MVP_PPVSK
ID MVP_PPVSK Reviewed; 1026 AA.
AC P0CK04;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 32.
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 Plum pox potyvirus (strain SK 68) (PPV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=103927;
OH NCBI_TaxID=36596; Prunus armeniaca (Apricot) (Armeniaca vulgaris).
OH NCBI_TaxID=36595; Prunus cerasifera (cherry plum).
OH NCBI_TaxID=3758; Prunus domestica (Garden plum).
OH NCBI_TaxID=105665; Prunus glandulosa.
OH NCBI_TaxID=3760; Prunus persica (Peach) (Amygdalus persica).
OH NCBI_TaxID=88123; Prunus salicina.
OH NCBI_TaxID=114937; Prunus spinosa (Blackthorn) (Prunus domestica var. spinosa).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8122394; DOI=10.1007/bf01703390;
RA Palkovics L., Burgyan J., Balazs E.;
RT "Comparative sequence analysis of four complete primary structures of plum
RT pox virus strains.";
RL Virus Genes 7:339-347(1993).
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=P0CK04-1; Sequence=Displayed;
CC Name=Genome polyprotein;
CC IsoId=Q84934-1; 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; M92280; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0CK04; -.
DR Proteomes; UP000007637; 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..1026
FT /note="P3N-PIPO polyprotein"
FT /id="PRO_0000420078"
FT CHAIN 1..308
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420079"
FT CHAIN 309..766
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420080"
FT CHAIN 767..1026
FT /note="Movement protein P3N-PIPO"
FT /id="PRO_0000408548"
FT DOMAIN 165..308
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 644..766
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT MOTIF 360..363
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 618..620
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT ACT_SITE 216
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 225
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 259
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 652
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 725
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 308..309
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 766..767
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT UNSURE 920..926
SQ SEQUENCE 1026 AA; 116782 MW; 8D1339961875CF72 CRC64;
MSTIVFGSFT CHLDAAIHQD NADRLAKAWT RPENRQVSNV HLLCRRAAKS LINTYESATA
SAWKGLEEKL QPMFAKREFS KTVTKRKGLR CFKESSEKFI EKKLKKQYKE ERERFQFLNG
PDAIVNQISV DKCEASVWVP FPHIIEKPSF TTPSMKKKVV FTKVRMSEAS LQLFMRRVAA
NAKANGQKVE IIGRKRVVGH YTTKSRLTYF RTHVRHLDGS KPRYDLVLDE ATKKILQLFA
NTSGFHHVHK KGEITPGMSG FVVNPMNLSD PMHVYDTDLF IVRGKHNSIL VDSRCKVSKE
QSNEIVHYSD PGKQFWDGFT NSFMQCKLRE TDHQCTSDLD VKECGYVAAL VCQAIIPCGK
ITCLQCAQKY SYMSQQEIRD RFSTVIEQHE KTVMDNYPQF SHVLAFLKRY RELMRVENQN
YEAFKDITHM IGERKEAPFS HLNKINELII KGGMMSAQDY IEASDHLREL ARYQKNRTEN
IRSGSIKAFR NKISSKAHVN MQLMCDNQLD TNGNFVWGQR EYHAKRFFRN YFDVIDVSEG
YRRHIVRENP RGIRKLAIGN LVMSTNLAAL RKQLLGEECI HFEVSKECTS KRGENFVYQC
CCVTHEDGTP LESEIISPTK NHLVVGNSGD SKYVDLPTAK GGAMFIAKAG YCYINIFLAM
LININEDEAK SFTKTVRDTI VPKLGTWPSM MDLATACHFL AVLYPETRNA ELPRILVDHE
AKIFHVVDSF GSLSTGMHVL KANTINQLIS FASDTLDSSM KTYLVGGLEV DKCDEFKNVK
LLIRSIYKPQ IMEQVLKEEP YLLLMSVLSP GVLMALFNSG SLEKATQYWI ARSHSLAAIT
AMLSALAAKV SLASTLNAQM SVIDEHAAVL CDSVFVGTKP YASYMMAVKT LERMKARTES
DHTLNDLGFS VLRQATPHLV EKKLSPGVGA GLERIKLVGK VLCNLGIAAV AKTYTKTFHP
ERRSRFRRQV RHLRSVITWQ PIQTPERRSS AEKRRRCLLH TPVDGKAILQ SYRNFHKFSS
KHSEDV
