ID   MVP_PEMVC               Reviewed;         985 AA.
AC   P0CK01;
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   Pepper mottle virus (isolate California) (PeMV) (PepMoV C).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Potyvirus.
OX   NCBI_TaxID=31737;
OH   NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH   NCBI_TaxID=4075; Datura inoxia (Downy thornapple) (Datura meteloides).
OH   NCBI_TaxID=4107; Solanum.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1413501; DOI=10.1016/0042-6822(92)90162-i;
RA   Vance V.B., Moore D., Turpen T.H., Bracker A., Hollowell V.C.;
RT   "The complete nucleotide sequence of pepper mottle virus genomic RNA:
RT   comparison of the encoded polyprotein with those of other sequenced
RT   potyviruses.";
RL   Virology 191:19-30(1992).
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=P0CK01-1; Sequence=Displayed;
CC       Name=Genome polyprotein;
CC         IsoId=Q01500-1; 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; M96425; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   SMR; P0CK01; -.
DR   Proteomes; UP000008157; 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..985
FT                   /note="P3N-PIPO polyprotein"
FT                   /id="PRO_0000420069"
FT   CHAIN           1..287
FT                   /note="P1 proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000420070"
FT   CHAIN           288..743
FT                   /note="Helper component proteinase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000420071"
FT   CHAIN           744..985
FT                   /note="Movement protein P3N-PIPO"
FT                   /id="PRO_0000408545"
FT   DOMAIN          144..287
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   DOMAIN          621..743
FT                   /note="Peptidase C6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   MOTIF           337..340
FT                   /note="Involved in interaction with stylet and aphid
FT                   transmission"
FT                   /evidence="ECO:0000250"
FT   MOTIF           595..597
FT                   /note="Involved in virions binding and aphid transmission"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        195
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        204
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        238
FT                   /note="For P1 proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   ACT_SITE        629
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   ACT_SITE        702
FT                   /note="For helper component proteinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   SITE            287..288
FT                   /note="Cleavage; by P1 proteinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT   SITE            743..744
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT   UNSURE          909..915
SQ   SEQUENCE   985 AA;  112002 MW;  6409DFA6F5EBEE3C CRC64;
     MATSVIQFGS FVCNLPKSQP LCTTVHCPKQ SMSTNIVRPS DPFAELEKHL EPYLQKRMDA
     TIRQTKGGTL VYKHMSEAKR ARKLRKKQRE EEEVRLFMNA APYIVSNITI GGGEVPSKME
     EVSIKRPLNK TPSRKIKKSL TPVTFRDGHM NKFLRELRDC ATRNSMTVHL IGKRKTELAF
     KRRASLNAVY ATLHHMRGVD RKRDIVLEEW MNDYVLNLSK VSTWGSLFHA ESLKRGDSGL
     ILNARALRGK FGRCSRGFFI VRGKSDGVVL DARSKLSMAT VTHMEQYSTP EAFWSGLEKK
     WSVVRKPTAH TCKPTYSVSN CGEVAAIIAQ ALFPCHKLTC GECSKEICDL TSNECVQELY
     KNTSLALERM NNLHPEFQHI VKVLSVVRQL TEASNHGTET FDEIFKMIGS KTQSPFTHLN
     KLNEFMLKGN ENTSGEWLTA RQHLRELVRF QKNRTDNIKK GDLASFRNKL SARAQYNLYL
     SCDNQLDKNA SFLWGQREYH ARRFFLNFFQ QIDPSKGYLA YEDRTIPNGS RKLAIGNLIV
     PLDLAEFRKR MNGIDTQQPP IGKYCTSQLD GNFVYPCCCT TLDDGQPIRS AVYAPTKKHL
     VVGNTGDTKY INLPKGDTEM LYIALDGYCY INIYLAMLVN ISEEEAKDFT KKVRDIFMPK
     LGKWPTLMDL ATTCAQLRIF HPDVHDAELP RILVDHNTQT CHVVDSYGSI STGYHILKAA
     TVSQLVLFAD DNLESEIKHY RVGGIVENHK VQIDNQPSRC GVSEFHAIRM LIKGIYRPSV
     MYELLSEEPY LLVFSILSPS ILIAMYNDRA FELAVQIWLE KEQSIPLIAT ILTNLAAKVS
     VATTLVQQLQ LIELSADQLL NVTCDGFRVS FAYQSALTLL TRMRDQAKAN SELISGGFNE
     YDQDLAWTLE KKLSRPLTRP MERIKLAGKI SLLLVLKKAK DSFAVKYQKQ KFARCQRNIQ
     FITETIYGKG FLPHESRSSV HQARN