ID VP7_ROTKU Reviewed; 326 AA. AC Q98031; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 05-JUN-2019, entry version 59. DE RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04131}; DE Flags: Precursor; OS Rotavirus A (strain RVA/Human/Japan/KUN/1980/G2P1B[4]) (RV-A). OC Viruses; Riboviria; Reoviridae; Sedoreovirinae; Rotavirus; OC Rotavirus A. OX NCBI_TaxID=578829; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=8657020; DOI=10.1111/j.1348-0421.1995.tb03277.x; RA Wen L., Ushijima H., Kakizawa J., Fang Z.Y., Nishio O., Morikawa S., RA Motohiro T.; RT "Genetic variation in VP7 gene of human rotavirus serotype 2 (G2 type) RT isolated in Japan, China, and Pakistan."; RL Microbiol. Immunol. 39:911-915(1995). CC -!- FUNCTION: Calcium-binding protein that interacts with rotavirus CC cell receptors once the initial attachment by VP4 has been CC achieved. Rotavirus attachment and entry into the host cell CC probably involves multiple sequential contacts between the outer CC capsid proteins VP4 and VP7, and the cell receptors. Following CC entry into the host cell, low intracellular or intravesicular CC Ca(2+) concentration probably causes the calcium-stabilized VP7 CC trimers to dissociate from the virion. This step is probably CC necessary for the membrane-disrupting entry step and the release CC 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. CC Interacts with the intermediate capsid protein VP6. Interacts with CC the outer capsid protein VP5*. {ECO:0000255|HAMAP-Rule:MF_04131}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04131}. CC Host endoplasmic reticulum lumen {ECO:0000255|HAMAP- CC Rule:MF_04131}. Note=The outer layer contains 780 copies of VP7, CC grouped as 260 trimers. Immature double-layered particles CC assembled in the cytoplasm bud across the membrane of the CC endoplasmic reticulum, acquiring during this process a transient CC lipid membrane that is modified with the ER resident viral CC glycoproteins NSP4 and VP7; these enveloped particles also contain CC VP4. As the particles move towards the interior of the ER CC cisternae, the transient lipid membrane and the non-structural CC protein NSP4 are lost, while the virus surface proteins VP4 and CC VP7 rearrange to form the outermost virus protein layer, yielding CC mature infectious triple-layered particles. {ECO:0000255|HAMAP- CC Rule:MF_04131}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=1; CC IsoId=Q98031-1; Sequence=Displayed; CC Name=2; CC IsoId=Q98031-2; Sequence=VSP_038622; CC Note=Produced by alternative initiation at Met-30 of isoform 1. CC No experimental confirmation available.; 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 CC and require sialic acid to attach to the cell surface. Some CC rotavirus strains are integrin-dependent. Some rotavirus strains CC depend on ganglioside for their entry into the host cell. Hsp70 CC also seems to be involved in the entry of some strains. CC {ECO:0000255|HAMAP-Rule:MF_04131}. CC -!- MISCELLANEOUS: In group A rotaviruses, VP7 defines the G serotype. CC {ECO:0000255|HAMAP-Rule:MF_04131}. CC -!- SIMILARITY: Belongs to the rotavirus VP7 family. CC {ECO:0000255|HAMAP-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; D50124; BAA08809.1; -; Genomic_RNA. DR SMR; Q98031; -. 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-KW. DR GO; GO:0039624; C:viral outer capsid; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.800; -; 1. DR Gene3D; 3.40.50.11130; -; 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. DR ProDom; PD000191; VP7; 1. PE 3: Inferred from homology; 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 {ECO:0000255|HAMAP-Rule:MF_04131}. FT CHAIN 51 326 Outer capsid glycoprotein VP7. FT {ECO:0000255|HAMAP-Rule:MF_04131}. FT /FTId=PRO_0000369114. FT REGION 51 78 Disorded; interaction with the FT intermediate capsid protein VP6. FT {ECO:0000255|HAMAP-Rule:MF_04131}. FT REGION 165 167 CNP motif; interaction with ITGAV/ITGB3. FT {ECO:0000255|HAMAP-Rule:MF_04131}. FT REGION 253 255 GPR motif; interaction with ITGAX/ITGB2. FT {ECO:0000255|HAMAP-Rule:MF_04131}. FT REGION 312 326 Disorded. {ECO:0000255|HAMAP- FT Rule:MF_04131}. FT METAL 95 95 Calcium 1. {ECO:0000255|HAMAP- FT Rule:MF_04131}. FT METAL 177 177 Calcium 2. {ECO:0000255|HAMAP- FT Rule:MF_04131}. FT METAL 206 206 Calcium 1; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_04131}. FT METAL 214 214 Calcium 1; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_04131}. FT METAL 216 216 Calcium 1. {ECO:0000255|HAMAP- FT Rule:MF_04131}. FT METAL 228 228 Calcium 2. {ECO:0000255|HAMAP- FT Rule:MF_04131}. FT METAL 229 229 Calcium 2; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_04131}. FT METAL 301 301 Calcium 2. {ECO:0000255|HAMAP- FT Rule:MF_04131}. FT CARBOHYD 69 69 N-linked (GlcNAc...) asparagine; by host. FT {ECO:0000255}. FT CARBOHYD 146 146 N-linked (GlcNAc...) asparagine; by host. FT {ECO:0000255}. FT CARBOHYD 238 238 N-linked (GlcNAc...) asparagine; by host. FT {ECO:0000255}. FT DISULFID 82 135 {ECO:0000255|HAMAP-Rule:MF_04131}. FT DISULFID 165 249 {ECO:0000255|HAMAP-Rule:MF_04131}. FT DISULFID 191 244 {ECO:0000255|HAMAP-Rule:MF_04131}. FT DISULFID 196 207 {ECO:0000255|HAMAP-Rule:MF_04131}. FT VAR_SEQ 1 29 Missing (in isoform 2). {ECO:0000305}. FT /FTId=VSP_038622. SQ SEQUENCE 326 AA; 37101 MW; 706B7C20BD7F2BD6 CRC64; MYGIGNTTIL TILISIILLN YILKTITNTM DYIIFRFLLL IALISPFVRT PNYGMYLPIT GSLDAVYTNS TSGESFLTST LCLYYPTEAK NEISDDEWEN TLSQLFLTKG WPTGSVYFKD YNDITTFSMN PQLYCDYNVV LMRYDNTSEL DASELADLIL NEWLCNPMDI SLHYYQQSSE SNKWISMGTD CTVKVCPLNT QTLGIGCKTT DVNTFEIVAS SEKLVITDVV NGVNHKINIS MSTCTIRNCN KLGPRENVAI IQVGGPNALD ITADPTTVPQ VQRIMRINWK KWWQVFYTVV DYINQIIQVM SKRSRSLDTA AFYYRI //