VP7_ROTBK
ID VP7_ROTBK Reviewed; 326 AA.
AC Q00254;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04131};
DE Flags: Precursor;
OS Rotavirus A (isolate RVA/Cow/Japan/KK3/1983/G10P8[11]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=1835657;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1662688; DOI=10.1099/0022-1317-72-12-2929;
RA Taniguchi K., Urasawa T., Pongsuwanna Y., Choonthanom M., Jayavasu C.,
RA Urasawa S.;
RT "Molecular and antigenic analyses of serotypes 8 and 10 of bovine
RT rotaviruses in Thailand.";
RL J. Gen. Virol. 72:2929-2937(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_04131}.
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_04131}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04131}. Host
CC endoplasmic reticulum lumen {ECO:0000255|HAMAP-Rule:MF_04131}. 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_04131}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q00254-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q00254-2; Sequence=VSP_038580;
CC -!- PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04131}.
CC -!- PTM: The N-terminus is blocked possibly by pyroglutamic acid.
CC {ECO:0000255|HAMAP-Rule:MF_04131}.
CC -!- MISCELLANEOUS: Some rotavirus strains are neuraminidase-sensitive and
CC require sialic acid to attach to the cell surface. Some rotavirus
CC strains are integrin-dependent. Some rotavirus strains depend on
CC ganglioside for their entry into the host cell. Hsp70 also seems to be
CC involved in the entry of some strains. {ECO:0000255|HAMAP-
CC Rule:MF_04131}.
CC -!- MISCELLANEOUS: In group A rotaviruses, VP7 defines the G serotype.
CC {ECO:0000255|HAMAP-Rule:MF_04131}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met-
CC 30 of isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the rotavirus VP7 family. {ECO:0000255|HAMAP-
CC Rule:MF_04131}.
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DR EMBL; D01056; BAA00858.1; -; mRNA.
DR SMR; Q00254; -.
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 HAMAP; MF_04131; Rota_VP7_A; 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 Alternative initiation; Calcium; Capsid protein; Disulfide bond;
KW Glycoprotein; Host endoplasmic reticulum; Host-virus interaction;
KW Metal-binding; Outer capsid protein; Signal;
KW T=13 icosahedral capsid protein; Virion.
FT SIGNAL 1..50
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT CHAIN 51..326
FT /note="Outer capsid glycoprotein VP7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT /id="PRO_0000149584"
FT REGION 165..167
FT /note="CNP motif; interaction with ITGAV/ITGB3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT REGION 237..239
FT /note="LVD motif; interaction with ITGA4/ITGB1 heterodimer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT REGION 253..255
FT /note="GPR motif; interaction with ITGAX/ITGB2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 82..135
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT DISULFID 165..249
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT DISULFID 191..244
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT DISULFID 196..207
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038580"
SQ SEQUENCE 326 AA; 37423 MW; 292F59C25B932728 CRC64;
MYGIEYTTFL IYLISIILFN YILKSITRMM DYIIYKFLLI VTITSIVVNA QNYGVNLPIT
GSMDTSYVNA TKGKPFLTST LCLYYPTEAR TEINDNEWTN TLSQLFLTKG WPTGSVYFKE
YDDIATFSVD PQLYCDYNIV LMRYNSNLEL DMSELANLIL NEWLCNPMDI TLYYYQQTDE
ANKWIAMGQS CTIKVCPLNT QTLGIGCQTT NTRTFEEVAT AEKLVITDVV DGVNHKLDVT
TATCTIRNCK KLGPRENVAV IQVGGADILD ITSDPTTNPQ TERIMRINWK KWWQVFYTIV
DYVNQIVQAM SKRSRSLNSA AFYYRV
