACA15C7D1 CRC64;
MASTTPITME DLQKALEAQS RALRAELAAG ASQSRRPRPP RQRDSSTSGD DSGRDSGGPR
RRRGNRGRGQ RRDWSRAPPP PEERQETRSQ TPAPKPSRAP PQQPQPPRMQ TGRGGSAPRP
ELGPPTNPFQ AAVARGLRPP LHDPDTEAPT EACVTSWLWS EGEGAVFYRV DLHFTNLGTP
PLDEDGRWDP ALMYNPCGPE PPAHVVRAYN QPAGDVRGVW GKGERTYAEQ DFRVGGTRWH
RLLRMPVRGL DGDSAPLPPH TTERIETRSA RHPWRIRFGA PQAFLAGLLL ATVAVGTARA
GLQPRADMAA PPTLPQPPCA HGQHYGHHHH QLPFLGHDGH HGGTLRVGQH YRNASDVLPG
HWLQGGWGCY NLSDWHQGTH VCHTKHMDFW CVEHDRPPPA TPTPLTTAAN STTAATPATA
PAPCHAGLND SCGGFLSGCG PMRLRHGADT RCGRLICGLS TTAQYPPTRF GCAMRWGLPP
WELVVLTARP EDGWTCRGVP AHPGARCPEL VSPMGRATCS PASALWLATA NALSLDHALA
AFVLLVPWVL IFMVCRRACR RRGAAAALTA VVLQGYNPPA YGEEAFTYLC TAPGCATQAP
VPVRLAGVRF ESKIVDGGCF APWDLEATGA CICEIPTDVS CEGLGAWVPA APCARIWNGT
QRACTFWAVN AYSSGGYAQL ASYFNPGGSY YKQYHPTACE VEPAFGHSDA ACWGFPTDTV
MSVFALASYV QHPHKTVRVK FHTETRTVWQ LSVAGVSCNV TTEHPFCNTP HGQLEVQVPP
DPGDLVEYIM NYTGNQQSRW GLGSPNCHGP DWASPVCQRH SPDCSRLVGA TPERPRLRLV
DADDPLLRTA PGPGEVWVTP VIGSQARKCG LHIRAGPYGH ATVEMPEWIH AHTTSDPWHP
PGPLGLKFKT VRPVALPRTL APPRNVRVTG CYQCGTPALV EGLAPGGGNC HLTVNGEDLG
AVPPGKFVTA ALLNTPPPYQ VSCGGESDRA TARVIDPAAQ SFTGVVYGTH TTAVSETRQT
WAEWAAAHWW QLTLGAICAL PLAGLLACCA KCLYYLRGAI APR


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