ID   MVP_TUMVQ               Reviewed;        1052 AA.
AC   P0CK12;
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   Turnip mosaic virus (strain Quebec) (TuMV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus.
OX   NCBI_TaxID=36396;
OH   NCBI_TaxID=3705; Brassica.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1431807; DOI=10.1099/0022-1317-73-11-2785;
RA   Nicolas O., Laliberte J.F.;
RT   "The complete nucleotide sequence of turnip mosaic potyvirus RNA.";
RL   J. Gen. Virol. 73:2785-2793(1992).
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=P0CK12-1; Sequence=Displayed;
CC       Name=Genome polyprotein;
CC         IsoId=Q02597-1; 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; D10927; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   SMR; P0CK12; -.
DR   Proteomes; UP000008263; 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..1052
FT                   /note="P3N-PIPO polyprotein"
FT                   /id="PRO_0000420098"
FT   CHAIN           1..362
FT                   /note="P1 proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000420099"
FT   CHAIN           363..820
FT                   /note="Helper component proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000420100"
FT   CHAIN           821..1052
FT                   /note="Movement protein P3N-PIPO"
FT                   /id="PRO_0000408555"
FT   DOMAIN          219..362
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   DOMAIN          698..820
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   MOTIF           414..417
FT                   /note="Involved in interaction with stylet and aphid
FT                   transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           672..674
FT                   /note="Involved in virions binding and aphid transmission"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        270
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        279
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        313
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        706
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        779
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            362..363
FT                   /note="Cleavage; by P1 proteinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   SITE            820..821
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   UNSURE          982..988
SQ   SEQUENCE   1052 AA;  117956 MW;  2D83F256D2BE6AA3 CRC64;
     MAAVTFASAI TNAITNKTTS TGMVQFGSFP PMPLRSTTVT TVATPVGQPK LYTVRFGSLD
     PVIVKGGAGS LAKATRQQPS VEIDVSLSEA AALEVAKPKS SAVLRMHEEA NKERALFLDW
     EASLKRRSYG IAENEKVVMT TRGVSKIVPR SSRAMKQKRA RERRRAQQPI ILKWEPKLSG
     FSIGGGFSAS AIEAEEVRTK WPLHKTPSMK KRMVHKTCKM SDQGVDMLIR SLVKIFKAKS
     ANIEYIGKKP IKVDFIRKER TKFARIQVAH LLGKRAQRDL LAGMEENHFI DILSEYSGNG
     TTINPGVVCA GWSGIVVRNE TLTQKRSRSP SKAFVIRGEH EDKLYDARIK ITKTMSLKIV
     HFSARGANFW KGFDRCFLAY RSDNREHTCY SGLDVTECGE VAALMCLAMF PCGKITCPDC
     VIDSELSQGQ ASGPSMKHRL TQLRDVIKSS YPRFKHAVQI LDRYEQSLSS ANENYQDFAE
     IQSISDGVEK AAFPHVNKLN AILIKGATAT GEEFSQATKH LLEIARYLKN RTENIEKGSL
     KSFRNKVSQK AHINPTLMCD NQLDKNGNFI WGERGYHAKR FFSNYFEIID PKKGYTQYET
     RVVPNGSRKL AIGKLIVPTN FEVLREQMRG EPVEPYPVTV ECVSKSQGDF VHACCCVTTE
     SGDPVLSEIK MPTKHHLVIG NSGDPKYIDL PEIEENKMYI AKEGYCYINI FLAMLVNVKE
     SQAKEFTKVV RDKLVSELGK WPTLLDVATA CYFLKVFYPD VANAELPRML VDHKTKIIHV
     VDSYGSLSTG YHVLKTNTVE QLIKFTRCNL ESSLKHYRVG GTEWENAHGA DNIDNPQWCI
     KRLVKGVYRP KQLKEDMLAN PFLPLYALLS PGVILAFYNS GSLEHLMNHY ISADSNVAVL
     LVVLKSLAKK VSTSQSVLAQ LQIIERSLPE LIEAKANING PDDAATRACN RFMGMLLHMA
     EPNYELANGG YTFLRDHSIS ILEKKLSADL GRGMERVKLV GALCYKILPV KASNLYTERF
     ANAKRSRFRR QIQRVGHILL RVEQTASKRS ER