MVP_SBMVN
ID MVP_SBMVN Reviewed; 992 AA.
AC P0CK08;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 28.
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 Soybean mosaic virus (strain N) (SMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12223;
OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Eggenberger A.L., Beachy R.N., Hill J.H.;
RT "Two genes of soybean mosaic virus are involved in the interaction with the
RT Rsv1 resistance allele of soybean.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=20170935; DOI=10.1016/j.virol.2010.01.022;
RA Wen R.H., Hajimorad M.R.;
RT "Mutational analysis of the putative pipo of soybean mosaic virus suggests
RT disruption of PIPO protein impedes movement.";
RL Virology 400:1-7(2010).
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=P0CK08-1; Sequence=Displayed;
CC Name=Genome polyprotein;
CC IsoId=P21231-1; 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; D00507; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0CK08; -.
DR Proteomes; UP000007016; 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 Reference proteome; Ribosomal frameshifting; Serine protease;
KW Suppressor of RNA silencing; Transport; Viral movement protein.
FT CHAIN 1..992
FT /note="P3N-PIPO polyprotein"
FT /id="PRO_0000420090"
FT CHAIN 1..308
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420110"
FT CHAIN 309..765
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420091"
FT CHAIN 766..992
FT /note="Movement protein P3N-PIPO"
FT /id="PRO_0000408552"
FT DOMAIN 168..308
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 643..765
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT MOTIF 361..364
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 617..619
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT ACT_SITE 221
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 230
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 262
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 651
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 724
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 308..309
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 765..766
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT UNSURE 916..922
SQ SEQUENCE 992 AA; 113900 MW; 8F5DF7C45421BCD1 CRC64;
MATIMIGSMA ISVPNTHVSC ASNSVMPVQA VQMAKQVPSA RGVLYTLKRE GSTQVHKHEE
ALRKFQEAFD QDVGIQRRLL VNKHSSIQST KKNGLTLRRL TLEQARAKEA AIARRKQEEE
DFLNGKYEQQ FYAGVSATKS MKFEGGSVGF RTKYWRPTPK KTKERRATSQ CRKPTYVLEE
VLSIASKSGK LVEFITGKGK RVKVCYVRKH GAILPKFSLP HEEGKYIHQE LQYASTYEFL
PYICMFAKYK SINADDITYG DSGLLFDERS SLTTNHTKLP YFVVRGRRNG KLVNALEVVE
NMEDIQHYSQ NPEAQFFRGW KKVFDKMPPH VENHECTTDF TNEQCGELAA AISQSIFPVK
KLSCKQCRQH IKHLSWEEYK QFLLAHMGCH GPEWETFQEI DGMRYVKRVI ETSTAENASL
QTSLEIVRLT QNYKSTHMLQ IQDINKALMK GPSVTQSELE QASKQLLAMT QWWKNHMTLT
DEDALKVFRN KRSSKALLNP SLLCDNQLDK NGNFVWGERG RHSKRFFANY FEEVVPSEGY
SKYVIRKNPN GQRELAIGSL IVPLDFERAR MALQGKSVTR EPITMSCISR QDGNFVYPCC
CVTHDDGKAF YSELRSPTKR HLVIGTSGDP KYIDLPATDA DRMYIAKEGF CYLNIFLAML
VNVNEDEAKD FTKMVRDVIV PRLGKWPTML DVATAAYMLT VFHPETRNAE LPRILVDHAC
QTMHVIDSFG SLTVGYHVLK AGTVNQLIQF ASNDLQSEMK FYRVGGEVQQ RMKCETALIT
SIFKPKRMIQ ILENDPYILL MGLVSPSILI HMYRMKHFEK GVELWISKEH SVAKIFIILE
QLTKRVAAND VLLEQLEMIS ETSERFMSIL EDCPQAPHSY KTAKDLLTMY IERKASNNQL
VENGFVDMND KLYMAYEKNL LRSLEAGMAR IKLVGKIFYN MAIEKICSTY GEMFDKESCR
RKQRIFRKLC ECVLHECPVT PKKCKKYTFP KM
