ID   VP7_ROTHC               Reviewed;         332 AA.
AC   Q89865;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   29-SEP-2021, entry version 76.
DE   RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04130};
DE   Flags: Precursor;
OS   Rotavirus C (isolate RVC/Human/United Kingdom/Bristol/1989) (RV-C).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=31567;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7852957; DOI=10.1002/jmv.1890440209;
RA   Grice A.S., Lambden P.R., Caul E.O., Clarke I.N.;
RT   "Sequence conservation of the major outer capsid glycoprotein of human
RT   group C rotaviruses.";
RL   J. Med. Virol. 44:166-171(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate clinical BF;
RX   PubMed=8634028; DOI=10.1007/bf01718407;
RA   Jiang B., Tsunemitsu H., Dennehy P.H., Oishi I., Brown D., Schnagl R.D.,
RA   Oseto M., Fang Z.Y., Avendano L.F., Saif L.J., Glass R.I.;
RT   "Sequence conservation and expression of the gene encoding the outer capsid
RT   glycoprotein among human group C rotaviruses of global distribution.";
RL   Arch. Virol. 141:381-390(1996).
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_04130}.
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_04130}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04130}. Host
CC       endoplasmic reticulum lumen {ECO:0000255|HAMAP-Rule:MF_04130}. 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_04130}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- PTM: Intramolecular disulfide bonds. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the rotavirus VP7 family. {ECO:0000255|HAMAP-
CC       Rule:MF_04130}.
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DR   EMBL; X77257; CAA54475.1; -; Genomic_RNA.
DR   EMBL; X77258; CAA54476.1; -; Genomic_RNA.
DR   EMBL; U20989; AAC54783.1; -; Genomic_RNA.
DR   PIR; S41417; S41417.
DR   RefSeq; YP_392513.1; NC_007571.1.
DR   SMR; Q89865; -.
DR   PRIDE; Q89865; -.
DR   GeneID; 3773131; -.
DR   KEGG; vg:3773131; -.
DR   Proteomes; UP000007664; Genome.
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   InterPro; IPR001963; VP7.
DR   InterPro; IPR042207; VP7_1.
DR   InterPro; IPR042210; VP7_2.
DR   Pfam; PF00434; VP7; 1.
PE   3: Inferred from homology;
KW   Calcium; Capsid protein; Disulfide bond; Glycoprotein;
KW   Host endoplasmic reticulum; Host-virus interaction; Metal-binding;
KW   Outer capsid protein; Reference proteome; Signal;
KW   T=13 icosahedral capsid protein; Virion.
FT   SIGNAL          1..49
FT                   /evidence="ECO:0000255"
FT   CHAIN           50..332
FT                   /note="Outer capsid glycoprotein VP7"
FT                   /id="PRO_0000369880"
SQ   SEQUENCE   332 AA;  37474 MW;  1DF2115F28FED28A CRC64;
     MVCTTLYTVC AILFILFIYI LLFRKMFHLI TDTLIVILIL SNCVEWSQGQ MFTDDIYYNG
     NVETIINSTD PFNVESLCIY FPNAVVGSQG PGKSDGHLND GNYAQTIATL FETKGFPKGS
     IILKTYTQTS DFINSVEMTC SYNIVIIPDS PNDSESIEQI AEWILNVWRC DDMNLEIYTY
     EQIGINNLWA AFGSDCDISV CPLDTTSNGI GCSPASTETY EVVSNDTQLA LINVVDNVRH
     RIQMNTAQCK LKNCIKGEAR LNTALIRIST SSSFDNSLSP LNNGQTTRSF KINAKKWWTI
     FYTIIDYINT IVQAMTPRHR AIYPEGWMLR YA