POLS_RUBVM
ID POLS_RUBVM Reviewed; 1063 AA.
AC P08563; P21480; Q86373; Q86374; Q86375;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 116.
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 M33) (RUBV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Hepelivirales; Matonaviridae; Rubivirus; Rubivirus rubellae.
OX NCBI_TaxID=11043;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3562245; DOI=10.1093/nar/15.7.3041;
RA Clarke D.M., Loo T.W., Hui I., Chong P., Gillam S.;
RT "Nucleotide sequence and in vitro expression of rubella virus 24S
RT subgenomic messenger RNA encoding the structural proteins E1, E2 and C.";
RL Nucleic Acids Res. 15:3041-3057(1987).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=3396880; DOI=10.1016/0378-1119(88)90413-1;
RA Clarke D.M., Loo T.W., McDonald H., Gillam S.;
RT "Expression of rubella virus cDNA coding for the structural proteins.";
RL Gene 65:23-30(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HPV77 vaccine;
RX PubMed=2583526; DOI=10.1016/0378-1119(89)90061-9;
RA Zheng D., Dickens L., Liu T.Y., Nakhasi H.L.;
RT "Nucleotide sequence of the 24S subgenomic messenger RNA of a vaccine
RT strain (HPV77) of rubella virus: comparison with a wild-type strain
RT (M33).";
RL Gene 82:343-349(1989).
RN [4]
RP SUBCELLULAR LOCATION (SPIKE GLYCOPROTEIN E2), AND DOMAIN (STRUCTURAL
RP POLYPROTEIN).
RX PubMed=2845137; DOI=10.1128/jvi.62.11.4259-4264.1988;
RA Hobman T.C., Shukin R., Gillam S.;
RT "Translocation of rubella virus glycoprotein E1 into the endoplasmic
RT reticulum.";
RL J. Virol. 62:4259-4264(1988).
RN [5]
RP SUBCELLULAR LOCATION (SPIKE GLYCOPROTEIN E2), AND DOMAIN (STRUCTURAL
RP POLYPROTEIN).
RX PubMed=2683361; DOI=10.1016/0042-6822(89)90240-7;
RA Hobman T.C., Gillam S.;
RT "In vitro and in vivo expression of rubella virus glycoprotein E2: the
RT signal peptide is contained in the C-terminal region of capsid protein.";
RL Virology 173:241-250(1989).
RN [6]
RP DOMAIN (CAPSID PROTEIN), AND SUBCELLULAR LOCATION (CAPSID PROTEIN).
RX PubMed=2214022; DOI=10.1128/jvi.64.11.5500-5509.1990;
RA Suomalainen M., Garoff H., Baron M.D.;
RT "The E2 signal sequence of rubella virus remains part of the capsid protein
RT and confers membrane association in vitro.";
RL J. Virol. 64:5500-5509(1990).
RN [7]
RP GLYCOSYLATION (SPIKE GLYCOPROTEIN E1).
RX PubMed=2014650; DOI=10.1016/0042-6822(91)90915-x;
RA Hobman T.C., Qiu Z., Chaye H., Gillam S.;
RT "Analysis of rubella virus E1 glycosylation mutants expressed in COS
RT cells.";
RL Virology 181:768-772(1991).
RN [8]
RP SUBCELLULAR LOCATION (SPIKE GLYCOPROTEIN E2), AND SUBCELLULAR LOCATION
RP (SPIKE GLYCOPROTEIN E1).
RX PubMed=8468347; DOI=10.1083/jcb.121.2.269;
RA Hobman T.C., Woodward L., Farquhar M.G.;
RT "The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi
RT complex.";
RL J. Cell Biol. 121:269-281(1993).
RN [9]
RP PROTEOLYTIC CLEAVAGE (STRUCTURAL POLYPROTEIN).
RX PubMed=8178466; DOI=10.1006/viro.1994.1250;
RA Qiu Z., McDonald H.L., Chen J., Hobman T.C., Gillam S.;
RT "Mutational analysis of the arginine residues in the E2-E1 junction region
RT on the proteolytic processing of the polyprotein precursor of rubella
RT virus.";
RL Virology 200:821-825(1994).
RN [10]
RP SUBCELLULAR LOCATION (SPIKE GLYCOPROTEIN E2).
RX PubMed=7749196; DOI=10.1091/mbc.6.1.7;
RA Hobman T.C., Woodward L., Farquhar M.G.;
RT "Targeting of a heterodimeric membrane protein complex to the Golgi:
RT rubella virus E2 glycoprotein contains a transmembrane Golgi retention
RT signal.";
RL Mol. Biol. Cell 6:7-20(1995).
RN [11]
RP MUTAGENESIS OF CYS-153, AND SUBUNIT (CAPSID PROTEIN).
RX PubMed=8614992; DOI=10.1006/viro.1996.0051;
RA Lee J.Y., Hwang D., Gillam S.;
RT "Dimerization of rubella virus capsid protein is not required for virus
RT particle formation.";
RL Virology 216:223-227(1996).
RN [12]
RP SUBCELLULAR LOCATION (SPIKE GLYCOPROTEIN E1).
RX PubMed=9311850; DOI=10.1128/jvi.71.10.7670-7680.1997;
RA Hobman T.C., Lemon H.F., Jewell K.;
RT "Characterization of an endoplasmic reticulum retention signal in the
RT rubella virus E1 glycoprotein.";
RL J. Virol. 71:7670-7680(1997).
RN [13]
RP MUTAGENESIS OF CYS-664; GLY-675 AND PRO-686, SUBUNIT (SPIKE GLYCOPROTEIN
RP E1), SUBUNIT (SPIKE GLYCOPROTEIN E2), AND FUNCTION (SPIKE GLYCOPROTEIN E1).
RX PubMed=9765418; DOI=10.1128/jvi.72.11.8747-8755.1998;
RA Yang D., Hwang D., Qiu Z., Gillam S.;
RT "Effects of mutations in the rubella virus E1 glycoprotein on E1-E2
RT interaction and membrane fusion activity.";
RL J. Virol. 72:8747-8755(1998).
RN [14]
RP MUTAGENESIS OF LEU-1046; CYS-1048; CYS-1049; CYS-1052 AND LEU-1053, AND
RP FUNCTION (SPIKE GLYCOPROTEIN E1).
RX PubMed=10233921; DOI=10.1128/jvi.73.6.4622-4630.1999;
RA Yao J., Gillam S.;
RT "Mutational analysis, using a full-length rubella virus cDNA clone, of
RT rubella virus E1 transmembrane and cytoplasmic domains required for virus
RT release.";
RL J. Virol. 73:4622-4630(1999).
RN [15]
RP INTERACTION WITH HUMAN C1QBP (CAPSID PROTEIN), FUNCTION (CAPSID PROTEIN),
RP AND SUBCELLULAR LOCATION (CAPSID PROTEIN).
RX PubMed=10823864; DOI=10.1128/jvi.74.12.5569-5576.2000;
RA Beatch M.D., Hobman T.C.;
RT "Rubella virus capsid associates with host cell protein p32 and localizes
RT to mitochondria.";
RL J. Virol. 74:5569-5576(2000).
RN [16]
RP MUTAGENESIS OF CYS-1052; LEU-1053; TYR-1054; TYR-1055; LEU-1056; ARG-1057;
RP GLY-1058; ALA-1059; ILE-1060; ALA-1061; PRO-1062 AND ARG-1063, AND FUNCTION
RP (SPIKE GLYCOPROTEIN E1).
RX PubMed=10708417; DOI=10.1128/jvi.74.7.3029-3036.2000;
RA Yao J., Gillam S.;
RT "A single-amino-acid substitution of a tyrosine residue in the rubella
RT virus E1 cytoplasmic domain blocks virus release.";
RL J. Virol. 74:3029-3036(2000).
RN [17]
RP MUTAGENESIS OF GLY-675 AND PRO-686.
RX PubMed=10864678; DOI=10.1128/jvi.74.14.6637-6642.2000;
RA Qiu Z., Yao J., Cao H., Gillam S.;
RT "Mutations in the E1 hydrophobic domain of rubella virus impair virus
RT infectivity but not virus assembly.";
RL J. Virol. 74:6637-6642(2000).
RN [18]
RP FUNCTION (CAPSID PROTEIN).
RX PubMed=11017784; DOI=10.1006/viro.2000.0467;
RA Duncan R., Esmaili A., Law L.M., Bertholet S., Hough C., Hobman T.C.,
RA Nakhasi H.L.;
RT "Rubella virus capsid protein induces apoptosis in transfected RK13
RT cells.";
RL Virology 275:20-29(2000).
RN [19]
RP DOMAIN (CAPSID PROTEIN), AND SUBCELLULAR LOCATION (CAPSID PROTEIN).
RX PubMed=11160697; DOI=10.1128/jvi.75.4.1978-1983.2001;
RA Law L.M., Duncan R., Esmaili A., Nakhasi H.L., Hobman T.C.;
RT "Rubella virus E2 signal peptide is required for perinuclear localization
RT of capsid protein and virus assembly.";
RL J. Virol. 75:1978-1983(2001).
RN [20]
RP GLYCOSYLATION AT ASN-658; ASN-759 AND ASN-791, AND MUTAGENESIS OF ASN-658;
RP ASN-759 AND ASN-791.
RX PubMed=11682134; DOI=10.1016/s0168-1702(01)00374-4;
RA Ramanujam M., Hofmann J., Nakhasi H.L., Atreya C.D.;
RT "Effect of site-directed asparagine to isoleucine substitutions at the N-
RT linked E1 glycosylation sites on rubella virus viability.";
RL Virus Res. 81:151-156(2001).
RN [21]
RP PHOSPHORYLATION AT SER-46, AND RNA-BINDING.
RX PubMed=12525610; DOI=10.1128/jvi.77.3.1764-1771.2003;
RA Law L.M., Everitt J.C., Beatch M.D., Holmes C.F., Hobman T.C.;
RT "Phosphorylation of rubella virus capsid regulates its RNA binding activity
RT and virus replication.";
RL J. Virol. 77:1764-1771(2003).
RN [22]
RP MUTAGENESIS OF 35-ARG--ARG-43 AND 60-ARG--ARG-68, INTERACTION WITH HUMAN
RP C1QBP (CAPSID PROTEIN), AND FUNCTION (CAPSID PROTEIN).
RX PubMed=16051872; DOI=10.1128/jvi.79.16.10807-10820.2005;
RA Beatch M.D., Everitt J.C., Law L.J., Hobman T.C.;
RT "Interactions between rubella virus capsid and host protein p32 are
RT important for virus replication.";
RL J. Virol. 79:10807-10820(2005).
RN [23]
RP INTERACTION WITH THE PROTEASE/METHYLTRANSFERASE P150 (CAPSID PROTEIN), AND
RP SUBCELLULAR LOCATION (CAPSID PROTEIN).
RC STRAIN=RVi/Japan/Hiroshima/2003;
RX PubMed=25056903; DOI=10.1128/jvi.01758-14;
RA Sakata M., Otsuki N., Okamoto K., Anraku M., Nagai M., Takeda M., Mori Y.;
RT "Short self-interacting N-terminal region of rubella virus capsid protein
RT is essential for cooperative actions of capsid and nonstructural p150
RT proteins.";
RL J. Virol. 88:11187-11198(2014).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 583-1018 IN COMPLEX WITH CALCIUM,
RP GLYCOSYLATION AT ASN-658; ASN-759; THR-1011 AND THR-1012, AND FUNCTION
RP (SPIKE GLYCOPROTEIN E1).
RX PubMed=23292515; DOI=10.1038/nature11741;
RA DuBois R.M., Vaney M.C., Tortorici M.A., Kurdi R.A., Barba-Spaeth G.,
RA Krey T., Rey F.A.;
RT "Functional and evolutionary insight from the crystal structure of rubella
RT virus protein E1.";
RL Nature 493:552-556(2013).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 127-277, SUBUNIT (CAPSID
RP PROTEIN), AND FUNCTION (CAPSID PROTEIN).
RX PubMed=24282305; DOI=10.1073/pnas.1316681110;
RA Mangala Prasad V., Willows S.D., Fokine A., Battisti A.J., Sun S.,
RA Plevka P., Hobman T.C., Rossmann M.G.;
RT "Rubella virus capsid protein structure and its role in virus assembly and
RT infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20105-20110(2013).
RN [26]
RP STRUCTURE BY ELECTRON MICROSCOPY (11.10 ANGSTROMS) OF 583-1018, SUBCELLULAR
RP LOCATION (CAPSID PROTEIN), FUNCTION (CAPSID PROTEIN), FUNCTION (SPIKE
RP GLYCOPROTEIN E2), AND FUNCTION (SPIKE GLYCOPROTEIN E1).
RX PubMed=28575072; DOI=10.1371/journal.ppat.1006377;
RA Mangala Prasad V., Klose T., Rossmann M.G.;
RT "Assembly, maturation and three-dimensional helical structure of the
RT teratogenic rubella virus.";
RL PLoS Pathog. 13:E1006377-E1006377(2017).
CC -!- FUNCTION: [Capsid protein]: Capsid protein interacts with genomic RNA
CC and assembles into icosahedric core particles 65-70 nm in diameter
CC (PubMed:28575072). The resulting nucleocapsid eventually associates
CC with the cytoplasmic domain of E2 at the cell membrane, leading to
CC budding and formation of mature virions from host Golgi membranes
CC (PubMed:28575072). Phosphorylation negatively regulates RNA-binding
CC activity, possibly delaying virion assembly during the viral
CC replication phase. Capsid protein dimerizes and becomes disulfide-
CC linked in the virion (PubMed:24282305). Modulates genomic RNA
CC replication. Modulates subgenomic RNA synthesis by interacting with
CC human C1QBP/SF2P32 (PubMed:10823864). Induces both perinuclear
CC clustering of mitochondria and the formation of electron-dense
CC intermitochondrial plaques, both hallmarks of rubella virus infected
CC cells (PubMed:16051872). Induces apoptosis when expressed in
CC transfected cells (PubMed:11017784). {ECO:0000269|PubMed:10823864,
CC ECO:0000269|PubMed:11017784, ECO:0000269|PubMed:16051872,
CC ECO:0000269|PubMed:24282305, ECO:0000269|PubMed:28575072}.
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 (PubMed:28575072).
CC {ECO:0000269|PubMed:28575072}.
CC -!- FUNCTION: [Spike glycoprotein E1]: Class II viral fusion protein
CC (PubMed:23292515). Fusion activity is inactive as long as E1 is bound
CC to E2 in mature virion. After virus attachment to target cell and
CC clathrin-mediated endocytosis, acidification of the endosome would
CC induce dissociation of E1/E2 heterodimer and concomitant trimerization
CC of the E1 subunits (By similarity). This E1 homotrimer is fusion
CC active, and promotes release of viral nucleocapsid in cytoplasm after
CC endosome and viral membrane fusion (PubMed:9765418). The cytoplasmic
CC tail of spike glycoprotein E1 modulates virus release (PubMed:10708417,
CC PubMed:10233921). The surface glycoproteins display an irregular
CC helical organization and a pseudo-tetrameric inner nucleocapsid
CC arrangement (PubMed:28575072). {ECO:0000250|UniProtKB:P07566,
CC ECO:0000269|PubMed:10233921, ECO:0000269|PubMed:10708417,
CC ECO:0000269|PubMed:23292515, ECO:0000269|PubMed:28575072,
CC ECO:0000269|PubMed:9765418}.
CC -!- SUBUNIT: [Capsid protein]: Homodimer; further assembles into
CC homooligomer (PubMed:8614992, PubMed:24282305). Interacts with human
CC C1QBP (PubMed:10823864, PubMed:16051872). Interacts (via N-terminus)
CC with protease/methyltransferase p150 (PubMed:25056903).
CC {ECO:0000269|PubMed:10823864, ECO:0000269|PubMed:25056903,
CC ECO:0000269|PubMed:8614992}.
CC -!- SUBUNIT: [Spike glycoprotein E1]: Heterodimer with spike glycoprotein
CC E2 (PubMed:9765418). {ECO:0000269|PubMed:9765418}.
CC -!- SUBUNIT: [Spike glycoprotein E2]: Heterodimer with spike glycoprotein
CC E1 (PubMed:9765418). {ECO:0000269|PubMed:9765418}.
CC -!- INTERACTION:
CC PRO_0000041302; Q07021: C1QBP; Xeno; NbExp=3; IntAct=EBI-11478341, EBI-347528;
CC PRO_0000041302; Q9Y6H1: CHCHD2; Xeno; NbExp=3; IntAct=EBI-11478341, EBI-2321769;
CC PRO_0000041303; P57735: RAB25; Xeno; NbExp=2; IntAct=EBI-11477912, EBI-1050500;
CC PRO_0000041304; P46091: CMKLR2; Xeno; NbExp=2; IntAct=EBI-11477759, EBI-11477864;
CC PRO_0000041304; Q8IWU4: SLC30A8; Xeno; NbExp=2; IntAct=EBI-11477759, EBI-10262251;
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion
CC {ECO:0000269|PubMed:28575072}. Host cytoplasm
CC {ECO:0000269|PubMed:25056903}. Host mitochondrion
CC {ECO:0000269|PubMed:10823864}. Note=The capsid protein is concentrated
CC around Golgi region (PubMed:11160697). In the virion, it is probably
CC associated to the viral membrane (PubMed:2214022).
CC {ECO:0000269|PubMed:11160697, ECO:0000269|PubMed:2214022}.
CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane; Single-
CC pass type I membrane protein {ECO:0000305}. Host Golgi apparatus
CC membrane; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:7749196, ECO:0000269|PubMed:8468347}. Note=E1 and
CC E2 form heterodimer in the endoplasmic reticulum before they are
CC transported to and retained in the Golgi complex, where virus assembly
CC occurs. E1 possesses an endoplasmic reticulum retention signal, and
CC unassembled E2 and E1 subunits are retained in the endoplasmic
CC reticulum. Presumably, assembly of E2 and E1 would mask the signal,
CC thereby allowing transport of the heterodimer to the Golgi complex.
CC {ECO:0000305|PubMed:2683361, ECO:0000305|PubMed:2845137,
CC ECO:0000305|PubMed:8468347}.
CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E1]: Virion membrane; Single-
CC pass type I membrane protein {ECO:0000305}. Host Golgi apparatus
CC membrane; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:8468347}. 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 (Probable). E1 possesses
CC an endoplasmic reticulum retention signal, and unassembled E2 and E1
CC subunits are retained in the endoplasmic reticulum (Probable).
CC Presumably, assembly of E2 and E1 would mask the signal, thereby
CC allowing transport of the heterodimer to the Golgi complex (Probable).
CC {ECO:0000305|PubMed:2845137, ECO:0000305|PubMed:7749196,
CC ECO:0000305|PubMed:8468347, ECO:0000305|PubMed:9311850}.
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:0000269|PubMed:2683361, ECO:0000269|PubMed:2845137}.
CC -!- DOMAIN: [Capsid protein]: The capsid protein is probably attached to
CC the viral membrane through the E2 signal peptide (PubMed:2214022). This
CC domain is also required for the localization of the capsid protein to
CC the juxtanuclear region and subsequent virus assembly at the Golgi
CC complex (PubMed:11160697). {ECO:0000269|PubMed:11160697,
CC ECO:0000269|PubMed:2214022}.
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:0000269|PubMed:8178466}.
CC -!- PTM: [Spike glycoprotein E1]: Contains three N-linked oligosaccharides.
CC {ECO:0000269|PubMed:11682134, ECO:0000269|PubMed:2014650,
CC ECO:0000269|PubMed:23292515}.
CC -!- PTM: Capsid is phosphorylated on Ser-46 by host (PubMed:12525610). This
CC phosphorylation negatively regulates capsid protein RNA-binding
CC activity (PubMed:12525610). Dephosphorylated by human PP1A (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:12525610}.
CC -!- MISCELLANEOUS: Structural polyprotein: Translated from a subgenomic RNA
CC synthesized during togaviruses replication. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA28880.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X05259; CAA28880.1; ALT_SEQ; mRNA.
DR EMBL; M30776; AAA47421.1; ALT_SEQ; Genomic_RNA.
DR PIR; A27505; GNWVR3.
DR PIR; JQ0087; GNWV77.
DR PDB; 4ADG; X-ray; 2.18 A; A/B/C=583-1018.
DR PDB; 4ADI; X-ray; 1.80 A; A/B/C=583-1018.
DR PDB; 4ADJ; X-ray; 1.94 A; A/B/C=583-1018.
DR PDB; 4B3V; X-ray; 1.98 A; A/B/C=583-1018.
DR PDB; 4HAR; X-ray; 2.66 A; A/B/C/D/E/F=127-277.
DR PDB; 4HBE; X-ray; 2.30 A; A/B=127-277.
DR PDB; 4HBO; X-ray; 3.24 A; A/B/C/D/E=147-277.
DR PDB; 5KHC; EM; 11.10 A; A=583-1018.
DR PDBsum; 4ADG; -.
DR PDBsum; 4ADI; -.
DR PDBsum; 4ADJ; -.
DR PDBsum; 4B3V; -.
DR PDBsum; 4HAR; -.
DR PDBsum; 4HBE; -.
DR PDBsum; 4HBO; -.
DR PDBsum; 5KHC; -.
DR SMR; P08563; -.
DR IntAct; P08563; 35.
DR iPTMnet; P08563; -.
DR Proteomes; UP000007143; 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 1: Evidence at protein level;
KW 3D-structure; Calcium; Capsid protein;
KW Clathrin-mediated endocytosis of virus by host; Disulfide bond;
KW 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; Reference proteome; RNA-binding;
KW T=4 icosahedral capsid protein; Transmembrane; Transmembrane helix;
KW 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_0000041302"
FT CHAIN 301..582
FT /note="Spike glycoprotein E2"
FT /evidence="ECO:0000269|PubMed:11160697"
FT /id="PRO_0000041303"
FT CHAIN 583..1063
FT /note="Spike glycoprotein E1"
FT /evidence="ECO:0000269|PubMed:11160697"
FT /id="PRO_0000041304"
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:0000269|PubMed:7749196"
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:0000269|PubMed:9311850"
FT TOPO_DOM 1050..1063
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..69
FT /note="Human C1QBP/SF2P32-binding"
FT /evidence="ECO:0000269|PubMed:16051872"
FT REGION 279..300
FT /note="Functions as E2 signal peptide"
FT /evidence="ECO:0000269|PubMed:2683361"
FT REGION 563..582
FT /note="Functions as E1 signal peptide"
FT /evidence="ECO:0000269|PubMed:2845137"
FT COMPBIAS 37..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 670
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:4ADG, ECO:0007744|PDB:4ADJ,
FT ECO:0007744|PDB:4B3V"
FT BINDING 671
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:4ADG, ECO:0007744|PDB:4ADJ,
FT ECO:0007744|PDB:4B3V"
FT BINDING 718
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:4ADJ, ECO:0007744|PDB:4B3V"
FT BINDING 719
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:4ADG, ECO:0007744|PDB:4ADJ,
FT ECO:0007744|PDB:4B3V"
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:0000269|PubMed:12525610"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:11682134,
FT ECO:0000269|PubMed:23292515"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:11682134,
FT ECO:0000269|PubMed:2014650, ECO:0000269|PubMed:23292515"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:11682134,
FT ECO:0000269|PubMed:2014650"
FT CARBOHYD 1011
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000269|PubMed:23292515"
FT CARBOHYD 1012
FT /note="O-linked (GalNAc...) threonine; by host"
FT /evidence="ECO:0000269|PubMed:23292515"
FT DISULFID 153..197
FT /evidence="ECO:0000269|PubMed:24282305"
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"
FT VARIANT 272
FT /note="H -> R (in strain: Isolate HPV77 vaccine)"
FT VARIANT 411
FT /note="S -> Y (in strain: Isolate HPV77 vaccine)"
FT VARIANT 412
FT /note="T -> I (in strain: Isolate HPV77 vaccine)"
FT VARIANT 413
FT /note="T -> A (in strain: Isolate HPV77 vaccine)"
FT VARIANT 609
FT /note="R -> G (in strain: Isolate HPV77 vaccine)"
FT MUTAGEN 35..43
FT /note="RRPRPPRQR->AAPAPPAQA: Complete loss of human
FT C1QBP/SF2P32-binding. 90% loss of virus production from
FT infected cell."
FT /evidence="ECO:0000269|PubMed:16051872"
FT MUTAGEN 60..68
FT /note="RRRRGNRGR->AAAAGNAGA: Complete loss of human
FT C1QBP/SF2P32-binding. 90% loss of virus production from
FT infected cell."
FT /evidence="ECO:0000269|PubMed:16051872"
FT MUTAGEN 153
FT /note="C->S: Complete loss of Capsid dimerization. No
FT effect on particle budding."
FT /evidence="ECO:0000269|PubMed:8614992"
FT MUTAGEN 658
FT /note="N->I: Complete loss of infectivity."
FT /evidence="ECO:0000269|PubMed:11682134"
FT MUTAGEN 664
FT /note="C->S: Prevents E1-E2 heterodimer formation, and
FT subsequent transport of to the plasma membrane. Complete
FT loss of fusion activity in vitro."
FT /evidence="ECO:0000269|PubMed:9765418"
FT MUTAGEN 675
FT /note="G->D: Complete loss of fusion activity in vitro. 90%
FT loss of infectivity in vivo. No effect on virus assembly."
FT /evidence="ECO:0000269|PubMed:10864678,
FT ECO:0000269|PubMed:9765418"
FT MUTAGEN 686
FT /note="P->G: 99.9% loss of infectivity. No effect on virus
FT assembly. No effect on fusion activity in vitro."
FT /evidence="ECO:0000269|PubMed:10864678,
FT ECO:0000269|PubMed:9765418"
FT MUTAGEN 759
FT /note="N->I: No effect on infectivity."
FT /evidence="ECO:0000269|PubMed:11682134"
FT MUTAGEN 791
FT /note="N->I: Complete loss of infectivity."
FT /evidence="ECO:0000269|PubMed:11682134"
FT MUTAGEN 1046
FT /note="L->A: No effect on virus production from infected
FT cell."
FT /evidence="ECO:0000269|PubMed:10233921"
FT MUTAGEN 1048
FT /note="C->A: No effect on virus production from infected
FT cell."
FT /evidence="ECO:0000269|PubMed:10233921"
FT MUTAGEN 1049
FT /note="C->A: No effect on virus production from infected
FT cell."
FT /evidence="ECO:0000269|PubMed:10233921"
FT MUTAGEN 1052
FT /note="C->A: No effect on virus production from infected
FT cell."
FT /evidence="ECO:0000269|PubMed:10233921,
FT ECO:0000269|PubMed:10708417"
FT MUTAGEN 1053
FT /note="L->A: 90% loss of virus production from infected
FT cell."
FT /evidence="ECO:0000269|PubMed:10233921,
FT ECO:0000269|PubMed:10708417"
FT MUTAGEN 1054
FT /note="Y->A: Complete loss of virus production from
FT infected cell."
FT /evidence="ECO:0000269|PubMed:10708417"
FT MUTAGEN 1055
FT /note="Y->S: Complete loss of virus production from
FT infected cell."
FT /evidence="ECO:0000269|PubMed:10708417"
FT MUTAGEN 1056
FT /note="L->A: 90% loss of virus production from infected
FT cell."
FT /evidence="ECO:0000269|PubMed:10708417"
FT MUTAGEN 1057
FT /note="R->S: 98% loss of virus production from infected
FT cell."
FT /evidence="ECO:0000269|PubMed:10708417"
FT MUTAGEN 1058
FT /note="G->C: 98% loss of virus production from infected
FT cell."
FT /evidence="ECO:0000269|PubMed:10708417"
FT MUTAGEN 1059
FT /note="A->S: 90% loss of virus production from infected
FT cell."
FT /evidence="ECO:0000269|PubMed:10708417"
FT MUTAGEN 1060
FT /note="I->V: No effect on virus production from infected
FT cell."
FT /evidence="ECO:0000269|PubMed:10708417"
FT MUTAGEN 1061
FT /note="A->S: 90% loss of virus production from infected
FT cell."
FT /evidence="ECO:0000269|PubMed:10708417"
FT MUTAGEN 1062
FT /note="P->S: 90% loss of virus production from infected
FT cell."
FT /evidence="ECO:0000269|PubMed:10708417"
FT MUTAGEN 1063
FT /note="R->S: 98% loss of virus production from infected
FT cell."
FT /evidence="ECO:0000269|PubMed:10708417"
FT CONFLICT 42..69
FT /note="QRDSSTSGDDSGRDSGGPRRRRGNRGRG -> HARLQHLPEMTPAVTPEGPA
FT PPRTGAW (in Ref. 1; CAA28880)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="T -> I (in Ref. 1; CAA28880)"
FT /evidence="ECO:0000305"
FT CONFLICT 445..471
FT /note="RHGADTRCGRLICGLSTTAQYPPTRFG -> PTALTPGAVGDLRAVHHRPVP
FT AYPVC (in Ref. 1; CAA28880)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="V -> I (in Ref. 1; CAA28880)"
FT /evidence="ECO:0000305"
FT CONFLICT 562..577
FT /note="RGAAAALTAVVLQGYN -> PAPPPPSPQSSCRGTT (in Ref. 1;
FT CAA28880)"
FT /evidence="ECO:0000305"
FT CONFLICT 993..994
FT /note="RV -> GH (in Ref. 1; CAA28880)"
FT /evidence="ECO:0000305"
FT CONFLICT 995..1063
FT /note="Missing (in Ref. 1; CAA28880)"
FT /evidence="ECO:0000305"
FT STRAND 151..160
FT /evidence="ECO:0007829|PDB:4HBE"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:4HBO"
FT STRAND 167..176
FT /evidence="ECO:0007829|PDB:4HBE"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:4HBE"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:4HBE"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:4HBE"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:4HBE"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:4HBE"
FT STRAND 585..589
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 599..601
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 603..621
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 625..634
FT /evidence="ECO:0007829|PDB:4ADI"
FT TURN 641..647
FT /evidence="ECO:0007829|PDB:4ADI"
FT HELIX 650..657
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 659..670
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 672..674
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 676..678
FT /evidence="ECO:0007829|PDB:4ADI"
FT HELIX 681..683
FT /evidence="ECO:0007829|PDB:4ADI"
FT HELIX 689..694
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 698..703
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 716..718
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 721..729
FT /evidence="ECO:0007829|PDB:4ADI"
FT HELIX 733..735
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 737..753
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 756..760
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 766..768
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 770..777
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 785..790
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 797..804
FT /evidence="ECO:0007829|PDB:4ADI"
FT TURN 807..813
FT /evidence="ECO:0007829|PDB:4ADI"
FT HELIX 815..817
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 818..821
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 824..826
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 836..839
FT /evidence="ECO:0007829|PDB:4ADI"
FT HELIX 845..848
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 855..862
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 869..875
FT /evidence="ECO:0007829|PDB:4ADI"
FT HELIX 878..880
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 881..883
FT /evidence="ECO:0007829|PDB:4ADI"
FT HELIX 885..892
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 894..896
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 904..910
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 924..936
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 938..944
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 946..948
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 950..954
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 957..962
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 964..971
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 980..989
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 991..995
FT /evidence="ECO:0007829|PDB:4ADI"
FT HELIX 997..1001
FT /evidence="ECO:0007829|PDB:4ADI"
FT TURN 1002..1004
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 1005..1008
FT /evidence="ECO:0007829|PDB:4ADI"
FT STRAND 1010..1014
FT /evidence="ECO:0007829|PDB:4ADI"
SQ SEQUENCE 1063 AA; 114736 MW; B546067276483ECB CRC64;
MASTTPITME DLQKALEAQS RALRAGLAAG ASQSRRPRPP RQRDSSTSGD DSGRDSGGPR
RRRGNRGRGQ RKDWSRAPPP PEERQESRSQ TPAPKPSRAP PQQPQPPRMQ TGRGGSAPRP
ELGPPTNPFQ AAVARGLRPP LHDPDTEAPT EACVTSWLWS EGEGAVFYRV DLHFTNLGTP
PLDEDGRWDP ALMYNPCGPE PPAHVVRAYN QPAGDVRGVW GKGERTYAEQ DFRVGGTRWH
RLLRMPVRGL DGDTAPLPPH TTERIETRSA RHPWRIRFGA PQAFLAGLLL AAVAVGTARA
GLQPRADMAA PPMPPQPPRA HGQHYGHHHH QLPFLGHDGH HGGTLRVGQH HRNASDVLPG
HWLQGGWGCY NLSDWHQGTH VCHTKHMDFW CVEHDRPPPA TPTSLTTAAN STTAATPATA
PPPCHAGLND SCGGFLSGCG PMRLRHGADT RCGRLICGLS TTAQYPPTRF GCAMRWGLPP
WELVVLTARP EDGWTCRGVP AHPGTRCPEL VSPMGRATCS PASALWLATA NALSLDHAFA
AFVLLVPWVL IFMVCRRACR RRGAAAALTA VVLQGYNPPA YGEEAFTYLC TAPGCATQTP
VPVRLAGVRF ESKIVDGGCF APWDLEATGA CICEIPTDVS CEGLGAWVPT 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 VRPVALPRAL APPRNVRVTG CYQCGTPALV EGLAPGGGNC HLTVNGEDVG
AFPPGKFVTA ALLNTPPPYQ VSCGGESDRA SARVIDPAAQ SFTGVVYGTH TTAVSETRQT
WAEWAAAHWW QLTLGAICAL LLAGLLACCA KCLYYLRGAI APR
