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Database: UniProt
Entry: Q2Q1E0_9REOV
LinkDB: Q2Q1E0_9REOV
Original site: Q2Q1E0_9REOV 
ID   Q2Q1E0_9REOV            Unreviewed;       529 AA.
AC   Q2Q1E0;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Outer capsid protein VP5 {ECO:0000256|ARBA:ARBA00015353};
OS   Peruvian horse sickness virus.
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Orbivirus.
OX   NCBI_TaxID=356862 {ECO:0000313|EMBL:ABB72774.1, ECO:0000313|Proteomes:UP000201659};
RN   [1] {ECO:0000313|EMBL:ABB72774.1, ECO:0000313|Proteomes:UP000201659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19766284; DOI=10.1016/j.virol.2009.08.032;
RA   Attoui H., Mendez-Lopez M.R., Rao S., Hurtado-Alendes A.,
RA   Lizaraso-Caparo F., Jaafar F.M., Samuel A.R., Belhouchet M.,
RA   Pritchard L.I., Melville L., Weir R.P., Hyatt A.D., Davis S.S., Lunt R.,
RA   Calisher C.H., Tesh R.B., Fujita R., Mertens P.P.;
RT   "Peruvian horse sickness virus and Yunnan orbivirus, isolated from
RT   vertebrates and mosquitoes in Peru and Australia.";
RL   Virology 394:298-310(2009).
CC   -!- FUNCTION: VP5 protein is one of the two proteins (with VP2) which
CC       constitute the virus particle outer capsid. Acts as a membrane
CC       permeabilization protein that mediates release of viral particles from
CC       endosomal compartments into the cytoplasm. Permeabilization activity is
CC       probably negatively regulated by VP2 and is triggered by endosomal
CC       degradation of VP2 and exposure to low pH.
CC       {ECO:0000256|ARBA:ARBA00024835}.
CC   -!- SIMILARITY: Belongs to the orbivirus VP5 family.
CC       {ECO:0000256|ARBA:ARBA00007624}.
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DR   EMBL; DQ248061; ABB72774.1; -; Genomic_RNA.
DR   RefSeq; YP_460042.1; NC_007752.1.
DR   SMR; Q2Q1E0; -.
DR   GeneID; 5076735; -.
DR   KEGG; vg:5076735; -.
DR   OrthoDB; 8954at10239; -.
DR   Proteomes; UP000201659; Genome.
DR   GO; GO:0019028; C:viral capsid; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR000145; Capsid_VP5_Orbivir.
DR   Pfam; PF00901; Orbi_VP5; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000201659}.
FT   COILED          92..179
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   529 AA;  59112 MW;  A301F05FC4E3332E CRC64;
     MGKITNTLSR LGRGFKNILT SDTTKRVVSG IGTTIAKVAE SEIGQRAIGG VVQGIAEATL
     TDSDYSSAIK KAVIGNVLQI HDEPVGPLNP TEQKLSKKLN TLEREVNHVQ LLERQSEKVE
     EKLAARIEKV KTALQKEGKI LNEEENQMEL LDTSVQSMLE IAEHENKNLA ELNDALLKES
     RARTLVENRL VEAMKQNFRT MSNVVKAEKG ALIEEALEQT IDIGGDISEH LAAEVPFIGE
     SIASGMATAR GVMQVYKLGQ LISKLTGINI EHTEVPAISP VLVETLLTEP TVNDAILQKV
     VYSKLKHVEE VKNELEHLSQ NVFNELAKKA KDDNLHLESS DTVIHHSTRS NYHVTTTRRP
     GAHIYTAPFD SDYIVIILVV SPYHQHRAVV LCVDLLNDFI MFQDVSHGGT RVHKGVRPTG
     FPSFRNAIKD FFKESARNVM STRMHSERMQ RGVGNEPIYI TSMLYPYSFL QTRRNAENIC
     RSQEIQRHIL RGPLNMQRKS ILNGLFHGVT LVTTQRTRSI QQSGKVFAH
//
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