UniProtKB - P07566 (POLS_RUBVT)
Structural polyprotein
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 similarityResponsible 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 similarityClass 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 (PubMed:15557740).
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 similarity1 PublicationMiscellaneous
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 Therien) (RUBV) |
Taxonomic identifieri | 11045 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Kitrinoviricota › Alsuviricetes › Hepelivirales › Matonaviridae › Rubivirus › Rubivirus rubellae › |
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_0000041308 | 1 – 300 | Capsid proteinAdd BLAST | 300 | |
ChainiPRO_0000041309 | 301 – 582 | Spike glycoprotein E2Add BLAST | 282 | |
ChainiPRO_0000041310 | 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 | 1 Publication | ||
Disulfide bondi | 619 ↔ 824 | 1 Publication | ||
Disulfide bondi | 641 ↔ 653 | 1 Publication | ||
Glycosylationi | 658 | N-linked (GlcNAc...) asparagine; by hostBy similarity | 1 | |
Disulfide bondi | 699 ↔ 712 | 1 Publication | ||
Disulfide bondi | 758 ↔ 767 | 1 Publication | ||
Glycosylationi | 759 | N-linked (GlcNAc...) asparagine; by hostBy similarity | 1 | |
Glycosylationi | 791 | N-linked (GlcNAc...) asparagine; by hostBy similarity | 1 | |
Disulfide bondi | 807 ↔ 817 | 1 Publication | ||
Disulfide bondi | 931 ↔ 934 | 1 Publication | ||
Disulfide bondi | 950 ↔ 983 | 1 Publication | ||
Glycosylationi | 1011 | O-linked (GalNAc...) threonine; by hostBy similarity | 1 | |
Glycosylationi | 1012 | O-linked (GalNAc...) threonine; by hostBy similarity | 1 |
Post-translational modificationi
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 similarityBinary interactionsi
Capsid protein (PRO_0000041308)
With | #Exp. | IntAct |
---|---|---|
C1QBP [Q07021] from Homo sapiens. | 3 | EBI-6377932,EBI-347528 |
C1QBP [Q9MZE0] from Chlorocebus aethiops. | 3 | EBI-6377932,EBI-6375765 |
Protein-protein interaction databases
IntActi | P07566, 2 interactors |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 131 | DisorderedSequence analysisAdd BLAST | 131 | |
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 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 37 – 62 | Basic and acidic residuesSequence analysisAdd BLAST | 26 |
Domaini
Keywords - Domaini
Transmembrane, Transmembrane helixFamily and domain databases
Gene3Di | 2.60.40.2650, 1 hit 2.60.98.30, 1 hit 3.10.50.50, 1 hit 3.30.67.20, 2 hits |
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
10 20 30 40 50
MASTTPITME DLQKALEAQS RALRAELAAG ASQSRRPRPP RQRDSSTSGD
60 70 80 90 100
DSGRDSGGPR RRRGNRGRGQ RRDWSRAPPP PEERQETRSQ 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 GKGERTYAEQ DFRVGGTRWH RLLRMPVRGL
260 270 280 290 300
DGDSAPLPPH TTERIETRSA RHPWRIRFGA PQAFLAGLLL ATVAVGTARA
310 320 330 340 350
GLQPRADMAA PPTLPQPPCA HGQHYGHHHH QLPFLGHDGH HGGTLRVGQH
360 370 380 390 400
YRNASDVLPG HWLQGGWGCY NLSDWHQGTH VCHTKHMDFW CVEHDRPPPA
410 420 430 440 450
TPTPLTTAAN STTAATPATA PAPCHAGLND SCGGFLSGCG PMRLRHGADT
460 470 480 490 500
RCGRLICGLS TTAQYPPTRF GCAMRWGLPP WELVVLTARP EDGWTCRGVP
510 520 530 540 550
AHPGARCPEL VSPMGRATCS PASALWLATA NALSLDHALA AFVLLVPWVL
560 570 580 590 600
IFMVCRRACR RRGAAAALTA VVLQGYNPPA YGEEAFTYLC TAPGCATQAP
610 620 630 640 650
VPVRLAGVRF ESKIVDGGCF APWDLEATGA CICEIPTDVS CEGLGAWVPA
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 VRPVALPRTL APPRNVRVTG CYQCGTPALV EGLAPGGGNC
960 970 980 990 1000
HLTVNGEDLG AVPPGKFVTA ALLNTPPPYQ VSCGGESDRA TARVIDPAAQ
1010 1020 1030 1040 1050
SFTGVVYGTH TTAVSETRQT WAEWAAAHWW QLTLGAICAL PLAGLLACCA
1060
KCLYYLRGAI APR
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 87 | T → S. | 1 | |
Natural varianti | 163 | E → Q. | 1 | |
Natural varianti | 319 | C → R. | 1 | |
Natural varianti | 395 | D → A. | 1 | |
Natural varianti | 545 | L → S. | 1 | |
Natural varianti | 613 | K → R. | 1 | |
Natural varianti | 825 | S → A. | 1 | |
Natural varianti | 959 | L → V. | 1 | |
Natural varianti | 991 | T → S. | 1 | |
Natural varianti | 1037 | I → T. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M15240 Genomic RNA Translation: AAA88529.1 D00242 Genomic RNA Translation: BAA00172.1 D00156 Genomic RNA Translation: BAA28178.1 |
PIRi | A24309 A29822, GNWVR4 |
RefSeqi | NP_062884.1, NC_001545.2 |
Genome annotation databases
GeneIDi | 1502162 |
KEGGi | vg:1502162 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M15240 Genomic RNA Translation: AAA88529.1 D00242 Genomic RNA Translation: BAA00172.1 D00156 Genomic RNA Translation: BAA28178.1 |
PIRi | A24309 A29822, GNWVR4 |
RefSeqi | NP_062884.1, NC_001545.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5KHE | electron microscopy | 35.00 | A/B | 9-277 | [»] | |
5KHF | electron microscopy | 35.00 | A/B | 9-277 | [»] | |
SMRi | P07566 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P07566, 2 interactors |
Genome annotation databases
GeneIDi | 1502162 |
KEGGi | vg:1502162 |
Family and domain databases
Gene3Di | 2.60.40.2650, 1 hit 2.60.98.30, 1 hit 3.10.50.50, 1 hit 3.30.67.20, 2 hits |
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 |
MobiDBi | Search... |
Entry informationi
Entry namei | POLS_RUBVT | |
Accessioni | P07566Primary (citable) accession number: P07566 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1988 |
Last sequence update: | August 1, 1988 | |
Last modified: | February 23, 2022 | |
This is version 113 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references