VP7_ROTJ1
ID VP7_ROTJ1 Reviewed; 258 AA.
AC Q45UF2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 23-FEB-2022, entry version 54.
DE RecName: Full=Outer capsid glycoprotein VP7;
OS Rotavirus X (strain RVX/Human/China/NADRV-J19/1997/GXP[X]) (RV ADRV-N)
OS (Rotavirus (isolate novel adult diarrhea rotavirus-J19)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX NCBI_TaxID=335103;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=18796732; DOI=10.1099/vir.0.2008/001933-0;
RA Jiang S., Ji S., Tang Q., Cui X., Yang H., Kan B., Gao S.;
RT "Molecular characterization of a novel adult diarrhoea rotavirus strain J19
RT isolated in China and its significance for the evolution and origin of
RT group B rotaviruses.";
RL J. Gen. Virol. 89:2622-2629(2008).
CC -!- FUNCTION: Outer capsid protein involved in attachment and possibly
CC entry into the host epithelial cell. It is subsequently lost, together
CC with VP4, following virus entry into the host cell. The outer layer
CC contains 780 copies of VP7, grouped as 260 trimers. Rotavirus
CC attachment and entry into the host cell probably involves multiple
CC sequential contacts between the outer capsid proteins VP4 and VP7, and
CC the cell receptors (By similarity). {ECO:0000250}.
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 entry,
CC the low calcium concentration in the cytoplasm is probably responsible
CC for the solubilization of the outer layer (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host rough endoplasmic
CC reticulum membrane {ECO:0000305}; Single-pass membrane protein
CC {ECO:0000305}; Lumenal side {ECO:0000305}. Note=Immature double-layered
CC particles assembled in the cytoplasm bud across the membrane of the
CC endoplasmic reticulum, acquiring during this process a transient lipid
CC membrane that is modified with the ER resident viral glycoproteins NSP4
CC and VP7; these enveloped particles also contain VP4. As the particles
CC move towards the interior of the ER cisternae, the transient lipid
CC membrane and the non-structural protein NSP4 are lost, while the virus
CC surface proteins VP4 and VP7 rearrange to form the outermost virus
CC protein layer, yielding mature infectious triple-layered particles (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the rotavirus VP7 family. {ECO:0000305}.
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DR EMBL; DQ113905; AAZ03493.1; -; Genomic_RNA.
DR RefSeq; YP_392498.1; NC_007556.1.
DR PRIDE; Q45UF2; -.
DR GeneID; 5076658; -.
DR KEGG; vg:5076658; -.
DR Proteomes; UP000007663; Genome.
DR GO; GO:0044169; C:host cell rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 InterPro; IPR008818; Rotavirus_VP7.
DR Pfam; PF05868; Rotavirus_VP7; 1.
PE 3: Inferred from homology;
KW Calcium; Capsid protein; Glycoprotein; Host endoplasmic reticulum;
KW Host membrane; Membrane; Outer capsid protein; Reference proteome;
KW T=13 icosahedral capsid protein; Transmembrane; Transmembrane helix;
KW Virion.
FT CHAIN 1..258
FT /note="Outer capsid glycoprotein VP7"
FT /id="PRO_0000369863"
FT TRANSMEM 1..?13
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 258 AA; 29265 MW; 55DFEC621B61DBB8 CRC64;
MLLFIILSVG VDAISYIQND RSNDLCIVYE MTSFGTSFNN ANDSLVKLHK HMGLKYEVCK
IESNANALTQ MQKCNCIYDD TPQIVVFTNF KKSSLKTLIG TENKCELLPQ TTIYTPTVDI
ESEYFIYGND VKICYLDKNL LGIGCDATDT TSWLDLDAGL PTNHALDIPE ITSDGFKLFA
KYSDSFLCQR LMDEPKKQIQ FYAEVDNVPS NDVIESSRSW ASVWKVVKTV LHFTYHILDL
FYGNRRATAR MIEHSPLG