VP7_ROTHW
ID VP7_ROTHW Reviewed; 326 AA.
AC P03532;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04131};
DE Flags: Precursor;
OS Rotavirus A (strain RVA/Human/United States/Wa/1974/G1P1A[8]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10962;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6088808; DOI=10.1128/jvi.51.3.860-862.1984;
RA Richardson M.A., Iwamoto A., Ikegami N., Nomoto A., Furuichi Y.;
RT "Nucleotide sequence of the gene encoding the serotype-specific antigen of
RT human (Wa) rotavirus: comparison with the homologous genes from simian SA11
RT and UK bovine rotaviruses.";
RL J. Virol. 51:860-862(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2412362; DOI=10.1016/0168-1702(85)90026-7;
RA Mason B.B., Dheer S.K., Hsiao C.-L., Zandle G., Kostek B., Rosanoff E.I.,
RA Hung P.P., Davis A.R.;
RT "Sequence of the serotype-specific glycoprotein of the human rotavirus Wa
RT strain and comparison with other human rotavirus serotypes.";
RL Virus Res. 2:291-299(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
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 [4]
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=P03532-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P03532-2; Sequence=VSP_038632;
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:0000305}.
CC -!- SIMILARITY: Belongs to the rotavirus VP7 family. {ECO:0000255|HAMAP-
CC Rule:MF_04131}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA47310.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; K02033; AAA47310.1; ALT_INIT; Genomic_RNA.
DR EMBL; M21843; AAA47342.1; -; Genomic_RNA.
DR PIR; A04137; VGXR7H.
DR PIR; D27620; VGXRWA.
DR SMR; P03532; -.
DR ABCD; P03532; 2 sequenced antibodies.
DR Proteomes; UP000006581; 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 3: Inferred from homology;
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_0000149609"
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 69
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_038632"
FT CONFLICT 149
FT /note="E -> K (in Ref. 2; AAA47342)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="M -> N (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 37341 MW; 310963A6223F00D4 CRC64;
MYGIEYTTIL IFLISIILLN YILKSVTRIM DYIIYRFLLI TVALFALTRA QNYGLNLPIT
GSMDAVYTNS TQEEVFLTST LCLYYPTEAS TQINDGDWKD SLSQMFLTKG WPTGSVYFKE
YSNIVDFSVD PQLYCDYNLV LMKYDQSLEL DMSELADLIL NEWLCNPMDV TLYYYQQSGE
SNKWISMGSS CTVKVCPLNT QTLGIGCQTT NVDSFEMIAE NEKLAIVDVV DGINHKINLT
TTTCTIRNCK KLGPRENVAV IQVGGSNVLD ITADPTTNPQ TERMMRVNWK KWWQVFYTIV
DYINQIVQVM SKRSRSLNSA AFYYRV
