| Tag |
Content |
LipidDB ID |
LipidDB-10625-00497 |
Entry Name |
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UniProt Accession |
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Theoretical PI |
6.16 |
Molecular Weight |
37358.47 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
Minor capsid protein VP2 |
Protein Synonyms/Alias |
Minor structural protein VP2; |
Gene Name |
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Gene Synonyms/Alias |
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Created Date |
01-JAN-1990 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGAIISAIA | [1] | N-Myristoylation |
|
Organism |
Budgerigar fledgling disease virus (BFPyV) |
NCBI Taxa ID |
10625 |
Reference |
[1] Schmidt M, Müller H, Schmidt MF, Rott R. Myristoylation of budgerigarfledgling disease virus capsid protein VP2. J Virol. 1989 Jan;63(1):429-31.[ PMID:2535744]
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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 |
Region: 262 297 D1.
Region: 302 341 DNA-binding.
Motif: 309 317 Nuclear localization signal.
|
Protein Length |
341 AA. |
Protein Sequence
(Canonical) |
MGAIISAIAG LFELGALGGL AVDAAVNTAE IEAFIGELVL QDFSVAEIFD AIETSGIPLA 60
NTAVPVAELQ QTAATSGLIG QALSAPSLIA ASVKAFAGDP VAAGNNMALQ VWRDQMDILF 120
PGAEWFSNAV HNINPLAWAQ SLYEQVGQSI WNYMTGNIGQ AVIHQIEERT TALIVYQSRG 180
IYDILARALE TARWTLTTAA VDTYQTLKSY YGELPAVSGR VEAFRRYHEV AQGRSFFEDS 240
DIQDVLEGKK AQKRIEGPQE MTGQTIEQQT PPGGAMQRHA NDWLLPLILG LYGDLTPEWR 300
YQLKERLNVP KRKRKLPTTS AGTSPPSKRR YRGVRRKVRS R 341
|
FASTA
(Canonical) |
>LipidDB-10625-00497|P13892
MGAIISAIAGLFELGALGGLAVDAAVNTAEIEAFIGELVLQDFSVAEIFDAIETSGIPLA
NTAVPVAELQQTAATSGLIGQALSAPSLIAASVKAFAGDPVAAGNNMALQVWRDQMDILF
PGAEWFSNAVHNINPLAWAQSLYEQVGQSIWNYMTGNIGQAVIHQIEERTTALIVYQSRG
IYDILARALETARWTLTTAAVDTYQTLKSYYGELPAVSGRVEAFRRYHEVAQGRSFFEDS
DIQDVLEGKKAQKRIEGPQEMTGQTIEQQTPPGGAMQRHANDWLLPLILGLYGDLTPEWR
YQLKERLNVPKRKRKLPTTSAGTSPPSKRRYRGVRRKVRSR
|
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:0005622; C:intracellular; IEA:GOC GO:0016020; C:membrane; IEA:UniProtKB-KW 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 |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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