MVP_TEV
ID MVP_TEV Reviewed; 1016 AA.
AC P0CK09;
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 Tobacco etch virus (TEV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12227;
OH NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH NCBI_TaxID=53851; Cassia.
OH NCBI_TaxID=4076; Datura stramonium (Jimsonweed) (Common thornapple).
OH NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
OH NCBI_TaxID=24663; Physalis.
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Allison R., Johnston R.E., Dougherty W.G.;
RT "The nucleotide sequence of the coding region of tobacco etch virus genomic
RT RNA: evidence for the synthesis of a single polyprotein.";
RL Virology 154:9-20(1986).
RN [2]
RP ACTIVE SITES OF HELPER COMPONENT PROTEINASE, AND MUTAGENESIS OF SER-610;
RP HIS-619; SER-625; ASP-627; ASP-632; CYS-649; ASP-675; ASP-689; CYS-694;
RP SER-698; ASP-715; HIS-716; HIS-722; ASP-725; SER-726; HIS-735; SER-743 AND
RP SER-755.
RX PubMed=2688301; DOI=10.1016/0042-6822(89)90582-5;
RA Oh C.-S., Carrington J.C.;
RT "Identification of essential residues in potyvirus proteinase HC-Pro by
RT site-directed mutagenesis.";
RL Virology 173:692-699(1989).
RN [3]
RP ACTIVE SITES OF P1 PROTEINASE, AND MUTAGENESIS OF HIS-214 AND SER-256.
RX PubMed=1962435; DOI=10.1016/0042-6822(91)90522-d;
RA Verchot J., Koonin E.V., Carrington J.C.;
RT "The 35-kDa protein from the N-terminus of the potyviral polyprotein
RT functions as a third virus-encoded proteinase.";
RL Virology 185:527-535(1991).
RN [4]
RP FUNCTION OF HELPER COMPONENT PROTEINASE, AND MUTAGENESIS OF PHE-314 AND
RP LYS-358.
RX PubMed=9880030; DOI=10.1099/0022-1317-79-12-3119;
RA Blanc S., Ammar E.D., Garcia-Lampasona S., Dolja V.V., Llave C., Baker J.,
RA Pirone T.P.;
RT "Mutations in the potyvirus helper component protein: effects on
RT interactions with virions and aphid stylets.";
RL J. Gen. Virol. 79:3119-3122(1998).
RN [5]
RP FUNCTION OF HELPER COMPONENT PROTEINASE.
RX PubMed=11414807; DOI=10.1006/viro.2001.0901;
RA Kasschau K.D., Carrington J.C.;
RT "Long-distance movement and replication maintenance functions correlate
RT with silencing suppression activity of potyviral HC-Pro.";
RL Virology 285:71-81(2001).
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. {ECO:0000269|PubMed:11414807,
CC ECO:0000269|PubMed:9880030}.
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=P0CK09-1; Sequence=Displayed;
CC Name=Genome polyprotein;
CC IsoId=P04517-1; 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; M15239; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0CK09; -.
DR Proteomes; UP000007404; 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 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..1016
FT /note="P3N-PIPO polyprotein"
FT /id="PRO_0000420092"
FT CHAIN 1..304
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420093"
FT CHAIN 305..763
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420094"
FT CHAIN 764..1016
FT /note="Movement protein P3N-PIPO"
FT /id="PRO_0000408553"
FT DOMAIN 163..304
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 641..763
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT REGION 997..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 358..361
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT MOTIF 615..617
FT /note="Involved in virions binding and aphid transmission"
FT /evidence="ECO:0000250"
FT ACT_SITE 214
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 223
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 256
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 649
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 722
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 304..305
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT SITE 763..764
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT MUTAGEN 214
FT /note="H->A: Complete loss of proteolytic activity of P1
FT proteinase."
FT /evidence="ECO:0000269|PubMed:1962435"
FT MUTAGEN 256
FT /note="S->A: Complete loss of proteolytic activity of P1
FT proteinase."
FT /evidence="ECO:0000269|PubMed:1962435"
FT MUTAGEN 314
FT /note="F->L: Complete loss of aphid transmission."
FT /evidence="ECO:0000269|PubMed:9880030"
FT MUTAGEN 358
FT /note="K->E: Complete loss of interaction with stylet and
FT aphid transmission; no effect on virion binding."
FT /evidence="ECO:0000269|PubMed:9880030"
FT MUTAGEN 610
FT /note="S->T: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 619
FT /note="H->S: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 625
FT /note="S->T: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 627
FT /note="D->E: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 632
FT /note="D->E: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 649
FT /note="C->S: Complete loss of proteolytic activity of HC-
FT pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 675
FT /note="D->E: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 689
FT /note="D->E: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 694
FT /note="C->S: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 698
FT /note="S->T: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 715
FT /note="D->E: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 716
FT /note="H->S: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 722
FT /note="H->S: Complete loss of proteolytic activity of HC-
FT pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 725
FT /note="D->E: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 726
FT /note="S->T: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 729
FT /note="S->T: No effect on proteolytic activity of HC-pro."
FT MUTAGEN 735
FT /note="H->S: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 743
FT /note="S->T: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT MUTAGEN 755
FT /note="S->T: No effect on proteolytic activity of HC-pro."
FT /evidence="ECO:0000269|PubMed:2688301"
FT UNSURE 916..922
SQ SEQUENCE 1016 AA; 115451 MW; 6FD0993D5AB190CC CRC64;
MALIFGTVNA NILKEVFGGA RMACVTSAHM AGANGSILKK AEETSRAIMH KPVIFGEDYI
TEADLPYTPL HLEVDAEMER MYYLGRRALT HGKRRKVSVN NKRNRRRKVA KTYVGRDSIV
EKIVVPHTER KVDTTAAVED ICNEATTQLV HNSMPKRKKQ KNFLPATSLS NVYAQTWSIV
RKRHMQVEII SKKSVRARVK RFEGSVQLFA SVRHMYGERK RVDLRIDNWQ QETLLDLAKR
FKNERVDQSK LTFGSSGLVL RQGSYGPAHW YRHGMFIVRG RSDGMLVDAR AKVTFAVCHS
MTHYSDKSIS EAFFIPYSKK FLELRPDGIS HECTRGVSVE RCGEVAAILT QALSPCGKIT
CKRCMVETPD IVEGESGESV TNQGKLLAML KEQYPDFPMA EKLLTRFLQQ KSLVNTNLTA
CVSVKQLIGD RKQAPFTHVL AVSEILFKGN KLTGADLEEA STHMLEIARF LNNRTENMRI
GHLGSFRNKI SSKAHVNNAL MCDNQLDQNG NFIWGLRGAH AKRFLKGFFT EIDPNEGYDK
YVIRKHIRGS RKLAIGNLIM STDFQTLRQQ IQGETIERKE IGNHCISMRN GNYVYPCCCV
TLEDGKAQYS DLKHPTKRHL VIGNSGDSKY LDLPVLNEEK MYIANEGYCY MNIFFALLVN
VKEEDAKDFT KFIRDTIVPK LGAWPTMQDV ATACYLLSIL YPDVLRAELP RILVDHDNKT
MHVLDSYGSR TTGYHMLKMN TTSQLIEFVH SGLESEMKTY NVGGMNRDVV TQGAIEMLIK
SIYKPHLMKQ LLEEEPYIIV LAIVSPSILI AMYNSGTFEQ ALQMWLPNTM RLANLAAILS
ALAQKLTLAD LFVQQRNLIN EYAQVILDNL IDGVRVNHSL SLAMEIVTIK LATQEMDMAL
REGGYAVTSE KVHEMLEKKL CKGFEGCMGR INLVGKILRN QAFKKALEIW AKAFNHEKHR
RLRRTYRLVC EIAFQVPLGT PEGNHLKSRK WWRKKGKSSE ECHDKRGFSQ NLQHAS
