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P3N-PIPO polyprotein [Cleaved into: P1 proteinase (EC 3.4.-.-) (N-terminal protein); Helper component proteinase (HC-pro) (EC 3.4.22.45); Movement protein P3N-PIPO (Pretty interesting potyviridae ORF) (PIPO)]

 MVP_TEV                 Reviewed;        1016 AA.
P0CK09;
31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
31-OCT-2012, sequence version 2.
07-NOV-2018, entry version 22.
RecName: Full=P3N-PIPO polyprotein;
Contains:
RecName: Full=P1 proteinase;
EC=3.4.-.-;
AltName: Full=N-terminal protein;
Contains:
RecName: Full=Helper component proteinase;
Short=HC-pro;
EC=3.4.22.45;
Contains:
RecName: Full=Movement protein P3N-PIPO;
AltName: Full=Pretty interesting potyviridae ORF;
Short=PIPO;
Tobacco etch virus (TEV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Potyviridae; Potyvirus.
NCBI_TaxID=12227;
NCBI_TaxID=4072; Capsicum annuum (Bell pepper).
NCBI_TaxID=53851; Cassia.
NCBI_TaxID=4076; Datura stramonium (Jimsonweed) (Common thornapple).
NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
NCBI_TaxID=24663; Physalis.
NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Allison R., Johnston R.E., Dougherty W.G.;
"The nucleotide sequence of the coding region of tobacco etch virus
genomic RNA: evidence for the synthesis of a single polyprotein.";
Virology 154:9-20(1986).
[2]
ACTIVE SITES OF HELPER COMPONENT PROTEINASE, AND MUTAGENESIS OF
SER-610; HIS-619; SER-625; ASP-627; ASP-632; CYS-649; ASP-675;
ASP-689; CYS-694; SER-698; ASP-715; HIS-716; HIS-722; ASP-725;
SER-726; HIS-735; SER-743 AND SER-755.
PubMed=2688301; DOI=10.1016/0042-6822(89)90582-5;
Oh C.-S., Carrington J.C.;
"Identification of essential residues in potyvirus proteinase HC-Pro
by site-directed mutagenesis.";
Virology 173:692-699(1989).
[3]
ACTIVE SITES OF P1 PROTEINASE, AND MUTAGENESIS OF HIS-214 AND SER-256.
PubMed=1962435; DOI=10.1016/0042-6822(91)90522-D;
Verchot J., Koonin E.V., Carrington J.C.;
"The 35-kDa protein from the N-terminus of the potyviral polyprotein
functions as a third virus-encoded proteinase.";
Virology 185:527-535(1991).
[4]
FUNCTION OF HELPER COMPONENT PROTEINASE, AND MUTAGENESIS OF PHE-314
AND LYS-358.
PubMed=9880030;
Blanc S., Ammar E.D., Garcia-Lampasona S., Dolja V.V., Llave C.,
Baker J., Pirone T.P.;
"Mutations in the potyvirus helper component protein: effects on
interactions with virions and aphid stylets.";
J. Gen. Virol. 79:3119-3122(1998).
[5]
FUNCTION OF HELPER COMPONENT PROTEINASE.
PubMed=11414807; DOI=10.1006/viro.2001.0901;
Kasschau K.D., Carrington J.C.;
"Long-distance movement and replication maintenance functions
correlate with silencing suppression activity of potyviral HC-Pro.";
Virology 285:71-81(2001).
-!- FUNCTION: Helper component proteinase: required for aphid
transmission and also has proteolytic activity. Only cleaves a
Gly-Gly dipeptide at its own C-terminus. Interacts with virions
and aphid stylets. Acts as a suppressor of RNA-mediated gene
silencing, also known as post-transcriptional gene silencing
(PTGS), a mechanism of plant viral defense that limits the
accumulation of viral RNAs. May have RNA-binding activity.
{ECO:0000269|PubMed:11414807, ECO:0000269|PubMed:9880030}.
-!- FUNCTION: Movement protein P3N-PIPO: allows efficient cell to cell
propagation, by bypassing the host cell wall barrier. Transports
viral genome to neighboring plant cells directly through
plasmosdesmata, without any budding (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Hydrolyzes a Gly-|-Gly bond at its own C-
terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the
processing of the potyviral polyprotein.
-!- SUBUNIT: Interacts (via PIPO domain) with host PCaP1 protein; this
interaction may help to anchor the movement complex to the plasma
membrane from which the complex could move to the plasmodesmata.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Host cell junction, host plasmodesma
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=P3N-PIPO polyprotein;
IsoId=P0CK09-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting in P3 ORF.;
Name=Genome polyprotein;
IsoId=P04517-1; Sequence=External;
Note=Produced by conventional translation.;
-!- DOMAIN: The N-terminus of helper component proteinase is involved
in interaction with stylets. The central part is involved in
interaction with virions and the C-terminus is involved in cell-to
cell movement of the virus (By similarity). {ECO:0000250}.
-!- PTM: Potyviral RNA is expressed as two polyproteins which undergo
post-translational proteolytic processing. Genome polyprotein is
processed by NIa-pro, P1 and HC-pro proteinases resulting in the
production of at least ten individual proteins. P3N-PIPO is
cleaved by P1 and HC-pro proteinases resulting in the production
of three individual proteins. The P1 proteinase and the HC-pro
cleave only their respective C-termini autocatalytically (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the potyviridae P3N-PIPO polyprotein
family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M15239; -; NOT_ANNOTATED_CDS; Genomic_RNA.
SMR; P0CK09; -.
PRIDE; P0CK09; -.
OrthoDB; VOG0900003L; -.
Proteomes; UP000007404; Genome.
GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0046740; P:transport of virus in host, cell to cell; IEA:UniProtKB-KW.
InterPro; IPR001456; HC-pro.
InterPro; IPR031159; HC_PRO_CPD_dom.
InterPro; IPR002540; Pept_S30_P1_potyvir.
InterPro; IPR039560; Potyvirid-P3.
Pfam; PF00851; Peptidase_C6; 1.
Pfam; PF01577; Peptidase_S30; 1.
Pfam; PF13608; Potyvirid-P3; 1.
PROSITE; PS51744; HC_PRO_CPD; 1.
PROSITE; PS51871; PV_P1_PRO; 1.
1: Evidence at protein level;
Complete proteome; Host cell junction; Host-virus interaction;
Hydrolase; Protease; Ribosomal frameshifting; Serine protease;
Suppressor of RNA silencing; Transport; Viral movement protein.
CHAIN 1 1016 P3N-PIPO polyprotein.
/FTId=PRO_0000420092.
CHAIN 1 304 P1 proteinase. {ECO:0000255}.
/FTId=PRO_0000420093.
CHAIN 305 763 Helper component proteinase.
{ECO:0000255}.
/FTId=PRO_0000420094.
CHAIN 764 1016 Movement protein P3N-PIPO.
/FTId=PRO_0000408553.
DOMAIN 163 304 Peptidase S30. {ECO:0000255|PROSITE-
ProRule:PRU01219}.
DOMAIN 641 763 Peptidase C6. {ECO:0000255|PROSITE-
ProRule:PRU01080}.
MOTIF 358 361 Involved in interaction with stylet and
aphid transmission.
MOTIF 615 617 Involved in virions binding and aphid
transmission. {ECO:0000250}.
ACT_SITE 214 214 For P1 proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU01219}.
ACT_SITE 223 223 For P1 proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU01219}.
ACT_SITE 256 256 For P1 proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU01219}.
ACT_SITE 649 649 For helper component proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU01080}.
ACT_SITE 722 722 For helper component proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU01080}.
SITE 304 305 Cleavage; by P1 proteinase.
{ECO:0000255|PROSITE-ProRule:PRU01219}.
SITE 763 764 Cleavage; by autolysis.
{ECO:0000255|PROSITE-ProRule:PRU01080}.
MUTAGEN 214 214 H->A: Complete loss of proteolytic
activity of P1 proteinase.
{ECO:0000269|PubMed:1962435}.
MUTAGEN 256 256 S->A: Complete loss of proteolytic
activity of P1 proteinase.
{ECO:0000269|PubMed:1962435}.
MUTAGEN 314 314 F->L: Complete loss of aphid
transmission.
{ECO:0000269|PubMed:9880030}.
MUTAGEN 358 358 K->E: Complete loss of interaction with
stylet and aphid transmission; no effect
on virion binding.
{ECO:0000269|PubMed:9880030}.
MUTAGEN 610 610 S->T: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 619 619 H->S: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 625 625 S->T: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 627 627 D->E: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 632 632 D->E: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 649 649 C->S: Complete loss of proteolytic
activity of HC-pro.
{ECO:0000269|PubMed:2688301}.
MUTAGEN 675 675 D->E: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 689 689 D->E: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 694 694 C->S: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 698 698 S->T: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 715 715 D->E: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 716 716 H->S: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 722 722 H->S: Complete loss of proteolytic
activity of HC-pro.
{ECO:0000269|PubMed:2688301}.
MUTAGEN 725 725 D->E: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 726 726 S->T: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 729 729 S->T: No effect on proteolytic activity
of HC-pro.
MUTAGEN 735 735 H->S: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 743 743 S->T: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
MUTAGEN 755 755 S->T: No effect on proteolytic activity
of HC-pro. {ECO:0000269|PubMed:2688301}.
UNSURE 916 922
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


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