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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //