Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10636-01361
Entry Name
UniProt Accession
Theoretical PI
5.36
Molecular Weight
34800.57
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
******MGAALTILV
[1]
N-Myristoylation
Organism
Murine polyomavirus (strain A2) (MPyV)
NCBI Taxa ID
10636
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. Participates in host cell receptor binding together with VP1. 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 (By similarity).
Sequence Annotation
Transmembrane: 287 307 Helical.
Region: 266 301 D1.
Region: 306 319 DNA-binding.
Motif: 311 319 Nuclear localization signal.
Protein Length
319 AA.
Protein Sequence
(Canonical)
MGAALTILVD LIEGLAEVST LTGLSAEAIL SGEALAALDG EITALTLEGV MSSETALATM  60
GISEEVYGFV STVPVFVSRT AGAIWLMQTV QGASTISLGI QRYLHNEEVP TVNRNMALIP  120
WRDPALLDIY FPGVNQFAHA LNVVHDWGHG LLHSVGRYVW QMVVQETQHR LEGAVRELTV  180
RQTHTFLDGL ARLLENTRWV VSNAPQSAID AINRGASSAS SGYSSLSDYY RQLGLNPPQR  240
RALFNRIEGS MGNGGPTPAA HIQDESGEVI KFYQAQVVSH QRVTPDWMLP LILGLYGDIT  300
PTWATVIEED GPQKKKRRL                                               319
FASTA
(Canonical)
>LipidDB-10636-01361|P03096
MGAALTILVDLIEGLAEVSTLTGLSAEAILSGEALAALDGEITALTLEGVMSSETALATM
GISEEVYGFVSTVPVFVSRTAGAIWLMQTVQGASTISLGIQRYLHNEEVPTVNRNMALIP
WRDPALLDIYFPGVNQFAHALNVVHDWGHGLLHSVGRYVWQMVVQETQHRLEGAVRELTV
RQTHTFLDGLARLLENTRWVVSNAPQSAIDAINRGASSASSGYSSLSDYYRQLGLNPPQR
RALFNRIEGSMGNGGPTPAAHIQDESGEVIKFYQAQVVSHQRVTPDWMLPLILGLYGDIT
PTWATVIEEDGPQKKKRRL
Gene Ontology
GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-KW
GO:0033644; C:host cell membrane; IEA:UniProtKB-KW
GO:0042025; C:host cell nucleus; IEA:UniProtKB-KW
GO:0016021; C:integral component of membrane; 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:0005198; F:structural molecule activity; IEA:InterPro
GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW
GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW
Interpro
InterPro; IPR001070; Polyoma_coat_VP2
Pfam
Pfam; PF00761; Polyoma_coat2;
SMART
PROSITE
PRINTS