Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10633-01359
Entry Name
UniProt Accession
Theoretical PI
6.99
Molecular Weight
38539.36
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Minor capsid protein VP2
Protein Synonyms/Alias
Minor structural protein VP2;
Gene Name
Gene Synonyms/Alias
Created Date
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGAALTLLG
[1]
N-Myristoylation
Organism
Simian virus 40 (SV40)
NCBI Taxa ID
10633
Reference
[1] Streuli CH, Griffin BE. Myristic acid is coupled to a structural protein ofpolyoma virus and SV40. Nature. 1987 Apr 9-15;326(6113):619-22.[PMID:3031509]
Functional Description
Isoform VP2 is a structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or Vp3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA- binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly. The viral progenies exit the cells by lytic release. Isoform VP2 may repress SP1 activation of the SV40 early promoter, via specific protein-protein and protein-DNA interactions.Isoform VP4 is a viroporin inducing perforation of cellular membranes to trigger virus progeny release. Forms pores of 3 nm inner diameter. VP4 is expressed about 24 hours after the late structural proteins and is not incorporated into the mature virion.
Sequence Annotation
Transmembrane: 290 310 Helical.
Region: 273 308 D1.
Region: 313 352 DNA-binding.
Motif: 316 324 Nuclear localization signal.
Protein Length
352 AA.
Protein Sequence
(Canonical)
MGAALTLLGD LIATVSEAAA ATGFSVAEIA AGEAAAAIEV QLASVATVEG LTTSEAIAAI  60
GLIPQAYAVI SGAPAAIAGF AALLQTVTGV SAVAQVGYRF FSDWDHKVST VGLYQQPGMA  120
VDLYRPDDYY DILFPGVQTF VHSVQYLDPR HWGPTLFNAI SQAFWRVIQN DIPRLTSQEL  180
ERRTQRYLRD SLARFLEETT WTVINAPVNW YNSLQDYYST LSPIRPTMVR QVANREGLQI  240
SFGHTYDNID EADSIQQVTE RWEAQSQSPN VQSGEFIEKF EAPGGANQRT APQWMLPLLL  300
GLYGSVTSAL KAYEDGPNKK KRKLSRGSSQ KTKGTSASAK ARHKRRNRSS RS          352
FASTA
(Canonical)
>LipidDB-10633-01359|P03093
MGAALTLLGDLIATVSEAAAATGFSVAEIAAGEAAAAIEVQLASVATVEGLTTSEAIAAI
GLIPQAYAVISGAPAAIAGFAALLQTVTGVSAVAQVGYRFFSDWDHKVSTVGLYQQPGMA
VDLYRPDDYYDILFPGVQTFVHSVQYLDPRHWGPTLFNAISQAFWRVIQNDIPRLTSQEL
ERRTQRYLRDSLARFLEETTWTVINAPVNWYNSLQDYYSTLSPIRPTMVRQVANREGLQI
SFGHTYDNIDEADSIQQVTERWEAQSQSPNVQSGEFIEKFEAPGGANQRTAPQWMLPLLL
GLYGSVTSALKAYEDGPNKKKRKLSRGSSQKTKGTSASAKARHKRRNRSSRS
Gene Ontology
GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-KW
GO:0042025; C:host cell nucleus; IEA:UniProtKB-KW
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW
GO:0005622; C:intracellular; IEA:GOC
GO:0019028; C:viral capsid; IEA:UniProtKB-KW
GO:0003677; F:DNA binding; IEA:UniProtKB-KW
GO:0005216; F:ion channel activity; IEA:UniProtKB-KW
GO:0005198; F:structural molecule activity; IEA:InterPro
GO:0039665; P:permeabilization of host organelle membrane involved in viral entry into host cell; IEA:UniProtKB-KW
GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW
GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW
GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW
GO:0019076; P:viral release from host cell; IEA:UniProtKB-KW
GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW
Interpro
InterPro; IPR001070; Polyoma_coat_VP2
Pfam
Pfam; PF00761; Polyoma_coat2;
SMART
PROSITE
PRINTS