ID   VP7_ROTBS               Reviewed;         332 AA.
AC   Q65527;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   29-SEP-2021, entry version 59.
DE   RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04130};
DE   Flags: Precursor;
OS   Rotavirus C (isolate RVC/Cow/Japan/Shintoku/1991/G2P[3]) (RV-C).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=33723;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8645106; DOI=10.1007/bf01718328;
RA   Tsunemitsu H., Jiang B., Saif L.J.;
RT   "Sequence comparison of the VP7 gene encoding the outer capsid glycoprotein
RT   among animal and human group C rotaviruses.";
RL   Arch. Virol. 141:705-713(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; U31750; AAC55011.1; -; Genomic_RNA.
DR   SMR; Q65527; -.
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; Signal; 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_0000369879"
SQ   SEQUENCE   332 AA;  37590 MW;  72C4F211ADA93FBB CRC64;
     MVCTTLYTVC VILCILLMYI ILFRKMIHFL IDLSLIAFVI SSCIRLSNAQ FFANDMLYNG
     NVEGVINTTN IFNVESLCIY FPNSAVGRPG PGKSDGLIND NNYAQTLAVL FETKGFPKGS
     VNFNTYTKIS DFINSIEMTC SYNIVIIPET LANSETIEQV AEWVLNVWKC DNMNVDIYTY
     EQIGKDNFWA AFGEDCDVAV CPLDTTMNGI GCTPASTETY EVLSNDTQLA LIDVVDNVKH
     RIQLNQVTCK LRNCVKGEAR LNTAIVRISN LSSFDNSLSP LNNGQKTRSF KINAKKWWKI
     FYTIIDYINT FIQSMTPRHR AIYPEGWMLR YA