MVP_PSBMV
ID MVP_PSBMV Reviewed; 1096 AA.
AC P0CJ99;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 31.
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 Pea seed-borne mosaic virus (strain DPD1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=31736;
OH NCBI_TaxID=3888; Pisum sativum (Garden pea).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1940858; DOI=10.1099/0022-1317-72-11-2625;
RA Johansen E., Rasmussen O.F., Heide M., Borkhardt B.;
RT "The complete nucleotide sequence of pea seed-borne mosaic virus RNA.";
RL J. Gen. Virol. 72:2625-2632(1991).
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=P0CJ99-1; Sequence=Displayed;
CC Name=Genome polyprotein;
CC IsoId=P29152-1; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D10930; -; NOT_ANNOTATED_CDS; mRNA.
DR SMR; P0CJ99; -.
DR Proteomes; UP000006689; 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 2: Evidence at transcript level;
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..1096
FT /note="P3N-PIPO polyprotein"
FT /id="PRO_0000420063"
FT CHAIN 1..397
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420064"
FT CHAIN 398..856
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420065"
FT CHAIN 857..1096
FT /note="Movement protein P3N-PIPO"
FT /id="PRO_0000408543"
FT DOMAIN 255..397
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 734..856
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT MOTIF 450..453
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 708..710
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT ACT_SITE 307
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 316
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 348
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 742
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 815
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 397..398
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 856..857
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT UNSURE 1016..1022
SQ SEQUENCE 1096 AA; 124210 MW; B473E2BB68A78ABF CRC64;
MSTLVCQAVA APVWSNGART RRIRDADGEY RCTQCDMGFD SMTMARPVNH CCDGIMIDEY
NLYDDDPIMH LVDSKTPIKR GSQETEGDGM AAEAIKVTGA EPVNCFMVGT IKCKINENSI
VAKGVMAAIP RQLTQDEVFM RKARLQAAVA KSTIEREEKE RQFAFSKLEE KLRARREKLK
DGIVIKTRKG LEWREATPNQ QRGKLQSTSF DASGGKTLTP HTIYCKTKSS KFSNGGVKCA
TSKKMRTVRK PQSLKMKTES IDVLIEQVMT IAGKHAKQVT LIDKQKTNRV WIRRVNGVRL
LQVETKHHKG IISQKDASLN NLTKRVARHF ARKTAYIHPS DSITHGHSGV VFLRANISGS
KSYSIDDLFV VRGKRNGKLM ESRNKVAWRK MFQIDHFSIV GIKIWNAFDA EYVKLRDESV
SDHDCVGGIT PEECGILAAQ ILRVFYPCWR ITCTKCISNW LSKPTSEQIE HIYERGNLAI
QDLNKRIPSA HHVTQMVELL RQRIKNTTFD MGNNTKVHEL IGHRQDGVFR HLNRLNNSIL
AANGSSTIEW ESMNESLLEL ARWHNKRTES IASGGISSFR NKISAKAQIN FALMCDNQLD
TNGNFVWGER GYHAKRFFSE FFTKIDPKDG YSHHTVRATP TGVRHLAIGN LIIPGDLQKL
REKLEGVSIT AVGISEKCVS RRNGDFVYPC SCVTSENGKP VLSDVILPTR NHLVIGNTGD
PKLVDLPKTE TGRMWIAKEG YCYINIFFAM LVNVSEKDAK DFTKFVRDEI MPQLGKWPTM
MDVATACYKL AIIYPDVRDA QLPRILVDHS EQIFHVIDSY GSMTTGYHIL KAGTVSQLIS
FAHGALLGEM KMYRVGGTQK MEINMCCCQR KNLLIKQLIR AIYRPKLLTE IIETEPFVLM
LAIVSPSILK AMFRSGTFNQ AIKFYMHRSK PTAQTLAFLE ALSERVSRSR VLSEQFNIID
GALKELKSLA NMSMRTQHTY PIVQNQLDIM IERVSADAEL LRDGFVVSKG RVQALIEKKL
SRRPEKFLHR LAICTTIATN YVIFKSEAWF WRIVRKQRLE LFQGSMDGAF ELIFGRRQTD
HPLGAHKVAA DVSKWW
