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MCAPS_PLRVW
ID   MCAPS_PLRVW             Reviewed;         716 AA.
AC   P11626;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Readthrough protein P3-RTD;
DE   AltName: Full=P3-P5 readthrough protein;
DE   AltName: Full=P74;
DE   AltName: Full=Readthrough protein;
DE            Short=RT protein;
DE   Contains:
DE     RecName: Full=Minor capsid readthrough protein {ECO:0000250|UniProtKB:P09514};
DE              Short=Minor capsid RT protein {ECO:0000250|UniProtKB:P09514};
DE     AltName: Full=54 kDa protein;
DE   Contains:
DE     RecName: Full=Cleaved product {ECO:0000305};
GN   ORFNames=ORF3/ORF5;
OS   Potato leafroll virus (strain Potato/Netherlands/Wageningen/1989) (PLrV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Sobelivirales; Solemoviridae; Polerovirus.
OX   NCBI_TaxID=12048;
OH   NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2466700; DOI=10.1016/0014-5793(89)80190-5;
RA   van der Wilk F., Huisman M.J., Cornelissen B.J.C., Huttinga H.,
RA   Goldbach R.W.;
RT   "Nucleotide sequence and organization of potato leafroll virus genomic
RT   RNA.";
RL   FEBS Lett. 245:51-56(1989).
CC   -!- FUNCTION: [Minor capsid readthrough protein]: Minor component of the
CC       viral capsid involved in aphid transmission and virus accumulation in
CC       the host (By similarity). Required for the virus to move through the
CC       aphid (By similarity). The RTD domain of the protein is exposed on the
CC       surface of the particle and determines the vector specificity and
CC       intestinal tropism in the aphid (By similarity). This domain might also
CC       determine the limitation of the virus to the host phloem (By
CC       similarity). {ECO:0000250|UniProtKB:P09514,
CC       ECO:0000250|UniProtKB:P09516, ECO:0000250|UniProtKB:P17525}.
CC   -!- FUNCTION: [Isoform P7]: Participates, together with the proteins P0 and
CC       P1, in the inhibition of the induction of aphid-induced host
CC       phytohormones. This could play a role in the attraction to the infected
CC       plants by aphids. {ECO:0000250|UniProtKB:P17525}.
CC   -!- SUBCELLULAR LOCATION: [Minor capsid readthrough protein]: Virion
CC       {ECO:0000250|UniProtKB:P17525}. Host cell junction, host plasmodesma
CC       {ECO:0000250|UniProtKB:P17525}. Host periplasm
CC       {ECO:0000250|UniProtKB:P17525}.
CC   -!- SUBCELLULAR LOCATION: [Cleaved product]: Virion
CC       {ECO:0000250|UniProtKB:P17525}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=2;
CC       Name=Readthrough protein P3-RTD;
CC         IsoId=P11626-1; Sequence=Displayed;
CC       Name=P7;
CC         IsoId=P11626-2; Sequence=VSP_038674;
CC   -!- DOMAIN: [Isoform Readthrough protein P3-RTD]: The N-terminus is highly
CC       basic like those of many plant virus capsid proteins. These regions may
CC       be involved in protein-RNA interaction (By similarity). The RTD N-
CC       terminus is responsible for aphid transmission and aphid endosymbiont
CC       interaction (By similarity). The readthrough domain is required for
CC       transport of virus through membranes of the aphid salivary glands (By
CC       similarity). {ECO:0000250|UniProtKB:P09514,
CC       ECO:0000250|UniProtKB:P09516, ECO:0000250|UniProtKB:P17525}.
CC   -!- PTM: [Isoform Readthrough protein P3-RTD]: In virus particles, more
CC       than 200 amino acids are proteolytically cleaved releasing the C-
CC       terminus part of the RTD domain. The cleaved product remains attached
CC       to the virus particle. {ECO:0000250|UniProtKB:P17525}.
CC   -!- MISCELLANEOUS: [Isoform Readthrough protein P3-RTD]: This protein is
CC       translated as a fusion protein by episodic readthrough of the major
CC       coat protein termination codon. It is composed of the major capsid
CC       protein fused to a long C-terminal extension called the readthrough
CC       domain (RTD). Readthrough of the terminator codon TAG occurs between
CC       the codons for 208-Lys and 210-Val. {ECO:0000250|UniProtKB:P17525}.
CC   -!- SIMILARITY: Belongs to the luteoviruses readthrough protein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA68799.1; Type=Miscellaneous discrepancy; Note=Readthrough of an in-frame TAG stop codon in position 209 translated as Tyr.; Evidence={ECO:0000305};
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DR   EMBL; Y07496; CAA68799.1; ALT_SEQ; Genomic_RNA.
DR   PIR; S03551; S03551.
DR   SMR; P11626; -.
DR   Proteomes; UP000000474; Genome.
DR   GO; GO:0044229; C:host cell periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   Gene3D; 2.60.120.20; -; 1.
DR   InterPro; IPR001517; Luteo_coat.
DR   InterPro; IPR002929; PLrV_ORF5.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF00894; Luteo_coat; 1.
DR   Pfam; PF01690; PLRV_ORF5; 1.
PE   3: Inferred from homology;
KW   Alternative promoter usage; Capsid protein; Host cell junction;
KW   Host periplasm; RNA suppression of termination; Virion.
FT   CHAIN           1..716
FT                   /note="Readthrough protein P3-RTD"
FT                   /id="PRO_0000222430"
FT   CHAIN           1..?443
FT                   /note="Minor capsid readthrough protein"
FT                   /id="PRO_0000455347"
FT   CHAIN           ?444..716
FT                   /note="Cleaved product"
FT                   /id="PRO_0000455348"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..716
FT                   /note="Readthrough domain (RTD)"
FT   REGION          438..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          694..698
FT                   /note="Involved in the efficient long distance movement of
FT                   the virus and the periplasmic subcellular location"
FT                   /evidence="ECO:0000250|UniProtKB:P17525"
FT   COMPBIAS        43..62
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..226
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..457
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..521
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            443..444
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:P09514"
FT   VAR_SEQ         1..591
FT                   /note="Missing (in isoform P7)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_038674"
SQ   SEQUENCE   716 AA;  79759 MW;  BBD2F9374542CAB0 CRC64;
     MSTVVVKGNV NGGVQQPRRR RRQSLRRRAN RVQPVVMVTA PGQPRRRRRR RGGNRRSRRT
     GVPRGRGSSE TFVFTKDNLM GNSQGSFTFG PSLSDCPAFK DGILKAYHEY KITSILLQFV
     SEASSTSSGS IAYELDPHCK VSSLQSYVNQ FQIPQGGAKT YQARMINGVE WHDSSEDQCR
     ILWKGNGKSS DTAGSFRVTI RVALQNPKYD SGPEPGPSPQ PTPTPTPQKH ERFIAYVGIP
     MLTIQARESD DQIILGSLGS QRMKYIEDEN QNYTNVSSEY YSQSSMQAVP MYYFNVPKGQ
     WSVDISCEGY QPTSSTSDPN RGRSDGMIAY SNADSDYWNV GEADGVKISK LRNDNTYRQG
     HPELEINSCH FREGQLLERD ATISFHVEAP TDGRFFLVGP AIQKTAKYNY TISYGDWTDR
     DMELGLITVV LDEHLEGTGS ANRVRRPPRE GHTYMASPRE PEGKPVGNKP RDETPIQTQE
     RQPDQTPSDD VSDAGSVNSG GSTESLQLEF GANSDSTYDA TVDGTDWPRI PPPRHPPEPR
     VSGNSRTVTD FSPKADLLEN WDAKHFDPGY SKEDVAAATI IAHGSIQDGR SMLEKREENV
     KNKTSSWKPP LPKAVSPAIA KLRSIRKSQP LEGGTLKKDA TDGVSSIGSG SLTGGTLKRK
     ETIEERLLQT LTTEQRLWYE NLKKTNPLAA TQWLFEYQPP PQVDRNLAEK PFQGRK
 
 
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