POLS_RUBVB
ID POLS_RUBVB Reviewed; 1063 AA.
AC Q6X2U3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Structural polyprotein;
DE AltName: Full=p110;
DE Contains:
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE Short=C;
DE Contains:
DE RecName: Full=Spike glycoprotein E2;
DE AltName: Full=E2 envelope glycoprotein;
DE Contains:
DE RecName: Full=Spike glycoprotein E1;
DE AltName: Full=E1 envelope glycoprotein;
OS Rubella virus (strain BRD1) (RUBV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Hepelivirales; Matonaviridae; Rubivirus; Rubivirus rubellae.
OX NCBI_TaxID=376262;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=14505094; DOI=10.1007/s00705-003-0132-7;
RA Zheng D.-P., Zhou Y.M., Zhao K., Han Y.-R., Frey T.K.;
RT "Characterization of genotype II Rubella virus strains.";
RL Arch. Virol. 148:1835-1850(2003).
CC -!- FUNCTION: [Capsid protein]: Capsid protein interacts with genomic RNA
CC and assembles into icosahedric core particles 65-70 nm in diameter. The
CC resulting nucleocapsid eventually associates with the cytoplasmic
CC domain of E2 at the cell membrane, leading to budding and formation of
CC mature virions from host Golgi membranes. Phosphorylation negatively
CC regulates RNA-binding activity, possibly delaying virion assembly
CC during the viral replication phase. Capsid protein dimerizes and
CC becomes disulfide-linked in the virion. Modulates genomic RNA
CC replication. Modulates subgenomic RNA synthesis by interacting with
CC human C1QBP/SF2P32. Induces both perinuclear clustering of mitochondria
CC and the formation of electron-dense intermitochondrial plaques, both
CC hallmarks of rubella virus infected cells. Induces apoptosis when
CC expressed in transfected cells. {ECO:0000250|UniProtKB:P08563}.
CC -!- FUNCTION: [Spike glycoprotein E2]: Responsible for viral attachment to
CC target host cell, by binding to the cell receptor. Its transport to the
CC plasma membrane depends on interaction with E1 protein. The surface
CC glycoproteins display an irregular helical organization and a pseudo-
CC tetrameric inner nucleocapsid arrangement.
CC {ECO:0000250|UniProtKB:P08563}.
CC -!- FUNCTION: [Spike glycoprotein E1]: Class II viral fusion protein (By
CC similarity). Fusion activity is inactive as long as E1 is bound to E2
CC in mature virion. After virus attachment to target cell and clathrin-
CC mediated endocytosis, acidification of the endosome would induce
CC dissociation of E1/E2 heterodimer and concomitant trimerization of the
CC E1 subunits (By similarity). This E1 homotrimer is fusion active, and
CC promotes release of viral nucleocapsid in cytoplasm after endosome and
CC viral membrane fusion. The cytoplasmic tail of spike glycoprotein E1
CC modulates virus release. The surface glycoproteins display an irregular
CC helical organization and a pseudo-tetrameric inner nucleocapsid
CC arrangement (By similarity). {ECO:0000250|UniProtKB:P07566,
CC ECO:0000250|UniProtKB:P08563}.
CC -!- SUBUNIT: [Capsid protein]: Homodimer; further assembles into
CC homooligomer. Interacts with human C1QBP. Interacts (via N-terminus)
CC with protease/methyltransferase p150. {ECO:0000250|UniProtKB:P08563}.
CC -!- SUBUNIT: [Spike glycoprotein E1]: Heterodimer with spike glycoprotein
CC E2. {ECO:0000250|UniProtKB:P08563}.
CC -!- SUBUNIT: [Spike glycoprotein E2]: Heterodimer with spike glycoprotein
CC E1. {ECO:0000250|UniProtKB:P08563}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion
CC {ECO:0000250|UniProtKB:P08563}. Host cytoplasm. Host mitochondrion
CC {ECO:0000250|UniProtKB:P08563}. Note=The capsid protein is concentrated
CC around Golgi region (By similarity). In the virion, it is probably
CC associated to the viral membrane (By similarity).
CC {ECO:0000250|UniProtKB:P08563}.
CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane
CC {ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P08563}. Host Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P08563}. Note=E1 and E2 form heterodimer in the
CC endoplasmic reticulum before they are transported to and retained in
CC the Golgi complex, where virus assembly occurs. E1 possesses an
CC endoplasmic reticulum retention signal, and unassembled E2 and E1
CC subunits are retained in the endoplasmic reticulum. Presumably,
CC assembly of E2 and E1 would mask the signal, thereby allowing transport
CC of the heterodimer to the Golgi complex.
CC {ECO:0000250|UniProtKB:P08563}.
CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E1]: Virion membrane
CC {ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P08563}. Host Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P08563}. Note=E1 and E2 form heterodimer in the
CC endoplasmic reticulum before they are transported to and retained in
CC the Golgi complex, where virus assembly occurs. E1 possesses an
CC endoplasmic reticulum retention signal, and unassembled E2 and E1
CC subunits are retained in the endoplasmic reticulum. Presumably,
CC assembly of E2 and E1 would mask the signal, thereby allowing transport
CC of the heterodimer to the Golgi complex.
CC {ECO:0000250|UniProtKB:P08563}.
CC -!- DOMAIN: Structural polyprotein: Contains two internal signal peptides
CC that are necessary for directing translocation of the glycoproteins
CC into the lumen of the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:P08563}.
CC -!- DOMAIN: [Capsid protein]: The capsid protein is probably attached to
CC the viral membrane through the E2 signal peptide. This domain is also
CC required for the localization of the capsid protein to the juxtanuclear
CC region and subsequent virus assembly at the Golgi complex.
CC {ECO:0000250|UniProtKB:P08563}.
CC -!- PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield
CC mature proteins. Two signal peptidase-mediated cleavages within the
CC polyprotein produce the structural proteins capsid, E2, and E1. The E2
CC signal peptide remains attached to the C-terminus of the capsid protein
CC after cleavage by the signal peptidase. Another signal peptide at E2 C-
CC terminus directs E1 to the ER, with a similar mechanism.
CC {ECO:0000250|UniProtKB:P08563}.
CC -!- PTM: [Spike glycoprotein E1]: Contains three N-linked oligosaccharides.
CC {ECO:0000250|UniProtKB:P08563}.
CC -!- PTM: Capsid is phosphorylated on Ser-46 by host. This phosphorylation
CC negatively regulates capsid protein RNA-binding activity (By
CC similarity). Dephosphorylated by human PP1A (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P08563}.
CC -!- MISCELLANEOUS: Structural polyprotein: Translated from a subgenomic RNA
CC synthesized during togaviruses replication.
CC {ECO:0000250|UniProtKB:P08563}.
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DR EMBL; AY258322; AAP82233.1; -; Genomic_RNA.
DR SMR; Q6X2U3; -.
DR Proteomes; UP000007185; Genome.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:InterPro.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.2650; -; 1.
DR Gene3D; 2.60.98.30; -; 1.
DR Gene3D; 3.10.50.50; -; 1.
DR Gene3D; 3.30.67.20; -; 2.
DR InterPro; IPR008819; Rubella_Capsid.
DR InterPro; IPR043106; Rubella_Capsid_sf.
DR InterPro; IPR008820; Rubella_E1.
DR InterPro; IPR042500; Rubella_E1_1.
DR InterPro; IPR042498; Rubella_E1_2.
DR InterPro; IPR042499; Rubella_E1_3.
DR InterPro; IPR008821; Rubella_E2.
DR Pfam; PF05750; Rubella_Capsid; 1.
DR Pfam; PF05748; Rubella_E1; 1.
DR Pfam; PF05749; Rubella_E2; 1.
PE 3: Inferred from homology;
KW Calcium; Capsid protein; Clathrin-mediated endocytosis of virus by host;
KW Disulfide bond; Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; Host cytoplasm;
KW Host Golgi apparatus; Host membrane; Host mitochondrion;
KW Host-virus interaction; Lipoprotein; Membrane; Metal-binding; Palmitate;
KW Phosphoprotein; RNA-binding; T=4 icosahedral capsid protein; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT CHAIN 1..300
FT /note="Capsid protein"
FT /id="PRO_0000238984"
FT CHAIN 301..582
FT /note="Spike glycoprotein E2"
FT /id="PRO_0000238985"
FT CHAIN 583..1063
FT /note="Spike glycoprotein E1"
FT /id="PRO_0000238986"
FT TOPO_DOM 301..534
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..555
FT /note="Helical; Note=Golgi retention signal"
FT /evidence="ECO:0000250|UniProtKB:P08563"
FT TOPO_DOM 556..582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..1028
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1029..1049
FT /note="Helical; Note=Endoplasmic reticulum retention
FT signal"
FT /evidence="ECO:0000250|UniProtKB:P08563"
FT TOPO_DOM 1050..1063
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 23..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..69
FT /note="Human C1QBP/SF2P32-binding"
FT /evidence="ECO:0000250"
FT REGION 279..300
FT /note="Functions as E2 signal peptide"
FT /evidence="ECO:0000250|UniProtKB:P08563"
FT REGION 305..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..582
FT /note="Functions as E1 signal peptide"
FT /evidence="ECO:0000250|UniProtKB:P08563"
FT COMPBIAS 37..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 670
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08563"
FT BINDING 671
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08563"
FT BINDING 718
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08563"
FT BINDING 719
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08563"
FT SITE 300..301
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000255"
FT SITE 582..583
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000255"
FT MOD_RES 46
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P08563"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P08563"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P08563"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P08563"
FT CARBOHYD 1011
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000250|UniProtKB:P08563"
FT CARBOHYD 1012
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000250|UniProtKB:P08563"
FT DISULFID 153..197
FT /evidence="ECO:0000250|UniProtKB:P08563"
FT DISULFID 590..595
FT /evidence="ECO:0000250|UniProtKB:P07566"
FT DISULFID 619..824
FT /evidence="ECO:0000250|UniProtKB:P07566"
FT DISULFID 641..653
FT /evidence="ECO:0000250|UniProtKB:P07566"
FT DISULFID 699..712
FT /evidence="ECO:0000250|UniProtKB:P07566"
FT DISULFID 758..767
FT /evidence="ECO:0000250|UniProtKB:P07566"
FT DISULFID 807..817
FT /evidence="ECO:0000250|UniProtKB:P07566"
FT DISULFID 931..934
FT /evidence="ECO:0000250|UniProtKB:P07566"
FT DISULFID 950..983
FT /evidence="ECO:0000250|UniProtKB:P07566"
SQ SEQUENCE 1063 AA; 114682 MW; 537FC9A156E45950 CRC64;
MASTTPITME DLQKALEAQS RALRAELAAG ASQLRRPRPP RQRDSSTSGD DSGRDSGGPR
RRRGNRGRGQ RKDWSKAPPP PEERQESRSQ TPAPKPPRAP PQPPQPPRMQ TGRGGTAPRP
ELGPPTNPFQ AAVARGLRPP LHDPDTEAPT EACVTSWLWS EGEGAVFYRV DLHFTNLGTP
PLDEDGRWDP ALMYNPCGPE PPAHVVRAYN QPAGDVRGIW GKGERTYAEQ DFRVGGTRWH
RLLRMPVRGL DGDSAPLPPH TTERIETRSA RHPWRIRFGA PQVFLAGLLL AAVAVGTARA
GLQPRTDIAA PPAPPQAPRA HGKHYGHHHH QLPFLGHDGH HGGTLRVGQH HRNASDVLPG
HWLQGSWGCY NLSDWHQGTH ICHTKHMDFW CVEHDRPPPV TPTPLTTAAN STTAATPATT
PAPCHAGLND SCGGFLSGCG PMRLRHGADT RCGRLICGLS TTAQYPPTRF GCTMRWGLPP
WELVVLTARP EDGWTCRGVP AHPGTRCPEL VSPMGHATCS PASALWLATA NALSLDHALA
AVVLLVPWVL IFMLCRRACR RRGAAAALTA VVLQGYNPPA YGEEAFTYLC TAPGCATQTP
VPVRLAGVRF ESKIVDGGCF APWDLEATGA CICEIPTDVS CEGLGAWVPA APCARIWNGT
QRACTLWAVN AYSSGGYAQL ASYFNPGGSY YKQYHPTACD VEPAFGHSDA ACWGFPTDTV
MSVFALASYV QHPDKTVRVK FHTETRTVWQ LSVAGVSCNV TTEHPFCNTP HGQLEVQVPP
DPGDLVEYIM NYTGNQQSRW GLGSPNCHGP DWASPVCQRH SPDCSRLVGA TPERPRLRLV
DADDPLLRTA PGPGEVWVTP VIGSQARKCG LHIRAGPYGH ATVEMPEWIH AHTTSDPWHP
PGPLGLKFKT VRPVALPRAL APPRNVRVTG CYQCGTPALV EGLAPGGGNC HLTVNGEDVG
AFPPGKFVTA ALLNTPPPYQ VSCGGESDRA SARVIDPAAQ SFTGVVYGTH TTAVSETRQT
WAEWAAAHWW QLTLGAICAL LLAGLLACCA KCLYYLRGAI APR
