ID VP1_SV40 Reviewed; 362 AA. AC P03087; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 03-JUL-2019, entry version 142. DE RecName: Full=Major capsid protein VP1; DE AltName: Full=Major structural protein VP1; OS Simian virus 40 (SV40). OC Viruses; Polyomaviridae; Betapolyomavirus. OX NCBI_TaxID=1891767; OH NCBI_TaxID=9539; Macaca (macaques). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=205947; DOI=10.1126/science.205947; RA Reddy V.B., Thimmappaya B., Dhar R., Subramanian K.N., Zain B.S., RA Pan J., Ghosh P.K., Celma M.L., Weissman S.M.; RT "The genome of simian virus 40."; RL Science 200:494-502(1978). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=776; RX PubMed=205802; DOI=10.1038/273113a0; RA Fiers W., Contreras R., Haegeman G., Rogiers R., van de Voorde A., RA van Heuverswyn H., van Herreweghe J., Volckaert G., Ysebaert M.; RT "Complete nucleotide sequence of SV40 DNA."; RL Nature 273:113-120(1978). RN [3] RP PROTEIN SEQUENCE. RX PubMed=224033; RA Kempe T.D., Beattie W.G., Weissman S., Konigsberg W.; RT "Correlation of the protein and nucleic acid sequences for the major RT structural protein of simian virus 40."; RL J. Biol. Chem. 254:7561-7569(1979). RN [4] RP VIRION ASSEMBLY. RX PubMed=13963379; DOI=10.1083/jcb.17.2.423; RA Granboulan N., Tournier P., Wicker R., Bernhard W.; RT "An electron microscope study of the development of SV40 virus."; RL J. Cell Biol. 17:423-441(1963). RN [5] RP PHOSPHORYLATION AT THR-338. RX PubMed=2464591; RA Babe L.M., Brew K., Matsuura S.E., Scott W.A.; RT "Epitopes on the major capsid protein of simian virus 40."; RL J. Biol. Chem. 264:2665-2671(1989). RN [6] RP NUCLEAR LOCALIZATION SIGNAL. RX PubMed=8551602; RA Ishii N., Minami N., Chen E.Y., Medina A.L., Chico M.M., Kasamatsu H.; RT "Analysis of a nuclear localization signal of simian virus 40 major RT capsid protein Vp1."; RL J. Virol. 70:1317-1322(1996). RN [7] RP DISULFIDE BONDS IN INTER-PENTAMER. RX PubMed=10501505; RA Jao C.C., Weidman M.K., Perez A.R., Gharakhanian E.; RT "Cys9, Cys104 and Cys207 of simian virus 40 Vp1 are essential for RT inter-pentamer disulfide-linkage and stabilization in cell-free RT lysates."; RL J. Gen. Virol. 80:2481-2489(1999). RN [8] RP INTERACTION WITH HOST HSPA8. RX PubMed=11147964; DOI=10.1379/1466-1268(2000)005<0132:HIWSVP>2.0.CO;2; RA Sainis L., Angelidis C., Pagoulatos G.N., Lazaridis L.; RT "HSC70 interactions with SV40 viral proteins differ between permissive RT and nonpermissive mammalian cells."; RL Cell Stress Chaperones 5:132-138(2000). RN [9] RP DNA-BINDING, NUCLEAR LOCALIZATION SIGNAL, AND SUBCELLULAR LOCATION. RX PubMed=11462004; DOI=10.1128/JVI.75.16.7321-7329.2001; RA Li P.P., Nakanishi A., Shum D., Sun P.C., Salazar A.M., RA Fernandez C.F., Chan S.W., Kasamatsu H.; RT "Simian virus 40 Vp1 DNA-binding domain is functionally separable from RT the overlapping nuclear localization signal and is required for RT effective virion formation and full viability."; RL J. Virol. 75:7321-7329(2001). RN [10] RP INTERACTION WITH HOST SP1. RX PubMed=12021324; DOI=10.1128/JVI.76.12.5915-5924.2002; RA Gordon-Shaag A., Ben-Nun-Shaul O., Roitman V., Yosef Y., Oppenheim A.; RT "Cellular transcription factor Sp1 recruits simian virus 40 capsid RT proteins to the viral packaging signal, ses."; RL J. Virol. 76:5915-5924(2002). RN [11] RP MUTAGENESIS OF GLU-49; GLU-217 AND GLU-331. RX PubMed=12805453; DOI=10.1128/JVI.77.13.7527-7538.2003; RA Li P.P., Naknanishi A., Tran M.A., Ishizu K., Kawano M., Phillips M., RA Handa H., Liddington R.C., Kasamatsu H.; RT "Importance of Vp1 calcium-binding residues in assembly, cell entry, RT and nuclear entry of simian virus 40."; RL J. Virol. 77:7527-7538(2003). RN [12] RP MUTAGENESIS OF CYS-50; CYS-88; CYS-255 AND CYS-268. RX PubMed=15567029; DOI=10.1016/j.virusres.2004.06.006; RA Gharakhanian E., Mana W., Norng M.; RT "Cys254 and Cys49/Cys87of simian virus 40 Vp1 are essential in RT formation of infectious virions."; RL Virus Res. 107:21-25(2005). RN [13] RP INTERACTION WITH VP2 AND VP3, AND MUTAGENESIS OF VAL-244 AND LEU-246. RX PubMed=16940501; DOI=10.1128/JVI.00781-06; RA Nakanishi A., Nakamura A., Liddington R., Kasamatsu H.; RT "Identification of amino acid residues within simian virus 40 capsid RT proteins Vp1, Vp2, and Vp3 that are required for their interaction and RT for viral infection."; RL J. Virol. 80:8891-8898(2006). RN [14] RP MUTAGENESIS OF GLU-158 AND GLU-161. RX PubMed=17360742; DOI=10.1128/JVI.02195-06; RA Li P.P., Nguyen A.P., Qu Q., Jafri Q.H., Aungsumart S., Cheng R.H., RA Kasamatsu H.; RT "Importance of calcium-binding site 2 in simian virus 40 infection."; RL J. Virol. 81:6099-6105(2007). RN [15] RP ISOMERIZATION OF DISULFIDE BONDS, AND FUNCTION. RX PubMed=17981119; DOI=10.1016/j.cell.2007.09.038; RA Schelhaas M., Malmstroem J., Pelkmans L., Haugstetter J., Ellgaard L., RA Gruenewald K., Helenius A.; RT "Simian Virus 40 depends on ER protein folding and quality control RT factors for entry into host cells."; RL Cell 131:516-529(2007). RN [16] RP REVIEW. RX PubMed=19157478; DOI=10.1016/j.virol.2008.12.021; RA Neu U., Stehle T., Atwood W.J.; RT "The Polyomaviridae: Contributions of virus structure to our RT understanding of virus receptors and infectious entry."; RL Virology 384:389-399(2009). RN [17] RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS). RX PubMed=1659663; DOI=10.1038/354278a0; RA Liddinngton R.C., Yan Y., Moulai J., Sahli R., Benjamin T.L., RA Harrison S.C.; RT "Structure of simian virus 40 at 3.8-A resolution."; RL Nature 354:278-284(1991). RN [18] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 2-362, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=8805523; DOI=10.1016/S0969-2126(96)00020-2; RA Stehle T., Gamblin S.J., Yan Y., Harrison S.C.; RT "The structure of simian virus 40 refined at 3.1-A resolution."; RL Structure 4:165-182(1996). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 31-298, AND FUNCTION. RX PubMed=18353982; DOI=10.1073/pnas.0710301105; RA Neu U., Woellner K., Gauglitz G., Stehle T.; RT "Structural basis of GM1 ganglioside recognition by simian virus 40."; RL Proc. Natl. Acad. Sci. U.S.A. 105:5219-5224(2008). CC -!- FUNCTION: Forms an icosahedral capsid with a T=7 symmetry and a 40 CC nm diameter. The capsid is composed of 72 pentamers linked to each CC other by disulfide bonds and associated with VP2 or VP3 proteins. CC Binds to N-glycolylneuraminic analog of the ganglioside GM1 on the CC cell surface to provide virion attachment to target cell CC (PubMed:18353982). Once attached, the virion is internalized by CC caveolin-mediated endocytosis and traffics to the endoplasmic CC reticulum. Inside the endoplasmic reticulum, the protein folding CC machinery isomerizes VP1 interpentamer disulfide bonds, thereby CC triggering initial uncoating (PubMed:17981119). Next, the virion CC uses the endoplasmic reticulum-associated degradation machinery to CC probably translocate in the cytosol before reaching the nucleus CC (PubMed:17981119). Nuclear entry of the viral DNA involves the CC selective exposure and importin recognition of VP2/Vp3 nuclear CC localization signal. The assembly takes place in the cell nucleus. CC Encapsulates the genomic DNA and participates in rearranging CC nucleosomes around the viral DNA. The viral progenies exit the CC cells by lytic release. {ECO:0000269|PubMed:17981119, CC ECO:0000269|PubMed:18353982, ECO:0000305|PubMed:19157478}. CC -!- SUBUNIT: Homomultimer; disulfide-linked. The virus capsid is CC composed of 72 icosahedral units, each one composed of five CC disulfide-linked copies of VP1. Interacts with agnoprotein (By CC similarity). Interacts with minor capsid proteins VP2 and VP3. CC Interacts with host HSPA8; this interaction probably participates CC in virus assembly. Interacts with host SP1; this interaction CC enhances the efficiency of viral packaging. {ECO:0000250, CC ECO:0000269|PubMed:10501505, ECO:0000269|PubMed:11147964, CC ECO:0000269|PubMed:12021324, ECO:0000269|PubMed:16940501, CC ECO:0000269|PubMed:8805523}. CC -!- INTERACTION: CC Self; NbExp=3; IntAct=EBI-1555770, EBI-1555770; CC P03093:-; NbExp=3; IntAct=EBI-1555770, EBI-1555798; CC P11103:Parp1 (xeno); NbExp=2; IntAct=EBI-1555770, EBI-642213; CC O92837:vp3; NbExp=3; IntAct=EBI-1555770, EBI-7196689; CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:8805523}. Host CC nucleus {ECO:0000269|PubMed:11462004}. Host endoplasmic reticulum CC {ECO:0000305|PubMed:19157478}. Note=Following host cell entry, the CC virion enters into the endoplasmic reticulum through a calveolar- CC dependent pathway. Then, viral DNA is translocated to the nucleus. CC Shortly after synthesis, a nuclear localization signal directs VP1 CC to the cell nucleus where virion assembly occurs. CC {ECO:0000305|PubMed:19157478}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=5; CC Name=VP1; Synonyms=Major capsid protein VP1; CC IsoId=P03087-1; Sequence=Displayed; CC Note=Produced by alternative splicing of the late mRNA (16s CC mRNA).; CC Name=VP2; Synonyms=Minor capsid protein VP2; CC IsoId=P03093-1; Sequence=External; CC Note=Produced by alternative splicing of the late mRNA (19s CC mRNA).; CC Name=VP3; Synonyms=Minor capsid protein VP3; CC IsoId=P03093-2; Sequence=External; CC Note=Produced by alternative initiation at Met-119 of isoform CC VP2.; CC Name=VP4; Synonyms=Viroporin VP4; CC IsoId=P03093-3; Sequence=External; CC Note=Produced by alternative initiation at Met-228 of isoform CC VP2.; CC Name=Agno; CC IsoId=P03084-1; Sequence=External; CC Note=Produced by alternative initiation of the late mRNA (16s CC and 19s mRNAs).; CC -!- DOMAIN: The intrinsically disordered C-terminal region interacts CC with neighboring pentamers. The unstructured nature of this region CC allows to make different interactions depending on the structural CC context: pentamers present at the 12 icosahedral fivefold axes CC bind five pentamers, whereas pentamers present at the 60 CC icosahedral six-fold axes interact with six pentamers. CC -!- DOMAIN: A DNA-binding domain overlapping a bipartite nuclear CC localization signal is present in the N-terminal region of the CC protein and is required for efficient virus formation. CC {ECO:0000269|PubMed:11462004}. CC -!- SIMILARITY: Belongs to the polyomaviruses coat protein VP1 family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral CC capsid structure; CC URL="http://viperdb.scripps.edu/info_page.php?VDB=1sva"; 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; J02400; AAB59923.1; -; Genomic_DNA. DR PIR; A31426; A31426. DR PIR; E03631; VVVP14. DR RefSeq; YP_003708381.1; NC_001669.1. DR PDB; 1SVA; X-ray; 3.10 A; 1/2/3/4/5/6=2-362. DR PDB; 3BWQ; X-ray; 2.30 A; A/B/C/D/E=31-298. DR PDB; 3BWR; X-ray; 2.25 A; A/B/C/D/E=31-298. DR PDBsum; 1SVA; -. DR PDBsum; 3BWQ; -. DR PDBsum; 3BWR; -. DR SMR; P03087; -. DR DIP; DIP-29870N; -. DR IntAct; P03087; 3. DR MINT; P03087; -. DR UniLectin; P03087; -. DR iPTMnet; P03087; -. DR GeneID; 29031018; -. DR KEGG; vg:29031018; -. DR OrthoDB; 9678at10239; -. DR EvolutionaryTrace; P03087; -. DR Proteomes; UP000007705; Genome. DR GO; GO:0046727; C:capsomere; IDA:CAFA. DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0039620; C:T=7 icosahedral viral capsid; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IDA:CAFA. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0075513; P:caveolin-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW. DR GO; GO:0051260; P:protein homooligomerization; IDA:CAFA. DR GO; GO:0019069; P:viral capsid assembly; IDA:CAFA. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR DisProt; DP00182; -. DR Gene3D; 2.60.175.10; -; 1. DR InterPro; IPR000662; Capsid_VP1_Polyomavir. DR InterPro; IPR011222; dsDNA_vir_gr_I_capsid. DR InterPro; IPR036931; Polyomavir_VP1_sf. DR Pfam; PF00718; Polyoma_coat; 1. DR PIRSF; PIRSF003376; Capsid_VP1_Polyomavir; 1. DR SUPFAM; SSF88648; SSF88648; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; Alternative splicing; KW Capsid protein; Caveolin-mediated endocytosis of virus by host; KW Complete proteome; Direct protein sequencing; Disulfide bond; KW Host endoplasmic reticulum; Host nucleus; Host-virus interaction; KW Late protein; Phosphoprotein; Reference proteome; KW T=7 icosahedral capsid protein; Viral attachment to host cell; KW Viral penetration into host cytoplasm; Virion; KW Virus endocytosis by host; Virus entry into host cell. FT INIT_MET 1 1 Removed; by host. FT CHAIN 2 362 Major capsid protein VP1. FT /FTId=PRO_0000115028. FT REGION 302 362 Intrinsically disordered. {ECO:0000255}. FT MOTIF 5 19 Bipartite nuclear localization signal. FT {ECO:0000269|PubMed:11462004, FT ECO:0000269|PubMed:8551602}. FT MOD_RES 338 338 Phosphothreonine; by host. FT {ECO:0000269|PubMed:2464591}. FT DISULFID 10 10 Interchain. FT {ECO:0000269|PubMed:10501505}. FT DISULFID 105 105 Interchain. FT {ECO:0000269|PubMed:10501505}. FT DISULFID 208 208 Interchain. FT {ECO:0000269|PubMed:10501505}. FT VARIANT 99 99 I -> L (in strain: 776). FT MUTAGEN 49 49 E->A: 99% loss of infectivity ex vivo. FT {ECO:0000269|PubMed:12805453}. FT MUTAGEN 50 50 C->S: No effect on infectivity ex vivo. FT {ECO:0000269|PubMed:15567029}. FT MUTAGEN 88 88 C->S: 99% loss of infectivity ex vivo. FT {ECO:0000269|PubMed:15567029}. FT MUTAGEN 158 158 E->K,R: Complete loss of infectivity ex FT vivo, defective in nuclear entry. FT {ECO:0000269|PubMed:17360742}. FT MUTAGEN 161 161 E->K,R: 95% loss of infectivity ex vivo. FT {ECO:0000269|PubMed:17360742}. FT MUTAGEN 217 217 E->K,R: 99% loss of infectivity ex vivo. FT {ECO:0000269|PubMed:12805453}. FT MUTAGEN 244 244 V->E: Complete loss of infectivity ex FT vivo. {ECO:0000269|PubMed:16940501}. FT MUTAGEN 246 246 L->E: Complete loss of infectivity ex FT vivo. {ECO:0000269|PubMed:16940501}. FT MUTAGEN 255 255 C->S: Complete loss of infectivity ex FT vivo. {ECO:0000269|PubMed:15567029}. FT MUTAGEN 268 268 C->S: No effect on infectivity ex vivo. FT {ECO:0000269|PubMed:15567029}. FT MUTAGEN 331 331 E->K,R: Complete loss of infectivity ex FT vivo, defective in adsorbing to cells. FT {ECO:0000269|PubMed:12805453}. FT HELIX 33 37 {ECO:0000244|PDB:1SVA}. FT STRAND 45 52 {ECO:0000244|PDB:3BWR}. FT HELIX 61 63 {ECO:0000244|PDB:3BWR}. FT HELIX 83 85 {ECO:0000244|PDB:3BWR}. FT STRAND 90 95 {ECO:0000244|PDB:3BWR}. FT STRAND 105 121 {ECO:0000244|PDB:3BWR}. FT HELIX 123 127 {ECO:0000244|PDB:3BWR}. FT STRAND 130 132 {ECO:0000244|PDB:3BWR}. FT STRAND 135 137 {ECO:0000244|PDB:3BWR}. FT STRAND 145 147 {ECO:0000244|PDB:3BWR}. FT STRAND 149 158 {ECO:0000244|PDB:3BWR}. FT STRAND 161 164 {ECO:0000244|PDB:3BWR}. FT HELIX 185 188 {ECO:0000244|PDB:3BWR}. FT HELIX 192 194 {ECO:0000244|PDB:1SVA}. FT STRAND 195 197 {ECO:0000244|PDB:3BWR}. FT TURN 201 203 {ECO:0000244|PDB:3BWR}. FT TURN 206 208 {ECO:0000244|PDB:3BWR}. FT STRAND 209 211 {ECO:0000244|PDB:3BWR}. FT TURN 213 215 {ECO:0000244|PDB:1SVA}. FT STRAND 219 226 {ECO:0000244|PDB:3BWR}. FT STRAND 234 240 {ECO:0000244|PDB:3BWR}. FT HELIX 256 258 {ECO:0000244|PDB:3BWR}. FT STRAND 259 272 {ECO:0000244|PDB:3BWR}. FT STRAND 278 282 {ECO:0000244|PDB:3BWR}. FT STRAND 285 297 {ECO:0000244|PDB:3BWR}. FT STRAND 304 306 {ECO:0000244|PDB:1SVA}. FT HELIX 324 326 {ECO:0000244|PDB:1SVA}. FT STRAND 348 351 {ECO:0000244|PDB:1SVA}. FT STRAND 353 359 {ECO:0000244|PDB:1SVA}. SQ SEQUENCE 362 AA; 39906 MW; 81C28EB7EA51D398 CRC64; MAPTKRKGSC PGAAPKKPKE PVQVPKLVIK GGIEVLGVKT GVDSFTEVEC FLNPQMGNPD EHQKGLSKSL AAEKQFTDDS PDKEQLPCYS VARIPLPNIN EDLTCGNILM WEAVTVKTEV IGVTAMLNLH SGTQKTHENG AGKPIQGSNF HFFAVGGEPL ELQGVLANYR TKYPAQTVTP KNATVDSQQM NTDHKAVLDK DNAYPVECWV PDPSKNENTR YFGTYTGGEN VPPVLHITNT ATTVLLDEQG VGPLCKADSL YVSAVDICGL FTNTSGTQQW KGLPRYFKIT LRKRSVKNPY PISFLLSDLI NRRTQRVDGQ PMIGMSSQVE EVRVYEDTEE LPGDPDMIRY IDEFGQTTTR MQ //