ID VP7_ROTB9 Reviewed; 329 AA. AC Q80IG9; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 22-FEB-2023, entry version 58. DE RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04131}; DE Flags: Precursor; OS Rotavirus A (isolate RVA/Cow/Germany/993/1983/G18P[17]) (RV-A). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A. OX NCBI_TaxID=45408; OH NCBI_TaxID=9913; Bos taurus (Bovine). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=9237354; DOI=10.1023/a:1007921418679; RA Rohwedder A., Hotop H., Minamoto N., Ito H., Nakagomi O., Brussow H.; RT "Bovine rotavirus 993/83 shows a third subtype of avian VP7 protein."; RL Virus Genes 14:147-151(1997). CC -!- FUNCTION: Calcium-binding protein that interacts with rotavirus cell CC receptors once the initial attachment by VP4 has been achieved. CC Rotavirus attachment and entry into the host cell probably involves CC multiple sequential contacts between the outer capsid proteins VP4 and CC VP7, and the cell receptors. Following entry into the host cell, low CC intracellular or intravesicular Ca(2+) concentration probably causes CC the calcium-stabilized VP7 trimers to dissociate from the virion. This CC step is probably necessary for the membrane-disrupting entry step and CC the release of VP4, which is locked onto the virion by VP7. CC {ECO:0000255|HAMAP-Rule:MF_04131}. CC -!- SUBUNIT: Homotrimer; disulfide-linked. 2 Ca(2+) ions bound at each CC subunit interface in the trimer hold the trimer together. Interacts CC with the intermediate capsid protein VP6. Interacts with the outer CC capsid protein VP5*. {ECO:0000255|HAMAP-Rule:MF_04131}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04131}. Host CC endoplasmic reticulum lumen {ECO:0000255|HAMAP-Rule:MF_04131}. Note=The CC outer layer contains 780 copies of VP7, grouped as 260 trimers. CC Immature double-layered particles assembled in the cytoplasm bud across CC the membrane of the endoplasmic reticulum, acquiring during this CC process a transient lipid membrane that is modified with the ER CC resident viral glycoproteins NSP4 and VP7; these enveloped particles CC also contain VP4. As the particles move towards the interior of the ER CC cisternae, the transient lipid membrane and the non-structural protein CC NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange CC to form the outermost virus protein layer, yielding mature infectious CC triple-layered particles. {ECO:0000255|HAMAP-Rule:MF_04131}. CC -!- PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04131}. CC -!- PTM: The N-terminus is blocked possibly by pyroglutamic acid. CC {ECO:0000255|HAMAP-Rule:MF_04131}. CC -!- MISCELLANEOUS: Some rotavirus strains are neuraminidase-sensitive and CC require sialic acid to attach to the cell surface. Some rotavirus CC strains are integrin-dependent. Some rotavirus strains depend on CC ganglioside for their entry into the host cell. Hsp70 also seems to be CC involved in the entry of some strains. {ECO:0000255|HAMAP- CC Rule:MF_04131}. CC -!- MISCELLANEOUS: In group A rotaviruses, VP7 defines the G serotype. CC {ECO:0000255|HAMAP-Rule:MF_04131}. CC -!- SIMILARITY: Belongs to the rotavirus VP7 family. {ECO:0000255|HAMAP- CC Rule:MF_04131}. 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; X98869; CAD83158.1; -; Genomic_RNA. DR SMR; Q80IG9; -. DR GO; GO:0044166; C:host cell endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0039621; C:T=13 icosahedral viral capsid; IEA:UniProtKB-UniRule. DR GO; GO:0039624; C:viral outer capsid; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.11130; Glycoprotein VP7, domain 1; 1. DR Gene3D; 2.60.120.800; Rotavirus outer-layer protein VP7, domain 2; 1. DR HAMAP; MF_04130; Rota_VP7; 1. DR HAMAP; MF_04131; Rota_VP7_A; 1. DR InterPro; IPR001963; VP7. DR InterPro; IPR042207; VP7_1. DR InterPro; IPR042210; VP7_2. DR Pfam; PF00434; VP7; 1. PE 3: Inferred from homology; KW Calcium; Capsid protein; Disulfide bond; Glycoprotein; KW Host endoplasmic reticulum; Host-virus interaction; Metal-binding; KW Outer capsid protein; Signal; T=13 icosahedral capsid protein; Virion. FT SIGNAL 1..53 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT CHAIN 54..329 FT /note="Outer capsid glycoprotein VP7" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT /id="PRO_0000369095" FT BINDING 98 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT BINDING 180 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT BINDING 209 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT BINDING 217 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT BINDING 219 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT BINDING 231 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT BINDING 232 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT BINDING 234 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT BINDING 304 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT CARBOHYD 72 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 241 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 321 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT DISULFID 85..138 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT DISULFID 168..252 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT DISULFID 194..247 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT DISULFID 199..210 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" SQ SEQUENCE 329 AA; 37178 MW; 2B203086D872C467 CRC64; MYSTECTILL IEIIFYFFAA VVVYDAIHKM ANSPIFCIAV LAVVFAVSPK CFAQNYGINV PITGSLDVAV PNKTDDQIGL TSSLCIYYPN EAEIEINDNE WKNTVAQLLL TKGWPTTSVY LNGYADLQSF SNNPQLNCDY NIVLVKYDQN AGLDMSELAE LLLYEWLCNE MDVNLYYYQQ TSEANKWIAM GSDCTIKVCP LNTQTLGIGC QTTDVATFEQ LTATEKLAII DVVDGVNHKV NYTIATCTLK NCIRLNQREN VAIIQVGGPE IIDVSEDPMI VPKMIRATRI NWKKWWQVFY TVVDYINTII QAMSKRSRSL NTSTYFLRI //