POLS_ABPVR
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 02-JUN-2021, entry version 63.
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.
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};
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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; Genome.
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.
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
