Capsid protein VP1
Details
- Name
- Capsid protein VP1
- Synonyms
- Not Available
- Gene Name
- Not Available
- Organism
- MPyV
- Amino acid sequence
>lcl|BSEQ0019379|Capsid protein VP1 MAPKRKSGVSKCETKCTKACPRPAPVPKLLIKGGMEVLDLVTGPDSVTEIEAFLNPRMGQ PPTPESLTEGGQYYGWSRGINLATSDTEDSPGNNTLPTWSMAKLQLPMLNEDLTCDTLQM WEAVSVKTEVVGSGSLLDVHGFNKPTDTVNTKGISTPVEGSQYHVFAVGGEPLDLQGLVT DARTKYKEEGVVTIKTITKKDMVNKDQVLNPISKAKLDKDGMYPVEIWHPDPAKNENTRY FGNYTGGTTTPPVLQFTNTLTTVLLDENGVGPLCKGEGLYLSCVDIMGWRVTRNYDVHHW RGLPRYFKITLRKRWVKNPYPMASLISSLFNNMLPQVQGQPMEGENTQVEEVRVYDGTEP VPGDPDMTRYVDRFGKTKTVFPGN
- Number of residues
- 384
- Molecular Weight
- 42505.275
- Theoretical pI
- 6.38
- GO Classification
- Functionsstructural molecule activityProcessescaveolin-mediated endocytosis of virus by host cell / virion attachment to host cellComponentshost cell nucleus / T=7 icosahedral viral capsid
- General Function
- Structural molecule activity
- Specific Function
- Forms an icosahedral capsid with a T=7 symmetry and a 40 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 terminal alpha(2,3)-linked sialic acids on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. Once attached, the virion is internalized by 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).
- Pfam Domain Function
- Polyoma_coat (PF00718)
- Transmembrane Regions
- Not Available
- Cellular Location
- Virion
- Gene sequence
>lcl|BSEQ0006183|1155 bp ATGGCCCCCAAAAGAAAAAGCGGCGTCTCTAAATGCGAGACAAAATGTACAAAGGCCTGT CCAAGACCCGCACCCGTTCCCAAACTGCTTATTAAAGGGGGTATGGAGGTGCTGGACCTT GTGACAGGGCCAGACAGTGTGACAGAAATAGAAGCTTTTCTGAACCCCAGAATGGGGCAG CCACCCACCCCTGAAAGCCTAACAGAGGGAGGGCAATACTATGGTTGGAGCAGAGGGATT AATTTGGCTACATCAGATACAGAGGATTCCCCAGGAAATAATACACTTCCCACATGGAGT ATGGCAAAGCTCCAGCTTCCCATGCTCAATGAGGACCTCACCTGTGACACCCTACAAATG TGGGAGGCAGTCTCAGTGAAAACCGAGGTGGTGGGCTCTGGCTCACTGTTAGATGTGCAT GGGTTCAACAAACCCACAGATACAGTAAACACAAAAGGAATTTCCACTCCAGTGGAAGGC AGCCAATATCATGTGTTTGCTGTGGGCGGGGAACCGCTTGACCTCCAGGGACTTGTGACA GATGCCAGAACAAAATACAAGGAAGAAGGGGTAGTAACAATCAAAACAATCACAAAGAAG GACATGGTCAACAAAGACCAAGTCCTGAATCCAATTAGCAAGGCCAAGCTGGATAAGGAC GGAATGTATCCAGTTGAAATCTGGCATCCAGATCCAGCAAAAAATGAGAACACAAGGTAC TTTGGCAATTACACTGGAGGCACAACAACTCCACCCGTCCTGCAGTTCACAAACACCCTG ACAACTGTGCTCCTAGATGAAAATGGAGTTGGGCCCCTCTGTAAAGGAGAGGGCCTATAC CTCTCCTGTGTAGATATAATGGGCTGGAGAGTTACAAGAAACTATGATGTCCATCACTGG AGAGGGCTTCCCAGATATTTCAAAATCACCCTGAGAAAAAGATGGGTCAAAAATCCCTAT CCCATGGCCTCCCTCATAAGTTCCCTTTTCAACAACATGCTCCCCCAAGTGCAGGGCCAA CCCATGGAAGGGGAGAACACCCAGGTAGAGGAGGTTAGAGTGTATGATGGGACTGAACCT GTACCGGGGGACCCTGATATGACGCGCTATGTTGACCGCTTTGGAAAAACAAAGACTGTA TTTCCTGGAAATTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P49302 UniProtKB Entry Name VP1_POVMP GenBank Gene ID M34958 - General References
- Freund R, Garcea RL, Sahli R, Benjamin TL: A single-amino-acid substitution in polyomavirus VP1 correlates with plaque size and hemagglutination behavior. J Virol. 1991 Jan;65(1):350-5. [Article]
- Neu U, Stehle T, Atwood WJ: The Polyomaviridae: Contributions of virus structure to our understanding of virus receptors and infectious entry. Virology. 2009 Feb 20;384(2):389-99. doi: 10.1016/j.virol.2008.12.021. Epub 2009 Jan 21. [Article]
- Stehle T, Yan Y, Benjamin TL, Harrison SC: Structure of murine polyomavirus complexed with an oligosaccharide receptor fragment. Nature. 1994 May 12;369(6476):160-3. [Article]
- Stehle T, Harrison SC: Crystal structures of murine polyomavirus in complex with straight-chain and branched-chain sialyloligosaccharide receptor fragments. Structure. 1996 Feb 15;4(2):183-94. [Article]
- Stehle T, Harrison SC: High-resolution structure of a polyomavirus VP1-oligosaccharide complex: implications for assembly and receptor binding. EMBO J. 1997 Aug 15;16(16):5139-48. [Article]