MVP_LMV0
ID MVP_LMV0 Reviewed; 1152 AA.
AC P0CJ97;
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 Lettuce mosaic virus (strain 0 / isolate French) (LMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=117132;
OH NCBI_TaxID=4222; Carthamus tinctorius (Safflower).
OH NCBI_TaxID=3827; Cicer arietinum (Chickpea) (Garbanzo).
OH NCBI_TaxID=114280; Cichorium endivia (Endive).
OH NCBI_TaxID=13427; Cichorium intybus (Chicory).
OH NCBI_TaxID=52518; Eustoma exaltatum subsp. russellianum (Bluebells) (Eustoma grandiflorum).
OH NCBI_TaxID=4235; Lactuca.
OH NCBI_TaxID=3888; Pisum sativum (Garden pea).
OH NCBI_TaxID=3562; Spinacia oleracea (Spinach).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9085548; DOI=10.1016/s0168-1702(96)01411-6;
RA Revers F., Yang S.J., Walter J., Souche S., Lot H., Le Gall O.,
RA Candresse T., Dunez J.;
RT "Comparison of the complete nucleotide sequences of two isolates of lettuce
RT mosaic virus differing in their biological properties.";
RL Virus Res. 47:167-177(1997).
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=P0CJ97-1; Sequence=Displayed;
CC Name=Genome polyprotein;
CC IsoId=P31999-1; 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; X97704; -; NOT_ANNOTATED_CDS; mRNA.
DR SMR; P0CJ97; -.
DR PRIDE; P0CJ97; -.
DR Proteomes; UP000008377; 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..1152
FT /note="P3N-PIPO polyprotein"
FT /id="PRO_0000420057"
FT CHAIN 1..437
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420058"
FT CHAIN 438..895
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420059"
FT CHAIN 896..1152
FT /note="Movement protein P3N-PIPO"
FT /id="PRO_0000408541"
FT DOMAIN 292..437
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 773..895
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT MOTIF 489..492
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 747..749
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT ACT_SITE 345
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 354
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 388
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 781
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 854
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 437..438
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 895..896
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT UNSURE 1076..1082
SQ SEQUENCE 1152 AA; 130214 MW; 3F61121F2B5131A6 CRC64;
MATLDNCTQV HHMFAYNREH GTNYTRNHFR RYLAAQRIGF YYDWDDDVYE CPTCEAIYHS
LDDIKNWHEC DPPAFDLNDF ITDARLKSAP VPDLGPVIIE IPKAEEKQEL NFFAATPAPE
VSQWKCRGLQ FGSFTELETS EPVASAPEPK CEEPARTIAK PEESVEQETR GDGKRLLQAQ
MEVDKAEQDL AFACLNASLK PRLEGRTTAT IARRRDGCLV YKTKPSWSQR RRAKKTLKVD
TLACENPYIP AIVDKISIAG GSSASVMHEQ QKPKTLHTTP SRKVATHYKR TVMNQQTLMA
FINQVGTILL NAEKEFEVVG CRKQKVTGKG TRHNGVRLVK LKTAHEEGHR RRVDIRIPNG
LRPIVMRISA RGGWHRTWTD SELSPGSSGY VLNSSKIIGK FGLRRHSIFV VRGRVDGEVI
DSQSKVTHSI THRMVQYSDV ARNFWNGYST CFMHNTPKDI LHTCTSDFDV KECGTVAALL
TQTLFQFGKI TCEKCAIEYK NLTRDELATR VNKEIDGTII SIQTQHPRFV HVLNFLRLIK
QVLNAKNGNF GAFQETERII GDRMDAPFSH VNKLNAIVIK GNQATSDEMA QASNHVLEIA
RYLKNRTENI QKGSLKSFRN KISGKAHLNP SLMCDNQLDK NGGFEWGQRS YHAKRFFDGY
FETIDPSDGY SKYTIRRNPN GHRKLAIGNL IVSTNFESHR RSMIGESIED PGLTNQCVSK
EGDTFIYPCC CVTDEYGKPT LSEIKMPTKH HLVLGNAGDP KYVDLPKEAE GKMFVTKDGY
CYINIFLAML VDVPEDQAKD FTKMAREIAV KQLGEWPSMM DVATACNILA TFHPDTRRSE
LPRILVDHAT KTFHVIDSYG SITTGFHILK ANTVTQLVKF AHESLESEMQ HYRVGGEPDK
APRKPAGSVP TLGISDLRDL GVELENEEHS IRPNLQRLIK AIYRPRMMRS LLTEEPYLLI
LSIVSPGVLM ALYNSGSLER TMHEFLQTDQ RLSATAQILK HLAKKVSLAK TLTIQNAILE
GGAGSLNEIL DAPAGRSLSY RLAKQTVEVM MARSDMDKEL VDVGFSVLRD QKNELIEKKL
SHGFGGFVAR TTIVWKIISN ASLAAMAGYF YSRSNPNRRR RFERQIQYLG WICFQKRDLA
PKGNLLRRSK ES
