ID VP4_ROTB2 Reviewed; 826 AA. AC A9Q1L0; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 16-JUN-2009, entry version 10. DE RecName: Full=Outer capsid protein VP4; DE AltName: Full=Hemagglutinin; DE Contains: DE RecName: Full=Outer capsid protein VP8*; DE Contains: DE RecName: Full=Outer capsid protein VP5*; OS Rotavirus (isolate Human/Bangladesh/ADRV-N B219/2002) (RV ADRV-N) OS (Rotavirus (isolate novel adult diarrhea rotavirus-B219)). OC Viruses; dsRNA viruses; Reoviridae; Rotavirus; OC unclassified rotaviruses. OX NCBI_TaxID=348136; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PUTATIVE CLEAVAGE SITES. RX PubMed=18814255; DOI=10.1002/jmv.21286; RA Nagashima S., Kobayashi N., Ishino M., Alam M.M., Ahmed M.U., RA Paul S.K., Ganesh B., Chawla-Sarkar M., Krishnan T., Naik T.N., RA Wang Y.-H.; RT "Whole genomic characterization of a human rotavirus strain B219 RT belonging to a novel group of the genus Rotavirus."; RL J. Med. Virol. 80:2023-2033(2008). CC -!- FUNCTION: Spike-forming protein that mediates virion attachment to CC the host epithelial cell receptors and plays a major role in cell CC penetration, determination of host range restriction and CC virulence. Rotavirus entry into the host cell probably involves CC multiple sequential contacts between the outer capsid proteins VP4 CC and VP7, and the cell receptors (By similarity). CC -!- FUNCTION: VP5* forms the spike "foot" and "body" (By similarity). CC -!- FUNCTION: VP8* forms the head of the spikes (By similarity). CC -!- SUBUNIT: VP4 is a homotrimer (Potential). CC -!- SUBCELLULAR LOCATION: Outer capsid protein VP4: Virion (By CC similarity). Host rough endoplasmic reticulum (Potential). CC Note=Immature double-layered particles assembled in the cytoplasm CC bud across the membrane of the endoplasmic reticulum, acquiring CC during this process a transient lipid membrane that is modified CC with the ER resident viral glycoproteins NSP4 and VP7; these CC enveloped particles also contain VP4. As the particles move CC towards the interior of the ER cisternae, the transient lipid CC membrane and the non-structural protein NSP4 are lost, while the CC virus surface proteins VP4 and VP7 rearrange to form the outermost CC virus protein layer, yielding mature infectious triple-layered CC particles (By similarity). CC -!- SUBCELLULAR LOCATION: Outer capsid protein VP8*: Virion (By CC similarity). Note=Outer capsid protein (By similarity). CC -!- SUBCELLULAR LOCATION: Outer capsid protein VP5*: Virion (By CC similarity). Note=Outer capsid protein (By similarity). CC -!- PTM: Proteolytic cleavage by trypsin results in activation of VP4 CC functions and greatly increases infectivity. The penetration into CC the host cell is dependent on trypsin treatment of VP4. It CC produces two peptides, VP5* and VP8* that remain associated with CC the virion (By similarity). CC -!- SIMILARITY: Belongs to the rotavirus VP4 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; EF453358; ABR32125.1; -; mRNA. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Capsid protein; Cleavage on pair of basic residues; Complete proteome; KW Endoplasmic reticulum; Glycoprotein; Hemagglutinin; Virion. FT CHAIN 1 826 Outer capsid protein VP4. FT /FTId=PRO_0000369842. FT CHAIN 1 249 Outer capsid protein VP8* (Potential). FT /FTId=PRO_0000369843. FT CHAIN 263 826 Outer capsid protein VP5* (Potential). FT /FTId=PRO_0000369844. FT COMPBIAS 260 263 Poly-Lys. FT SITE 249 250 Cleavage (Potential). FT SITE 262 263 Cleavage (Potential). FT CARBOHYD 143 143 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 153 153 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 198 198 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 333 333 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 487 487 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 494 494 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 514 514 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 561 561 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 804 804 N-linked (GlcNAc...); by host FT (Potential). SQ SEQUENCE 826 AA; 93311 MW; B8CC3EDD7D540505 CRC64; MSLRSLLITT EAVGETTQTS DHQTSFSTRT YNEINDRPSL RVEKDGEKAY CFKNLDPVRY DTRMGEYPFD YGGQSTENNQ LQFDLFTKDL MADTDIGLSD DVRDDLKRQI KEYYQQGYRA IFLIRPQNQE QQYIASYSST NLNFTSQLSV GVNLSVLNKI QENKLHIYST QPHIPSVGCE MITKIFRTDV DNENSLINYS VPVTVTISVT KATFEDTFVW NQNNDYPNMN YKDLIPAVTK NSIYHDVKRI TKIHEYINSK KKKNGVGKIG GIQIAESKDG FWKILTKNYQ IKLKFGIEGY GVMGGTFGNW LIDSGFKTVE TNYEYQRNGK TINATTVASV KPSRKCGTRS PVFGQLQFSG EMMVLSHNDI LTVFYTEREW ALSNAIYAKN FATDFKRQFE VTAQSDELLV RTNVVPHTIK NTPGKALMEY SHGGFGQIDT SDYTGMALTF RFRCVSEDLP EGYYDKDKAL TFANVGLTSF QDRQETNGTY WVYNTSTVGF GSCYPKKEFE YDINVTYTTL LPSDPEFTTG GTNYAQSVTA VLEESFINLQ NQVNEMLTRM NISDLTSGVM SVFSVATSFP QILDGISDLL KAASSAFKKV KGKVGNVAKR LRGKRYVRLF DEDISIEETP RFLDSIRSSR RPSILSNMFN DDETFTALHT LASRTNSVAS DVTYIQPIIT TRIANSTPPV IAPASSVTYA KLKDISKIIN AEIDPKSIME FNQVSNTISI LDSTKKLAQY AVDPDVIDGI LNKMVGGHAR SLFSLKVRKH LLDAVEKDAF VKYNYHDLMG KLLNDRELLD ITNNLSSQKQ FELAKEFRDL LINALA //