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Capsid protein VP1 (Coat protein VP1)

 CAPSD_PAVCD             Reviewed;         727 AA.
P17455; P30129; Q6LDR5; Q84389;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
31-MAY-2011, sequence version 2.
25-OCT-2017, entry version 107.
RecName: Full=Capsid protein VP1;
AltName: Full=Coat protein VP1;
Canine parvovirustype 2 (isolate Dog/United States/CPV-d/1988)
(CPV-2).
Viruses; ssDNA viruses; Parvoviridae; Parvovirinae; Protoparvovirus.
NCBI_TaxID=10790;
NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3176341; DOI=10.1016/0042-6822(88)90500-4;
Parrish C.R., Aquadro C.F., Carmichael L.E.;
"Canine host range and a specific epitope map along with variant
sequences in the capsid protein gene of canine parvovirus and related
feline, mink, and raccoon parvoviruses.";
Virology 166:293-307(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 234-727.
STRAIN=Y1;
PubMed=8207398; DOI=10.1099/0022-1317-75-6-1319;
Horiuchi M., Goto H., Ishiguro N., Shinagawa M.;
"Mapping of determinants of the host range for canine cells in the
genome of canine parvovirus using canine parvovirus/mink enteritis
virus chimeric viruses.";
J. Gen. Virol. 75:1319-1328(1994).
[3]
FUNCTION, AND NUCLEAR LOCALIZATION SIGNAL.
PubMed=11799183; DOI=10.1128/JVI.76.4.1884-1891.2002;
Vihinen-Ranta M., Wang D., Weichert W.S., Parrish C.R.;
"The VP1 N-terminal sequence of canine parvovirus affects nuclear
transport of capsids and efficient cell infection.";
J. Virol. 76:1884-1891(2002).
[4]
FUNCTION.
PubMed=12970411; DOI=10.1128/JVI.77.19.10270-10279.2003;
Suikkanen S., Aaltonen T., Nevalainen M., Valilehto O., Lindholm L.,
Vuento M., Vihinen-Ranta M.;
"Exploitation of microtubule cytoskeleton and dynein during parvoviral
traffic toward the nucleus.";
J. Virol. 77:10270-10279(2003).
[5]
FUNCTION, AND INTERACTION WITH CANINE TFRC.
PubMed=19656887; DOI=10.1128/JVI.00295-09;
Harbison C.E., Lyi S.M., Weichert W.S., Parrish C.R.;
"Early steps in cell infection by parvoviruses: host-specific
differences in cell receptor binding but similar endosomal
trafficking.";
J. Virol. 83:10504-10514(2009).
[6]
X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS).
PubMed=2006420; DOI=10.1126/science.2006420;
Tsao J., Chapman M.S., Agbandje M., Keller W., Smith K., Wu H.,
Luo M., Smith T.J., Rossmann M.G., Compans R.W., Parish C.R.;
"The three-dimensional structure of canine parvovirus and its
functional implications.";
Science 251:1456-1464(1991).
[7]
X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 1-584.
PubMed=8918534; DOI=10.1006/viro.1996.0575;
Llamas-Saiz A.L., Agbandje-McKenna M., Parker J.S., Wahid A.T.,
Parrish C.R., Rossmann M.G.;
"Structural analysis of a mutation in canine parvovirus which controls
antigenicity and host range.";
Virology 225:65-71(1996).
[8]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 154-737.
PubMed=8969301; DOI=10.1006/jmbi.1996.0657;
Xie Q., Chapman M.S.;
"Canine parvovirus capsid structure, analyzed at 2.9 A resolution.";
J. Mol. Biol. 264:497-520(1996).
[9]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
PubMed=10884355; DOI=10.1006/jmbi.2000.3868;
Simpson A.A., Chandrasekar V., Hebert B., Sullivan G.M.,
Rossmann M.G., Parrish C.R.;
"Host range and variability of calcium binding by surface loops in the
capsids of canine and feline parvoviruses.";
J. Mol. Biol. 300:597-610(2000).
[10]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 37-737.
PubMed=14581558; DOI=10.1128/JVI.77.22.12211-12221.2003;
Govindasamy L., Hueffer K., Parrish C.R., Agbandje-McKenna M.;
"Structures of host range-controlling regions of the capsids of canine
and feline parvoviruses and mutants.";
J. Virol. 77:12211-12221(2003).
-!- 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 (By similarity). Intracytoplasmic transport involves
microtubules and interaction between capsid proteins and host
dynein. Exposure of nuclear localization signal probably allows
nuclear import of capsids. {ECO:0000250,
ECO:0000269|PubMed:11799183, ECO:0000269|PubMed:12970411,
ECO:0000269|PubMed:19656887}.
-!- SUBUNIT: Interacts with host TFRC. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Virion. Host nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=VP1;
IsoId=P17455-1; Sequence=Displayed;
Note=Minor splicing isoform.;
Name=VP2;
IsoId=P17455-2; Sequence=VSP_041137;
Note=Major splicing isoform produced by deletion of the
initiating AUG for VP1 and downstream translation of VP2.;
-!- 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.
-!- 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.
-!- SIMILARITY: Belongs to the parvoviridae capsid protein family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA47158.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1p5w";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
empty capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=2cas";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
capsid structure;
URL="http://viperdb.scripps.edu/info_page.php?VDB=4dpv";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral
empty capsid structure at pH 5,5;
URL="http://viperdb.scripps.edu/info_page.php?VDB=1c8h";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M23255; AAA47158.1; ALT_SEQ; Genomic_DNA.
EMBL; M23255; AAA47159.1; -; Genomic_DNA.
EMBL; D26081; BAA05075.1; -; Genomic_DNA.
PIR; A31163; VCPVCD.
PDB; 1C8D; X-ray; 3.00 A; A=144-727.
PDB; 1C8H; X-ray; 3.50 A; A=144-727.
PDB; 1IJS; X-ray; 3.25 A; P=144-727.
PDB; 1P5W; X-ray; 3.30 A; A=180-727.
PDB; 1P5Y; X-ray; 3.20 A; A=180-727.
PDB; 4DPV; X-ray; 2.90 A; Z=144-727.
PDBsum; 1C8D; -.
PDBsum; 1C8H; -.
PDBsum; 1IJS; -.
PDBsum; 1P5W; -.
PDBsum; 1P5Y; -.
PDBsum; 4DPV; -.
ProteinModelPortal; P17455; -.
SMR; P17455; -.
PRIDE; P17455; -.
EvolutionaryTrace; P17455; -.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0039615; C:T=1 icosahedral viral capsid; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-KW.
GO; GO:0039665; P:permeabilization of host organelle membrane involved in viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0099008; P:viral entry via permeabilization of inner membrane; IEA:UniProtKB-KW.
GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
Gene3D; 2.170.30.10; -; 1.
InterPro; IPR016184; Capsid/spike_ssDNA_virus.
InterPro; IPR001403; Parvovirus_coat.
InterPro; IPR013607; Parvovirus_coat_VP1_N.
InterPro; IPR036952; VP1/VP2.
Pfam; PF00740; Parvo_coat; 1.
Pfam; PF08398; Parvo_coat_N; 1.
SUPFAM; SSF88645; SSF88645; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Capsid protein;
Clathrin-mediated endocytosis of virus by host;
Cytoplasmic inwards viral transport; Disulfide bond; Host nucleus;
Host-virus interaction; Magnesium; Metal-binding;
Microtubular inwards viral transport; T=1 icosahedral capsid protein;
Viral attachment to host adhesion receptor;
Viral attachment to host cell;
Viral attachment to host entry receptor;
Viral penetration into host cytoplasm;
Viral penetration into host nucleus;
Viral penetration via permeabilization of host membrane; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 727 Capsid protein VP1.
/FTId=PRO_0000039425.
REGION 19 64 Phospholipase A2-like. {ECO:0000250}.
MOTIF 4 13 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 165 182 Gly-rich.
METAL 323 323 Magnesium 1.
DISULFID 633 637
VAR_SEQ 1 143 Missing (in isoform VP2). {ECO:0000305}.
/FTId=VSP_041137.
VARIANT 244 244 I -> T (in strain: Y1).
STRAND 192 196 {ECO:0000244|PDB:4DPV}.
STRAND 200 215 {ECO:0000244|PDB:4DPV}.
STRAND 223 227 {ECO:0000244|PDB:4DPV}.
HELIX 230 234 {ECO:0000244|PDB:4DPV}.
STRAND 235 237 {ECO:0000244|PDB:1P5W}.
HELIX 239 241 {ECO:0000244|PDB:4DPV}.
STRAND 245 254 {ECO:0000244|PDB:4DPV}.
HELIX 260 263 {ECO:0000244|PDB:4DPV}.
HELIX 266 275 {ECO:0000244|PDB:4DPV}.
STRAND 276 297 {ECO:0000244|PDB:4DPV}.
TURN 302 304 {ECO:0000244|PDB:1C8D}.
STRAND 307 310 {ECO:0000244|PDB:4DPV}.
STRAND 316 320 {ECO:0000244|PDB:4DPV}.
HELIX 331 334 {ECO:0000244|PDB:4DPV}.
STRAND 349 355 {ECO:0000244|PDB:4DPV}.
STRAND 358 361 {ECO:0000244|PDB:4DPV}.
STRAND 374 378 {ECO:0000244|PDB:4DPV}.
HELIX 381 383 {ECO:0000244|PDB:4DPV}.
HELIX 389 392 {ECO:0000244|PDB:4DPV}.
STRAND 396 398 {ECO:0000244|PDB:4DPV}.
STRAND 404 410 {ECO:0000244|PDB:1C8H}.
STRAND 416 418 {ECO:0000244|PDB:1P5Y}.
STRAND 419 421 {ECO:0000244|PDB:4DPV}.
HELIX 425 427 {ECO:0000244|PDB:4DPV}.
STRAND 440 442 {ECO:0000244|PDB:1C8D}.
TURN 453 455 {ECO:0000244|PDB:4DPV}.
TURN 470 472 {ECO:0000244|PDB:4DPV}.
STRAND 476 480 {ECO:0000244|PDB:4DPV}.
STRAND 488 491 {ECO:0000244|PDB:4DPV}.
STRAND 494 497 {ECO:0000244|PDB:4DPV}.
TURN 507 512 {ECO:0000244|PDB:4DPV}.
HELIX 513 516 {ECO:0000244|PDB:1C8D}.
STRAND 520 523 {ECO:0000244|PDB:4DPV}.
HELIX 525 527 {ECO:0000244|PDB:4DPV}.
STRAND 539 542 {ECO:0000244|PDB:4DPV}.
HELIX 553 555 {ECO:0000244|PDB:4DPV}.
HELIX 569 571 {ECO:0000244|PDB:4DPV}.
STRAND 575 577 {ECO:0000244|PDB:4DPV}.
STRAND 579 581 {ECO:0000244|PDB:1IJS}.
STRAND 582 586 {ECO:0000244|PDB:1P5W}.
HELIX 587 589 {ECO:0000244|PDB:4DPV}.
STRAND 613 615 {ECO:0000244|PDB:4DPV}.
STRAND 619 621 {ECO:0000244|PDB:4DPV}.
STRAND 630 635 {ECO:0000244|PDB:4DPV}.
STRAND 641 645 {ECO:0000244|PDB:4DPV}.
STRAND 657 659 {ECO:0000244|PDB:4DPV}.
STRAND 666 682 {ECO:0000244|PDB:4DPV}.
STRAND 687 689 {ECO:0000244|PDB:4DPV}.
TURN 698 700 {ECO:0000244|PDB:4DPV}.
HELIX 701 704 {ECO:0000244|PDB:4DPV}.
STRAND 717 719 {ECO:0000244|PDB:1C8D}.
STRAND 722 724 {ECO:0000244|PDB:4DPV}.
SEQUENCE 727 AA; 80343 MW; 115F3E1A79098EBE CRC64;
MAPPAKRARR GLVPPGYKYL GPGNSLDQGE PTNPSDAAAK EHDEAYAAYL RSGKNPYLYF
SPADQRFIDQ TKDAKDWGGK IGHYFFRAKK AIAPVLTDTP DHPSTSRPTK PTKRSKPPPH
IFINLAKKKK AGAGQVKRDN LAPMSDGAVQ PDGGQPAVRN ERATGSGNGS GGGGGGGSGG
VGISTGTFNN QTEFKFLENG WVEITANSSR LVHLNMPESE NYRRVVVNNM DKTAVNGNMA
LDDIHAQIVT PWSLVDANAW GVWFNPGDWQ LIVNTMSELH LVSFEQEIFN VVLKTVSESA
TQPPTKVYNN DLTASLMVAL DSNNTMPFTP AAMRSETLGF YPWKPTIPTP WRYYFQWDRT
LIPSHTGTSG TPTNIYHGTD PDDVQFYTIE NSVPVHLLRT GDEFATGTFF FDCKPCRLTH
TWQTNRALGL PPFLNSLPQS EGATNFGDIG VQQDKRRGVT QMGNTNYITE ATIMRPAEVG
YSAPYYSFEA STQGPFKTPI AAGRGGAQTD ENQAADGNPR YAFGRQHGQK TTTTGETPER
FTYIAHQDTG RYPEGDWIQN INFNLPVTND NVLLPTDPIG GKTGINYTNI FNTYGPLTAL
NNVPPVYPNG QIWDKEFDTD LKPRLHVNAP FVCQNNCPGQ LFVKVAPNLT NEYDPDASAN
MSRIVTYSDF WWKGKLVFKA KLRASHTWNP IQQMSINVDN QFNYVPSNIG GMKIVYEKSQ
LAPRKLY


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Pathways :
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining
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Related Genes :
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VP1-pX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[] Major capsid protein VP1 (Major structural protein VP1)
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)] (Fragments)
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B)] (Fragment)
[] Major capsid protein VP1 (Major structural protein VP1)
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B)] (Fragment)
[] Genome polyprotein [Cleaved into: P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Leader protease (Lb(pro)) (EC 3.4.22.46); Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protein 2A (P2A) (P52); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Protein 3B-1 (P3B-1) (Genome-linked protein VPg1); Protein 3B-2 (P3B-2) (Genome-linked protein VPg2); Protein 3B-3 (P3B-3) (Genome-linked protein VPg3); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C) (Protease P20B); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48) (P56A)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

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