P03137 (CAPSD_MUMIP) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 58.
History...
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Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Capsid protein VP1 Alternative name(s): Coat protein VP1 |
| Organism | Murine minute virus (strain MVM prototype) (MVM) (Murine minute virus (strain MVM(p))) |
| Taxonomic identifier | 648235 [NCBI] |
| Taxonomic lineage | Viruses › ssDNA viruses › Parvoviridae › Parvovirinae › Parvovirus |
| Virus host | Mus musculus (Mouse) [TaxID: 10090] |
Protein attributes
| Sequence length | 729 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and putative nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus. Ref.3 |
| Subcellular location | Virion By similarity. Host nucleus Potential. |
| Domain | The N-terminus of VP1 is sequestered within the mature capsid. It contains a phospholipase A2-like region and putative nuclear localization signals. |
| Miscellaneous | The capsids of autonomous parvoviruses expose a proportion of VP2 N-terminus and part of that sequence can be cleaved of to form VP3. |
| Sequence similarities | Belongs to the parvoviridae capsid protein family. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform VP1 (identifier: P03137-1) 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: Minor splicing isoform. | ||||||
| Isoform VP2 (identifier: P03137-2) The sequence of this isoform differs from the canonical sequence as follows: 1-142: Missing. | ||||||
| Note: Major splicing isoform (approximately 70% of the molecules), produced by deletion of the initiating AUG for VP1 and downstream translation of VP2. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 729 | 729 | Capsid protein VP1 | PRO_0000039419 | |||||
Regions | |||||||||
| Region | 19 – 64 | 46 | Phospholipase A2-like | ||||||
| Motif | 4 – 13 | 10 | Nuclear localization signal Potential | ||||||
| Compositional bias | 167 – 183 | 17 | Gly-rich | ||||||
Sites | |||||||||
| Metal binding | 325 | 1 | Magnesium 1 By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 142 | 142 | Missing in isoform VP2. | VSP_041135 | |||||
Experimental info | |||||||||
| Sequence conflict | 385 – 387 | 3 | MNS → IP in CAA24310. Ref.1 | ||||||
Sequences
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References
| [1] | "The complete DNA sequence of minute virus of mice, an autonomous parvovirus." Astell C.R., Thomson M., Merchlinsky M., Ward D.C. Nucleic Acids Res. 11:999-1018(1983) [PubMed: 6298737] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Three splicing patterns are used to excise the small intron common to all minute virus of mice RNAs." Morgan W.R., Ward D.C. J. Virol. 60:1170-1174(1986) [PubMed: 3783817] [Abstract] Cited for: ALTERNATIVE SPLICING. |
| [3] | "Parvoviral virions deploy a capsid-tethered lipolytic enzyme to breach the endosomal membrane during cell entry." Farr G.A., Zhang L.G., Tattersall P. Proc. Natl. Acad. Sci. U.S.A. 102:17148-17153(2005) [PubMed: 16284249] [Abstract] Cited for: FUNCTION OF VP1, PHOSPHOLIPASE A2-LIKE REGION, NUCLEAR LOCALIZATION SIGNALS. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | V01115 Genomic DNA. Translation: CAA24310.1. Sequence problems. J02275 Genomic DNA. Translation: AAA67111.1. |
| PIR | VCPV2M. A03700. |
| RefSeq | NP_041244.1. NC_001510.1. |
3D structure databases | |
| ProteinModelPortal | P03137. |
| SMR | P03137. Positions 181-729. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1489592. |
Family and domain databases | |
| InterPro | IPR016184. Capsid/spike_ssDNA_virus. IPR001403. Parvovirus_coat. IPR013607. Parvovirus_coat_VP1_N. [Graphical view] |
| Gene3D | G3DSA:2.170.30.10. Parvo_coat. 1 hit. |
| Pfam | PF00740. Parvo_coat. 1 hit. PF08398. Parvo_coat_N. 1 hit. [Graphical view] |
| SUPFAM | SSF88645. Capsid/spike_ssDNA_virus. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | CAPSD_MUMIP | ||||||||
| Accession | Primary (citable) accession number: P03137 Secondary accession number(s): Q84366 | ||||||||
| 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 |