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 24-JAN-2024, entry version 121. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-8248; -. DR SMR; P08563; -. DR IntAct; P08563; 37. 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:0016020; C: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; 2.60.98.30; Rubella membrane glycoprotein E1, domain 1; 1. DR Gene3D; 3.30.67.20; Rubella membrane glycoprotein E1, domain 2; 2. DR Gene3D; 2.60.40.2650; Rubella membrane glycoprotein E1, domain 3; 1. DR Gene3D; 3.10.50.50; Rubella virus capsid protein; 1. 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; 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_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 //