P14996 (VP1_POVBA) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 19, 2011.
Version 57.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Major capsid protein VP1 Alternative name(s): Major structural protein VP1 |
| Organism | BK polyomavirus (strain AS) (BKPyV) [Complete proteome] |
| Taxonomic identifier | 10631 [NCBI] |
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Polyomaviridae › Polyomavirus |
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
Protein attributes
| Sequence length | 362 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with gangliosides GT1b and GD1b containing terminal alpha(2-8)-linked sialic acids on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA By similarity. |
| Subunit structure | Homomultimer; disulfide-linked. The virus capsid is composed of 72 icosahedral units, each one composed of five disulfide-linked copies of VP1. Interacts with minor capsid proteins VP2 and VP3 By similarity. |
| Subcellular location | Virion. Host nucleus By similarity. |
| Domain | The N-terminal region contains a nuclear signal but the presence of VP2 and VP3 proteins is required for efficient nuclear transport By similarity. The intrinsically disordered C-terminal region interacts with neighboring pentamers. The unstructured nature of this region allows to make different interactions depending on the stuctural context: pentamers present at the 12 icosahedral fivefold axes bind five pentamers, when pentamers present at the 60 icosahedral six-fold axes interacts with six pentamers By similarity. |
| Sequence similarities | Belongs to the polyomaviruses coat protein VP1 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Caveolin-mediated endocytosis of virus by host Host-virus interaction Initiation of viral infection Viral attachment to host cell Viral penetration into host cytoplasm Virus endocytosis by host |
| Cellular component | Host nucleus Virion |
| Coding sequence diversity | Alternative initiation Alternative splicing |
| Developmental stage | Late protein |
| Molecular function | Capsid protein T=7 icosahedral capsid protein |
| PTM | Disulfide bond Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell viral capsidInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | structural molecule activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 5 isoforms produced by alternative splicing and alternative initiation. [Align] [Select] | ||||||
| Isoform VP1 (identifier: P14996-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Note: Produced by alternative splicing of the late mRNA. | ||||||
| Isoform VP2 (identifier: P14997-1) Also known as: Minor capsid protein VP2; The sequence of this isoform can be found in the external entry P14997. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly. | ||||||
| Note: Produced by alternative splicing of the late mRNA. | ||||||
| Isoform VP3 (identifier: P14997-2) Also known as: Minor capsid protein VP3; The sequence of this isoform can be found in the external entry P14997. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly. | ||||||
| Note: Produced by alternative initiation at Met-120 of isoform VP2. | ||||||
| Isoform VP4 (identifier: P14997-3) Also known as: Viroporin VP4; The sequence of this isoform can be found in the external entry P14997. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly. | ||||||
| Note: Produced by alternative initiation at Met-229 of isoform VP2. | ||||||
| Isoform Agno (identifier: P14998-1) The sequence of this isoform can be found in the external entry P14998. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly. | ||||||
| Note: Produced by alternative initiation of the late mRNA. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 362 | 362 | Major capsid protein VP1 | PRO_0000115017 | |||||
Regions | |||||||||
| Region | 302 – 362 | 61 | Intrinsically disordered By similarity | ||||||
| Motif | 2 – 17 | 16 | Bipartite nuclear localization signal By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 338 | 1 | Phosphothreonine; by host By similarity | ||||||
| Disulfide bond | 10 | Interchain (with C-10) By similarity | |||||||
| Disulfide bond | 105 | Interchain (with C-105) By similarity | |||||||
Sequences
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References
| [1] | "Nucleotide sequence of the human polyomavirus AS virus, an antigenic variant of BK virus." Tavis J.E., Walker D.L., Gardner S.D., Frisque R.J. J. Virol. 63:901-911(1989) [PubMed: 2536111] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The Polyomaviridae: Contributions of virus structure to our understanding of virus receptors and infectious entry." Neu U., Stehle T., Atwood W.J. Virology 384:389-399(2009) [PubMed: 19157478] [Abstract] Cited for: REVIEW. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M23122 Genomic DNA. Translation: AAA46882.1. |
| PIR | VVVP1S. D33278. |
3D structure databases | |
| ProteinModelPortal | P14996. |
| SMR | P14996. Positions 15-361. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR000662. Capsid_VP1_Polyomavir. IPR011222. dsDNA_vir_gr_I_capsid. [Graphical view] |
| Gene3D | G3DSA:2.60.175.10. Polyoma_coat_VP1. 1 hit. |
| Pfam | PF00718. Polyoma_coat. 1 hit. [Graphical view] |
| PIRSF | PIRSF003376. Capsid_VP1_Polyomavir. 1 hit. |
| SUPFAM | SSF88648. dsDNA_vir_gr_I_capsid. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | VP1_POVBA | ||||||||
| Accession | Primary (citable) accession number: P14996 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with