VP7_ROTHA
ID VP7_ROTHA Reviewed; 326 AA.
AC P04328;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04131};
DE Flags: Precursor;
OS Rotavirus A (isolate RVA/Human/Australia/Hu5/1977/G2P[X]) (RV-A) (Rotavirus
OS A (isolate Hu/5)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10948;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6328448; DOI=10.1093/nar/12.9.3973;
RA Dyall-Smith M.L., Holmes I.H.;
RT "Sequence homology between human and animal rotavirus serotype-specific
RT glycoproteins.";
RL Nucleic Acids Res. 12:3973-3982(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2823458; DOI=10.1016/0042-6822(87)90181-4;
RA Green K.Y., Midthun K., Gorziglia M., Hoshino Y., Kapikian A.Z.,
RA Chanock R.M., Flores J.;
RT "Comparison of the amino acid sequences of the major neutralization protein
RT of four human rotavirus serotypes.";
RL Virology 161:153-159(1987).
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. 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=P04328-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04328-2; Sequence=VSP_038594;
CC -!- PTM: Intramolecular disulfide bonds. {ECO:0000250}.
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:0000303|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}.
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; X00572; CAA25236.1; -; mRNA.
DR EMBL; A01028; CAA00124.1; -; Unassigned_RNA.
DR PIR; G27620; VGXRHU.
DR SMR; P04328; -.
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_0000149595"
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 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 CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
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_038594"
SQ SEQUENCE 326 AA; 37203 MW; 2D438E6EEC86FCB0 CRC64;
MYGIEYTTIL TILISIILLN YILKTITNTM DYIIFRFLLL IALISPFVRT QNYGMYLPIT
GSLDAVYTNS TSGEPFLTST LCLYYPAEAK NEISDDEWEN TLSQLFLTKG WPIGSVYFKD
YNDINTFSVN PQLYCDYNVV LMRYDNTSEL DASELADLIL NEWLCNPMDI SLYYYQQSSE
SNKWISMGTD CTVKVCPLNT QTLGIGCKTT DVNTFEIVAS SEKLVITDVV NGVNHNINIS
INTCTIRNCN KLGPRENVAI IQVGGPNALD ITADPTTVPQ VQRIMRINWK KWWQVFYTVV
DYINQVIQVM SKRSRSLDAA AFYYRI
