VP7_ROTGI
ID VP7_ROTGI Reviewed; 246 AA.
AC P30889;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 23-FEB-2022, entry version 74.
DE RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04130};
DE Flags: Precursor;
OS Rotavirus B (isolate RVB/Rat/United States/IDIR/1984/G1P[X]) (RV-B)
OS (Rotavirus B (isolate infectious diarrhea of infant rats)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX NCBI_TaxID=28877;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1658208; DOI=10.1099/0022-1317-72-11-2801;
RA Petric M., Mayur K., Vonderfecht S., Eiden J.J.;
RT "Comparison of group B rotavirus genes 9 and 11.";
RL J. Gen. Virol. 72:2801-2804(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 -!- SIMILARITY: Belongs to the rotavirus VP7 family. {ECO:0000255|HAMAP-
CC Rule:MF_04130}.
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DR EMBL; D00911; BAA00757.1; -; Genomic_RNA.
DR PIR; JQ1311; JQ1311.
DR SMR; P30889; -.
DR GO; GO:0044166; C:host cell endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
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 HAMAP; MF_04130; Rota_VP7; 1.
DR InterPro; IPR008818; Rotavirus_VP7.
DR InterPro; IPR001963; VP7.
DR Pfam; PF05868; Rotavirus_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..16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04130"
FT CHAIN 17..246
FT /note="Outer capsid glycoprotein VP7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04130"
FT /id="PRO_0000041132"
SQ SEQUENCE 246 AA; 28319 MW; BF28CC5BF9A169A7 CRC64;
MTTMLLLLVV AALANGQLTI LPHEESQICF LQPDNPGFDF DGNFTNIFRD YASVKISSFT
YKAQDADIVE ILNVDRDRSC TILAIYIADS TLDFNTFLQS ENECVKYAAS KKHYIKLPRD
REYFALAKNL SFCPLNDDLI GIYCDTQLET TYFSVARSSN YDVTDIPEFT ELGYVFHSND
HFYICERKSE GNWIDYQLFY QNDAPLGTVS QRVNWGNVWS NVKTVAQMVY KILDIFFGKR
NIEPRA