ID VP7_ROTGI Reviewed; 246 AA. AC P30889; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 08-NOV-2023, entry version 77. DE RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04130}; DE Flags: Precursor; OS Rotavirus B (isolate RVB/Rat/United States/IDIR/1984/G1P[X]) (RV-B) OS (Rotavirus B (isolate infectious diarrhea of infant rats)). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus B. OX NCBI_TaxID=28877; OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=10116; Rattus norvegicus (Rat). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=1658208; DOI=10.1099/0022-1317-72-11-2801; RA Petric M., Mayur K., Vonderfecht S., Eiden J.J.; RT "Comparison of group B rotavirus genes 9 and 11."; RL J. Gen. Virol. 72:2801-2804(1991). 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_04130}. 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_04130}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04130}. Host CC endoplasmic reticulum lumen {ECO:0000255|HAMAP-Rule:MF_04130}. 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_04130}. CC -!- SIMILARITY: Belongs to the rotavirus VP7 family. {ECO:0000255|HAMAP- CC Rule:MF_04130}. 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; D00911; BAA00757.1; -; Genomic_RNA. DR PIR; JQ1311; JQ1311. DR SMR; P30889; -. DR GO; GO:0044166; C:host cell endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:InterPro. 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 HAMAP; MF_04130; Rota_VP7; 1. DR InterPro; IPR008818; Rotavirus_VP7. DR InterPro; IPR001963; VP7. DR Pfam; PF05868; Rotavirus_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..16 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04130" FT CHAIN 17..246 FT /note="Outer capsid glycoprotein VP7" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04130" FT /id="PRO_0000041132" SQ SEQUENCE 246 AA; 28319 MW; BF28CC5BF9A169A7 CRC64; MTTMLLLLVV AALANGQLTI LPHEESQICF LQPDNPGFDF DGNFTNIFRD YASVKISSFT YKAQDADIVE ILNVDRDRSC TILAIYIADS TLDFNTFLQS ENECVKYAAS KKHYIKLPRD REYFALAKNL SFCPLNDDLI GIYCDTQLET TYFSVARSSN YDVTDIPEFT ELGYVFHSND HFYICERKSE GNWIDYQLFY QNDAPLGTVS QRVNWGNVWS NVKTVAQMVY KILDIFFGKR NIEPRA //