ID A0A024CFA7_9REOV Unreviewed; 775 AA. AC A0A024CFA7; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 12-AUG-2020, entry version 35. DE RecName: Full=Outer capsid protein VP4 {ECO:0000256|HAMAP-Rule:MF_04125}; DE AltName: Full=Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04125}; GN Name=VP4 {ECO:0000313|EMBL:AHZ33086.1}; GN ORFNames=L312_46656gpVP4 {ECO:0000313|EMBL:AHZ33086.1}; OS Rotavirus A. OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus. OX NCBI_TaxID=28875 {ECO:0000313|EMBL:AHZ33086.1, ECO:0000313|Proteomes:UP000155231}; RN [1] {ECO:0000313|EMBL:AHZ33086.1, ECO:0000313|Proteomes:UP000155231} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 VP4: Spike-forming protein that mediates CC virion attachment to the host epithelial cell receptors and plays a CC major role in cell penetration, determination of host range restriction CC and virulence. Rotavirus attachment and entry into the host cell CC probably involves multiple sequential contacts between the outer capsid CC proteins VP4 and VP7, and the cell receptors. It is subsequently lost, CC together with VP7, following virus entry into the host cell. Following CC entry into the host cell, low intracellular or intravesicular Ca(2+) CC concentration probably causes the calcium-stabilized VP7 trimers to CC dissociate from the virion. This step is probably necessary for the CC membrane-disrupting entry step and the release of VP4, which is locked CC onto the virion by VP7. {ECO:0000256|HAMAP-Rule:MF_04125}. CC -!- SUBCELLULAR LOCATION: [Outer capsid protein VP4]: Virion CC {ECO:0000256|HAMAP-Rule:MF_04125}. Host rough endoplasmic reticulum CC {ECO:0000256|HAMAP-Rule:MF_04125}. Host cell membrane CC {ECO:0000256|HAMAP-Rule:MF_04125}. Host endoplasmic reticulum-Golgi CC intermediate compartment {ECO:0000256|HAMAP-Rule:MF_04125}. Note=The CC outer layer contains 180 copies of VP4, grouped as 60 dimers. Immature CC double-layered particles assembled in the cytoplasm bud across the CC membrane of the endoplasmic reticulum, acquiring during this process a CC transient lipid membrane that is modified with the ER resident viral CC glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. CC As the particles move towards the interior of the ER cisternae, the CC transient lipid membrane and the non-structural protein NSP4 are lost, CC while the virus surface proteins VP4 and VP7 rearrange to form the CC outermost virus protein layer, yielding mature infectious triple- CC layered particles. {ECO:0000256|HAMAP-Rule:MF_04125}. CC -!- DOMAIN: Outer capsid protein VP4: The VP4 spike is divided into a foot, CC a stalk and body, and a head. {ECO:0000256|HAMAP-Rule:MF_04125}. CC -!- PTM: Outer capsid protein VP4: Proteolytic cleavage by trypsin results CC in activation of VP4 functions and greatly increases infectivity. The CC penetration into the host cell is dependent on trypsin treatment of CC VP4. It produces two peptides, VP5* and VP8* that remain associated CC with the virion. Cleavage of VP4 by trypsin probably occurs in vivo in CC the lumen of the intestine prior to infection of enterocytes. Trypsin CC seems to be incorporated into the three-layered viral particles but CC remains inactive as long as the viral outer capsid is intact and would CC only be activated upon the solubilization of the latter. CC {ECO:0000256|HAMAP-Rule:MF_04125}. CC -!- SIMILARITY: Belongs to the rotavirus VP4 family. {ECO:0000256|HAMAP- CC Rule:MF_04125}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04125}. 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 Proteomes; UP000155231; Genome. DR GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044168; C:host cell rough endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0044163; C:host cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0039624; C:viral outer capsid; IEA:UniProtKB-UniRule. DR GO; GO:0039665; P:permeabilization of host organelle membrane involved in viral entry into host cell; IEA:UniProtKB-UniRule. DR GO; GO:0099008; P:viral entry via permeabilization of inner membrane; IEA:UniProtKB-KW. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule. DR HAMAP; MF_04125; Rota_VP4; 1. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR042546; Rota_A_VP4. DR InterPro; IPR035330; Rota_VP4_MID. DR InterPro; IPR038017; Rota_VP4_MID_sf. DR InterPro; IPR035329; VP4_helical. DR Pfam; PF17477; Rota_VP4_MID; 1. DR Pfam; PF17478; VP4_helical; 1. DR SUPFAM; SSF111379; SSF111379; 1. DR SUPFAM; SSF49899; SSF49899; 1. PE 3: Inferred from homology; KW Capsid protein {ECO:0000256|ARBA:ARBA00022561, ECO:0000256|HAMAP- KW Rule:MF_04125}; KW Cleavage on pair of basic residues {ECO:0000256|HAMAP-Rule:MF_04125}; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP- KW Rule:MF_04125}; KW Hemagglutinin {ECO:0000256|ARBA:ARBA00022546, ECO:0000256|HAMAP- KW Rule:MF_04125}; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511, ECO:0000256|HAMAP- KW Rule:MF_04125}; Host cytoplasm {ECO:0000256|ARBA:ARBA00023200}; KW Host cytoskeleton {ECO:0000256|ARBA:ARBA00023111}; KW Host endoplasmic reticulum {ECO:0000256|ARBA:ARBA00023184, KW ECO:0000256|HAMAP-Rule:MF_04125}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870, ECO:0000256|HAMAP- KW Rule:MF_04125}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP- KW Rule:MF_04125}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04125}; KW Outer capsid protein {ECO:0000256|ARBA:ARBA00022770, ECO:0000256|HAMAP- KW Rule:MF_04125}; KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804, KW ECO:0000256|HAMAP-Rule:MF_04125}; KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595, KW ECO:0000256|HAMAP-Rule:MF_04125}; KW Viral penetration via permeabilization of host membrane KW {ECO:0000256|ARBA:ARBA00022648, ECO:0000256|HAMAP-Rule:MF_04125}; KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04125}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296, KW ECO:0000256|HAMAP-Rule:MF_04125}. FT CHAIN 1..775 FT /note="Outer capsid protein VP4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04125" FT /id="PRO_5023354187" FT DOMAIN 249..473 FT /note="Rota_VP4_MID" FT /evidence="ECO:0000259|Pfam:PF17477" FT DOMAIN 485..775 FT /note="VP4_helical" FT /evidence="ECO:0000259|Pfam:PF17478" FT COILED 483..510 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04125" 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 //