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P14996 (VP1_POVBA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Major capsid protein VP1
Alternative name(s):
Major structural protein VP1
OrganismBK polyomavirus (strain AS) (BKPyV) [Complete proteome]
Taxonomic identifier10631 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stagePolyomaviridaePolyomavirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Protein existenceInferred 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 362362Major capsid protein VP1
PRO_0000115017

Regions

Region302 – 36261Intrinsically disordered By similarity
Motif2 – 1716Bipartite nuclear localization signal By similarity

Amino acid modifications

Modified residue3381Phosphothreonine; by host By similarity
Disulfide bond10Interchain (with C-10) By similarity
Disulfide bond105Interchain (with C-105) By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform VP1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 5BDCEC52F247F238

FASTA36240,113
        10         20         30         40         50         60 
MAPTKRKGEC PGAAPKKPKE PVQVPKLLIK GGVEVLEVKT GVDAITEVEC FLNPEMGDPD 

        70         80         90        100        110        120 
DNLRGYSQHL SAENAFESDS PDRKMLPCYS TARIPLPNLN EDLTCGNLLM WEAVTVKTEV 

       130        140        150        160        170        180 
IGITSMLNLH AGSQKVHENG GGKPVQGSNF HFFAVGGDPL EMQGVLMNYR TKYPQGTITP 

       190        200        210        220        230        240 
KNPTAQSQVM NTDHKAYLDK NNAYPVECWI PDPSRNENTR YFGTYTGGEN VPPVLHVTNT 

       250        260        270        280        290        300 
ATTVLLDEQG VGPLCKADSL YVSAADICGL FTNSSGTQQW RGLARYFKIR LRKRSVKNPY 

       310        320        330        340        350        360 
PISFLLSDLI NRRTQKVDGQ PMYGMESQVE EVRVFDGTEQ LPGDPDMIRY IDRQGQLQTK 


MV 

« Hide

Isoform VP2 (Minor capsid protein VP2) [UniParc].

See P14997.

Isoform VP3 (Minor capsid protein VP3) [UniParc].

See P14997.

Isoform VP4 (Viroporin VP4) [UniParc].

See P14997.

Isoform Agno [UniParc].

See P14998.

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23122 Genomic DNA. Translation: AAA46882.1.
PIRVVVP1S. D33278.

3D structure databases

ProteinModelPortalP14996.
SMRP14996. Positions 15-361.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.175.10. 1 hit.
InterProIPR000662. Capsid_VP1_Polyomavir.
IPR011222. dsDNA_vir_gr_I_capsid.
[Graphical view]
PfamPF00718. Polyoma_coat. 1 hit.
[Graphical view]
PIRSFPIRSF003376. Capsid_VP1_Polyomavir. 1 hit.
SUPFAMSSF88648. dsDNA_vir_gr_I_capsid. 1 hit.
ProtoNetSearch...

Entry information

Entry nameVP1_POVBA
AccessionPrimary (citable) accession number: P14996
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 3, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families