ID POLS_ABPVR Reviewed; 904 AA. AC Q9DSN8; DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2013, sequence version 2. DT 13-SEP-2023, entry version 65. DE RecName: Full=Structural polyprotein; DE Contains: DE RecName: Full=Protein VP1; DE AltName: Full=Virion protein 2; DE Contains: DE RecName: Full=Protein VP4; DE AltName: Full=Virion protein 4; DE Contains: DE RecName: Full=Protein VP2; DE AltName: Full=Virion protein 3; DE Contains: DE RecName: Full=Protein VP3; DE AltName: Full=Virion protein 1; GN ORFNames=ORF2; OS Acute bee paralysis virus (strain Rothamsted) (ABPV). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Picornavirales; Dicistroviridae; Aparavirus; Aparavirus apisacutum. OX NCBI_TaxID=1217067; OH NCBI_TaxID=7460; Apis mellifera (Honeybee). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=11080493; DOI=10.1006/viro.2000.0616; RA Govan V.A., Leat N., Allsopp M., Davison S.; RT "Analysis of the complete genome sequence of acute bee paralysis virus RT shows that it belongs to the novel group of insect-infecting RNA viruses."; RL Virology 277:457-463(2000). RN [2] RP PROTEOLYTIC PROCESSING OF POLYPROTEIN. RX PubMed=22258854; DOI=10.1007/s00705-012-1223-0; RA Azzami K., Ritter W., Tautz J., Beier H.; RT "Infection of honey bees with acute bee paralysis virus does not trigger RT humoral or cellular immune responses."; RL Arch. Virol. 157:689-702(2012). CC -!- FUNCTION: Structural polyprotein: precursor of all the viral capsid CC proteins. CC -!- FUNCTION: [Protein VP1]: Forms, together with protein VP2 and protein CC VP3, an icosahedral capsid protecting the viral RNA genome. The CC icosahedral capsid has a pseudo-T=3 symmetry with a diameter of CC approximately 300 Angstroms, and is composed of 60 copies of each CC capsid proteins. CC -!- FUNCTION: [Protein VP2]: Forms, together with protein VP1 and protein CC VP3, an icosahedral capsid protecting the viral RNA genome. The CC icosahedral capsid has a pseudo-T=3 symmetry with a diameter of CC approximately 300 Angstroms, and is composed of 60 copies of each CC capsid proteins. CC -!- FUNCTION: [Protein VP3]: Forms, together with protein VP1 and protein CC VP2, an icosahedral capsid protecting the viral RNA genome. The CC icosahedral capsid has a pseudo-T=3 symmetry with a diameter of CC approximately 300 Angstroms, and is composed of 60 copies of each CC capsid proteins. CC -!- SUBCELLULAR LOCATION: [Protein VP1]: Virion. Host cytoplasm CC {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Protein VP2]: Virion. Host cytoplasm CC {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Protein VP3]: Virion. Host cytoplasm CC {ECO:0000305}. CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. CC {ECO:0000269|PubMed:22258854}. CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family. CC {ECO:0000305}. CC -!- CAUTION: Translation initiates on an Ala codon through an unusual CC Internal Ribosome Entry Site (IRES). {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG13119.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AF150629; AAG13119.1; ALT_INIT; Genomic_RNA. DR RefSeq; NP_066242.1; NC_002548.1. DR SMR; Q9DSN8; -. DR GeneID; 911836; -. DR KEGG; vg:911836; -. DR Proteomes; UP000006040; Segment. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR CDD; cd00205; rhv_like; 2. DR Gene3D; 2.60.120.20; -; 3. DR InterPro; IPR014872; Dicistrovirus_capsid-polyPr_C. DR InterPro; IPR001676; Picornavirus_capsid. DR InterPro; IPR033703; Rhv-like. DR InterPro; IPR029053; Viral_coat. DR InterPro; IPR024343; VP4_dicistrovir. DR Pfam; PF08762; CRPV_capsid; 1. DR Pfam; PF11492; Dicistro_VP4; 1. DR Pfam; PF00073; Rhv; 1. DR SUPFAM; SSF88633; Positive stranded ssRNA viruses; 3. PE 1: Evidence at protein level; KW Capsid protein; Host cytoplasm; Reference proteome; Virion. FT CHAIN 1..314 FT /note="Protein VP1" FT /evidence="ECO:0000255" FT /id="PRO_0000423154" FT CHAIN 315..396 FT /note="Protein VP4" FT /evidence="ECO:0000255" FT /id="PRO_0000423155" FT CHAIN 397..696 FT /note="Protein VP2" FT /evidence="ECO:0000255" FT /id="PRO_0000423156" FT CHAIN 697..904 FT /note="Protein VP3" FT /evidence="ECO:0000255" FT /id="PRO_0000423157" FT REGION 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 35..54 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 320..348 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 904 AA; 100879 MW; F9AA1FF575432CCE CRC64; ADQETNTSNV HNTQLASTSE ENSVETEQIT TFHDVETPNR INTPMAQDTS SARSMDDTHS IIQFLQRPVL IDHIEVIAGS TADDNKPLNR YVLNRQNPQP FVKSWTLPSV VLSAGGKGQK LANFKYLRCD VKVKIVLNAN PFIAGRLYLA YSPYDDRVDP ARSILNTSRA GVTGYPGIEI DFQLDNSVEM TIPYASFQEA YDLVTGTEDF VKLYLFTITP ILSPTSTSAS SKVDLSVYMW LDNISLVIPT YRVNTSIVPN VGTVVQTVQN MTTRDSETIR KAMVALRKNN KSTYDYIVQA LSSAVPEVKN VTMQINSKKN NSNKMATPVK EKTKNIPKPK TENPKIGPIS ELATGVNKVA NGIERIPVIG EMAKPVTSTI KWVADKIGSV AAIFGWSKPR NLEQVNLYQN VPGWGYSLYK GIDNSVPLAF DPNNELGDLR DVFPSGVDEM AIGYVCGNPA VKHVLSWNTT DKVQAPISNG DDWGGVIPVG MPCYSKIIRT TENDTTRTNT EIMDPAPCEY VCNMFSYWRA TMCYRIAIVK TAFHTGRLGI FFGPGKIPIT TTKDNISPDL TQLDGIKAPS DNNYKYILDL TNDTEITIRV PFVSNKMFMK STGIYGGNSE NNWDFSESFT GFLCIRPITK FMCPETVSNN VSIVVWKWAE DVVVVEPKPL LSGPTQVFQP PVTSADSINT IDASMQINLA NKADENVVTF FDSDDAEERN MEALLKGSGE QIMNLRSLLR TFRTISENWN LPPNTKTAIT DLTDVADKEG RDYMSYLSYI YRFYRGGRRY KFFNTTALKQ SQTCYVRSFL IPRYYTADNT NNDGPSHITY PVLNPVHEVE VPYYCQYRKL PVASTTDKGY DASLMYYSNV GTNQIVARAG NDDFTFGWLI GTPQTQGITR TETK //