ID   VP7_ROTPC               Reviewed;         332 AA.
AC   P30217;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   23-FEB-2022, entry version 77.
DE   RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04130};
DE   Flags: Precursor;
OS   Rotavirus C (strain RVC/Pig/United States/Cowden/1980) (RV-C).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=10916;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1850919; DOI=10.1016/0042-6822(91)90597-5;
RA   Qian Y.A., Jiang B., Saif L.J., Kang S.Y., Ishimaru Y., Yamashita Y.,
RA   Oseto M., Green K.Y.;
RT   "Sequence conservation of gene 8 between human and porcine group C
RT   rotaviruses and its relationship to the VP7 gene of group A rotaviruses.";
RL   Virology 182:562-569(1991).
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}.
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; M61101; AAA47351.1; -; mRNA.
DR   PIR; A39988; VGXRCN.
DR   SMR; P30217; -.
DR   Proteomes; UP000008175; 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   2: Evidence at transcript level;
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..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..332
FT                   /note="Outer capsid glycoprotein VP7"
FT                   /id="PRO_0000041130"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   332 AA;  37348 MW;  DD9D45A8C3F31699 CRC64;
     MVCTTLYTVC VILCILFIYM LLFRKMFHLI ADALVITLII SNCIGWSQGQ MFIDDIHYNG
     NVETIVNATD PFDVRSLCIY FPNAVVGSQG PGKTDGYLND GNYAQTIAAL FETKGFPRGS
     IVLKTYTKVS DFVDSVEMTC SYNIVIIPDS PTNSESIERI AEWILNVWRC DDMNLDIYTY
     EQTGIDNLWA AFGSDCDVSV CPLDTTMNGI GCSPASTETY EVLSNDTQLA LLNVVDNVKH
     RIQMNTASCK LKNCIKGEAR LNTALIRIST SSSFDNSLSP LNDGQTTRSF KINAKKWWTI
     FYTIIDYINT IIQTMTPRHR AIYPEGWMLR YA