P03135 · CAPSD_AAV2S
- ProteinCapsid protein VP1
- GeneVP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids735 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
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 three size variants of the capsid protein VP1, VP2 and VP3 which differ in their N-terminus. The capsid encapsulates the genomic ssDNA. Binds to host cell heparan sulfate and uses host ITGA5-ITGB1 as coreceptor on the cell surface to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptor 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.
Miscellaneous
The ratio at which VP1, VP2 and VP3 proteins are synthesized in vivo is about 1:1:10, which is the same as in the mature virus particle.
Biotechnology
AAV capsids serve as viral gene transfer vectors that have been shown to affect long-term gene expression and disease correction with low toxicity in animal models, and are well tolerated in human clinical trials.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell nucleolus | |
Cellular Component | T=1 icosahedral viral capsid | |
Molecular Function | structural molecule activity | |
Biological Process | clathrin-dependent endocytosis of virus by host cell | |
Biological Process | symbiont entry into host cell via permeabilization of host membrane | |
Biological Process | virion attachment to host cell |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCapsid protein VP1
Gene names
Organism names
- Taxonomic lineageViruses > Monodnaviria > Shotokuvirae > Cossaviricota > Quintoviricetes > Piccovirales > Parvoviridae > Parvovirinae > Dependoparvovirus > Dependoparvovirus primate1
- Virus hosts
Accessions
- Primary accessionP03135
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Capsid proteins are first observed in the host nucleolus where capsid assembly may occur, and then are present over the whole nucleoplasm where encapsidation of the viral DNA takes place.
Keywords
- Cellular component
Phenotypes & Variants
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000222455 | 1-735 | Capsid protein VP1 | |||
Sequence: MAADGYLPDWLEDTLSEGIRQWWKLKPGPPPPKPAERHKDDSRGLVLPGYKYLGPFNGLDKGEPVNEADAAALEHDKAYDRQLDSGDNPYLKYNHADAEFQERLKEDTSFGGNLGRAVFQAKKRVLEPLGLVEEPVKTAPGKKRPVEHSPVEPDSSSGTGKAGQQPARKRLNFGQTGDADSVPDPQPLGQPPAAPSGLGTNTMATGSGAPMADNNEGADGVGNSSGNWHCDSTWMGDRVITTSTRTWALPTYNNHLYKQISSQSGASNDNHYFGYSTPWGYFDFNRFHCHFSPRDWQRLINNNWGFRPKRLNFKLFNIQVKEVTQNDGTTTIANNLTSTVQVFTDSEYQLPYVLGSAHQGCLPPFPADVFMVPQYGYLTLNNGSQAVGRSSFYCLEYFPSQMLRTGNNFTFSYTFEDVPFHSSYAHSQSLDRLMNPLIDQYLYYLSRTNTPSGTTTQSRLQFSQAGASDIRDQSRNWLPGPCYRQQRVSKTSADNNNSEYSWTGATKYHLNGRDSLVNPGPAMASHKDDEEKFFPQSGVLIFGKQGSEKTNVDIEKVMITDEEEIRTTNPVATEQYGSVSTNLQRGNRQAATADVNTQGVLPGMVWQDRDVYLQGPIWAKIPHTDGHFHPSPLMGGFGLKHPPPQILIKNTPVPANPSTTFSAAKFASFITQYSTGQVSVEIEWELQKENSKRWNPEIQYTSNYNKSVNVDFTVDTNGVYSEPRPIGTRYLTRNL |
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 22-44 | Disordered | ||||
Sequence: WWKLKPGPPPPKPAERHKDDSRG | ||||||
Region | 52-97 | Phospholipase A2-like | ||||
Sequence: YLGPFNGLDKGEPVNEADAAALEHDKAYDRQLDSGDNPYLKYNHAD | ||||||
Region | 136-224 | Disordered | ||||
Sequence: VKTAPGKKRPVEHSPVEPDSSSGTGKAGQQPARKRLNFGQTGDADSVPDPQPLGQPPAAPSGLGTNTMATGSGAPMADNNEGADGVGNS | ||||||
Compositional bias | 195-209 | Polar residues | ||||
Sequence: PSGLGTNTMATGSGA |
Domain
The N-terminus of VP1 is sequestered within the mature capsid. It contains a phospholipase A2-like region and putative nuclear localization signals.
Sequence similarities
Belongs to the parvoviridae capsid protein family.
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing & Alternative initiation.
P03135-1
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.
- NameVP1
- NoteProduced by alternative splicing (2.6 kb mRNA).
- Length735
- Mass (Da)81,945
- Last updated2011-04-05 v2
- Checksum980BEEF46908390B
P03135-2
- NameVP2
- NoteProduced by alternative splicing (2.3 kb mRNA), with initiatory methionine encoded by an ACG codon.
P03135-3
- NameVP3
- NoteProduced by alternative initiation of the 2.3 kb mRNA.
- Differences from canonical
- 1-202: Missing
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_040829 | 1-137 | in isoform VP2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_040828 | 1-202 | in isoform VP3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_040830 | 138 | in isoform VP2 | |||
Sequence: T → M | ||||||
Compositional bias | 195-209 | Polar residues | ||||
Sequence: PSGLGTNTMATGSGA | ||||||
Sequence conflict | 520-521 | in Ref. 3; AAA42376 | ||||
Sequence: Missing | ||||||
Sequence conflict | 553 | in Ref. 3; AAA42376 | ||||
Sequence: D → N | ||||||
Sequence conflict | 566 | in Ref. 3; AAA42376 | ||||
Sequence: R → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J01901 EMBL· GenBank· DDBJ | AAA42376.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
AF043303 EMBL· GenBank· DDBJ | AAC03779.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF043303 EMBL· GenBank· DDBJ | AAC03780.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF043303 EMBL· GenBank· DDBJ | AAC03778.1 EMBL· GenBank· DDBJ | Genomic DNA |