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 13-OCT-2009, entry version 37. DE RecName: Full=Outer capsid glycoprotein VP7; DE Flags: Precursor; OS Rotavirus A (strain Human/Japan/KUN/1980 OS G2-P1B[4]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-E2-H2) (RV-A). OC Viruses; dsRNA viruses; Reoviridae; Rotavirus; Rotavirus A. OX NCBI_TaxID=578829; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX MEDLINE=96245552; PubMed=8657020; 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: Outer capsid protein involved in attachment and possibly CC entry into the host epithelial cell. It is subsequently lost, CC together with VP4, following virus entry into the host cell. The CC outer layer contains 780 copies of VP7, grouped as 260 trimers. CC Rotavirus attachment and entry into the host cell probably CC involves multiple sequential contacts between the outer capsid CC proteins VP4 and VP7, and the cell receptors. In integrin- CC dependent strains, VP7 seems to essentially target the integrin CC heterodimers ITGAX/ITGB2 and ITGA5/ITGB3 at a postbinding stage, CC once the initial attachment by VP4 has been achieved (By CC similarity). CC -!- SUBUNIT: Homotrimer; in the presence of calcium (By similarity). CC Acquisition of the capsid outer layer requires a high calcium CC concentration inside the endoplasmic reticulum. Following cell CC entry, the low calcium concentration in the cytoplasm is probably CC responsible for the solubilization of the outer layer. Interacts CC with host integrin heterodimers ITGAX/ITGB2 and ITGA5/ITGB3 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Virion (Potential). Host rough endoplasmic CC reticulum membrane; Multi-pass membrane protein; Lumenal side CC (Potential). Note=Immature double-layered particles assembled in CC the cytoplasm bud across the membrane of the endoplasmic CC reticulum, acquiring during this process a transient lipid CC membrane that is modified with the ER resident viral glycoproteins CC NSP4 and VP7; these enveloped particles also contain VP4. As the CC particles move towards the interior of the ER cisternae, the CC transient lipid membrane and the non-structural protein NSP4 are CC lost, while the virus surface proteins VP4 and VP7 rearrange to CC form the outermost virus protein layer, yielding mature infectious CC triple-layered particles (By similarity). CC -!- PTM: The N-terminus is blocked possibly by pyroglutamic acid (By CC similarity). CC -!- PTM: N-glycosylated (By similarity). CC -!- PTM: Intramolecular disulfide bonds (By similarity). CC -!- MISCELLANEOUS: In group A rotaviruses, VP7 defines the G serotype. CC -!- SIMILARITY: Belongs to the rotavirus VP7 family. 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 GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW. DR GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW. DR InterPro; IPR001963; VP7. DR Pfam; PF00434; VP7; 1. DR ProDom; PD000191; VP7; 1. PE 3: Inferred from homology; KW Calcium; Capsid protein; Disulfide bond; Endoplasmic reticulum; KW Glycoprotein; Host-virus interaction; Membrane; Signal; Transmembrane; KW Virion. FT SIGNAL 1 50 Potential. FT CHAIN 51 326 Outer capsid glycoprotein VP7 FT (Potential). FT /FTId=PRO_0000369114. FT TRANSMEM 3 23 Potential. FT TRANSMEM 28 48 Potential. FT CARBOHYD 69 69 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 146 146 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 238 238 N-linked (GlcNAc...); by host FT (Potential). 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 //