ID   MVP_BTMV                Reviewed;        1038 AA.
AC   P0CJ96;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=P3N-PIPO polyprotein;
DE   Contains:
DE     RecName: Full=P1 proteinase;
DE              EC=3.4.-.-;
DE     AltName: Full=N-terminal protein;
DE   Contains:
DE     RecName: Full=Helper component proteinase;
DE              Short=HC-pro;
DE              EC=3.4.22.45;
DE   Contains:
DE     RecName: Full=Movement protein P3N-PIPO;
DE     AltName: Full=Pretty interesting potyviridae ORF;
DE              Short=PIPO;
OS   Beet mosaic virus (BtMV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus.
OX   NCBI_TaxID=114921;
OH   NCBI_TaxID=124763; Amaranthus retroflexus (Redroot amaranth) (American pigweed).
OH   NCBI_TaxID=350892; Beta vulgaris subsp. maritima (Sea beet) (Beta maritima).
OH   NCBI_TaxID=3555; Beta vulgaris subsp. vulgaris (Beet).
OH   NCBI_TaxID=3559; Chenopodium album (Fat-hen).
OH   NCBI_TaxID=200951; Melilotus indicus (Sourclover) (Yellow sweet clover).
OH   NCBI_TaxID=50192; Sonchus arvensis (Perennial sowthistle).
OH   NCBI_TaxID=3562; Spinacia oleracea (Spinach).
OH   NCBI_TaxID=60916; Trifolium incarnatum (Crimson clover).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15168206; DOI=10.1007/s00705-003-0278-3;
RA   Nemchinov L.G., Hammond J., Jordan R., Hammond R.W.;
RT   "The complete nucleotide sequence, genome organization, and specific
RT   detection of beet mosaic virus.";
RL   Arch. Virol. 149:1201-1214(2004).
CC   -!- FUNCTION: [Helper component proteinase]: Required for aphid
CC       transmission and also has proteolytic activity. Only cleaves a Gly-Gly
CC       dipeptide at its own C-terminus. Interacts with virions and aphid
CC       stylets. Acts as a suppressor of RNA-mediated gene silencing, also
CC       known as post-transcriptional gene silencing (PTGS), a mechanism of
CC       plant viral defense that limits the accumulation of viral RNAs. May
CC       have RNA-binding activity (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: [Movement protein P3N-PIPO]: Allows efficient cell to cell
CC       propagation, by bypassing the host cell wall barrier. Transports viral
CC       genome to neighboring plant cells directly through plasmosdesmata,
CC       without any budding (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in
CC         the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the
CC         potyviral polyprotein.; EC=3.4.22.45;
CC   -!- SUBUNIT: Interacts (via PIPO domain) with host PCaP1 protein; this
CC       interaction may help to anchor the movement complex to the plasma
CC       membrane from which the complex could move to the plasmodesmata.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host cell junction, host plasmodesma
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CJ96-1; Sequence=Displayed;
CC       Name=Genome polyprotein;
CC         IsoId=Q6XW15-1; Sequence=External;
CC   -!- DOMAIN: The N-terminus of helper component proteinase is involved in
CC       interaction with stylets. The central part is involved in interaction
CC       with virions and the C-terminus is involved in cell-to cell movement of
CC       the virus (By similarity). {ECO:0000250}.
CC   -!- PTM: Potyviral RNA is expressed as two polyproteins which undergo post-
CC       translational proteolytic processing. Genome polyprotein is processed
CC       by NIa-pro, P1 and HC-pro proteinases resulting in the production of at
CC       least ten individual proteins. P3N-PIPO is cleaved by P1 and HC-pro
CC       proteinases resulting in the production of three individual proteins.
CC       The P1 proteinase and the HC-pro cleave only their respective C-termini
CC       autocatalytically (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform P3N-PIPO polyprotein]: Produced by -1 ribosomal
CC       frameshifting in P3 ORF.
CC   -!- SIMILARITY: Belongs to the potyviridae P3N-PIPO polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AY206394; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   SMR; P0CJ96; -.
DR   PRIDE; P0CJ96; -.
DR   Proteomes; UP000007617; Genome.
DR   GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046740; P:transport of virus in host, cell to cell; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.70.150; -; 1.
DR   InterPro; IPR001456; HC-pro.
DR   InterPro; IPR031159; HC_PRO_CPD_dom.
DR   InterPro; IPR042308; HC_PRO_CPD_sf.
DR   InterPro; IPR002540; Pept_S30_P1_potyvir.
DR   InterPro; IPR039560; Potyvirid-P3.
DR   Pfam; PF00851; Peptidase_C6; 1.
DR   Pfam; PF01577; Peptidase_S30; 1.
DR   Pfam; PF13608; Potyvirid-P3; 1.
DR   PROSITE; PS51744; HC_PRO_CPD; 1.
DR   PROSITE; PS51871; PV_P1_PRO; 1.
PE   3: Inferred from homology;
KW   Host cell junction; Host-virus interaction; Hydrolase; Protease;
KW   Ribosomal frameshifting; Serine protease; Suppressor of RNA silencing;
KW   Transport; Viral movement protein.
FT   CHAIN           1..1038
FT                   /note="P3N-PIPO polyprotein"
FT                   /id="PRO_0000420051"
FT   CHAIN           1..313
FT                   /note="P1 proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000420052"
FT   CHAIN           314..770
FT                   /note="Helper component proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000420053"
FT   CHAIN           771..1038
FT                   /note="Movement protein P3N-PIPO"
FT                   /id="PRO_0000408539"
FT   DOMAIN          170..313
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   DOMAIN          648..770
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   MOTIF           365..368
FT                   /note="Involved in interaction with stylet and aphid
FT                   transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           622..624
FT                   /note="Involved in virions binding and aphid transmission"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        224
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        233
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        266
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        656
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        729
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            313..314
FT                   /note="Cleavage; by P1 proteinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   SITE            770..771
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   UNSURE          922..928
SQ   SEQUENCE   1038 AA;  117627 MW;  ADADC66A5B6E1C6C CRC64;
     MATMMHFGQF PSNIPLRAAT CCTKVHSTLV TKEMMASSVK PAESSSVARP IIYSSAATDG
     YEKAQRAFEA SFREKYSGKL EAMKYGKMVK KGGLTYVKRA GPQAIAKGIE MDAAIEKFNT
     AFNAGELENV TLEGDITAGI SVARGESVWL RSVFWSRSLK KQARKKTPKL VAKSDFDDLF
     NKVLKVASLG NIPVEIVGKK ANKILRCGYR RVNTSTIPYF HLPHHNSNYI CRELHPQRVR
     WLVPLLVRHR KIRDQFSDSM IARGWSGLIL PKYIASTCGR RYDEVIVRGR LYGRVEDART
     KLPAGDVGRT MHYSSGEERF FAGWKEGFEK LVPAQKEHIC KIVQDNKFCG KLAASIVQIA
     FPCHKMACDV CRNKFNEMTP EAYSELIDKH IDQRMNEINE AIVRFPGLKQ VVSNFRSKHI
     ASTNIKDNLE VAKLTQGHKA NQMMQLARIN SILIKGNTAT PSEISDASGL LLEITRWFNN
     HLSVIDKGSL RAFRNKRSSK ALVNPSLLCD NQRDKNGNFI WGERGYHSKR FFASHFDEVT
     PGDGYKEYII RKGPQGQRKL AIGNLIVSFD LEKTRQALKG EEVEKLPLSN SCVSKRNGNY
     VYTSCCVTLD DGTPLYSNIK NPTKRHLVVG TTGDPKIVDL PATDTDKMYI AKEGYCYLNI
     FLAMLINVNE NEAKAFTKMV RDIIIPMLGT WPTMQDLATA CFMMTAFFPE TSSAELPRIL
     VDHTNQTMHV IDSFGSLTTG YHVLKAGTAA QLIDFASTEL EGEMKWYRVG GHGLPVKEKM
     ISALITSIFR PKKLVYLIEE DPYVLIMAMC SPRLIISLFN NGALELAAKH WISRDKNVSA
     IFAMLMDLST EMSKAELLIE QHRMINECAK RVHDTQNYLD EVGPHQQEVR TFLALISDEL
     EADKELHKTG FANFSERFHS LTEKNVCGRV RRGMARFKLV RQILLCHLCV QAQTAFNIRF
     APEKVRRYRC QIRHIAQLVR WKDEGTPKWR PEVCYKPDHP IHELHQARYA RQSHAHHVQL
     PKGPRILYEC CLGDSFAH