VP7_ROTRF
ID VP7_ROTRF Reviewed; 326 AA.
AC Q86515;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04131};
DE Flags: Precursor;
OS Rotavirus A (strain RVA/Cow/France/RF/1975/G6P6[1]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10933;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cohen J.;
RT "Sequence of the gene encoding the outer glycoprotein of the bovine
RT rotavirus (RF strain) and comparison with homologous genes from four
RT bovine, simian and human rotaviruses.";
RL Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH THE INTERMEDIATE CAPSID PROTEIN VP6, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11285213; DOI=10.1093/emboj/20.7.1485;
RA Mathieu M., Petitpas I., Navaza J., Lepault J., Kohli E., Pothier P.,
RA Prasad B.V.V., Cohen J., Rey F.A.;
RT "Atomic structure of the major capsid protein of rotavirus: implications
RT for the architecture of the virion.";
RL EMBO J. 20:1485-1497(2001).
RN [3]
RP REVIEW.
RX PubMed=15165605; DOI=10.1016/j.tim.2004.04.003;
RA Lopez S., Arias C.F.;
RT "Multistep entry of rotavirus into cells: a Versaillesque dance.";
RL Trends Microbiol. 12:271-278(2004).
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 (By
CC similarity). Interacts with the intermediate capsid protein VP6
CC (PubMed:11285213). Interacts with the outer capsid protein VP5* (By
CC similarity). {ECO:0000255|HAMAP-Rule:MF_04131,
CC ECO:0000269|PubMed:11285213}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04131,
CC ECO:0000269|PubMed:11285213}. Host endoplasmic reticulum lumen
CC {ECO:0000255|HAMAP-Rule:MF_04131}. Note=The outer layer contains 780
CC copies of VP7, grouped as 260 trimers. Immature double-layered
CC particles assembled in the cytoplasm bud across the membrane of the
CC endoplasmic reticulum, acquiring during this process a transient lipid
CC membrane that is modified with the ER resident viral glycoproteins NSP4
CC and VP7; these enveloped particles also contain VP4. As the particles
CC move towards the interior of the ER cisternae, the transient lipid
CC membrane and the non-structural protein NSP4 are lost, while the virus
CC surface proteins VP4 and VP7 rearrange to form the outermost virus
CC protein layer, yielding mature infectious triple-layered particles.
CC {ECO:0000255|HAMAP-Rule:MF_04131, ECO:0000269|PubMed:11285213}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q86515-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86515-2; Sequence=VSP_038611;
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, ECO:0000269|PubMed:15165605}.
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:0000250|UniProtKB:P03533}.
CC -!- SIMILARITY: Belongs to the rotavirus VP7 family. {ECO:0000255|HAMAP-
CC Rule:MF_04131}.
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DR EMBL; X65940; CAA46743.1; -; mRNA.
DR PIR; S25546; S25546.
DR SMR; Q86515; -.
DR Proteomes; UP000007179; 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 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 1: Evidence at protein 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_0000369108"
FT REGION 165..167
FT /note="CNP motif; interaction with ITGAV/ITGB3"
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 238
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
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_038611"
SQ SEQUENCE 326 AA; 37085 MW; 66C66C7156889B9D CRC64;
MYGIEYTTIL IFLTSITLLN YMLKSITRIM DYIIYRFLLI VVILATIIKA QNYGVNLPIT
GSMDTAYADS TQSEPFLTST LCLYYPVEAS NEIADTEWKD TLSQLFLTKG WPTGSVYLKE
YADIAAFSVE PQLYCDYNLV LMKYDSTQEL DMSELADLIL NEWLCNPMDI TLYYYQQTDE
ANKWISTGSS CTVKVCPLNT QTLGIGCLIT NPDTFETVAT TEKLVITDVV DGVNHKLNVT
TATCTIRNCK KLGPRENVAV IQVGGANILD ITADPTTTPQ TERMMRINWK KWWQVFYTVV
DYVNQIIQTM SKRSRSLNSS AFYYRV
