Q80J94 · CAPSD_MNV1
- ProteinCapsid protein VP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids541 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulates the genomic RNA and is decorated with VP2 proteins (By similarity).
Mediates virion attachment to the host cell receptor CD300LF (PubMed:27540007, PubMed:30194229).
Mediates virion attachment to the host cell receptor CD300LF (PubMed:27540007, PubMed:30194229).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | host cell cytoplasm | |
Cellular Component | virion component |
Names & Taxonomy
Protein names
- Recommended nameCapsid protein VP1
- Short namesCP
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Picornavirales > Caliciviridae > Norovirus > Norwalk virus
Accessions
- Primary accessionQ80J94
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000460243 | 1-541 | Capsid protein VP1 | |||
Sequence: MRMSDGAAPKANGSEASGQDLVPAAVEQAVPIQPVAGAALAAPAAGQINQIDPWIFQNFVQCPLGEFSISPRNTPGEILFDLALGPGLNPYLAHLSAMYTGWVGNMEVQLVLAGNAFTAGKVVVALVPPYFPKGSLTTAQITCFPHVMCDVRTLEPIQLPLLDVRRVLWHATQDQEESMRLVCMLYTPLRTNSPGDESFVVSGRLLSKPAADFNFVYLTPPIERTIYRMVDLPVIQPRLCTHARWPAPVYGLLVDPSLPSNPQWQNGRVHVDGTLLGTTPISGSWVSCFAAEAAYKFQSGTGEVATFTLIEQDGSAYVPGDRAAPLGYPDFSGQLEIEVQTETTKTGDKLKVTTFEMILGPTTNADQAPYQGRVFASVTAAASLDLVDGRVRAVPRSIYGFQDTIPEYNDGLLVPLAPPIGPFLPGEVLLRFRTYMRQIDTADAAAEAIDCALPQEFVSWFASNAFTVQSEALLLRYRNTLTGQLLFECKLYNEGYIALSYSGSGPLTFPTDGIFEVVSWVPRLYQLASVGSLATGRMLKQ |
Interaction
Subunit
Homodimer (PubMed:30194229).
Homomultimer (By similarity).
Interacts with the minor capsid protein VP2 (By similarity).
Interacts (via P2 subdomain) with host receptor CD300LF (via N-terminus); this interaction requires Mg2+ and Ca2+, and allows viral binding and entry into the host cell (PubMed:27681626, PubMed:30194229).
Stochioimetry is 2:2 (PubMed:30194229).
Bile acids interact with the P domain dimer interface and act as cofactors enhancing virus binding and infectivity (PubMed:30194229).
Interacts with host receptor CD300LD; this interaction allows viral binding and entry into the host cell (PubMed:27681626).
Homomultimer (By similarity).
Interacts with the minor capsid protein VP2 (By similarity).
Interacts (via P2 subdomain) with host receptor CD300LF (via N-terminus); this interaction requires Mg2+ and Ca2+, and allows viral binding and entry into the host cell (PubMed:27681626, PubMed:30194229).
Stochioimetry is 2:2 (PubMed:30194229).
Bile acids interact with the P domain dimer interface and act as cofactors enhancing virus binding and infectivity (PubMed:30194229).
Interacts with host receptor CD300LD; this interaction allows viral binding and entry into the host cell (PubMed:27681626).
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-224 | Shell domain | ||||
Sequence: MRMSDGAAPKANGSEASGQDLVPAAVEQAVPIQPVAGAALAAPAAGQINQIDPWIFQNFVQCPLGEFSISPRNTPGEILFDLALGPGLNPYLAHLSAMYTGWVGNMEVQLVLAGNAFTAGKVVVALVPPYFPKGSLTTAQITCFPHVMCDVRTLEPIQLPLLDVRRVLWHATQDQEESMRLVCMLYTPLRTNSPGDESFVVSGRLLSKPAADFNFVYLTPPIER | ||||||
Region | 225-277 | P1 sub-domain 1 | ||||
Sequence: TIYRMVDLPVIQPRLCTHARWPAPVYGLLVDPSLPSNPQWQNGRVHVDGTLLG | ||||||
Region | 225-541 | Protruding domain | ||||
Sequence: TIYRMVDLPVIQPRLCTHARWPAPVYGLLVDPSLPSNPQWQNGRVHVDGTLLGTTPISGSWVSCFAAEAAYKFQSGTGEVATFTLIEQDGSAYVPGDRAAPLGYPDFSGQLEIEVQTETTKTGDKLKVTTFEMILGPTTNADQAPYQGRVFASVTAAASLDLVDGRVRAVPRSIYGFQDTIPEYNDGLLVPLAPPIGPFLPGEVLLRFRTYMRQIDTADAAAEAIDCALPQEFVSWFASNAFTVQSEALLLRYRNTLTGQLLFECKLYNEGYIALSYSGSGPLTFPTDGIFEVVSWVPRLYQLASVGSLATGRMLKQ | ||||||
Region | 278-416 | P2 sub-domain | ||||
Sequence: TTPISGSWVSCFAAEAAYKFQSGTGEVATFTLIEQDGSAYVPGDRAAPLGYPDFSGQLEIEVQTETTKTGDKLKVTTFEMILGPTTNADQAPYQGRVFASVTAAASLDLVDGRVRAVPRSIYGFQDTIPEYNDGLLVPL | ||||||
Region | 298-366 | Interaction with host receptor CD300LF | ||||
Sequence: QSGTGEVATFTLIEQDGSAYVPGDRAAPLGYPDFSGQLEIEVQTETTKTGDKLKVTTFEMILGPTTNAD | ||||||
Region | 417-541 | P1 sub-domain 2 | ||||
Sequence: APPIGPFLPGEVLLRFRTYMRQIDTADAAAEAIDCALPQEFVSWFASNAFTVQSEALLLRYRNTLTGQLLFECKLYNEGYIALSYSGSGPLTFPTDGIFEVVSWVPRLYQLASVGSLATGRMLKQ |
Domain
The shell domain (S domain) contains elements essential for the formation of the icosahedron. The Protruding domain (P domain) is divided into sub-domains P1 and P2 (PubMed:22258242).
P domain interacts in dimeric contacts that increase the stability of the capsid and form the protrusions on the virion (PubMed:20335264).
An hypervariable region in P2 is thought to play an important role in receptor binding and immune reactivity (By similarity).
P domain interacts in dimeric contacts that increase the stability of the capsid and form the protrusions on the virion (PubMed:20335264).
An hypervariable region in P2 is thought to play an important role in receptor binding and immune reactivity (By similarity).
Sequence similarities
Belongs to the caliciviridae capsid protein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length541
- Mass (Da)58,661
- Last updated2005-12-06 v2
- ChecksumDCF3DD7E960082E8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY228235 EMBL· GenBank· DDBJ | AAO63099.2 EMBL· GenBank· DDBJ | Genomic RNA | ||
EF014462 EMBL· GenBank· DDBJ | ABJ98944.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
EU004654 EMBL· GenBank· DDBJ | ABU55541.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
EU004655 EMBL· GenBank· DDBJ | ABU55544.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
EU004657 EMBL· GenBank· DDBJ | ABU55550.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
EU004658 EMBL· GenBank· DDBJ | ABU55553.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
EU004661 EMBL· GenBank· DDBJ | ABU55562.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
EU004662 EMBL· GenBank· DDBJ | ABU55565.1 EMBL· GenBank· DDBJ | Genomic RNA |