ID VP7_ROTHU Reviewed; 326 AA. AC Q07156; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 22-FEB-2023, entry version 84. DE RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04131}; DE Flags: Precursor; OS Rotavirus A (isolate RVA/Human/India/116E/1986/G9P8[11]) (RV-A). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A. OX NCBI_TaxID=638299; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8212599; DOI=10.1006/viro.1993.1570; RA Das B.K., Gentsch J.R., Hoshino Y., Ishida S., Nakagomi O., Bhan M.K., RA Kumar R., Glass R.I.; RT "Characterization of the G serotype and genogroup of New Delhi newborn RT rotavirus strain 116E."; RL Virology 197:99-107(1993). 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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=1; CC IsoId=Q07156-1; Sequence=Displayed; CC Name=2; CC IsoId=Q07156-2; Sequence=VSP_038596; 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 -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met- CC 30 of isoform 1. {ECO:0000305}. 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; L14072; AAA03613.1; -; mRNA. DR SMR; Q07156; -. 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 2: Evidence at transcript 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_0000149607" FT REGION 165..167 FT /note="CNP motif; interaction with ITGAV/ITGB3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT REGION 237..239 FT /note="LVD motif; interaction with ITGA4/ITGB1 heterodimer" 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 69 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 145 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_038596" SQ SEQUENCE 326 AA; 37163 MW; C3A78ADFAAB0AC66 CRC64; MYGIEYTTVL TFLISIILLN YILKSVTSAM DFIIYRFLLI IVVVSPFVKT QNYGINVPIT GSMDTAYTNS SQQETFLTST LCLYYPIEAS TQIGDTEWKG TLSQLFLTKG WPTGSVYFKE YTDIASFSID PQFYCDYNVV LVKYNSTLEL DMSELADLIL NEWLCNPMDI ALYYYQQTNE ANKWISMGQS CTIKVCPLNT QTLGIGCTTT NTATFEEVAT NEKLVITDVV DGVNHKLDVT TNTCTIRNCR KLGPRENVAK LQVGGSEVLD ITADPTTTPQ TERMMQINWK KWWQVFYTVV DYINQIVQVM SKRSRSFNSA AFYYRI //