ID   VP4_AQRVG               Reviewed;         650 AA.
AC   B2BNE4;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   23-FEB-2022, entry version 52.
DE   RecName: Full=Outer capsid protein VP4;
GN   Name=S6;
OS   Aquareovirus G (isolate American grass carp/USA/PB01-155/-) (AQRV-G).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Aquareovirus.
OX   NCBI_TaxID=648234;
OH   NCBI_TaxID=7959; Ctenopharyngodon idella (Grass carp) (Leuciscus idella).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=18191982; DOI=10.1016/j.virol.2007.12.006;
RA   Mohd Jaafar F., Goodwin A.E., Belhouchet M., Merry G., Fang Q.,
RA   Cantaloube J.F., Biagini P., de Micco P., Mertens P.P., Attoui H.;
RT   "Complete characterisation of the American grass carp reovirus genome
RT   (genus Aquareovirus: family Reoviridae) reveals an evolutionary link
RT   between aquareoviruses and coltiviruses.";
RL   Virology 373:310-321(2008).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH VP6 AND VP7.
RC   STRAIN=GCRV;
RX   PubMed=18625243; DOI=10.1016/j.jmb.2008.06.075;
RA   Cheng L., Fang Q., Shah S., Atanasov I.C., Zhou Z.H.;
RT   "Subnanometer-resolution structures of the grass carp reovirus core and
RT   virion.";
RL   J. Mol. Biol. 382:213-222(2008).
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:0000269|PubMed:18625243}.
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; EF589103; ABV01044.1; -; Genomic_RNA.
DR   RefSeq; YP_001837099.1; NC_010589.1.
DR   SMR; B2BNE4; -.
DR   MEROPS; N07.002; -.
DR   GeneID; 6218804; -.
DR   KEGG; vg:6218804; -.
DR   Proteomes; UP000001674; 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   1: Evidence at protein level;
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:0000250"
FT   CHAIN           2..650
FT                   /note="Outer capsid protein VP4"
FT                   /id="PRO_0000404188"
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        110
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        407
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   650 AA;  68988 MW;  FCB9BF49F8DFC095 CRC64;
     MGNVQTSTNV YNIDGNGNTF APSSQMASTA SPAIDLKPGV LNPTGKLWQT MGTGAPSADS
     LVLVVDNKGE YTYLSENMRE TLNKAVTDVN MWQPLFQATK SGCGPVVLAN FTTISTGYVG
     ATADDAFSNG LVSNGPFLAT MHIMELQKTI AARMRDVAIW QKHLDTAMTL MTPDVSAGDV
     TCKWRSLLEF AQDILPLDNL CRSYPNEFYT VAAQRYPAIR PGQPDTQVAL PQPHPLGEVA
     GSFNAPTSEV GSLVGAGAAL SDAISTLASK DLDLVEADTP LPVSVFTPSL APRTYRPAFI
     DPQDAAWIAQ WNGDANIRII TTYQSTDYTV QLGPGPTRVI DMNAMIDAKL TLDVSGTILP
     FQENNDLSSA IPAFVLIQTK VPLHSVTQAS DVEGITVVSA AESSAINLSV NVRGDPRFDM
     LHLHAMFERE TIAGIPYIYG IGTFLIPSIT SSSSFCNPTL MDGELTVTPL LLRETTYKGA
     VVDTVTPSEV MANQTSEEVA SALANDAVLL VSGQLERLAT VVGDVIPIAS GEDDAATSAI
     VGRLAIEATM RARHGGDTRA LPNFGQLWKR AKRAASMFAS NPALALQVGV PVLADSGILS
     ALTSGVSTAI RTGSLGKGVS DASSKLNARQ SLTLARKTFF KKVEELWPSQ