UniProtKB - Q8VA10 (POLS_RUBVN)
Protein
Structural polyprotein
Gene
N/A
Organism
Rubella virus (strain RN-UK86) (RUBV)
Status
Functioni
Capsid protein interacts with genomic RNA and assembles into icosahedric core particles 65-70 nm in diameter. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions from host Golgi membranes. 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. 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.By similarity
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. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement.By similarity
Class II viral fusion protein (By similarity). 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 (By similarity). This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. The cytoplasmic tail of spike glycoprotein E1 modulates virus release. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement (By similarity).By similarity
Miscellaneous
Structural polyprotein: Translated from a subgenomic RNA synthesized during togaviruses replication.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 670 | CalciumBy similarity | 1 | |
Metal bindingi | 671 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 718 | CalciumBy similarity | 1 | |
Metal bindingi | 719 | Calcium; via carbonyl oxygenBy similarity | 1 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- RNA binding Source: UniProtKB-KW
GO - Biological processi
- clathrin-dependent endocytosis of virus by host cell Source: UniProtKB-KW
- fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
- virion attachment to host cell Source: UniProtKB-KW
Keywordsi
Names & Taxonomyi
Protein namesi | Recommended name: Structural polyproteinAlternative name(s): p110 Cleaved into the following 3 chains: Alternative name(s): Coat protein Short name: C Alternative name(s): E2 envelope glycoprotein Alternative name(s): E1 envelope glycoprotein |
Organismi | Rubella virus (strain RN-UK86) (RUBV) |
Taxonomic identifieri | 376267 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Kitrinoviricota › Alsuviricetes › Hepelivirales › Matonaviridae › Rubivirus › |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] |
Proteomesi |
|
Subcellular locationi
- Virion By similarity
- Host cytoplasm
- Host mitochondrion By similarity Note: The capsid protein is concentrated around Golgi region (By similarity). In the virion, it is probably associated to the viral membrane (By similarity).By similarity
- Virion membrane By similarity; Single-pass type I membrane protein By similarity
- Host Golgi apparatus membrane By similarity; Single-pass type I membrane protein By similarity 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
- Virion membrane By similarity; Single-pass type I membrane protein By similarity
- Host Golgi apparatus membrane By similarity; Single-pass type I membrane protein By similarity 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
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 301 – 534 | ExtracellularSequence analysisAdd BLAST | 234 | |
Transmembranei | 535 – 555 | Helical; Note=Golgi retention signalBy similarityAdd BLAST | 21 | |
Topological domaini | 556 – 582 | CytoplasmicSequence analysisAdd BLAST | 27 | |
Topological domaini | 583 – 1028 | ExtracellularSequence analysisAdd BLAST | 446 | |
Transmembranei | 1029 – 1049 | Helical; Note=Endoplasmic reticulum retention signalBy similarityAdd BLAST | 21 | |
Topological domaini | 1050 – 1063 | ExtracellularSequence analysisAdd BLAST | 14 |
Keywords - Cellular componenti
Capsid protein, Host cytoplasm, Host Golgi apparatus, Host membrane, Host mitochondrion, Membrane, T=4 icosahedral capsid protein, Viral envelope protein, VirionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000238993 | 1 – 300 | Capsid proteinAdd BLAST | 300 | |
ChainiPRO_0000238994 | 301 – 582 | Spike glycoprotein E2Add BLAST | 282 | |
ChainiPRO_0000238995 | 583 – 1063 | Spike glycoprotein E1Add BLAST | 481 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 46 | Phosphoserine; by hostBy similarity | 1 | |
Disulfide bondi | 153 ↔ 197 | By similarity | ||
Glycosylationi | 353 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 371 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 410 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 429 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Disulfide bondi | 590 ↔ 595 | By similarity | ||
Disulfide bondi | 619 ↔ 824 | By similarity | ||
Disulfide bondi | 641 ↔ 653 | By similarity | ||
Glycosylationi | 658 | N-linked (GlcNAc...) asparagine; by hostBy similarity | 1 | |
Disulfide bondi | 699 ↔ 712 | By similarity | ||
Disulfide bondi | 758 ↔ 767 | By similarity | ||
Glycosylationi | 759 | N-linked (GlcNAc...) asparagine; by hostBy similarity | 1 | |
Glycosylationi | 791 | N-linked (GlcNAc...) asparagine; by hostBy similarity | 1 | |
Disulfide bondi | 807 ↔ 817 | By similarity | ||
Disulfide bondi | 931 ↔ 934 | By similarity | ||
Disulfide bondi | 950 ↔ 983 | By similarity | ||
Glycosylationi | 1011 | O-linked (GalNAc...) threonine; by hostBy similarity | 1 | |
Glycosylationi | 1012 | O-linked (GalNAc...) threonine; by hostBy similarity | 1 |
Post-translational modificationi
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.By similarity
Contains three N-linked oligosaccharides.By similarity
Capsid is phosphorylated on Ser-46 by host. This phosphorylation negatively regulates capsid protein RNA-binding activity (By similarity). Dephosphorylated by human PP1A (By similarity).By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 300 – 301 | Cleavage; by host signal peptidaseSequence analysis | 2 | |
Sitei | 582 – 583 | Cleavage; by host signal peptidaseSequence analysis | 2 |
Keywords - PTMi
Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, PhosphoproteinInteractioni
Subunit structurei
Homodimer; further assembles into homooligomer.
Interacts with human C1QBP.
Interacts (via N-terminus) with protease/methyltransferase p150.
By similarityFamily & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 30 – 69 | Human C1QBP/SF2P32-bindingBy similarityAdd BLAST | 40 | |
Regioni | 279 – 300 | Functions as E2 signal peptideBy similarityAdd BLAST | 22 | |
Regioni | 563 – 582 | Functions as E1 signal peptideBy similarityAdd BLAST | 20 |
Domaini
Structural polyprotein: Contains two internal signal peptides that are necessary for directing translocation of the glycoproteins into the lumen of the endoplasmic reticulum.By similarity
The capsid protein is probably attached to the viral membrane through the E2 signal peptide. This domain is also required for the localization of the capsid protein to the juxtanuclear region and subsequent virus assembly at the Golgi complex.By similarity
Keywords - Domaini
Transmembrane, Transmembrane helixFamily and domain databases
Gene3Di | 2.60.40.2650, 1 hit 2.60.98.30, 2 hits 3.10.50.50, 1 hit 3.30.67.20, 1 hit |
InterProi | View protein in InterPro IPR008819, Rubella_Capsid IPR043106, Rubella_Capsid_sf IPR008820, Rubella_E1 IPR042500, Rubella_E1_1 IPR042498, Rubella_E1_2 IPR042499, Rubella_E1_3 IPR008821, Rubella_E2 |
Pfami | View protein in Pfam PF05750, Rubella_Capsid, 1 hit PF05748, Rubella_E1, 1 hit PF05749, Rubella_E2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q8VA10-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MASTTPITME DLQKALEAQS RALRAELAAG ASQSRRPRPP RQRDSSTSGD
60 70 80 90 100
DSGRDSGGPR RRRGNRGRGQ RKDWSMAPPP PEERQESRSQ TPAPKPSRAP
110 120 130 140 150
PQQPQPPRMQ TGRGGSAPRP ELGPPTNPFQ AAVARGLRPP LHDPDTEAPT
160 170 180 190 200
EACVTSWLWS EGEGAVFYRV DLHFTNLGTP PLDEDGRWDP ALMYNPCGPE
210 220 230 240 250
PPAHVVRAYN QPAGDVRGVW GKGERTYTEQ DFRVGGTRWH RLLRMPVRGL
260 270 280 290 300
DGDSAPLPPH TTERIETRSA RHPWRIRFGA PQAFLAGLLL AAVAVGTARA
310 320 330 340 350
GLQPRADMAA PPAPPQPPCA HGQHYGHHHH QLPFLGHDGH HGGTLRVGQH
360 370 380 390 400
HRNASDVLPG HCLQGGWGCY NLSDWHQGTH VCHTKHMDFW CVEHDRPPPA
410 420 430 440 450
TPTPLTTAAN STTAATPATA PAPCHAGLND SCGGFLSGCG PMRLRHGADT
460 470 480 490 500
RCGRLICGLS TTAQYPPTRF ACAMRWGLPP WELVVLTARP EDGWTCRGVP
510 520 530 540 550
AHPGTRCPEL VSPMGRATCS PASALWLATA NALSLDHALA AFVLLFPWVL
560 570 580 590 600
IFMVCRRACR RRGAAAALTA VVLQGYNPPA YGEEAFTYLC TAPGCATQTP
610 620 630 640 650
VPVRLAGVRF ESKIVDGGCF APWDLEATGA CICEIPTDVS CEGLGAWVPT
660 670 680 690 700
APCARIWNGT QRACTFWAVN AYSSGGYAQL ASYFNPGGSY YKQYHPTACE
710 720 730 740 750
VEPAFGHSDA ACWGFPTDTV MSVFALASYV QHPHKTVRVK FHTETRTVWQ
760 770 780 790 800
LSVAGVSCNV TTEHPFCNTP HGQLEVQVPP DPGDLVEYIM NYTGNQQSRW
810 820 830 840 850
GLGSPNCHGP DWASPVCQRH SPDCSRLVGA TPERPRLRLV DADDPLLRTA
860 870 880 890 900
PGPGEVWVTP VIGSQARKCG LHIRAGPYGH ATVEMPEWIH AHTTSDPWHP
910 920 930 940 950
PGPLGLKFKT VRPVALPRAL APPRNVRVTG CYQCGTPALV EGLAPGGGNC
960 970 980 990 1000
HLTVNGEDVG AVPPGKFVTA ALLNTPPPYQ VSCGGESDRA SARVIDPAAQ
1010 1020 1030 1040 1050
SFTGVVYGTH TTAVSETRQT WAEWAAAHWW QLTLGAVCAL LLAGLLACCA
1060
KCLYYLRGAI APR
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 362 | C → W in strain: Isolate Ulrike. | 1 | |
Natural varianti | 599 | T → A in strain: Isolate Ulrike. | 1 | |
Natural varianti | 794 | G → D in strain: Isolate Ulrike. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF435866 Genomic RNA Translation: AAL31568.1 AF435865 Genomic RNA Translation: AAL31566.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF435866 Genomic RNA Translation: AAL31568.1 AF435865 Genomic RNA Translation: AAL31566.1 |
3D structure databases
SMRi | Q8VA10 |
ModBasei | Search... |
Family and domain databases
Gene3Di | 2.60.40.2650, 1 hit 2.60.98.30, 2 hits 3.10.50.50, 1 hit 3.30.67.20, 1 hit |
InterProi | View protein in InterPro IPR008819, Rubella_Capsid IPR043106, Rubella_Capsid_sf IPR008820, Rubella_E1 IPR042500, Rubella_E1_1 IPR042498, Rubella_E1_2 IPR042499, Rubella_E1_3 IPR008821, Rubella_E2 |
Pfami | View protein in Pfam PF05750, Rubella_Capsid, 1 hit PF05748, Rubella_E1, 1 hit PF05749, Rubella_E2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | POLS_RUBVN | |
Accessioni | Q8VA10Primary (citable) accession number: Q8VA10 Secondary accession number(s): Q8VA12 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2006 |
Last sequence update: | March 1, 2002 | |
Last modified: | April 7, 2021 | |
This is version 81 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |