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 23-FEB-2022, entry version 65. 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; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; 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 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=Q98031-1; Sequence=Displayed; CC Name=2; CC IsoId=Q98031-2; Sequence=VSP_038622; 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; 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-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; 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. 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 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_0000369114" 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 METAL 95 FT /note="Calcium 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT METAL 177 FT /note="Calcium 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT METAL 206 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT METAL 214 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT METAL 216 FT /note="Calcium 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT METAL 228 FT /note="Calcium 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT METAL 229 FT /note="Calcium 2; via carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131" FT METAL 301 FT /note="Calcium 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 146 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 238 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_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 //