ID   VP7_ROTB2               Reviewed;         258 AA.
AC   Q0H8C3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Outer capsid glycoprotein VP7;
OS   Rotavirus X (isolate RVX/Human/Bangladesh/NADRV-B219/2002/GXP[X]) (RV
OS   ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-B219)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; unclassified Rotavirus.
OX   NCBI_TaxID=348136;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=16900303; DOI=10.1007/s00705-006-0831-y;
RA   Alam M.M., Kobayashi N., Ishino M., Ahmed M.S., Ahmed M.U., Paul S.K.,
RA   Muzumdar B.K., Hussain Z., Wang Y.H., Naik T.N.;
RT   "Genetic analysis of an ADRV-N-like novel rotavirus strain B219 detected in
RT   a sporadic case of adult diarrhea in Bangladesh.";
RL   Arch. Virol. 152:199-208(2007).
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; DQ168034; ABA60394.1; -; Genomic_RNA.
DR   Proteomes; UP000174021; 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_0000369862"
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;  29261 MW;  03ADE4771936F3CF CRC64;
     MLLFIILSVG VDAISYIQND RSNDLCIIYE MTSFGASFNN ANDSLVKLHR HMGLKYEICK
     IESNANALTQ MQKCNCLYDD TPQIVVFTNF RKSSLKTLIG TENKCELLPQ TTIYTPTVDI
     ESEYFIYGND VKICYLDKNL LGIGCDATDT TSWLDLDAGL PTNHAIDIPE ITSDGFKLFA
     KYGDSFLCQR LMDEPKKQIQ FYAEVDNVPS NDVIESSRSW ASVWKVVKTV LHFTYHILDL
     FYGNKRATAR MIEHSPLG