VP7_ROTSH
ID VP7_ROTSH Reviewed; 326 AA.
AC A2T3P5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04131};
DE Flags: Precursor;
OS Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A)
OS (Simian Agent 11 (isolate SI/South Africa/H96/58)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=450149;
OH NCBI_TaxID=60710; Chlorocebus pygerythrus (Vervet monkey) (Cercopithecus pygerythrus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=17059839; DOI=10.1016/j.virol.2006.09.024;
RA Small C., Barro M., Brown T.L., Patton J.T.;
RT "Genome heterogeneity of SA11 rotavirus due to reassortment with 'O'
RT agent.";
RL Virology 359:415-424(2007).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=1649333; DOI=10.1128/jvi.65.8.4334-4340.1991;
RA Anthony I.D., Bullivant S., Dayal S., Bellamy A.R., Berriman J.A.;
RT "Rotavirus spike structure and polypeptide composition.";
RL J. Virol. 65:4334-4340(1991).
RN [3]
RP FUNCTION, INTERACTION WITH INTEGRIN HETERODIMER ITGA4/ITGB1, AND
RP INTERACTION WITH INTEGRIN HETERODIMER ITGAX/ITGB2.
RX PubMed=9144247; DOI=10.1073/pnas.94.10.5389;
RA Coulson B.S., Londrigan S.L., Lee D.J.;
RT "Rotavirus contains integrin ligand sequences and a disintegrin-like domain
RT that are implicated in virus entry into cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:5389-5394(1997).
RN [4]
RP FUNCTION, INTERACTION WITH INTEGRIN HETERODIMER ITGA4/ITGB1, AND
RP INTERACTION WITH INTEGRIN HETERODIMER ITGA2/ITGB1.
RX PubMed=10590110; DOI=10.1128/jvi.74.1.228-236.2000;
RA Hewish M.J., Takada Y., Coulson B.S.;
RT "Integrins alpha2beta1 and alpha4beta1 can mediate SA11 rotavirus
RT attachment and entry into cells.";
RL J. Virol. 74:228-236(2000).
RN [5]
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).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY OF CAPSID SHELL, INTERACTION WITH THE
RP INTERMEDIATE PROTEIN VP6, AND SUBCELLULAR LOCATION.
RC STRAIN=SA11-4F;
RX PubMed=19036817; DOI=10.1128/jvi.01855-08;
RA Li Z., Baker M.L., Jiang W., Estes M.K., Prasad B.V.V.;
RT "Rotavirus architecture at subnanometer resolution.";
RL J. Virol. 83:1754-1766(2009).
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 (PubMed:9144247, PubMed:10590110).
CC Following entry into the host cell, low intracellular or intravesicular
CC Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers
CC to dissociate from the virion. This step is probably necessary for the
CC membrane-disrupting entry step and the release of VP4, which is locked
CC onto the virion by VP7 (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_04131, ECO:0000269|PubMed:10590110, ECO:0000269|PubMed:9144247,
CC ECO:0000303|PubMed:15165605}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked (By similarity). 2 Ca(2+) ions
CC bound at each subunit interface in the trimer hold the trimer together
CC (By similarity). Interacts with the intermediate capsid protein VP6
CC (PubMed:19036817). Interacts with the outer capsid protein VP5* (By
CC similarity). Interacts with host integrin heterodimer ITGAX/ITGB2
CC (PubMed:9144247). Interacts with host integrin heterodimer ITGA4/ITGB1
CC (PubMed:9144247, PubMed:10590110). Interacts with host integrin
CC heterodimer ITGA2/ITGB1 (PubMed:10590110). {ECO:0000255|HAMAP-
CC Rule:MF_04131, ECO:0000269|PubMed:10590110,
CC ECO:0000269|PubMed:19036817, ECO:0000305|PubMed:9144247}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04131,
CC ECO:0000269|PubMed:1649333, ECO:0000269|PubMed:19036817}. 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=A2T3P5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2T3P5-2; Sequence=VSP_038601;
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; DQ838620; ABG75794.1; -; Genomic_RNA.
DR RefSeq; YP_002302222.1; NC_011503.2.
DR SMR; A2T3P5; -.
DR GeneID; 7011359; -.
DR KEGG; vg:7011359; -.
DR Proteomes; UP000001119; Genome.
DR GO; GO:0044166; C:host cell endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0039621; C:T=13 icosahedral viral capsid; IDA:UniProtKB.
DR GO; GO:0039624; C:viral outer capsid; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:UniProtKB.
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; Reference proteome; 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_0000369103"
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 ECO:0000269|PubMed:9144247"
FT REGION 253..255
FT /note="GPR motif; interaction with ITGAX/ITGB2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131,
FT ECO:0000269|PubMed:9144247"
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:0000250|UniProtKB:P12476"
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_038601"
SQ SEQUENCE 326 AA; 37198 MW; 2F72FBB9A3D09BA9 CRC64;
MYGIEYTTVL TFLISIILLN YILKSLTRIM DFIIYRFLFI IVILSPFLRA QNYGINLPIT
GSMDTAYANS TQEETFLTST LCLYYPTEAA TEINDNSWKD TLSQLFLTKG WPTGSVYFKE
YTNIASFSVD PQLYCDYNVV LMKYDATLQL DMSELADLIL NEWLCNPMDI TLYYYQQTDE
ANKWISMGSS CTIKVCPLNT QTLGIGCLTT DATTFEEVAT AEKLVITDVV DGVNHKLDVT
TATCTIRNCK KLGPRENVAV IQVGGSDILD ITADPTTAPQ TERMMRINWK KWWQVFYTVV
DYVDQIIQVM SKRSRSLNSA AFYYRV
