VAP_CAMVS
ID VAP_CAMVS Reviewed; 129 AA.
AC P03551;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 29-SEP-2021, entry version 69.
DE RecName: Full=Virion-associated protein;
DE Short=Vap;
DE AltName: Full=Protein 3;
DE Short=P3;
GN ORFNames=ORF III;
OS Cauliflower mosaic virus (strain Strasbourg) (CaMV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Caulimoviridae; Caulimovirus.
OX NCBI_TaxID=10648;
OH NCBI_TaxID=3702; Arabidopsis thaliana (Mouse-ear cress).
OH NCBI_TaxID=3705; Brassica.
OH NCBI_TaxID=3725; Raphanus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7407912; DOI=10.1016/0092-8674(80)90136-1;
RA Franck A., Guilley H., Jonard G., Richards K., Hirth L.;
RT "Nucleotide sequence of cauliflower mosaic virus DNA.";
RL Cell 21:285-294(1980).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=8030207; DOI=10.1006/viro.1994.1435;
RA Dautel S., Guidasci T., Pique M., Mougeot J.L., Lebeurier G., Yot P.,
RA Mesnard J.M.;
RT "The full-length product of cauliflower mosaic virus open reading frame III
RT is associated with the viral particle.";
RL Virology 202:1043-1045(1994).
RN [3]
RP HOMOTETRAMER.
RX PubMed=9786907; DOI=10.1074/jbc.273.44.29015;
RA Leclerc D., Burri L., Kajava A.V., Mougeot J.L., Hess D., Lustig A.,
RA Kleemann G., Hohn T.;
RT "The open reading frame III product of cauliflower mosaic virus forms a
RT tetramer through a N-terminal coiled-coil.";
RL J. Biol. Chem. 273:29015-29021(1998).
RN [4]
RP INTERACTION WITH CAPSID PROTEIN, MUTAGENESIS OF ASN-127; GLN-128 AND
RP PHE-129, AND FUNCTION.
RX PubMed=11324752; DOI=10.1023/a:1008121228637;
RA Leclerc D., Stavolone L., Meier E., Guerra-Peraza O., Herzog E., Hohn T.;
RT "The product of ORF III in cauliflower mosaic virus interacts with the
RT viral coat protein through its C-terminal proline rich domain.";
RL Virus Genes 22:159-165(2001).
RN [5]
RP HOMOTRIMER.
RX PubMed=15663943; DOI=10.1016/j.jmb.2004.11.052;
RA Plisson C., Uzest M., Drucker M., Froissart R., Dumas C., Conway J.,
RA Thomas D., Blanc S., Bron P.;
RT "Structure of the mature P3-virus particle complex of cauliflower mosaic
RT virus revealed by cryo-electron microscopy.";
RL J. Mol. Biol. 346:267-277(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-95, INTERACTION WITH MP, AND
RP DISULFIDE BOND.
RX PubMed=20181714; DOI=10.1128/jvi.02662-09;
RA Hoh F., Uzest M., Drucker M., Plisson-Chastang C., Bron P., Blanc S.,
RA Dumas C.;
RT "Structural insights into the molecular mechanisms of cauliflower mosaic
RT virus transmission by its insect vector.";
RL J. Virol. 84:4706-4713(2010).
CC -!- FUNCTION: Plays a role in virus cell-to-cell and plant-to-plant
CC transmission. Interacts with virion icosahedral capsid and movement
CC protein, thereby facilitating virion cell-to-cell transmission through
CC plasmodesmata opened by viral movement protein. Also interacts with
CC aphid transmission factor, attaching the virion to aphid stylet when
CC the animal feeds on an virus infected plant. Aphid saliva may later
CC detach the virion, inducing release of infectious particles when the
CC animal feeds on a new plant. {ECO:0000269|PubMed:11324752}.
CC -!- SUBUNIT: Homotetramer, through coiled-coil domain. Homotrimer when
CC bound on icosehadral capsid. Interacts with capsid protein, and with
CC movement protein. {ECO:0000269|PubMed:11324752,
CC ECO:0000269|PubMed:20181714}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:8030207}. Host cell
CC junction, host plasmodesma {ECO:0000269|PubMed:8030207}.
CC -!- SIMILARITY: Belongs to the caulimovirus ORF III family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; V00141; CAA23458.1; -; Genomic_DNA.
DR PIR; C90799; QQCV3.
DR RefSeq; NP_056726.1; NC_001497.1.
DR PDB; 3F6N; X-ray; 3.10 A; A/B/C/D=1-129.
DR PDB; 3K4T; X-ray; 2.59 A; A/B/C/D=1-95.
DR PDBsum; 3F6N; -.
DR PDBsum; 3K4T; -.
DR SMR; P03551; -.
DR GeneID; 1489543; -.
DR KEGG; vg:1489543; -.
DR EvolutionaryTrace; P03551; -.
DR Proteomes; UP000002501; Genome.
DR GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR InterPro; IPR004986; Caulimo_virion-assoc.
DR Pfam; PF03310; Cauli_DNA-bind; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Disulfide bond; Host cell junction;
KW Reference proteome; Virion.
FT CHAIN 1..129
FT /note="Virion-associated protein"
FT /id="PRO_0000222080"
FT REGION 122..129
FT /note="Capsid binding"
FT /evidence="ECO:0000305|PubMed:11324752"
FT COILED 1..31
FT /evidence="ECO:0000255"
FT COILED 38..59
FT /evidence="ECO:0000255"
FT DISULFID 60
FT /note="Interchain (with C-62 in multimeric partner 1)"
FT /evidence="ECO:0000269|PubMed:20181714"
FT DISULFID 62
FT /note="Interchain (with C-60 in multimeric partner 2)"
FT /evidence="ECO:0000269|PubMed:20181714"
FT MUTAGEN 127
FT /note="N->A: Partial loss of capsid binding."
FT /evidence="ECO:0000269|PubMed:11324752"
FT MUTAGEN 128
FT /note="Q->A: Partial loss of capsid binding."
FT /evidence="ECO:0000269|PubMed:11324752"
FT MUTAGEN 129
FT /note="F->A: Complete loss of capsid binding."
FT /evidence="ECO:0000269|PubMed:11324752"
FT HELIX 3..32
FT /evidence="ECO:0007829|PDB:3K4T"
FT HELIX 38..59
FT /evidence="ECO:0007829|PDB:3K4T"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:3K4T"
SQ SEQUENCE 129 AA; 14153 MW; C391DEBE6E660706 CRC64;
MANLNQIQKE VSEILSDQKS MKADIKAILE LLGSQNPIKE SLETVAAKIV NDLTKLINDC
PCNKEILEAL GTQPKEQLIE QPKEKGKGLN LGKYSYPNYG VGNEELGSSG NPKALTWPFK
APAGWPNQF
