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Entry version 111 (07 Apr 2021)
Sequence version 2 (30 May 2006)
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Protein

Structural polyprotein

Gene
N/A
Organism
Rubella virus (strain M33) (RUBV)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Capsid protein interacts with genomic RNA and assembles into icosahedric core particles 65-70 nm in diameter (PubMed:28575072). 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 (PubMed:28575072). 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 (PubMed:24282305). Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP/SF2P32 (PubMed:10823864). Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells (PubMed:16051872). Induces apoptosis when expressed in transfected cells (PubMed:11017784).5 Publications
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 (PubMed:28575072).1 Publication
Class II viral fusion protein (PubMed:23292515). 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 (PubMed:9765418). The cytoplasmic tail of spike glycoprotein E1 modulates virus release (PubMed:10708417, PubMed:10233921). The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement (PubMed:28575072).By similarity5 Publications

Miscellaneous

Structural polyprotein: Translated from a subgenomic RNA synthesized during togaviruses replication.Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi670CalciumCombined sources1
Metal bindingi671Calcium; via carbonyl oxygenCombined sources1
Metal bindingi718CalciumCombined sources1
Metal bindingi719Calcium; via carbonyl oxygenCombined sources1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRNA-binding
Biological processClathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus endocytosis by host, Virus entry into host cell
LigandCalcium, Metal-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Structural polyprotein
Alternative 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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRubella virus (strain M33) (RUBV)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri11043 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesRiboviriaOrthornaviraeKitrinoviricotaAlsuviricetesHepeliviralesMatonaviridaeRubivirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiHomo sapiens (Human) [TaxID: 9606]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000007143 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini301 – 534ExtracellularSequence analysisAdd BLAST234
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei535 – 555Helical; Note=Golgi retention signal1 PublicationAdd BLAST21
Topological domaini556 – 582CytoplasmicSequence analysisAdd BLAST27
Topological domaini583 – 1028ExtracellularSequence analysisAdd BLAST446
Transmembranei1029 – 1049Helical; Note=Endoplasmic reticulum retention signal1 PublicationAdd BLAST21
Topological domaini1050 – 1063CytoplasmicSequence analysisAdd BLAST14

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host Golgi apparatus, Host membrane, Host mitochondrion, Membrane, T=4 icosahedral capsid protein, Viral envelope protein, Virion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi35 – 43RRPRPPRQR → AAPAPPAQA: Complete loss of human C1QBP/SF2P32-binding. 90% loss of virus production from infected cell. 1 Publication9
Mutagenesisi60 – 68RRRRGNRGR → AAAAGNAGA: Complete loss of human C1QBP/SF2P32-binding. 90% loss of virus production from infected cell. 1 Publication9
Mutagenesisi153C → S: Complete loss of Capsid dimerization. No effect on particle budding. 1 Publication1
Mutagenesisi658N → I: Complete loss of infectivity. 1 Publication1
Mutagenesisi664C → S: Prevents E1-E2 heterodimer formation, and subsequent transport of to the plasma membrane. Complete loss of fusion activity in vitro. 1 Publication1
Mutagenesisi675G → D: Complete loss of fusion activity in vitro. 90% loss of infectivity in vivo. No effect on virus assembly. 2 Publications1
Mutagenesisi686P → G: 99.9% loss of infectivity. No effect on virus assembly. No effect on fusion activity in vitro. 2 Publications1
Mutagenesisi759N → I: No effect on infectivity. 1 Publication1
Mutagenesisi791N → I: Complete loss of infectivity. 1 Publication1
Mutagenesisi1046L → A: No effect on virus production from infected cell. 1 Publication1
Mutagenesisi1048C → A: No effect on virus production from infected cell. 1 Publication1
Mutagenesisi1049C → A: No effect on virus production from infected cell. 1 Publication1
Mutagenesisi1052C → A: No effect on virus production from infected cell. 2 Publications1
Mutagenesisi1053L → A: 90% loss of virus production from infected cell. 2 Publications1
Mutagenesisi1054Y → A: Complete loss of virus production from infected cell. 1 Publication1
Mutagenesisi1055Y → S: Complete loss of virus production from infected cell. 1 Publication1
Mutagenesisi1056L → A: 90% loss of virus production from infected cell. 1 Publication1
Mutagenesisi1057R → S: 98% loss of virus production from infected cell. 1 Publication1
Mutagenesisi1058G → C: 98% loss of virus production from infected cell. 1 Publication1
Mutagenesisi1059A → S: 90% loss of virus production from infected cell. 1 Publication1
Mutagenesisi1060I → V: No effect on virus production from infected cell. 1 Publication1
Mutagenesisi1061A → S: 90% loss of virus production from infected cell. 1 Publication1
Mutagenesisi1062P → S: 90% loss of virus production from infected cell. 1 Publication1
Mutagenesisi1063R → S: 98% loss of virus production from infected cell. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000413021 – 300Capsid proteinAdd BLAST300
ChainiPRO_0000041303301 – 582Spike glycoprotein E21 PublicationAdd BLAST282
ChainiPRO_0000041304583 – 1063Spike glycoprotein E11 PublicationAdd BLAST481

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei46Phosphoserine; by host1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi153 ↔ 1971 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi353N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi371N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi410N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Glycosylationi429N-linked (GlcNAc...) asparagine; by hostPROSITE-ProRule annotation1
Disulfide bondi590 ↔ 595By similarity
Disulfide bondi619 ↔ 824By similarity
Disulfide bondi641 ↔ 653By similarity
Glycosylationi658N-linked (GlcNAc...) asparagine; by host2 Publications1
Disulfide bondi699 ↔ 712By similarity
Disulfide bondi758 ↔ 767By similarity
Glycosylationi759N-linked (GlcNAc...) asparagine; by host3 Publications1
Glycosylationi791N-linked (GlcNAc...) asparagine; by host2 Publications1
Disulfide bondi807 ↔ 817By similarity
Disulfide bondi931 ↔ 934By similarity
Disulfide bondi950 ↔ 983By similarity
Glycosylationi1011O-linked (GalNAc...) threonine; by host1 Publication1
Glycosylationi1012O-linked (GalNAc...) threonine; by host1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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.1 Publication
Contains three N-linked oligosaccharides.3 Publications
Capsid is phosphorylated on Ser-46 by host (PubMed:12525610). This phosphorylation negatively regulates capsid protein RNA-binding activity (PubMed:12525610). Dephosphorylated by human PP1A (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei300 – 301Cleavage; by host signal peptidaseSequence analysis2
Sitei582 – 583Cleavage; by host signal peptidaseSequence analysis2

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P08563

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; further assembles into homooligomer (PubMed:8614992, PubMed:24282305).

Interacts with human C1QBP (PubMed:10823864, PubMed:16051872).

Interacts (via N-terminus) with protease/methyltransferase p150 (PubMed:25056903).

3 Publications

Heterodimer with spike glycoprotein E2 (PubMed:9765418).

1 Publication

Heterodimer with spike glycoprotein E1 (PubMed:9765418).

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P08563, 35 interactors

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11063
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P08563

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni30 – 69Human C1QBP/SF2P32-binding1 PublicationAdd BLAST40
Regioni279 – 300Functions as E2 signal peptide1 PublicationAdd BLAST22
Regioni563 – 582Functions as E1 signal peptide1 PublicationAdd BLAST20

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Structural polyprotein: Contains two internal signal peptides that are necessary for directing translocation of the glycoproteins into the lumen of the endoplasmic reticulum.2 Publications
The capsid protein is probably attached to the viral membrane through the E2 signal peptide (PubMed:2214022). This domain is also required for the localization of the capsid protein to the juxtanuclear region and subsequent virus assembly at the Golgi complex (PubMed:11160697).2 Publications

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
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

Integrated resource of protein families, domains and functional sites

More...
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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05750, Rubella_Capsid, 1 hit
PF05748, Rubella_E1, 1 hit
PF05749, Rubella_E2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P08563-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASTTPITME DLQKALEAQS RALRAGLAAG ASQSRRPRPP RQRDSSTSGD
60 70 80 90 100
DSGRDSGGPR RRRGNRGRGQ RKDWSRAPPP 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 GKGERTYAEQ DFRVGGTRWH RLLRMPVRGL
260 270 280 290 300
DGDTAPLPPH TTERIETRSA RHPWRIRFGA PQAFLAGLLL AAVAVGTARA
310 320 330 340 350
GLQPRADMAA PPMPPQPPRA HGQHYGHHHH QLPFLGHDGH HGGTLRVGQH
360 370 380 390 400
HRNASDVLPG HWLQGGWGCY NLSDWHQGTH VCHTKHMDFW CVEHDRPPPA
410 420 430 440 450
TPTSLTTAAN STTAATPATA PPPCHAGLND SCGGFLSGCG PMRLRHGADT
460 470 480 490 500
RCGRLICGLS TTAQYPPTRF GCAMRWGLPP WELVVLTARP EDGWTCRGVP
510 520 530 540 550
AHPGTRCPEL VSPMGRATCS PASALWLATA NALSLDHAFA AFVLLVPWVL
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 AFPPGKFVTA ALLNTPPPYQ VSCGGESDRA SARVIDPAAQ
1010 1020 1030 1040 1050
SFTGVVYGTH TTAVSETRQT WAEWAAAHWW QLTLGAICAL LLAGLLACCA
1060
KCLYYLRGAI APR
Length:1,063
Mass (Da):114,736
Last modified:May 30, 2006 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB546067276483ECB
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA28880 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti42 – 69QRDSS…NRGRG → HARLQHLPEMTPAVTPEGPA PPRTGAW in CAA28880 (PubMed:3562245).CuratedAdd BLAST28
Sequence conflicti175T → I in CAA28880 (PubMed:3562245).Curated1
Sequence conflicti445 – 471RHGAD…PTRFG → PTALTPGAVGDLRAVHHRPV PAYPVC in CAA28880 (PubMed:3562245).CuratedAdd BLAST27
Sequence conflicti485V → I in CAA28880 (PubMed:3562245).Curated1
Sequence conflicti562 – 577RGAAA…LQGYN → PAPPPPSPQSSCRGTT in CAA28880 (PubMed:3562245).CuratedAdd BLAST16
Sequence conflicti993 – 994RV → GH in CAA28880 (PubMed:3562245).Curated2
Sequence conflicti995 – 1063Missing in CAA28880 (PubMed:3562245).CuratedAdd BLAST69

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti272H → R in strain: Isolate HPV77 vaccine. 1
Natural varianti411S → Y in strain: Isolate HPV77 vaccine. 1
Natural varianti412T → I in strain: Isolate HPV77 vaccine. 1
Natural varianti413T → A in strain: Isolate HPV77 vaccine. 1
Natural varianti609R → G in strain: Isolate HPV77 vaccine. 1

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X05259 mRNA Translation: CAA28880.1 Sequence problems.
M30776 Genomic RNA Translation: AAA47421.1 Sequence problems.

Protein sequence database of the Protein Information Resource

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PIRi
A27505, GNWVR3
JQ0087, GNWV77

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05259 mRNA Translation: CAA28880.1 Sequence problems.
M30776 Genomic RNA Translation: AAA47421.1 Sequence problems.
PIRiA27505, GNWVR3
JQ0087, GNWV77

3D structure databases

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Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ADGX-ray2.18A/B/C583-1018[»]
4ADIX-ray1.80A/B/C583-1018[»]
4ADJX-ray1.94A/B/C583-1018[»]
4B3VX-ray1.98A/B/C583-1018[»]
4HARX-ray2.66A/B/C/D/E/F127-277[»]
4HBEX-ray2.30A/B127-277[»]
4HBOX-ray3.24A/B/C/D/E147-277[»]
5KHCelectron microscopy11.10A583-1018[»]
SMRiP08563
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP08563, 35 interactors

PTM databases

iPTMnetiP08563

Family and domain databases

Gene3Di2.60.40.2650, 1 hit
2.60.98.30, 2 hits
3.10.50.50, 1 hit
3.30.67.20, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF05750, Rubella_Capsid, 1 hit
PF05748, Rubella_E1, 1 hit
PF05749, Rubella_E2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLS_RUBVM
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P08563
Secondary accession number(s): P21480
, Q86373, Q86374, Q86375
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 30, 2006
Last modified: April 7, 2021
This is version 111 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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