VP1_SV40
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-AUG-2022, entry version 156.
DE RecName: Full=Major capsid protein VP1;
DE AltName: Full=Major structural protein VP1;
OS Simian virus 40 (SV40).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; 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., Pan J.,
RA 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; DOI=10.1016/s0021-9258(18)35981-7;
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; DOI=10.1016/s0021-9258(19)81665-4;
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; DOI=10.1128/jvi.70.2.1317-1322.1996;
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 capsid
RT protein Vp1.";
RL J. Virol. 70:1317-1322(1996).
RN [7]
RP DISULFIDE BONDS IN INTER-PENTAMER.
RX PubMed=10501505; DOI=10.1099/0022-1317-80-9-2481;
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 inter-
RT pentamer disulfide-linkage and stabilization in cell-free 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 and
RT 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., Fernandez C.F.,
RA Chan S.W., Kasamatsu H.;
RT "Simian virus 40 Vp1 DNA-binding domain is functionally separable from the
RT overlapping nuclear localization signal and is required for effective
RT 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 proteins
RT 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, and
RT 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 formation of
RT 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 for
RT 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 factors
RT 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 understanding
RT 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 SUBCELLULAR
RP 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 nm
CC diameter. The capsid is composed of 72 pentamers linked to each other
CC by disulfide bonds and associated with VP2 or VP3 proteins. Binds to N-
CC glycolylneuraminic analog of the ganglioside GM1 on the cell surface to
CC provide virion attachment to target cell (PubMed:18353982). Once
CC attached, the virion is internalized by caveolin-mediated endocytosis
CC and traffics to the endoplasmic reticulum. Inside the endoplasmic
CC reticulum, the protein folding machinery isomerizes VP1 interpentamer
CC disulfide bonds, thereby triggering initial uncoating
CC (PubMed:17981119). Next, the virion uses the endoplasmic reticulum-
CC associated degradation machinery to probably translocate in the cytosol
CC before reaching the nucleus (PubMed:17981119). Nuclear entry of the
CC viral DNA involves the selective exposure and importin recognition of
CC VP2/Vp3 nuclear localization signal. The assembly takes place in the
CC cell nucleus. Encapsulates the genomic DNA and participates in
CC rearranging nucleosomes around the viral DNA. The viral progenies exit
CC the 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 composed
CC of 72 icosahedral units, each one composed of five disulfide-linked
CC copies of VP1. Interacts with agnoprotein (By similarity). Interacts
CC with minor capsid proteins VP2 and VP3. Interacts with host HSPA8; this
CC interaction probably participates in virus assembly. Interacts with
CC host SP1; this interaction enhances the efficiency of viral packaging.
CC {ECO:0000250, 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 P03087; P03087: -; NbExp=3; IntAct=EBI-1555770, EBI-1555770;
CC P03087; O92837: VP3; NbExp=3; IntAct=EBI-1555770, EBI-7196689;
CC P03087; P03093; NbExp=3; IntAct=EBI-1555770, EBI-1555798;
CC P03087; P11103: Parp1; Xeno; NbExp=2; IntAct=EBI-1555770, EBI-642213;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:8805523}. Host nucleus
CC {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 to
CC 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 Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=P03093-1; Sequence=External;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P03093-2; Sequence=External;
CC Name=VP4; Synonyms=Viroporin VP4;
CC IsoId=P03093-3; Sequence=External;
CC Name=Agno;
CC IsoId=P03084-1; Sequence=External;
CC -!- DOMAIN: The intrinsically disordered C-terminal arm interacts with
CC neighboring pentamers. The unstructured nature of this region allows to
CC make different interactions depending on the structural context:
CC pentamers present at the 12 icosahedral fivefold axes bind five
CC pentamers, whereas pentamers present at the 60 icosahedral six-fold
CC axes interact with six pentamers. {ECO:0000269|PubMed:1659663,
CC ECO:0000269|PubMed:8805523}.
CC -!- DOMAIN: A DNA-binding domain overlapping a bipartite nuclear
CC localization signal is present in the N-terminal region of the protein
CC and is required for efficient virus formation.
CC {ECO:0000269|PubMed:11462004}.
CC -!- MISCELLANEOUS: [Isoform VP1]: Produced by alternative splicing of the
CC late mRNA (16s mRNA).
CC -!- SIMILARITY: Belongs to the polyomaviruses coat protein VP1 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1sva";
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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 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: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; Capsid protein;
KW Caveolin-mediated endocytosis of virus by host; Direct protein sequencing;
KW Disulfide bond; Host endoplasmic reticulum; Host nucleus;
KW Host-virus interaction; Late protein; Phosphoprotein; Reference proteome;
KW T=7 icosahedral capsid protein; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT CHAIN 2..362
FT /note="Major capsid protein VP1"
FT /id="PRO_0000115028"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..362
FT /note="C-terminal arm"
FT /evidence="ECO:0000269|PubMed:1659663,
FT ECO:0000269|PubMed:8805523"
FT MOTIF 5..19
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:11462004,
FT ECO:0000269|PubMed:8551602"
FT MOD_RES 338
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000269|PubMed:2464591"
FT DISULFID 10
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:10501505"
FT DISULFID 105
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:10501505"
FT DISULFID 208
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:10501505"
FT VARIANT 99
FT /note="I -> L (in strain: 776)"
FT MUTAGEN 49
FT /note="E->A: 99% loss of infectivity ex vivo."
FT /evidence="ECO:0000269|PubMed:12805453"
FT MUTAGEN 50
FT /note="C->S: No effect on infectivity ex vivo."
FT /evidence="ECO:0000269|PubMed:15567029"
FT MUTAGEN 88
FT /note="C->S: 99% loss of infectivity ex vivo."
FT /evidence="ECO:0000269|PubMed:15567029"
FT MUTAGEN 158
FT /note="E->K,R: Complete loss of infectivity ex vivo,
FT defective in nuclear entry."
FT /evidence="ECO:0000269|PubMed:17360742"
FT MUTAGEN 161
FT /note="E->K,R: 95% loss of infectivity ex vivo."
FT /evidence="ECO:0000269|PubMed:17360742"
FT MUTAGEN 217
FT /note="E->K,R: 99% loss of infectivity ex vivo."
FT /evidence="ECO:0000269|PubMed:12805453"
FT MUTAGEN 244
FT /note="V->E: Complete loss of infectivity ex vivo."
FT /evidence="ECO:0000269|PubMed:16940501"
FT MUTAGEN 246
FT /note="L->E: Complete loss of infectivity ex vivo."
FT /evidence="ECO:0000269|PubMed:16940501"
FT MUTAGEN 255
FT /note="C->S: Complete loss of infectivity ex vivo."
FT /evidence="ECO:0000269|PubMed:15567029"
FT MUTAGEN 268
FT /note="C->S: No effect on infectivity ex vivo."
FT /evidence="ECO:0000269|PubMed:15567029"
FT MUTAGEN 331
FT /note="E->K,R: Complete loss of infectivity ex vivo,
FT defective in adsorbing to cells."
FT /evidence="ECO:0000269|PubMed:12805453"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:1SVA"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:3BWR"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3BWR"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3BWR"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:3BWR"
FT STRAND 105..121
FT /evidence="ECO:0007829|PDB:3BWR"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:3BWR"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:3BWR"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3BWR"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3BWR"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:3BWR"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:3BWR"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:3BWR"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:1SVA"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:3BWR"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:3BWR"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:3BWR"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:3BWR"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:1SVA"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:3BWR"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:3BWR"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:3BWR"
FT STRAND 259..272
FT /evidence="ECO:0007829|PDB:3BWR"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:3BWR"
FT STRAND 285..297
FT /evidence="ECO:0007829|PDB:3BWR"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1SVA"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1SVA"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:1SVA"
FT STRAND 353..359
FT /evidence="ECO:0007829|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
