P8_RDVA
ID P8_RDVA Reviewed; 421 AA.
AC Q85449;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-DEC-2020, entry version 79.
DE RecName: Full=Outer capsid protein P8;
DE AltName: Full=Structural protein P8;
DE Contains:
DE RecName: Full=Outer capsid protein P8';
DE Contains:
DE RecName: Full=Small peptide 1;
DE Short=Sp1;
OS Rice dwarf virus (isolate Akita) (RDV).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Phytoreovirus.
OX NCBI_TaxID=142803;
OH NCBI_TaxID=114194; Alopecurus aequalis.
OH NCBI_TaxID=90397; Echinochloa crus-galli (Barnyard grass) (Panicum crus-galli).
OH NCBI_TaxID=94400; Nephotettix cincticeps (Green rice leafhopper) (Selenocephalus cincticeps).
OH NCBI_TaxID=4530; Oryza sativa (Rice).
OH NCBI_TaxID=147271; Paspalum.
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8503785; DOI=10.1007/bf01319009;
RA Suzuki N.;
RT "In vitro translation of rice dwarf phytoreovirus genome segments S4 to
RT S10.";
RL Arch. Virol. 130:201-208(1993).
CC -!- FUNCTION: Capsid protein which self-assembles to form the outer
CC icosahedral capsid with a T=13 symmetry, about 70 nm in diameter and
CC consisting of 780 molecules capsid proteins.
CC -!- SUBUNIT: Homotrimer (By similarity). Homomultimer (By similarity).
CC Interacts with host peroxisomal glycolate oxidase (GOX). This
CC interaction mediates its relocation to virus factories peripheral to
CC host peroxisomes (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q85449; O22544: GOX; Xeno; NbExp=4; IntAct=EBI-7184126, EBI-7184099;
CC -!- SUBCELLULAR LOCATION: [Outer capsid protein P8]: Virion {ECO:0000305}.
CC Host cytoplasm {ECO:0000250}. Note=Found in the peripheral regions of
CC spherical cytoplasmic structures, called virus factories, that appear
CC early after infection and are the site of viral replication and
CC packaging. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phytoreovirus outer capsid protein P8
CC family. {ECO:0000305}.
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DR EMBL; D10219; BAA01071.1; -; mRNA.
DR SMR; Q85449; -.
DR IntAct; Q85449; 1.
DR MINT; Q85449; -.
DR GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR GO; GO:0044161; C:host cell cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0019031; C:viral envelope; IEA:InterPro.
DR GO; GO:0039624; C:viral outer capsid; IEA:UniProtKB-KW.
DR GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
DR GO; GO:0019048; P:modulation by virus of host process; ISS:UniProtKB.
DR InterPro; IPR008980; Capsid_hemagglutn.
DR InterPro; IPR009807; Phytoreo_P8.
DR InterPro; IPR008935; Virus_capsid_a-hlx_vir.
DR Pfam; PF07124; Phytoreo_P8; 1.
DR SUPFAM; SSF48345; SSF48345; 1.
DR SUPFAM; SSF49818; SSF49818; 1.
PE 1: Evidence at protein level;
KW Capsid protein; Host cytoplasm; Host-virus interaction;
KW Outer capsid protein; Virion.
FT CHAIN 1..421
FT /note="Outer capsid protein P8"
FT /id="PRO_0000040668"
FT CHAIN 1..362
FT /note="Outer capsid protein P8'"
FT /id="PRO_0000040669"
FT CHAIN 363..421
FT /note="Small peptide 1"
FT /id="PRO_0000040670"
SQ SEQUENCE 421 AA; 46484 MW; 3CB62513EBA5D8D6 CRC64;
MSRQMWLDTS ALLEAISEYV VRCNGDTFSG LTTGDFNALS NMFTQLSVSS AGYVSDPRVP
LQTMSNMFVS FITSTDRCGY MLRKTWFNSD TKPTVSDDFI TTYIRPRLQV PMSDTVRQLN
NLSLQPSAKP KLYERQNAIM KGLDIPYSEP IEPCKLFRSV AGQTGNIPMM GILATPPAAQ
QQPFFVAERR RILFGIRSNA AIPAGAYQFV VPAWASVLSV TGAYVYFTNS FFGTTIAGVT
ATATAADAAT TFTVPTDANN LPVQTDSRLS FSLGGGNINL ELGVAKTGFC VAIEGEFTIL
ANRSQAYYTL NSITQTPTSI DDFDVSDFLT TFLSQLRACG QYEIFSDAMD QLTNSLITNY
MDPPALPAGL AFTSPWFRFS ERARTILALQ NVDLNIRKLI VRHLWVITSL IAVFGRYYRP
N