MVP_PVMA
ID MVP_PVMA Reviewed; 993 AA.
AC P0CK05;
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 Potato virus A (PVA).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12215;
OH NCBI_TaxID=45843; Solanum betaceum (Tamarillo) (Cyphomandra betacea).
OH NCBI_TaxID=4112; Solanum nigrum (Black nightshade).
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8113771; DOI=10.1099/0022-1317-75-2-457;
RA Puurand U., Makinen K., Paulin L., Saarma M.;
RT "The nucleotide sequence of potato virus A genomic RNA and its sequence
RT similarities with otherpotyviruses.";
RL J. Gen. Virol. 75:457-461(1994).
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=P0CK05-1; Sequence=Displayed;
CC Name=Genome polyprotein;
CC IsoId=Q85197-1; 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; Z21670; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0CK05; -.
DR Proteomes; UP000008484; 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..993
FT /note="P3N-PIPO polyprotein"
FT /id="PRO_0000420081"
FT CHAIN 1..298
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420082"
FT CHAIN 299..755
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420083"
FT CHAIN 756..993
FT /note="Movement protein P3N-PIPO"
FT /id="PRO_0000408549"
FT DOMAIN 154..298
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 633..755
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT MOTIF 349..352
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 607..609
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT ACT_SITE 207
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 216
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 249
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 641
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 714
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 298..299
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 755..756
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT UNSURE 909..915
SQ SEQUENCE 993 AA; 111268 MW; 9B3F637C5E98AC8C CRC64;
MATQVIMVGE FKILEVNCKP HAPVAAIHVP TQTPKTNDIK WADLEFTLAK SLQRQAHGVV
KVDKHGTARI KRASKHHMSC LEQQMADEVA EKEAFMAAPT QLVTSIIFAG TTPPSMMETE
TIVKKIHTVG KRAKVMRKRS YITPPTDKSL RNHGVTPYSV QQLCRTLGNL SKRTGISLEV
VGKTSKATKL RFTKTSFGHM ARVQLKHHDG RMHRRDLVVD TSTTTIMQTL FLKTARTNAN
LDVLTHGSSG LVFWNYLVTG QRMRTRDNFI IVRGRCNGIL VDARAKLSES TMLSTHHYST
GDVFWRGFNR TFLENKPINL DHVCSSDFSV EECGSIAALI CQSLLPCGKI TCRACAAKNL
NMDEDTFKEF QTQRAREISA VIISEHPNFA CVSQFIDRYF SHQRVLNPNV NAYREILKIV
GGFTQSPYTH IQELNEILVL GGRATPEQLG SASAHLLEIT RFVRNRTDNI KKGSLALFRN
KISAKAHVNT ALMCDNQLDR NGNLIWGERG YHAKRFFSNY FDIITPGGGY KQYIERRVPN
GIRKLAIGNL IVTTNLEALR EQLEGESIEK KAVTKACVSM SDNNYKYPCC CVTLDDGTPL
YSTFIMPTKN HLVIGNSGDP KFLDLPADIS TQMYIAKSGY CYINIFLAML VNVDESDAKD
FTKKVRDIIV PDLGEWPTLI DVATSCSLLS AFYPATSAAE LPRILVDHDL KTMHVIDSYG
SLNTGYHVLK ANTIRQLIQF ASNSLDSEMK HYRVGGTSNS QINGYATIKM LAKAVYRPKL
MKEIIHEQPF MLVMSLMSPG ILIALANSGA LEMGIHHWIR EGDSLVKMAH MLRTVAQNVS
VARATWVQQE IISDSAQQML ETILNGTIPN VSYFQAIQYL TMLAASKEVD AEVRVTGYYT
FKLQTSELLE KNLLEPVGGF MARVKLFWKI SSNKTFAKVL HCGYNCCQAR KARRLRRNLR
YILSVCTGQT DGILQESSLS GCEWIASPIQ QHH
