MVP_PPVD
ID MVP_PPVD Reviewed; 1024 AA.
AC P0CK03;
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 D) (PPV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12212;
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=2602121; DOI=10.1093/nar/17.23.10115;
RA Teycheney P.Y., Tavert G., Delbos R., Ravelonandro M., Dunez J.;
RT "The complete nucleotide sequence of plum pox virus RNA (strain D).";
RL Nucleic Acids Res. 17:10115-10116(1989).
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=P0CK03-1; Sequence=Displayed;
CC Name=Genome polyprotein;
CC IsoId=P13529-1; 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; X16415; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0CK03; -.
DR Proteomes; UP000006849; 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..1024
FT /note="P3N-PIPO polyprotein"
FT /id="PRO_0000420075"
FT CHAIN 1..308
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420076"
FT CHAIN 309..767
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420077"
FT CHAIN 768..1024
FT /note="Movement protein P3N-PIPO"
FT /id="PRO_0000408547"
FT DOMAIN 165..308
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 645..767
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 619..621
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 653
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 726
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 767..768
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT UNSURE 921..927
SQ SEQUENCE 1024 AA; 116549 MW; DD17634367BB0567 CRC64;
MSTIVFGSFT CHLDAAIHQD NADRLAKAWT RPENRQVSNV HLLCRRAAKS LINTYESATA
SAWKGLEEKL QPMFAKREFS KTVTKRKGLR CFKESSEKFI EKKLRKQYQE ERERFQFVNG
PDAIVNQISV DKCEASVWVP FPHIIEKPSF ATPSMKKKVV FTKVRMSEAS LQLFMRRVAA
NAKANGQKVE IIGRKRVVGN YTTKSRLTYF RTHVRHLDGS KPRYDLVLDE ATKKILQLFA
NTSRFHHVHK KGEVTPGMSG FVVNPINLSD PMQVYDTDLF IVRGKHNSIL VDSRCKVSKK
QSNEIIHYSD PGKQFSDGFT NSFMQCKLRE TDHQSTSDLD VKECGDVAAL VCQAIIPCGK
ITCLQCAQKY SYMSQQEIRD RFSTVIEQHE KTAMDNYPQF SHVLAFLKRY RELMRVENQN
YEAFKDITHM IGEDRKEAPF SHLQQINELI IKGGMMSAQD YIEASDHLRE LARYQKNRTE
NIRSGSIKAF RNKISSKAHV NMQLMCDNQL DTNGNFVWGQ REYHAKRFFR NYFDVIDVSE
GYRRHIVREN PRGIRKLAIG NLVISTNLAA LRKQLLGEEC IHFEVSKECT SRRGENFVYQ
CCCVTHEDGT PLESEIISPT KNHLVVGNTG DSKYVDLPTA KGGAMFIAKA GYCYINIFLA
MLININEDEA KSFTKTVRDT LVPKLGTWPS MMDLATACHF LAVLYPETRN AELPRILVDH
EAKIFHVVDS FGSLSTGMHV LKANTINQLI SFASDTLDSN MKTYLVGGSE VDKCDEFKNV
KLLIRSIYKP QIMEQVLKEE PYLLLMSVLS PGVLMALFNS GSLEKATQYW ITRSHTLAAI
TSMLSALAAK VSLASTLNAQ MSVIDEHAAV LCDSVFDGTK PYASYMMAVK TLERMKARTE
SDHTLNDLGF SVLRQATPHL VEKKLSPGIG ASLERVKLVG KILCNLGIAA VAKTYTKTFH
PKRRRRFRRQ VRHLRSVITW QPVQTPERRS PTEKRRCGLL YTPVDGEAIL QSHRNFHKFS
SKHS
