ID VP7_ROTRF Reviewed; 326 AA. AC Q86515; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 78. DE RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04131}; DE Flags: Precursor; OS Rotavirus A (strain RVA/Cow/France/RF/1975/G6P6[1]) (RV-A). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A. OX NCBI_TaxID=10933; OH NCBI_TaxID=9913; Bos taurus (Bovine). RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Cohen J.; RT "Sequence of the gene encoding the outer glycoprotein of the bovine RT rotavirus (RF strain) and comparison with homologous genes from four RT bovine, simian and human rotaviruses."; RL Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases. RN [2] RP INTERACTION WITH THE INTERMEDIATE CAPSID PROTEIN VP6, AND SUBCELLULAR RP LOCATION. RX PubMed=11285213; DOI=10.1093/emboj/20.7.1485; RA Mathieu M., Petitpas I., Navaza J., Lepault J., Kohli E., Pothier P., RA Prasad B.V.V., Cohen J., Rey F.A.; RT "Atomic structure of the major capsid protein of rotavirus: implications RT for the architecture of the virion."; RL EMBO J. 20:1485-1497(2001). RN [3] RP REVIEW. RX PubMed=15165605; DOI=10.1016/j.tim.2004.04.003; RA Lopez S., Arias C.F.; RT "Multistep entry of rotavirus into cells: a Versaillesque dance."; RL Trends Microbiol. 12:271-278(2004). 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 (By CC similarity). Interacts with the intermediate capsid protein VP6 CC (PubMed:11285213). Interacts with the outer capsid protein VP5* (By CC similarity). {ECO:0000255|HAMAP-Rule:MF_04131, CC ECO:0000269|PubMed:11285213}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04131, CC ECO:0000269|PubMed:11285213}. Host endoplasmic reticulum lumen CC {ECO:0000255|HAMAP-Rule:MF_04131}. Note=The outer layer contains 780 CC copies of VP7, grouped as 260 trimers. Immature double-layered CC particles assembled in the cytoplasm bud across the membrane of the CC endoplasmic reticulum, acquiring during this process a transient lipid CC membrane that is modified with the ER resident viral glycoproteins NSP4 CC and VP7; these enveloped particles also contain VP4. As the particles CC move towards the interior of the ER cisternae, the transient lipid CC membrane and the non-structural protein NSP4 are lost, while the virus CC surface proteins VP4 and VP7 rearrange to form the outermost virus CC protein layer, yielding mature infectious triple-layered particles. CC {ECO:0000255|HAMAP-Rule:MF_04131, ECO:0000269|PubMed:11285213}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=1; CC IsoId=Q86515-1; Sequence=Displayed; CC Name=2; CC IsoId=Q86515-2; Sequence=VSP_038611; 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, ECO:0000269|PubMed:15165605}. CC -!- MISCELLANEOUS: In group A rotaviruses, VP7 defines the G serotype. CC {ECO:0000255|HAMAP-Rule:MF_04131}. CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met- CC 30 of isoform 1. {ECO:0000250|UniProtKB:P03533}. 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; X65940; CAA46743.1; -; mRNA. DR PIR; S25546; S25546. DR SMR; Q86515; -. DR Proteomes; UP000007179; Genome. 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 1: Evidence at protein level; KW Alternative initiation; Calcium; Capsid protein; Disulfide bond; KW Glycoprotein; Host endoplasmic reticulum; Host-virus interaction; KW Metal-binding; Outer capsid protein; Signal; KW T=13 icosahedral capsid protein; Virion. FT SIGNAL 1..50 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT CHAIN 51..326 FT /note="Outer capsid glycoprotein VP7" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT /id="PRO_0000369108" FT REGION 165..167 FT /note="CNP motif; interaction with ITGAV/ITGB3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT REGION 253..255 FT /note="GPR motif; interaction with ITGAX/ITGB2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT BINDING 95 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT BINDING 177 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT BINDING 206 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT BINDING 214 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT BINDING 216 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT BINDING 228 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT BINDING 229 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" 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 301 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT CARBOHYD 238 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 318 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT DISULFID 82..135 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT DISULFID 165..249 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT DISULFID 191..244 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT DISULFID 196..207 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT VAR_SEQ 1..29 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_038611" SQ SEQUENCE 326 AA; 37085 MW; 66C66C7156889B9D CRC64; MYGIEYTTIL IFLTSITLLN YMLKSITRIM DYIIYRFLLI VVILATIIKA QNYGVNLPIT GSMDTAYADS TQSEPFLTST LCLYYPVEAS NEIADTEWKD TLSQLFLTKG WPTGSVYLKE YADIAAFSVE PQLYCDYNLV LMKYDSTQEL DMSELADLIL NEWLCNPMDI TLYYYQQTDE ANKWISTGSS CTVKVCPLNT QTLGIGCLIT NPDTFETVAT TEKLVITDVV DGVNHKLNVT TATCTIRNCK KLGPRENVAV IQVGGANILD ITADPTTTPQ TERMMRINWK KWWQVFYTVV DYVNQIIQTM SKRSRSLNSS AFYYRV //