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 22-FEB-2023, entry version 60. 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; Sedoreoviridae; 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}. 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; 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; 3.40.50.11130; Glycoprotein VP7, domain 1; 1. DR Gene3D; 2.60.120.800; Rotavirus outer-layer protein VP7, domain 2; 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 //