ID VAP_CAMVD Reviewed; 129 AA. AC P03553; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 13-SEP-2023, entry version 65. 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 D/H) (CaMV). OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC Ortervirales; Caulimoviridae; Caulimovirus; Caulimovirus tessellobrassicae. OX NCBI_TaxID=10645; 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=7152260; DOI=10.1016/0378-1119(82)90013-0; RA Balazs E., Guilley H., Jonard G., Richards K.; RT "Nucleotide sequence of DNA from an altered-virulence isolate D/H of the RT cauliflower mosaic virus."; RL Gene 19:239-249(1982). 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 (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homotetramer, through coiled-coil domain. Homotrimer when CC interacts with icosehadral capsid. Interacts with capsid protein, and CC with Movement protein (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Host cell junction, host CC plasmodesma. 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; M10376; AAA46347.1; -; Genomic_DNA. DR SMR; P03553; -. DR Proteomes; UP000008439; Genome. DR GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell. DR GO; GO:0044423; C:virion component; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 6.10.250.630; -; 1. DR InterPro; IPR004986; Caulimo_virion-assoc. DR Pfam; PF03310; Cauli_DNA-bind; 1. PE 3: Inferred from homology; KW Coiled coil; Disulfide bond; Host cell junction; Virion. FT CHAIN 1..129 FT /note="Virion-associated protein" FT /id="PRO_0000222077" FT REGION 122..129 FT /note="Capsid binding" FT /evidence="ECO:0000250" FT COILED 1..31 FT /evidence="ECO:0000250" FT COILED 38..59 FT /evidence="ECO:0000250" FT DISULFID 60 FT /note="Interchain (with C-62 in multimeric partner 1)" FT /evidence="ECO:0000250" FT DISULFID 62 FT /note="Interchain (with C-60 in multimeric partner 2)" FT /evidence="ECO:0000250" SQ SEQUENCE 129 AA; 14110 MW; D1184908AC9C0706 CRC64; MANLNQIQKE VSEILSDQKS MKADIKAILE LLGSQNPIKE SLETVAAKIV NDLTKLINDC PCNKEILEAL GNQPKEQLIG QPKEKGKGLN LGKYSYPNYG VGNEELGSSG NPKALTWPFK APAGWPNQY //