VP7_ROTS1
ID VP7_ROTS1 Reviewed; 326 AA.
AC P03533;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Outer capsid glycoprotein VP7 {ECO:0000255|HAMAP-Rule:MF_04131};
DE Flags: Precursor;
OS Rotavirus A (strain RVA/SA11-Both/G3P5B[2]) (RV-A) (Simian Agent 11 (strain
OS Both)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=37137;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6304692; DOI=10.1073/pnas.80.10.3091;
RA Both G.W., Mattick J.S., Bellamy A.R.;
RT "Serotype-specific glycoprotein of simian 11 rotavirus: coding assignment
RT and gene sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:3091-3095(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6323768; DOI=10.1128/jvi.50.2.657-661.1984;
RA Arias C.F., Lopez S., Bell J.R., Strauss J.H.;
RT "Primary structure of the neutralization antigen of simian rotavirus SA11
RT as deduced from cDNA sequence.";
RL J. Virol. 50:657-661(1984).
RN [3]
RP GLYCOSYLATION AT ASN-69.
RX PubMed=2995404; DOI=10.1083/jcb.101.4.1270;
RA Kabcenell A.K., Atkinson P.H.;
RT "Processing of the rough endoplasmic reticulum membrane glycoproteins of
RT rotavirus SA11.";
RL J. Cell Biol. 101:1270-1280(1985).
RN [4]
RP SIGNAL SEQUENCE CLEAVAGE SITE, ALTERNATIVE INITIATION, AND MUTAGENESIS OF
RP MET-30 AND ALA-50.
RX PubMed=2826493; DOI=10.1083/jcb.105.6.2897;
RA Stirzaker S.C., Whitfeld P.L., Christie D.L., Bellamy A.R., Both G.W.;
RT "Processing of rotavirus glycoprotein VP7: implications for the retention
RT of the protein in the endoplasmic reticulum.";
RL J. Cell Biol. 105:2897-2903(1987).
RN [5]
RP INTERACTION WITH HUMAN INTEGRIN HETERODIMER ITGAX/ITGB2, INTERACTION WITH
RP INTEGRIN HETERODIMER ITGA5/ITGB3, AND FUNCTION.
RX PubMed=12941907; DOI=10.1128/jvi.77.18.9969-9978.2003;
RA Graham K.L., Halasz P., Tan Y., Hewish M.J., Takada Y., Mackow E.R.,
RA Robinson M.K., Coulson B.S.;
RT "Integrin-using rotaviruses bind alpha2beta1 integrin alpha2 I domain via
RT VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by using VP7
RT during cell entry.";
RL J. Virol. 77:9969-9978(2003).
RN [6]
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 (By
CC similarity). Rotavirus attachment and entry into the host cell probably
CC involves multiple sequential contacts between the outer capsid proteins
CC VP4 and VP7, and the cell receptors (PubMed:12941907). Following entry
CC into the host cell, low intracellular or intravesicular Ca(2+)
CC concentration probably causes the calcium-stabilized VP7 trimers to
CC 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}.
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 (By similarity). Interacts
CC with the outer capsid protein VP5* (By similarity). Interacts with host
CC integrin heterodimer ITGAX/ITGB2 (PubMed:12941907). Interacts with host
CC integrin heterodimer ITGA5/ITGB3 (PubMed:12941907). {ECO:0000255|HAMAP-
CC Rule:MF_04131, ECO:0000269|PubMed:12941907}.
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=P03533-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P03533-2; Sequence=VSP_036750;
CC -!- PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04131,
CC ECO:0000269|PubMed:2995404}.
CC -!- PTM: The N-terminus is blocked possibly by pyroglutamic acid.
CC {ECO:0000255|HAMAP-Rule:MF_04131, ECO:0000269|PubMed:2826493}.
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:0000269|PubMed:2826493}.
CC -!- SIMILARITY: Belongs to the rotavirus VP7 family. {ECO:0000255|HAMAP-
CC Rule:MF_04131}.
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DR EMBL; V01190; CAA24510.1; -; Unassigned_RNA.
DR EMBL; V01546; CAA24788.1; -; Genomic_RNA.
DR EMBL; K02028; AAA47307.1; -; Genomic_RNA.
DR PIR; A04135; VGXR1S.
DR SMR; P03533; -.
DR iPTMnet; P03533; -.
DR Proteomes; UP000007180; 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 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 ECO:0000269|PubMed:2826493"
FT CHAIN 51..326
FT /note="Outer capsid glycoprotein VP7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04131"
FT /id="PRO_0000149621"
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:0000305|PubMed:2995404"
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_036750"
FT MUTAGEN 30
FT /note="M->L: Isoform 2 is no longer synthesized."
FT /evidence="ECO:0000269|PubMed:2826493"
FT MUTAGEN 50
FT /note="A->V: Complete loss of signal processing."
FT /evidence="ECO:0000269|PubMed:2826493"
FT CONFLICT 16
FT /note="I -> T (in Ref. 2; AAA47307)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="C -> F (in Ref. 2; AAA47307)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="L -> F (in Ref. 2; AAA47307)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="T -> A (in Ref. 2; AAA47307)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="T -> P (in Ref. 2; AAA47307)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="G -> E (in Ref. 2; AAA47307)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="A -> P (in Ref. 2; AAA47307)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="L -> H (in Ref. 1; CAA24788)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 37120 MW; C75549FD1F2A0C31 CRC64;
MYGIEYTTVL TFLISIILLN YILKSLTRIM DCIIYRLLFI 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
