MVP_ZYMVC
ID MVP_ZYMVC Reviewed; 991 AA.
AC P0CK13;
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 Zucchini yellow mosaic virus (strain California) (ZYMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=117128;
OH NCBI_TaxID=3654; Citrullus lanatus (Watermelon) (Citrullus vulgaris).
OH NCBI_TaxID=3656; Cucumis melo (Muskmelon).
OH NCBI_TaxID=3659; Cucumis sativus (Cucumber).
OH NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7844540; DOI=10.1099/0022-1317-76-1-37;
RA Wisler G.C., Purcifull D.E., Hiebert E.;
RT "Characterization of the P1 protein and coding region of the zucchini
RT yellow mosaic virus.";
RL J. Gen. Virol. 76:37-45(1995).
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=P0CK13-1; Sequence=Displayed;
CC Name=Genome polyprotein;
CC IsoId=P18479-1; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L31350; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0CK13; -.
DR Proteomes; UP000008610; 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..991
FT /note="P3N-PIPO polyprotein"
FT /id="PRO_0000420101"
FT CHAIN 1..310
FT /note="P1 proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420102"
FT CHAIN 311..766
FT /note="Helper component proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420103"
FT CHAIN 767..991
FT /note="Movement protein P3N-PIPO"
FT /id="PRO_0000408556"
FT DOMAIN 170..310
FT /note="Peptidase S30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT DOMAIN 644..766
FT /note="Peptidase C6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT MOTIF 362..365
FT /note="Involved in interaction with stylet and aphid
FT transmission"
FT /evidence="ECO:0000250"
FT MOTIF 618..620
FT /note="Involved in virions binding and aphid transmission"
FT ACT_SITE 223
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 232
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 264
FT /note="For P1 proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01219"
FT ACT_SITE 652
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT ACT_SITE 725
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT SITE 310..311
FT /note="Cleavage; by P1 proteinase"
FT /evidence="ECO:0000255"
FT SITE 766..767
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01080"
FT UNSURE 915..921
SQ SEQUENCE 991 AA; 113426 MW; D2194E71CEEF26E1 CRC64;
MASIMIGSIS VPIAKTEQCA NTQVSNRANI VAPGHMATCP LPLKTHMYYR HESKKLMQSN
KSIDILNNFF STDEMKFRLT RNEMSKLKKG PSGRIVLRKP SKQRVFARIE QDEAARKEEA
VFLEGNYDDS ITNLARVLPP AVTHNVDVSL RSPFYKRTYK KERKKVAQKQ IVQAPLNSLC
TRVLKIARNK NIPVEMIGNK KTRHTLTFKR FRGCFVGKVS VAHEEGRMRH TEMSYEQFKW
LLKAICQVTH TERIREEDIK PGCSGWVLGT NHTLTKRYSR LPHLVIRGRD DDGIVNALEQ
VLFYSEVDHS SSQPEVQFFQ GWRRIFDKFR PSPDHVCKAD HNNEECGELA AIFCQALFPV
VKLSCQTCRE SLVEVSFEEF KDSLNANFII HKDEWGSFKE GSQYDNIFKL IKVATQATQN
LKLSSEVMKL VQNHTSTHMK QIQDINKALM KGSLVAQDEL DLALKQLLEM TQWFKNHMHL
TGEEALKMFR NKRSSKAMIN PSLLCGNQLD KNGNFVWGER GYHSKRLFKN FFEEVIPSEG
YTKYVVRNFP NGTRKLAIGS LIVPLNLDRA RTALLGESIE KKPLTSACVS QQNGNYIHSC
CCVTMDDGTP MYSELKSPTK RHLVIGASSD PKYIDLPASE AERMYIAKEG YCYLSIFLAM
LVNVNENEAK DFTKMIRDVL IPMLGQWPSL MDVATAAYIL GVFHPETRCA ELPRILVDHA
TQTMHVIDSY GSLTVGYHVL KAGTVNHLIQ FASNDLQSEM KHYRVGGTPT QRIKLEEQLI
KGIFKPKLMM QLLHDDPYIL LLGMISPTIL VHMYRMRHFE RGIEIWIKRD HEIGKIFVIL
EQLTRKVALA EVLVDQLNLI SEASPHLLEI MKGCQDNQRA YVPALDLLTI QVEREFSNKE
LKTNGYPDLQ QTLFDMREKN VCKAAAQFMA RAKLAGKILC NRAIEAILDF YGKKFNPASK
RRKARIFATI CSRVFYHDPS TCEEHSRCRR A
