Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q11213 (CAPSD_PAVCB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Capsid protein VP1
Alternative name(s):
Coat protein VP1
OrganismCanine parvovirus type 2 (isolate Dog/United States/CPV-b/1978) (CPV-2)
Taxonomic identifier59284 [NCBI]
Taxonomic lineageVirusesssDNA virusesParvoviridaeParvovirinaeParvovirus
Virus hostCanis familiaris (Dog) (Canis lupus familiaris) [TaxID: 9615]
Felis catus (Cat) (Felis silvestris catus) [TaxID: 9685]

Protein attributes

Sequence length727 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 receptor TFRC. This attachment induces virion internalization predominantly through clathrin-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 nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell. Intracytoplasmic transport involves microtubules and interaction between capsid proteins and host dynein. Exposure of nuclear localization signal probably allows nuclear import of capsids By similarity.

Subunit structure

Interacts with host TFRC By similarity.

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 nuclear localization signals that might be exposed by capsid modifications during virus entry By similarity.

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 By similarity.

Sequence similarities

Belongs to the parvoviridae capsid protein family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform VP1 (identifier: Q11213-1)

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: Q11213-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-143: Missing.
Note: Major splicing isoform produced by deletion of the initiating AUG for VP1 and downstream translation of VP2.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 727727Capsid protein VP1
PRO_0000039427

Regions

Region19 – 6446Phospholipase A2-like By similarity
Motif4 – 1310Nuclear localization signal Potential
Compositional bias165 – 18218Gly-rich

Sites

Metal binding3231Magnesium 1 By similarity

Amino acid modifications

Disulfide bond633 ↔ 637 By similarity

Natural variations

Alternative sequence1 – 143143Missing in isoform VP2.
VSP_041138

Secondary structure

..................................................................................... 727
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 1996. Version 1.
Checksum: 115F3E1A79098EBE

FASTA72780,343
        10         20         30         40         50         60 
MAPPAKRARR GLVPPGYKYL GPGNSLDQGE PTNPSDAAAK EHDEAYAAYL RSGKNPYLYF 

        70         80         90        100        110        120 
SPADQRFIDQ TKDAKDWGGK IGHYFFRAKK AIAPVLTDTP DHPSTSRPTK PTKRSKPPPH 

       130        140        150        160        170        180 
IFINLAKKKK AGAGQVKRDN LAPMSDGAVQ PDGGQPAVRN ERATGSGNGS GGGGGGGSGG 

       190        200        210        220        230        240 
VGISTGTFNN QTEFKFLENG WVEITANSSR LVHLNMPESE NYRRVVVNNM DKTAVNGNMA 

       250        260        270        280        290        300 
LDDIHAQIVT PWSLVDANAW GVWFNPGDWQ LIVNTMSELH LVSFEQEIFN VVLKTVSESA 

       310        320        330        340        350        360 
TQPPTKVYNN DLTASLMVAL DSNNTMPFTP AAMRSETLGF YPWKPTIPTP WRYYFQWDRT 

       370        380        390        400        410        420 
LIPSHTGTSG TPTNIYHGTD PDDVQFYTIE NSVPVHLLRT GDEFATGTFF FDCKPCRLTH 

       430        440        450        460        470        480 
TWQTNRALGL PPFLNSLPQS EGATNFGDIG VQQDKRRGVT QMGNTNYITE ATIMRPAEVG 

       490        500        510        520        530        540 
YSAPYYSFEA STQGPFKTPI AAGRGGAQTD ENQAADGNPR YAFGRQHGQK TTTTGETPER 

       550        560        570        580        590        600 
FTYIAHQDTG RYPEGDWIQN INFNLPVTND NVLLPTDPIG GKTGINYTNI FNTYGPLTAL 

       610        620        630        640        650        660 
NNVPPVYPNG QIWDKEFDTD LKPRLHVNAP FVCQNNCPGQ LFVKVAPNLT NEYDPDASAN 

       670        680        690        700        710        720 
MSRIVTYSDF WWKGKLVFKA KLRASHTWNP IQQMSINVDN QFNYVPSNIG GMKIVYEKSQ 


LAPRKLY 

« Hide

Isoform VP2 [UniParc].

Checksum: A048283350279D0F
Show »

FASTA58464,652

References

[1]"Mapping specific functions in the capsid structure of canine parvovirus and feline panleukopenia virus using infectious plasmid clones."
Parrish C.R.
Virology 183:195-205(1991) [PubMed: 1647068] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The canine parvovirus empty capsid structure."
Wu H., Rossmann M.G.
J. Mol. Biol. 233:231-244(1993) [PubMed: 8377200] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 180-727.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M38245 Genomic DNA. Translation: AAB02799.1.
M38245 Genomic DNA. Translation: AAB02800.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CASX-ray3.00A180-727[»]
ProteinModelPortalQ11213.
SMRQ11213. Positions 180-727.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR016184. Capsid/spike_ssDNA_virus.
IPR001403. Parvovirus_coat.
IPR013607. Parvovirus_coat_VP1_N.
[Graphical view]
Gene3DG3DSA:2.170.30.10. Parvo_coat. 1 hit.
PfamPF00740. Parvo_coat. 1 hit.
PF08398. Parvo_coat_N. 1 hit.
[Graphical view]
SUPFAMSSF88645. Capsid/spike_ssDNA_virus. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCAPSD_PAVCB
AccessionPrimary (citable) accession number: Q11213
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 28, 2011
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families