MVP_TUMVJ
ID MVP_TUMVJ Reviewed; 1043 AA.
AC P0CK11;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 33.
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 Turnip mosaic virus (strain Japanese) (TuMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12230;
OH NCBI_TaxID=126270; Alliaria petiolata (Garlic mustard) (Arabis petiolata).
OH NCBI_TaxID=3705; Brassica.
OH NCBI_TaxID=38206; Calanthe.
OH NCBI_TaxID=3719; Capsella bursa-pastoris (Shepherd's purse) (Thlaspi bursa-pastoris).
OH NCBI_TaxID=264418; Hesperis matronalis.
OH NCBI_TaxID=13274; Stellaria media (Common chickweed) (Alsine media).
OH NCBI_TaxID=74517; Trifolium hybridum (Alsike clover).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8920830; DOI=10.1007/bf01718209;
RA Ohshima K., Tanaka M., Sako N.;
RT "The complete nucleotide sequence of turnip mosaic virus RNA Japanese
RT strain.";
RL Arch. Virol. 141:1991-1997(1996).
RN [2]
RP CHARACTERIZATION, FUNCTION, AND SUBCELLULAR LOCATION OF MOVEMENT PROTEIN
RP P3N-PIPO.
RX PubMed=18408156; DOI=10.1073/pnas.0800468105;
RA Chung B.Y.-W., Miller W.A., Atkins J.F., Firth A.E.;
RT "An overlapping essential gene in the Potyviridae.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5897-5902(2008).
RN [3]
RP FUNCTION OF MOVEMENT PROTEIN P3N-PIPO.
RX PubMed=20585568; DOI=10.1371/journal.ppat.1000962;
RA Wei T., Zhang C., Hong J., Xiong R., Kasschau K.D., Zhou X.,
RA Carrington J.C., Wang A.;
RT "Formation of complexes at plasmodesmata for potyvirus intercellular
RT movement is mediated by the viral protein P3N-PIPO.";
RL PLoS Pathog. 6:E1000962-E1000962(2010).
RN [4]
RP FUNCTION OF MOVEMENT PROTEIN P3N-PIPO, RIBOSOMAL FRAMESHIFTING, AND
RP INTERACTION WITH HOST PCAP1.
RX PubMed=22511869; DOI=10.1371/journal.ppat.1002639;
RA Vijayapalani P., Maeshima M., Nagasaki-Takekuchi N., Miller W.A.;
RT "Interaction of the trans-frame potyvirus protein P3N-PIPO with host
RT protein PCaP1 facilitates potyvirus movement.";
RL PLoS Pathog. 8:E1002639-E1002639(2012).
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. {ECO:0000269|PubMed:18408156,
CC ECO:0000269|PubMed:20585568, ECO:0000269|PubMed:22511869}.
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:0000269|PubMed:22511869}.
CC -!- SUBCELLULAR LOCATION: Host cell junction, host plasmodesma
CC {ECO:0000269|PubMed:18408156}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=P3N-PIPO polyprotein;
CC IsoId=P0CK11-1; Sequence=Displayed;
CC Name=Genome polyprotein;
CC IsoId=P89509-1; 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; D83184; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0CK11; -.
DR Proteomes; UP000008262; 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; IMP:CACAO.
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 1: Evidence at protein 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..1043
FT /note="P3N-PIPO polyprotein"
FT /id="PRO_0000420039"
FT CHAIN 1..362
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420040"
FT CHAIN 363..820
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420041"
FT CHAIN 821..1043
FT /note="Movement protein P3N-PIPO"
FT /id="PRO_0000408535"
FT DOMAIN 219..362
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 698..820
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT MOTIF 414..417
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 672..674
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT ACT_SITE 270
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 279
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 313
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 706
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 779
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 362..363
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 820..821
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT UNSURE 982..988
SQ SEQUENCE 1043 AA; 117285 MW; 78FF0622D7E3FAE4 CRC64;
MAAVTFATAI TNTTASKPAL TGMIQFGNFP PVPLRSTTVT TVATSVAQPK LHTVQFGSLD
PVVVKSGAGS FAKATRQQPN VEIDVSLSEA AALEVAKPRP NAVLRMHEEA NKERALFLDW
EASLKRSSYG IAENEKVVMT TRGVSKIVPR SSGAMKQKRA RERRRAQQPI ILKWEPKLSG
ISIGGGLSAS AIEVEEARTK WPLHKTPSMK RKTVHRRCKM NDQGIDMLMR SLIKIFKAKS
ANIEFIGRKS IKVDFVKKEQ TKFARVQVVH LLGKRAQRDL STGMEENHFI DILSGYSGNK
TTINPGVVCA GWSGIVVRDG ILTQKRSRSP SEAFVIRGEH EGKLYDARIK ITRTMSHKIV
HFSAAGANFW KGFDRCFLAY RSDNREHTCY SGLDVTECGE VAALMCLAMF PCGKITCPDC
VTDSELSQGQ ASGPSMKHRL VQLRDVIKSS YPRFKHAVQI LDRYEQSLRS ANENYQDFAE
IQSISDGVEK AAFPHVNKLN AILIKGATAT GEEFSQATKH LLEIARYLKN RTENIEKGSL
KSFRNKISQK AHINPTLMCD NQLDRNGNFI WGERGYHAKR FFSNYFEIID PKKGYTQYET
RVVPNGSRKL AIGKLIVPTN FEVLREQMKG EPVEPYPVTV ECVSKLQGDF VHACCCVTTE
SGDPVLSEIK MPTKHHLVIG NSGDPKYIDL PEIEENKMYI AKEGYCYINI FLAMLVNVKE
SQAKEFTKVV RDKLVGELGK WPTLLDVATA CYFLKVFYPD VANAELPRML VDHKTKIIHV
VDSYGSLSTG YHVLKTNTVE QLIKFTRCNL ESSLKHYRVG GTEWEDTHGA KNIDDPQWCI
KRLIKGVYRP KQLKEDMLAN PFLPLYALLS PGVILAFYNS GSLEYLMNHY IRVDSNVAVL
LVVLKSLAKK VSTSQSVLAQ LQIIDRSLPE LVEARANINR PDDEAARACN RFMGMLLHMS
EPNWELADGG YTILRDHSIS ILEKKLSTNL GRSMERVKLV GALCYKILLV KASNFYTERF
ANEKRSRFRR QIQRVSRVIL RME
