true1989-10-012024-01-24101VP7_ROTRHComparison of the amino acid sequences of the major neutralization protein of four human rotavirus serotypes.Green K.Y.Midthun K.Gorziglia M.Hoshino Y.Kapikian A.Z.Chanock R.M.Flores J.doi:10.1016/0042-6822(87)90181-41987Virology161153-159NUCLEOTIDE SEQUENCE [GENOMIC RNA]Isolate MMU-18006Characterization of homotypic and heterotypic VP7 neutralization sites of rhesus rotavirus.Mackow E.R.Shaw R.D.Matsui S.M.Vo P.T.Benfield D.A.Greenberg H.B.doi:10.1016/0042-6822(88)90595-81988Virology165511-517NUCLEOTIDE SEQUENCE [GENOMIC RNA]Purified recombinant rotavirus VP7 forms soluble, calcium-dependent trimers.Dormitzer P.R.Greenberg H.B.Harrison S.C.doi:10.1006/viro.2000.06252000Virology277420-428NUCLEOTIDE SEQUENCE [MRNA]SUBUNITCell-line-induced mutation of the rotavirus genome alters expression of an IRF3-interacting protein.Kearney K.Chen D.Taraporewala Z.F.Vende P.Hoshino Y.Tortorici M.A.Barro M.Patton J.T.doi:10.1038/sj.emboj.76004082004EMBO J.234072-4081NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]Full genome-based classification of rotaviruses reveals a common origin between human Wa-Like and porcine rotavirus strains and human DS-1-like and bovine rotavirus strains.Matthijnssens J.Ciarlet M.Heiman E.M.Arijs I.Delbeke T.McDonald S.M.Palombo E.A.Iturriza-Gomara M.Maes P.Patton J.T.Rahman M.Van Ranst M.doi:10.1128/jvi.02257-072008J. Virol.823204-3219NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]Zhao B.P.Ren Z.A.Li C.D.2011-01EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]Rotashield RRVSequence Analysis of the Tetravalent Rotavirus Vaccine (United States Patent US 7,485,415 B2 (Feb. 3, 2009); International Publication number WO 03/072716 A2 (Sept. 4, 2003)).Buonagurio D.A.Georgiu A.F.Lerch R.A.Mason B.B.Murthy S.C.Rappaport R.S.Sidhu M.S.Udem S.A.Zamb T.J.2011-07EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]Reconciliation of rotavirus temperature-sensitive mutant collections and assignment of reassortment groups D, J, and K to genome segments.Criglar J.Greenberg H.B.Estes M.K.Ramig R.F.doi:10.1128/jvi.02691-102011J. Virol.855048-5060NUCLEOTIDE SEQUENCE [GENOMIC RNA]Intracellular manipulation of disulfide bond formation in rotavirus proteins during assembly.Svensson L.Dormitzer P.R.von Bonsdorff C.-H.Maunula L.Greenberg H.B.doi:10.1128/jvi.68.8.5204-5215.19941994J. Virol.685204-5215GLYCOSYLATIONSUBUNITATP is required for correct folding and disulfide bond formation of rotavirus VP7.Mirazimi A.Svensson L.doi:10.1128/jvi.74.17.8048-8052.20002000J. Virol.748048-8052SUBUNITVP7 mediates the interaction of rotaviruses with integrin alphavbeta3 through a novel integrin-binding site.Zarate S.Romero P.Espinosa R.Arias C.F.Lopez S.doi:10.1128/jvi.78.20.10839-10847.20042004J. Virol.7810839-10847INTERACTION WITH INTEGRIN HETERODIMER ITGAV/ITGB3Multistep entry of rotavirus into cells: a Versaillesque dance.Lopez S.Arias C.F.doi:10.1016/j.tim.2004.04.0032004Trends Microbiol.12271-278REVIEWSilencing the morphogenesis of rotavirus.Lopez T.Camacho M.Zayas M.Najera R.Sanchez R.Arias C.F.Lopez S.doi:10.1128/jvi.79.1.184-192.20052005J. Virol.79184-192SUBCELLULAR LOCATIONCross-linking of rotavirus outer capsid protein VP7 by antibodies or disulfides inhibits viral entry.Aoki S.T.Trask S.D.Coulson B.S.Greenberg H.B.Dormitzer P.R.Harrison S.C.doi:10.1128/jvi.00234-112011J. Virol.8510509-10517FUNCTIONStructural correlates of rotavirus cell entry.Abdelhakim A.H.Salgado E.N.Fu X.Pasham M.Nicastro D.Kirchhausen T.Harrison S.C.doi:10.1371/journal.ppat.10043552014PLoS Pathog.10E1004355FUNCTIONThree-dimensional structure of rotavirus.Prasad B.V.Wang G.J.Clerx J.P.Chiu W.doi:10.1016/0022-2836(88)90313-01988J. Mol. Biol.199269-275STRUCTURE BY ELECTRON MICROSCOPY OF THE VIRAL PARTICLE (40 ANGSTROMS)SUBCELLULAR LOCATIONMolecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM.Chen J.Z.Settembre E.C.Aoki S.T.Zhang X.Bellamy A.R.Dormitzer P.R.Harrison S.C.Grigorieff N.doi:10.1073/pnas.09040241062009Proc. Natl. Acad. Sci. U.S.A.10610644-10648STRUCTURE BY ELECTRON MICROSCOPY OF THE VIRAL PARTICLE (3.80 ANGSTROMS) OF 58-312 IN COMPLEX WITH CALCIUM AND N-ACETYL-D-GLUCOSAMINEGLYCOSYLATION AT ASN-69DISULFIDE BONDSSUBCELLULAR LOCATIONStructure of rotavirus outer-layer protein VP7 bound with a neutralizing Fab.Aoki S.T.Settembre E.C.Trask S.D.Greenberg H.B.Harrison S.C.Dormitzer P.R.doi:10.1126/science.11704812009Science3241444-1447X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 51-326 IN COMPLEX WITH CALCIUMSUBUNITSUBCELLULAR LOCATIONAtomic model of an infectious rotavirus particle.Settembre E.C.Chen J.Z.Dormitzer P.R.Grigorieff N.Harrison S.C.doi:10.1038/emboj.2010.3222011EMBO J.30408-416STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 51-326GLYCOSYLATION AT ASN-69INTERACTION WITH THE INTERMEDIATE PROTEIN VP6INTERACTION WITH THE OUTER CAPSID PROTEIN VP5*FUNCTIONSUBCELLULAR LOCATIONVGXRRH3.40A=51-3263.80B/F/G/H/I/J/K/L/M/N/O/P/Q=58-3123.80BA/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO/BP/BQ=51-3263.40a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r=1-3264.30a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r=1-3263.30a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r=1-3261 sequenced antibodyGlycoprotein VP7, domain 1Rotavirus outer-layer protein VP7, domain 2Rota_VP7Rota_VP7_AVP7VP7_1VP7_2VP7Outer capsid glycoprotein VP7Calcium-binding protein that interacts with rotavirus cell receptors once the initial attachment by VP4 has been achieved. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion (PubMed:25211455, PubMed:21849465). This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7 (PubMed:25211455, PubMed:21849465, PubMed:21157433).Homotrimer; disulfide-linked (PubMed:11080489, PubMed:19520960, PubMed:8035518, PubMed:10933714). 2 Ca(2+) ions bound at each subunit interface in the trimer hold the trimer together (PubMed:19520960). Interacts with the intermediate capsid protein VP6 (PubMed:21157433). Interacts with the outer capsid protein VP5* (PubMed:21157433). Interacts with host integrin heterodimer ITGAV/ITGB3 (PubMed:15452204).The outer layer contains 780 copies of VP7, grouped as 260 trimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles.N-glycosylated.The N-terminus is blocked possibly by pyroglutamic acid.Some rotavirus strains are neuraminidase-sensitive and require sialic acid to attach to the cell surface. Some rotavirus strains are integrin-dependent. Some rotavirus strains depend on ganglioside for their entry into the host cell. Hsp70 also seems to be involved in the entry of some strains.In group A rotaviruses, VP7 defines the G serotype.Produced by alternative initiation at Met-30 of isoform 1.Belongs to the rotavirus VP7 family.150Outer capsid glycoprotein VP73121151326CNP motif; interaction with ITGAV/ITGB3165167LVD motif; interaction with ITGA4/ITGB1 heterodimer237239GPR motif; interaction with ITGAX/ITGB225325595177206214216228229231301N-linked (GlcNAc...) asparagine; by host6982135249191244196207In isoform 2.29C32A171N3248186879398108116122124129143146148152159160170172182198204212215227234238241243254258264273276284287292303308122018-05-232true3711204e80ca7caa9bd12199cba66fedbfb381MYGIEYTTVLTFLISLILLNYILKSLTRMMDFIIYRFLFIVVILSPLLKAQNYGINLPITGSMDTAYANSTQEETFLTSTLCLYYPTEAATEINDNSWKDTLSQLFLTKGWPTGSVYFKEYTDIASFSVDPQLYCDYNVVLMKYDATLQLDMSELADLILNEWLCNPMDITLYYYQQTDEANKWISMGSSCTIKVCPLNTQTLGIGCLTTDTATFEEVATAEKLVITDVVDGVNHKLDVTTATCTIRNCKKLGPRENVAVIQVGGSDVLDITADPTTAPQTERMMRINWKKWWQVFYTVVDYVNQIIQAMSKRSRSLNSAAFYYRI2MDFIIYRFLFIVVILSPLLKAQNYGINLPITGSMDTAYANSTQEETFLTSTLCLYYPTEAATEINDNSWKDTLSQLFLTKGWPTGSVYFKEYTDIASFSVDPQLYCDYNVVLMKYDATLQLDMSELADLILNEWLCNPMDITLYYYQQTDEANKWISMGSSCTIKVCPLNTQTLGIGCLTTDTATFEEVATAEKLVITDVVDGVNHKLDVTTATCTIRNCKKLGPRENVAVIQVGGSDVLDITADPTTAPQTERMMRINWKKWWQVFYTVVDYVNQIIQAMSKRSRSLNSAAFYYRItruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue