ID VP7_ROTRH Reviewed; 326 AA. AC P12476; C3RX25; E7EDR5; P11855; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-MAY-2018, sequence version 2. DT 24-JAN-2024, entry version 101. DE RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04131}; DE Flags: Precursor; OS Rotavirus A (strain RVA/Monkey/United States/RRV/1975/G3P5B[3]) (RV-A). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A. OX NCBI_TaxID=444185; OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate MMU-18006; RX PubMed=2823458; DOI=10.1016/0042-6822(87)90181-4; RA Green K.Y., Midthun K., Gorziglia M., Hoshino Y., Kapikian A.Z., RA Chanock R.M., Flores J.; RT "Comparison of the amino acid sequences of the major neutralization protein RT of four human rotavirus serotypes."; RL Virology 161:153-159(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=2457279; DOI=10.1016/0042-6822(88)90595-8; RA Mackow E.R., Shaw R.D., Matsui S.M., Vo P.T., Benfield D.A., RA Greenberg H.B.; RT "Characterization of homotypic and heterotypic VP7 neutralization sites of RT rhesus rotavirus."; RL Virology 165:511-517(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT. RX PubMed=11080489; DOI=10.1006/viro.2000.0625; RA Dormitzer P.R., Greenberg H.B., Harrison S.C.; RT "Purified recombinant rotavirus VP7 forms soluble, calcium-dependent RT trimers."; RL Virology 277:420-428(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372078; DOI=10.1038/sj.emboj.7600408; RA Kearney K., Chen D., Taraporewala Z.F., Vende P., Hoshino Y., RA Tortorici M.A., Barro M., Patton J.T.; RT "Cell-line-induced mutation of the rotavirus genome alters expression of an RT IRF3-interacting protein."; RL EMBO J. 23:4072-4081(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18216098; DOI=10.1128/jvi.02257-07; RA Matthijnssens J., Ciarlet M., Heiman E.M., Arijs I., Delbeke T., RA McDonald S.M., Palombo E.A., Iturriza-Gomara M., Maes P., Patton J.T., RA Rahman M., Van Ranst M.; RT "Full genome-based classification of rotaviruses reveals a common origin RT between human Wa-Like and porcine rotavirus strains and human DS-1-like and RT bovine rotavirus strains."; RL J. Virol. 82:3204-3219(2008). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rotashield RRV; RA Zhao B.P., Ren Z.A., Li C.D.; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rotashield RRV; RA Buonagurio D.A., Georgiu A.F., Lerch R.A., Mason B.B., Murthy S.C., RA Rappaport R.S., Sidhu M.S., Udem S.A., Zamb T.J.; RT "Sequence Analysis of the Tetravalent Rotavirus Vaccine (United States RT Patent US 7,485,415 B2 (Feb. 3, 2009); International Publication number WO RT 03/072716 A2 (Sept. 4, 2003))."; RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=21367894; DOI=10.1128/jvi.02691-10; RA Criglar J., Greenberg H.B., Estes M.K., Ramig R.F.; RT "Reconciliation of rotavirus temperature-sensitive mutant collections and RT assignment of reassortment groups D, J, and K to genome segments."; RL J. Virol. 85:5048-5060(2011). RN [9] RP GLYCOSYLATION, AND SUBUNIT. RX PubMed=8035518; DOI=10.1128/jvi.68.8.5204-5215.1994; RA Svensson L., Dormitzer P.R., von Bonsdorff C.-H., Maunula L., RA Greenberg H.B.; RT "Intracellular manipulation of disulfide bond formation in rotavirus RT proteins during assembly."; RL J. Virol. 68:5204-5215(1994). RN [10] RP SUBUNIT. RX PubMed=10933714; DOI=10.1128/jvi.74.17.8048-8052.2000; RA Mirazimi A., Svensson L.; RT "ATP is required for correct folding and disulfide bond formation of RT rotavirus VP7."; RL J. Virol. 74:8048-8052(2000). RN [11] RP INTERACTION WITH INTEGRIN HETERODIMER ITGAV/ITGB3. RX PubMed=15452204; DOI=10.1128/jvi.78.20.10839-10847.2004; RA Zarate S., Romero P., Espinosa R., Arias C.F., Lopez S.; RT "VP7 mediates the interaction of rotaviruses with integrin alphavbeta3 RT through a novel integrin-binding site."; RL J. Virol. 78:10839-10847(2004). RN [12] 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). RN [13] RP SUBCELLULAR LOCATION. RX PubMed=15596814; DOI=10.1128/jvi.79.1.184-192.2005; RA Lopez T., Camacho M., Zayas M., Najera R., Sanchez R., Arias C.F., RA Lopez S.; RT "Silencing the morphogenesis of rotavirus."; RL J. Virol. 79:184-192(2005). RN [14] RP FUNCTION. RX PubMed=21849465; DOI=10.1128/jvi.00234-11; RA Aoki S.T., Trask S.D., Coulson B.S., Greenberg H.B., Dormitzer P.R., RA Harrison S.C.; RT "Cross-linking of rotavirus outer capsid protein VP7 by antibodies or RT disulfides inhibits viral entry."; RL J. Virol. 85:10509-10517(2011). RN [15] RP FUNCTION. RX PubMed=25211455; DOI=10.1371/journal.ppat.1004355; RA Abdelhakim A.H., Salgado E.N., Fu X., Pasham M., Nicastro D., RA Kirchhausen T., Harrison S.C.; RT "Structural correlates of rotavirus cell entry."; RL PLoS Pathog. 10:E1004355-E1004355(2014). RN [16] RP STRUCTURE BY ELECTRON MICROSCOPY OF THE VIRAL PARTICLE (40 ANGSTROMS), AND RP SUBCELLULAR LOCATION. RX PubMed=2832610; DOI=10.1016/0022-2836(88)90313-0; RA Prasad B.V., Wang G.J., Clerx J.P., Chiu W.; RT "Three-dimensional structure of rotavirus."; RL J. Mol. Biol. 199:269-275(1988). RN [17] RP STRUCTURE BY ELECTRON MICROSCOPY OF THE VIRAL PARTICLE (3.80 ANGSTROMS) OF RP 58-312 IN COMPLEX WITH CALCIUM AND N-ACETYL-D-GLUCOSAMINE, GLYCOSYLATION AT RP ASN-69, DISULFIDE BONDS, AND SUBCELLULAR LOCATION. RX PubMed=19487668; DOI=10.1073/pnas.0904024106; RA Chen J.Z., Settembre E.C., Aoki S.T., Zhang X., Bellamy A.R., RA Dormitzer P.R., Harrison S.C., Grigorieff N.; RT "Molecular interactions in rotavirus assembly and uncoating seen by high- RT resolution cryo-EM."; RL Proc. Natl. Acad. Sci. U.S.A. 106:10644-10648(2009). RN [18] {ECO:0007744|PDB:3FMG} RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 51-326 IN COMPLEX WITH CALCIUM, RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=19520960; DOI=10.1126/science.1170481; RA Aoki S.T., Settembre E.C., Trask S.D., Greenberg H.B., Harrison S.C., RA Dormitzer P.R.; RT "Structure of rotavirus outer-layer protein VP7 bound with a neutralizing RT Fab."; RL Science 324:1444-1447(2009). RN [19] RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 51-326, GLYCOSYLATION RP AT ASN-69, INTERACTION WITH THE INTERMEDIATE PROTEIN VP6, INTERACTION WITH RP THE OUTER CAPSID PROTEIN VP5*, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21157433; DOI=10.1038/emboj.2010.322; RA Settembre E.C., Chen J.Z., Dormitzer P.R., Grigorieff N., Harrison S.C.; RT "Atomic model of an infectious rotavirus particle."; RL EMBO J. 30:408-416(2011). 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 CC (PubMed:25211455, PubMed:21849465). This step is probably necessary for CC the membrane-disrupting entry step and the release of VP4, which is CC locked onto the virion by VP7 (PubMed:25211455, PubMed:21849465, CC PubMed:21157433). {ECO:0000255|HAMAP-Rule:MF_04131, CC ECO:0000269|PubMed:21157433, ECO:0000269|PubMed:21849465, CC ECO:0000269|PubMed:25211455, ECO:0000303|PubMed:15165605}. CC -!- SUBUNIT: Homotrimer; disulfide-linked (PubMed:11080489, CC PubMed:19520960, PubMed:8035518, PubMed:10933714). 2 Ca(2+) ions bound CC at each subunit interface in the trimer hold the trimer together CC (PubMed:19520960). Interacts with the intermediate capsid protein VP6 CC (PubMed:21157433). Interacts with the outer capsid protein VP5* CC (PubMed:21157433). Interacts with host integrin heterodimer ITGAV/ITGB3 CC (PubMed:15452204). {ECO:0000255|HAMAP-Rule:MF_04131, CC ECO:0000269|PubMed:10933714, ECO:0000269|PubMed:11080489, CC ECO:0000269|PubMed:15452204, ECO:0000269|PubMed:19520960, CC ECO:0000269|PubMed:21157433, ECO:0000269|PubMed:8035518}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04131, CC ECO:0000269|PubMed:19487668, ECO:0000269|PubMed:19520960, CC ECO:0000269|PubMed:21157433, ECO:0000269|PubMed:2832610}. 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 ECO:0000269|PubMed:15596814, ECO:0000269|PubMed:21157433, CC ECO:0000269|PubMed:2832610}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=1; CC IsoId=P12476-1; Sequence=Displayed; CC Name=2; CC IsoId=P12476-2; Sequence=VSP_038635; CC -!- PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04131, CC ECO:0000269|PubMed:19487668, ECO:0000269|PubMed:21157433, CC ECO:0000269|PubMed:8035518}. 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; M21650; AAA47346.1; -; Genomic_RNA. DR EMBL; AF295303; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; EU636932; ACC94320.1; -; Genomic_RNA. DR EMBL; HQ846851; AEK32834.1; -; Genomic_RNA. DR EMBL; HQ665466; ADU24500.1; -; Genomic_RNA. DR PIR; A29247; VGXRRH. DR PDB; 3FMG; X-ray; 3.40 A; A=51-326. DR PDB; 3GZT; EM; 3.80 A; B/F/G/H/I/J/K/L/M/N/O/P/Q=58-312. DR PDB; 4V7Q; EM; 3.80 A; BA/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO/BP/BQ=51-326. DR PDB; 6WXE; EM; 3.40 A; a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r=1-326. DR PDB; 6WXF; EM; 4.30 A; a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r=1-326. DR PDB; 6WXG; EM; 3.30 A; a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r=1-326. DR PDBsum; 3FMG; -. DR PDBsum; 3GZT; -. DR PDBsum; 4V7Q; -. DR PDBsum; 6WXE; -. DR PDBsum; 6WXF; -. DR PDBsum; 6WXG; -. DR EMDB; EMD-21955; -. DR EMDB; EMD-21956; -. DR EMDB; EMD-21957; -. DR SMR; P12476; -. DR iPTMnet; P12476; -. DR ABCD; P12476; 1 sequenced antibody. DR EvolutionaryTrace; P12476; -. DR Proteomes; UP000123891; Genome. DR Proteomes; UP000174556; Genome. DR GO; GO:0044166; C:host cell endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0039621; C:T=13 icosahedral viral capsid; IDA:UniProtKB. DR GO; GO:0039624; C:viral outer capsid; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:UniProtKB. 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 3D-structure; Alternative initiation; Calcium; Capsid protein; KW Disulfide bond; Glycoprotein; Host endoplasmic reticulum; KW Host-virus interaction; 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_0000149620" FT REGION 165..167 FT /note="CNP motif; interaction with ITGAV/ITGB3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131, FT ECO:0000269|PubMed:15452204" 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 ECO:0000269|PubMed:19520960" 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 ECO:0000269|PubMed:19520960" 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 ECO:0000269|PubMed:19520960" 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 ECO:0000269|PubMed:19487668, ECO:0000269|PubMed:19520960" 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 ECO:0000269|PubMed:19487668, ECO:0000269|PubMed:19520960" 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 ECO:0000269|PubMed:19520960" 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 ECO:0000269|PubMed:19520960" 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 ECO:0000269|PubMed:19487668, ECO:0000269|PubMed:19520960" 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 ECO:0000269|PubMed:19520960" FT CARBOHYD 69 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000269|PubMed:19487668, FT ECO:0000269|PubMed:21157433" FT DISULFID 82..135 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131, FT ECO:0000269|PubMed:19487668" FT DISULFID 165..249 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131, FT ECO:0000269|PubMed:19487668" FT DISULFID 191..244 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131, FT ECO:0000269|PubMed:19487668" FT DISULFID 196..207 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131, FT ECO:0000269|PubMed:19487668" FT VAR_SEQ 1..29 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_038635" FT VARIANT 32 FT /note="F -> C" FT /evidence="ECO:0000305" FT VARIANT 171 FT /note="T -> A" FT /evidence="ECO:0000305" FT VARIANT 324 FT /note="Y -> N" FT /evidence="ECO:0000305" FT STRAND 81..86 FT /evidence="ECO:0007829|PDB:3FMG" FT HELIX 87..93 FT /evidence="ECO:0007829|PDB:3FMG" FT HELIX 98..108 FT /evidence="ECO:0007829|PDB:3FMG" FT STRAND 116..122 FT /evidence="ECO:0007829|PDB:3FMG" FT HELIX 124..129 FT /evidence="ECO:0007829|PDB:3FMG" FT STRAND 135..143 FT /evidence="ECO:0007829|PDB:3FMG" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:3FMG" FT HELIX 152..159 FT /evidence="ECO:0007829|PDB:3FMG" FT STRAND 160..167 FT /evidence="ECO:0007829|PDB:3FMG" FT TURN 170..172 FT /evidence="ECO:0007829|PDB:3FMG" FT STRAND 182..198 FT /evidence="ECO:0007829|PDB:3FMG" FT STRAND 204..207 FT /evidence="ECO:0007829|PDB:3FMG" FT HELIX 212..214 FT /evidence="ECO:0007829|PDB:3FMG" FT STRAND 215..227 FT /evidence="ECO:0007829|PDB:3FMG" FT STRAND 234..238 FT /evidence="ECO:0007829|PDB:3FMG" FT TURN 241..243 FT /evidence="ECO:0007829|PDB:3FMG" FT STRAND 244..254 FT /evidence="ECO:0007829|PDB:3FMG" FT STRAND 258..264 FT /evidence="ECO:0007829|PDB:3FMG" FT STRAND 273..276 FT /evidence="ECO:0007829|PDB:3FMG" FT STRAND 284..287 FT /evidence="ECO:0007829|PDB:3FMG" FT HELIX 292..301 FT /evidence="ECO:0007829|PDB:3FMG" FT HELIX 303..308 FT /evidence="ECO:0007829|PDB:3FMG" SQ SEQUENCE 326 AA; 37112 MW; F84A49C30945AAAF CRC64; MYGIEYTTVL TFLISLILLN YILKSLTRMM DFIIYRFLFI VVILSPLLKA QNYGINLPIT GSMDTAYANS TQEETFLTST LCLYYPTEAA TEINDNSWKD TLSQLFLTKG WPTGSVYFKE YTDIASFSVD PQLYCDYNVV LMKYDATLQL DMSELADLIL NEWLCNPMDI TLYYYQQTDE ANKWISMGSS CTIKVCPLNT QTLGIGCLTT DTATFEEVAT AEKLVITDVV DGVNHKLDVT TATCTIRNCK KLGPRENVAV IQVGGSDVLD ITADPTTAPQ TERMMRINWK KWWQVFYTVV DYVNQIIQAM SKRSRSLNSA AFYYRI //