ID   A0A024CFA7_9REOV        Unreviewed;       775 AA.
AC   A0A024CFA7;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   11-MAY-2016, entry version 12.
DE   RecName: Full=Outer capsid protein VP4 {ECO:0000256|RuleBase:RU004344, ECO:0000256|SAAS:SAAS00136896};
GN   Name=VP4 {ECO:0000313|EMBL:AHZ33086.1};
GN   ORFNames=L312_46656gpVP4 {ECO:0000313|EMBL:AHZ33086.1};
OS   Rotavirus A.
OC   Viruses; dsRNA viruses; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=28875 {ECO:0000313|EMBL:AHZ33086.1};
RN   [1] {ECO:0000313|EMBL:AHZ33086.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RVA/Human-wt/ZAF/MRC-DPRU1052/2008/G1P[8]
RC   {ECO:0000313|EMBL:AHZ33086.1};
RA   Wentworth D.E., Halpin R.A., Stucker K.M., Akopov A., Fedorova N.,
RA   Tsitrin T., Puri V., Stockwell T., Amedeo P., Bishop B., Gupta N.,
RA   Hoover J., Katzel D., Schobel S., Shrivastava S., Nyaga M.M.,
RA   Magagula N.B., Peenze I., Seheri M.L., Mphahlele J., Steele A.D.,
RA   Mwenda M.J.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Outer capsid protein VP5*: forms the spike "foot" and
CC       "body". Acts as a membrane permeabilization protein that mediates
CC       release of viral particles from endosomal compartments into the
CC       cytoplasm. In integrin-dependent strains, VP5* targets the
CC       integrin heterodimer ITGA2/ITGB1 for cell attachment.
CC       {ECO:0000256|SAAS:SAAS00136874}.
CC   -!- FUNCTION: VP8* forms the head of the spikes. It is the viral
CC       hemagglutinin and an important target of neutralizing antibodies.
CC       In sialic acid-dependent strains, VP8* binds to host cell sialic
CC       acid, most probably a ganglioside, providing the initial contact.
CC       {ECO:0000256|SAAS:SAAS00136880}.
CC   -!- SUBUNIT: VP4 is a homotrimer (Potential). VP4 adopts a dimeric
CC       appearance above the capsid surface, while forming a trimeric base
CC       anchored inside the capsid layer. Only hints of the third molecule
CC       are observed above the capsid surface. It probably performs a
CC       series of molecular rearrangements during viral entry. Prior to
CC       trypsin cleavage, it is flexible. The priming trypsin cleavage
CC       triggers its rearrangement into rigid spikes with approximate two-
CC       fold symmetry of their protruding parts. After an unknown second
CC       triggering event, cleaved VP4 may undergo another rearrangement,
CC       in which two VP5* subunits fold back on themselves and join a
CC       third subunit to form a tightly associated trimer, shaped like a
CC       folded umbrella. VP5* is a homotrimer (Potential). The trimer is
CC       coiled-coil stabilized by its C-terminus, however, its N-terminus,
CC       known as antigen domain or "body", seems to be flexible allowing
CC       it to self-associate either as a dimer or a trimer. The two- to
CC       three-fold reorganization and fold-back of VP5* may be linked to
CC       membrane penetration, by exposing its hydrophobic region.
CC       {ECO:0000256|SAAS:SAAS00594438}.
CC   -!- SUBCELLULAR LOCATION: Host rough endoplasmic reticulum
CC       {ECO:0000256|SAAS:SAAS00594431}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|RuleBase:RU004344,
CC       ECO:0000256|SAAS:SAAS00594454}.
CC   -!- SIMILARITY: Belongs to the rotavirus VP4 family.
CC       {ECO:0000256|RuleBase:RU004344, ECO:0000256|SAAS:SAAS00594432}.
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DR   EMBL; KJ752276; AHZ33086.1; -; Genomic_RNA.
DR   GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0039624; C:viral outer capsid; IEA:UniProtKB-KW.
DR   GO; GO:0039665; P:permeabilization of host organelle membrane involved in viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom.
DR   InterPro; IPR000416; Haemagglutinin_VP4.
DR   Pfam; PF00426; VP4_haemagglut; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
PE   3: Inferred from homology;
KW   Capsid protein {ECO:0000256|RuleBase:RU004344,
KW   ECO:0000256|SAAS:SAAS00487957};
KW   Coiled coil {ECO:0000256|SAAS:SAAS00487929, ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00487880};
KW   Hemagglutinin {ECO:0000256|SAAS:SAAS00487857};
KW   Host endoplasmic reticulum {ECO:0000256|SAAS:SAAS00487838};
KW   Host-virus interaction {ECO:0000256|SAAS:SAAS00487874};
KW   Outer capsid protein {ECO:0000256|SAAS:SAAS00487958};
KW   Viral attachment to host cell {ECO:0000256|SAAS:SAAS00487870};
KW   Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS00487847};
KW   Viral penetration via permeabilization of host membrane
KW   {ECO:0000256|SAAS:SAAS00487884};
KW   Virion {ECO:0000256|RuleBase:RU004344, ECO:0000256|SAAS:SAAS00487950};
KW   Virus entry into host cell {ECO:0000256|SAAS:SAAS00487888}.
FT   COILED      483    510       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   775 AA;  87409 MW;  DCB7BF9CC9639466 CRC64;
     MASLIYRQLL TNSYSVDLYD EIKQIGSEKT QNVTVNPGPF AQTRYAPVNW GHGEINDSTT
     VEPILDGPYQ PTTFTPPTDY WILINSNTNG VVYESTNNSD FWTAVIAVEP HVNPVDRQYN
     VFGENKQFNV RNDSDKWKFL EMFRGSSQND FYNRRTLTSD TRLVGILKYG GRIWTFHGET
     PRATTDSSST ANLNGISITI HSEFYIIPRS QESKCNEYIN NGLPPIQNTR NVVPLSLSSR
     SIQYTRAQVN EDITISKTSL WKEMQYNRDI IIRFKFGNSI IKLGGLGYKW SEISYKAANY
     QYNYLRDGEQ VTAHTTCSVN GVNNFSYNGG SLPTDFSISR YEVIKENSYV YVDYWDDSKA
     FRNMVYVRSL AANLNSVKCT GGSYDFSIPV GAWPVMNGGA VSLHFAGVTL STQFTDFVSL
     NSLRFRFSLT VDEPSFSILR TRTVNLYGLP AANPNNGNEY YEISGRFSLI SLVPTNDDYQ
     TPIMNSVTVR QDLERQLTDL REEFNSLSQE IAMSQLIDLA LLPLDMFSMF SGIKSTIDLT
     KSMATSVMKK FRKSKLATSV SEMTNSLSDA ASSASRSVSV RSNVSAFSNW TNVSNDVSNV
     TNSVNDISTQ TSTISKNLRL KEMITQTEGM SFDDISAAVL KTKIDMSTQI GKNTLPDIVT
     EASEKFIPKR SYRILKDDEV MEINTEGKFF AYKIDTLNEV PFDVNKFAEL VTNSPVISAI
     IDFKTLKNLN DNYGITRIEA LNLIKSNPNV LRNFINQNNP IIRNRIEQLI LQCKL
//