VP2_SV40
ID VP2_SV40 Reviewed; 352 AA.
AC P03093;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Minor capsid protein VP2;
DE AltName: Full=Minor structural protein VP2;
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 ALTERNATIVE INITIATION (ISOFORM VP3).
RX PubMed=199354; DOI=10.1016/0092-8674(77)90129-5;
RA Contreras R., Rogiers R., Van de Voorde A., Fiers W.;
RT "Overlapping of the VP2-VP3 gene and the VP1 gene in the SV40 genome.";
RL Cell 12:529-538(1977).
RN [4]
RP ALTERNATIVE SPLICING.
RX PubMed=211423; DOI=10.1038/273070a0;
RA Haegeman G., Fiers W.;
RT "Evidence for 'splicing' of SV40 16S mRNA.";
RL Nature 273:70-73(1978).
RN [5]
RP MYRISTOYLATION AT GLY-2, AND FUNCTION (ISOFORM VP2).
RX PubMed=3031509; DOI=10.1038/326619a0;
RA Streuli C.H., Griffin B.E.;
RT "Myristic acid is coupled to a structural protein of polyoma virus and
RT SV40.";
RL Nature 326:619-622(1987).
RN [6]
RP NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION (ISOFORM VP2), AND
RP SUBCELLULAR LOCATION (ISOFORM VP3).
RX PubMed=1847270; DOI=10.1016/0042-6822(91)90472-n;
RA Clever J., Kasamatsu H.;
RT "Simian virus 40 Vp2/3 small structural proteins harbor their own nuclear
RT transport signal.";
RL Virology 181:78-90(1991).
RN [7]
RP DNA-BINDING, AND DOMAIN.
RX PubMed=8407920; DOI=10.1016/s0021-9258(19)36868-1;
RA Clever J., Dean D.A., Kasamatsu H.;
RT "Identification of a DNA binding domain in simian virus 40 capsid proteins
RT Vp2 and Vp3.";
RL J. Biol. Chem. 268:20877-20883(1993).
RN [8]
RP MUTAGENESIS OF LYS-344 AND ARG-348, FUNCTION (ISOFORM VP2), AND FUNCTION
RP (ISOFORM VP3).
RX PubMed=7815491; DOI=10.1128/jvi.69.2.1115-1121.1995;
RA Dean D.A., Li P.P., Lee L.M., Kasamatsu H.;
RT "Essential role of the Vp2 and Vp3 DNA-binding domain in simian virus 40
RT morphogenesis.";
RL J. Virol. 69:1115-1121(1995).
RN [9]
RP INTERACTION WITH HOST SP1 (ISOFORM VP3), AND FUNCTION (ISOFORM VP3).
RX PubMed=9466902; DOI=10.1006/jmbi.1997.1461;
RA Gordon-Shaag A., Ben-Nun-Shaul O., Kasamatsu H., Oppenheim A.B.,
RA Oppenheim A.;
RT "The SV40 capsid protein VP3 cooperates with the cellular transcription
RT factor Sp1 in DNA-binding and in regulating viral promoter activity.";
RL J. Mol. Biol. 275:187-195(1998).
RN [10]
RP FUNCTION (ISOFORM VP3), AND INTERACTION WITH IMPORTIN ALPHA2-BETA
RP HETERODIMER.
RX PubMed=12186919; DOI=10.1128/jvi.76.18.9368-9377.2002;
RA Nakanishi A., Shum D., Morioka H., Otsuka E., Kasamatsu H.;
RT "Interaction of the Vp3 nuclear localization signal with the importin alpha
RT 2/beta heterodimer directs nuclear entry of infecting simian virus 40.";
RL J. Virol. 76:9368-9377(2002).
RN [11]
RP INTERACTION WITH VP1 (ISOFORM VP2), INTERACTION WITH VP1 (ISOFORM VP3),
RP MUTAGENESIS OF 276-PHE-ILE-277; 283-PRO--GLY-285; LEU-296 AND LEU-300, AND
RP DOMAIN.
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 [12]
RP FUNCTION (ISOFORM VP2), FUNCTION (ISOFORM VP3), SUBUNIT, SUBCELLULAR
RP LOCATION (ISOFORM VP2), AND SUBCELLULAR LOCATION (ISOFORM VP3).
RX PubMed=17189196; DOI=10.1016/j.molcel.2006.11.001;
RA Daniels R., Rusan N.M., Wadsworth P., Hebert D.N.;
RT "SV40 VP2 and VP3 insertion into ER membranes is controlled by the capsid
RT protein VP1: implications for DNA translocation out of the ER.";
RL Mol. Cell 24:955-966(2006).
RN [13]
RP ALTERNATIVE INITIATION (ISOFORM VP4), AND SUBCELLULAR LOCATION (ISOFORM
RP VP4).
RX PubMed=17658947; DOI=10.1371/journal.ppat.0030098;
RA Daniels R., Sadowicz D., Hebert D.N.;
RT "A very late viral protein triggers the lytic release of SV40.";
RL PLoS Pathog. 3:E98-E98(2007).
RN [14]
RP FUNCTION (ISOFORM VP4).
RX PubMed=21738474; DOI=10.1371/journal.ppat.1002116;
RA Raghava S., Giorda K.M., Romano F.B., Heuck A.P., Hebert D.N.;
RT "The SV40 late protein VP4 is a viroporin that forms pores to disrupt
RT membranes for viral release.";
RL PLoS Pathog. 7:E1002116-E1002116(2011).
CC -!- FUNCTION: Isoform VP2 is a structural protein that resides within the
CC core of the capsid surrounded by 72 VP1 pentamers. Following virus
CC endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3
CC form oligomers and integrate into the endoplasmic reticulum membrane.
CC Heterooligomer VP2-VP3 may create a viroporin for transporting the
CC viral genome across the endoplasmic reticulum membrane to the
CC cytoplasm. Nuclear entry of the viral DNA involves the selective
CC exposure and importin recognition of VP2 or Vp3 nuclear localization
CC signal (shared C-terminus). Plays a role in virion assembly within the
CC nucleus in particular through a DNA-binding domain located in the C-
CC terminal region. A N-terminal myristoylation suggests a scaffold
CC function for virion assembly. The viral progenies exit the cells by
CC lytic release. Isoform VP2 may repress SP1 activation of the SV40 early
CC promoter, via specific protein-protein and protein-DNA interactions.
CC {ECO:0000269|PubMed:17189196, ECO:0000269|PubMed:3031509,
CC ECO:0000269|PubMed:7815491}.
CC -!- FUNCTION: Isoform VP3 is a structural protein that resides within the
CC core of the capsid surrounded by 72 VP1 pentamers. Following virus
CC entry, VP2 and VP3 form oligomers and integrate into the endoplasmic
CC reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for
CC transporting the viral genome across the endoplasmic reticulum
CC membrane. Nuclear entry of the viral DNA involves the selective
CC exposure and importin recognition of VP2 or Vp3 nuclear localization
CC signal (shared C-terminus). Isoform VP3 represses SP1 activation of the
CC SV40 early promoter, via specific protein-protein and protein-DNA
CC interactions. SP1 additionally participates in recruiting VP3 to the
CC SV40 minichromosome during SV40 assembly. Isoform VP3 plays a role in
CC virion assembly within the nucleus. May initiate host cell lysis when
CC associated with VP4. {ECO:0000269|PubMed:12186919,
CC ECO:0000269|PubMed:17189196, ECO:0000269|PubMed:7815491,
CC ECO:0000269|PubMed:9466902}.
CC -!- FUNCTION: Isoform VP4 is a viroporin inducing perforation of cellular
CC membranes to trigger virus progeny release. Forms pores of 3 nm inner
CC diameter. VP4 is expressed about 24 hours after the late structural
CC proteins and is not incorporated into the mature virion.
CC {ECO:0000269|PubMed:21738474}.
CC -!- SUBUNIT: Isoform VP2 forms homooligomers, and heterooligomers with VP3
CC in the endoplasmic reticulum membrane. Isoform VP2 interacts (via D1
CC domain) with VP1. Isoform VP3 interacts (via D1 domain) with VP1. VP4
CC oligomerizes with VP3 in the nucleus. Isoform VP3 (via C-terminus)
CC interacts with host SP1, this is probably also the case for VP2; this
CC interaction represses SP1 activation of the SV40 early promoter and
CC participates in virion assembly. Interacts (via nuclear localization
CC signal) with host importin alpha2-beta heterodimer.
CC {ECO:0000269|PubMed:12186919, ECO:0000269|PubMed:16940501,
CC ECO:0000269|PubMed:17189196, ECO:0000269|PubMed:9466902}.
CC -!- INTERACTION:
CC P03093; P03087; NbExp=3; IntAct=EBI-1555798, EBI-1555770;
CC -!- SUBCELLULAR LOCATION: [Isoform VP2]: Virion {ECO:0000305}. Host nucleus
CC {ECO:0000269|PubMed:1847270}. Host endoplasmic reticulum
CC {ECO:0000269|PubMed:17189196}. Host endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17189196}. Note=Following host cell entry, the
CC virion enters into the endoplasmic reticulum through a calveolar-
CC dependent pathway. Then, isoform VP2 integrates into the endoplasmic
CC reticulum membrane and participates in the translocation of viral DNA
CC to the nucleus. Shortly after synthesis, a nuclear localization signal
CC directs isoform VP2 to the cell nucleus where virion assembly occurs.
CC {ECO:0000269|PubMed:17189196, ECO:0000269|PubMed:1847270}.
CC -!- SUBCELLULAR LOCATION: [Isoform VP3]: Virion {ECO:0000305}. Host nucleus
CC {ECO:0000269|PubMed:1847270}. Host endoplasmic reticulum
CC {ECO:0000269|PubMed:17189196}. Host endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17189196}. Note=Following host cell entry, the
CC virion enters into the endoplasmic reticulum through a calveolar-
CC dependent pathway. Then, isoform VP3 integrates into the endoplasmic
CC reticulum membrane and participates in the translocation of viral DNA
CC to the nucleus. Shortly after synthesis, a nuclear localization signal
CC directs isoform VP3 to the cell nucleus where virion assembly occurs.
CC {ECO:0000269|PubMed:17189196, ECO:0000269|PubMed:1847270}.
CC -!- SUBCELLULAR LOCATION: [Isoform VP4]: Host nucleus
CC {ECO:0000269|PubMed:17658947}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=5;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=P03093-1; Sequence=Displayed;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P03093-2; Sequence=VSP_018925;
CC Name=VP4; Synonyms=Viroporin VP4;
CC IsoId=P03093-3; Sequence=VSP_035892;
CC Name=VP1; Synonyms=Major capsid protein VP1;
CC IsoId=P03087-1; Sequence=External;
CC Name=Agno;
CC IsoId=P03084-1; Sequence=External;
CC -!- DOMAIN: The D1 region of isoform VP2 and isoform VP3 is necessary and
CC sufficient to direct the interaction with VP1.
CC {ECO:0000269|PubMed:16940501}.
CC -!- DOMAIN: The basic-rich C-terminal region of isoforms VP2 and VP3 is
CC sufficient for DNA-binding and may cause compaction of the DNA.
CC {ECO:0000269|PubMed:8407920}.
CC -!- DOMAIN: The transmembrane region is only used when isoform VP2 and
CC isoform VP3 form oligomers and integrate into the endoplasmic reticulum
CC membrane.
CC -!- MISCELLANEOUS: [Isoform VP2]: Produced by alternative splicing of the
CC late mRNA (19s mRNA).
CC -!- MISCELLANEOUS: [Isoform VP3]: Produced by alternative initiation at
CC Met-119 of isoform VP2. {ECO:0000269|PubMed:199354}.
CC -!- MISCELLANEOUS: [Isoform VP4]: Produced by alternative initiation at
CC Met-228 of isoform VP2. {ECO:0000269|PubMed:17658947}.
CC -!- SIMILARITY: Belongs to the polyomaviruses capsid protein VP2 family.
CC {ECO:0000305}.
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DR EMBL; J02400; AAB59921.1; -; Genomic_DNA.
DR EMBL; J02400; AAB59922.1; -; Genomic_DNA.
DR PIR; A03631; VVVP24.
DR RefSeq; YP_003708379.1; NC_001669.1.
DR RefSeq; YP_003708380.1; NC_001669.1.
DR IntAct; P03093; 2.
DR MINT; P03093; -.
DR TCDB; 1.A.83.1.1; the sv40 virus viroporin vp2 (sv40 vp2) family.
DR iPTMnet; P03093; -.
DR Proteomes; UP000007705; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0039665; P:permeabilization of host organelle membrane involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0099008; P:viral entry via permeabilization of inner membrane; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR001070; Polyoma_coat_VP2.
DR Pfam; PF00761; Polyoma_coat2; 1.
DR PIRSF; PIRSF003377; Polyoma_coat2; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Alternative splicing; Capsid protein; DNA-binding;
KW Host endoplasmic reticulum; Host membrane; Host nucleus;
KW Host-virus interaction; Ion channel; Ion transport; Late protein;
KW Lipoprotein; Membrane; Myristate; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Viral attachment to host cell;
KW Viral ion channel; Viral penetration into host cytoplasm;
KW Viral penetration into host nucleus;
KW Viral penetration via permeabilization of host membrane;
KW Viral release from host cell; Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000305"
FT CHAIN 2..352
FT /note="Minor capsid protein VP2"
FT /id="PRO_0000039223"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 273..308
FT /note="D1"
FT /evidence="ECO:0000269|PubMed:16940501"
FT REGION 313..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..352
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:8407920"
FT MOTIF 316..324
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:1847270"
FT COMPBIAS 337..352
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000269|PubMed:3031509"
FT VAR_SEQ 1..227
FT /note="Missing (in isoform VP4)"
FT /evidence="ECO:0000305"
FT /id="VSP_035892"
FT VAR_SEQ 1..118
FT /note="Missing (in isoform VP3)"
FT /evidence="ECO:0000305"
FT /id="VSP_018925"
FT VARIANT 63
FT /note="I -> T (in strain: 776)"
FT MUTAGEN 276..277
FT /note="FI->EE: Complete loss of interaction with VP1."
FT /evidence="ECO:0000269|PubMed:16940501"
FT MUTAGEN 283..285
FT /note="PGG->RER: Complete loss of interaction with VP1."
FT /evidence="ECO:0000269|PubMed:16940501"
FT MUTAGEN 296
FT /note="L->E: Partial loss of interaction with VP1."
FT /evidence="ECO:0000269|PubMed:16940501"
FT MUTAGEN 300
FT /note="L->E: Partial loss of interaction with VP1."
FT /evidence="ECO:0000269|PubMed:16940501"
FT MUTAGEN 344
FT /note="K->T: Partial loss of DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:7815491"
FT MUTAGEN 348
FT /note="R->T: Partial loss of DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:7815491"
SQ SEQUENCE 352 AA; 38539 MW; 79A1C73604646923 CRC64;
MGAALTLLGD LIATVSEAAA ATGFSVAEIA AGEAAAAIEV QLASVATVEG LTTSEAIAAI
GLIPQAYAVI SGAPAAIAGF AALLQTVTGV SAVAQVGYRF FSDWDHKVST VGLYQQPGMA
VDLYRPDDYY DILFPGVQTF VHSVQYLDPR HWGPTLFNAI SQAFWRVIQN DIPRLTSQEL
ERRTQRYLRD SLARFLEETT WTVINAPVNW YNSLQDYYST LSPIRPTMVR QVANREGLQI
SFGHTYDNID EADSIQQVTE RWEAQSQSPN VQSGEFIEKF EAPGGANQRT APQWMLPLLL
GLYGSVTSAL KAYEDGPNKK KRKLSRGSSQ KTKGTSASAK ARHKRRNRSS RS
