MVP_TVMV
ID MVP_TVMV Reviewed; 977 AA.
AC P0CK10;
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 Tobacco vein mottling virus (TVMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12228;
OH NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
OH NCBI_TaxID=3618; Rumex.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3737407; DOI=10.1093/nar/14.13.5417;
RA Domier L.L., Franklin K.M., Shahabuddin M., Hellmann G.M., Overmeyer J.H.,
RA Hiremath S.T., Siaw M.F.E., Lomonossoff G.P., Shaw J.G., Rhoads R.E.;
RT "The nucleotide sequence of tobacco vein mottling virus RNA.";
RL Nucleic Acids Res. 14:5417-5430(1986).
RN [2]
RP SEQUENCE REVISION.
RA Shaw J.G.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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=P0CK10-1; Sequence=Displayed;
CC Name=Genome polyprotein;
CC IsoId=P09814-1; 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; X04083; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0CK10; -.
DR Proteomes; UP000007549; 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..977
FT /note="P3N-PIPO polyprotein"
FT /id="PRO_0000420095"
FT CHAIN 1..274
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420096"
FT CHAIN 275..731
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420097"
FT CHAIN 732..977
FT /note="Movement protein P3N-PIPO"
FT /id="PRO_0000408554"
FT DOMAIN 132..274
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 609..731
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT MOTIF 325..328
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 583..585
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT ACT_SITE 183
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 192
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 617
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 690
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 274..275
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 731..732
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT UNSURE 885..891
SQ SEQUENCE 977 AA; 109980 MW; 141317F73BBE81ED CRC64;
MAATMIFGSF THDLLGKAMS TIHSAVTAEK DIFSSIKERL ERKRHGKICR MKNGSIYIKA
ASSTKVEKIN AAAKKLADDK AAFLKAQPTI VDKIIVNEKI QVVEAEEVHK REDVQTVFFK
KTKKRAPKLR ATCSSSGLDN LYNAVANIAK ASSLRVEVIH KKRVCGEFKQ TRFGRALFID
VAHAKGHRRR IDCRMHRREQ RTMHMFMRKT TKTEVRSKHL RKGDSGIVLL TQKIKGHLSG
VRDEFFIVRG TCDDSLLEAR ARFSQSITLR ATHFSTGDIF WKGFNASFQE QKAIGLDHTC
TSDLPVEACG HVAALMCQSL FPCGKITCKR CIANLSNLDF DTFSELQGDR AMRILDVMRA
RFPSFTHTIR FLHDLFTQRR VTNPNTAAFR EILRLIGDRN EAPFAHVNRL NEILLLGSKA
NPDSLAKASD SLLELARYLN NRTENIRNGS LKHFRNKISS KAHSNLALSC DNQLDQNGNF
LWGLAGIAAK RFLNNYFETI DPEQGYDKYV IRKNPNGERK LAIGNFIIST NLEKLRDQLE
GESIARVGIT EECVSRKDGN YRYPCCCVTL EDGSPMYSEL KMPTKNHLVI GNSGDPKYLD
LPGEISNLMY IAKEGYCYIN IFLAMLVNVD EANAKDFTKR VRDESVQKLG KWPSLIDVAT
ECALLSTYYP AAASAELPRL LVDHAQKTIH VVDSYGSLNT GYHILKANTV SQLEKFASNT
LESPMAQYKV GGLVYSENND ASAVKALTQA IFRPDVLSEL IEKEPYLMVF ALVSPGILMA
MSNSGALEFG ISKWISSDHS LVRMASILKT LASKVSVADT LALQKHIMRQ NANFLCGELI
NGFQKKKSYT HATRFLLMIS EENEMDDPVL NAGYRVLEAS SHEIMEKNLS RTVRDILVRL
KLVWKIQVNL VYAKALWKIQ SRIVPKRADR LARTLQQLVA VSLPEYAQAL EKQGESVSRK
IFGKHFKCKT QDNMCSF
