ID   VP4_AQRVC               Reviewed;         648 AA.
AC   Q8JU57;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   23-FEB-2022, entry version 66.
DE   RecName: Full=Outer capsid protein VP4;
GN   Name=S6;
OS   Aquareovirus C (isolate Golden shiner/USA/GSRV/1977) (AQRV-C).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Aquareovirus.
OX   NCBI_TaxID=185783;
OH   NCBI_TaxID=28800; Notemigonus crysoleucas (Golden shiner) (Cyprinus crysoleucas).
OH   NCBI_TaxID=90988; Pimephales promelas (Fathead minnow).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12124458; DOI=10.1099/0022-1317-83-8-1941;
RA   Attoui H., Fang Q., Mohd Jaafar F., Cantaloube J.F., Biagini P.,
RA   de Micco P., de Lamballerie X.;
RT   "Common evolutionary origin of aquareoviruses and orthoreoviruses revealed
RT   by genome characterization of Golden shiner reovirus, Grass carp reovirus,
RT   Striped bass reovirus and golden ide reovirus (genus Aquareovirus, family
RT   Reoviridae).";
RL   J. Gen. Virol. 83:1941-1951(2002).
CC   -!- FUNCTION: Interacts with VP7 to form the outer icosahedral capsid with
CC       an incomplete T=13 symmetry, about 80 nm in diameter, and consisting of
CC       200 VP4-VP7 trimers. Myristoylated N-terminal peptide may be released
CC       in the endosome and involved in permeabilization and delivery of
CC       transcriptionally active viral particles into the host cell cytoplasm
CC       (Potential). {ECO:0000305}.
CC   -!- SUBUNIT: Interacts with VP6 and VP7. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- PTM: Cleaved during the endosomal proteolytic disassembly of the outer
CC       capsid. {ECO:0000250}.
CC   -!- PTM: N-terminally myristoylated. This acylation is essential for the
CC       membrane fusion activity (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aquareoviridae outer capsid VP4 protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF403403; AAM92749.1; -; Genomic_RNA.
DR   RefSeq; NP_938065.1; NC_005171.1.
DR   SMR; Q8JU57; -.
DR   MEROPS; N07.002; -.
DR   GeneID; 2648334; -.
DR   KEGG; vg:2648334; -.
DR   Proteomes; UP000006713; Genome.
DR   GO; GO:0039621; C:T=13 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0039624; C:viral outer capsid; IEA:UniProtKB-KW.
DR   GO; GO:0046812; F:host cell surface binding; IEA:InterPro.
DR   GO; GO:0039665; P:permeabilization of host organelle membrane involved in viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0099008; P:viral entry via permeabilization of inner membrane; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.2040.10; -; 1.
DR   Gene3D; 1.10.2050.10; -; 1.
DR   Gene3D; 2.60.120.420; -; 1.
DR   InterPro; IPR009113; Mu1/VP4.
DR   InterPro; IPR036256; Mu1/VP4_sf.
DR   InterPro; IPR015962; Mu1_membr_pen_domII.
DR   InterPro; IPR044937; Mu1_membr_pen_domIII.
DR   InterPro; IPR015960; Mu1_membr_pen_domIV.
DR   Pfam; PF05993; Reovirus_M2; 1.
DR   SUPFAM; SSF69908; SSF69908; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Glycoprotein; Lipoprotein; Myristate; Outer capsid protein;
KW   Reference proteome; T=13 icosahedral capsid protein;
KW   Viral penetration into host cytoplasm;
KW   Viral penetration via permeabilization of host membrane; Virion;
KW   Virus entry into host cell.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..648
FT                   /note="Outer capsid protein VP4"
FT                   /id="PRO_0000404187"
FT   SITE            42..43
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        12
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        390
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        453
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        492
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   648 AA;  68555 MW;  A6FA4DA4164826D2 CRC64;
     MGNVQTSVNT YNITGDGNSF TPTSDMTSTA APAIDLKPGV LNPTGKLWRP VGTSVATIDS
     LAIVSDRFGQ YSFVNEGMRE TFSKALFDIN MWQPLFQATK TGCGPIVLSS FTTTTSGYVG
     ATAGDALDNP VTNGVFISTV QVMNLQRTIA ARMRDVALWQ QHLDTAMTML TPDISAGSAS
     CNWKSLLAFA KDILPLDNLC LTYPNEFYNV AIHRYPALKP GNPDTKLPDA QAHPLGEVAG
     AFNAATSEVG SLVGSSSTLS QAISTMAGKD LDLIEADTPL PVSVFTPSLA PRSYRPAFIK
     PEDAKWIAEF NNSSLIRKTL TYSGATYAVQ LGPGPTRVID MNAMIDSVLT LDVSGTILPY
     DTNPDLSTSV PAFVLIQTSV PIQQVTTAAN ITAITVVSAA GASAINLAIN VRGQPRFNML
     HLQATFERET ITGIPYIYGL GTFLIPSPTS SSNFSNPTLM DGLLTVTPVL LRETTYKGEV
     VDAIVPATVM ANQTSEEVAS ALANDAIVLV SNHLNKLANV VGDAIPVASK TDDSATSAIV
     SRLAVQHKLS QVGQTSPTPP DYPLLWRRAK RAASMFVSNP SLALQVGIPV LTQSGMLSAL
     TSGVGTALRT GSLGKGVTDA SEKLRARQSL TVAKQAFFDQ IGSLWPGK