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Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus B (isolate RVB/Human/China/ADRV/1982) (RV-B) (Rotavirus B (isolate adult diarrhea rotavirus))
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors (By similarity).By similarity
Outer capsid protein VP5*: forms the spike "foot" and "body". Acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm (By similarity).By similarity
VP8* forms the head of the spikes.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hemagglutinin

Keywords - Biological processi

Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Viral penetration via permeabilization of host membrane, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Outer capsid protein VP4
Alternative name(s):
Hemagglutinin
Cleaved into the following 2 chains:
OrganismiRotavirus B (isolate RVB/Human/China/ADRV/1982) (RV-B) (Rotavirus B (isolate adult diarrhea rotavirus))
Taxonomic identifieri10942 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

Outer capsid protein VP4 :
  • Virion By similarity
  • Host rough endoplasmic reticulum Curated

  • Note: Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles (By similarity).By similarity
Outer capsid protein VP8* :
  • Virion By similarity

  • Note: Outer capsid protein.By similarity
Outer capsid protein VP5* :
  • Virion By similarity

  • Note: Outer capsid protein.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host endoplasmic reticulum, Outer capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001495381 – 749Outer capsid protein VP4Add BLAST749
ChainiPRO_00003698381 – 206Outer capsid protein VP8*Sequence analysisAdd BLAST206
ChainiPRO_0000369839214 – 749Outer capsid protein VP5*Sequence analysisAdd BLAST536

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi29N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi53N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi109N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi133N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi407N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi527N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi568N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi620N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi681N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi698N-linked (GlcNAc...); by hostSequence analysis1

Post-translational modificationi

Proteolytic cleavage by trypsin results in activation of VP4 functions and greatly increases infectivity. The penetration into the host cell is dependent on trypsin treatment of VP4. It produces two peptides, VP5* and VP8* that remain associated with the virion (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei206 – 207CleavageSequence analysis2
Sitei213 – 214CleavageSequence analysis2

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

VP4 is a homotrimer.Curated

Structurei

3D structure databases

ProteinModelPortaliQ04916.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the rotavirus VP4 family.Curated

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q04916-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTYLRREWQ SFGETVTIKN TFNAQEDNNQ SGRKTDNRPV KTEGRYCYKA
60 70 80 90 100
DVNRSKYYHD VQGFSLGQSD LHIDPTQFIM YSGTISNGIS YVNQAPSCVQ
110 120 130 140 150
LSLKFTPGNS SLIEDLHIEP YKVEVLKIEH VGNVSRATLL SDIVSLSIAQ
160 170 180 190 200
KKLLLYGFTQ LGIQGLTGDV VSVETKRIPT PTQTNLLTIE DSMQCFTWDM
210 220 230 240 250
NCANVRSTKQ DSRLIIYEQE DGFWKIVTET LSIKVKPYFK AYGTMGGAFK
260 270 280 290 300
NWLVDSGFEK YQHDLAYVRD GVTVNAHTIT YVNPSGKAGL QQDWRPATDY
310 320 330 340 350
NGQITVLQPG DGFSVWYYED KWQINQAIYA KNFQSDTRAQ GYLENVGTLK
360 370 380 390 400
FKMNYIPAFA EIRNKPGKVN YAYLNGGFAQ VDASGYTGMS IILNFVCTGE
410 420 430 440 450
RFYASDNNSR VDNKITPFIS YIGDYYTLSG GDFYRQGCCA GFAAGYDDVS
460 470 480 490 500
PEHGITVSYT VMKPSDPDFI TGGENYGESI TSDLEVSIRN LQDQINSIIA
510 520 530 540 550
EMNIQQVTSA VFTAITNLGE LPGLFSNITK VFSKTKEALS KLKSRKKTSP
560 570 580 590 600
MPIAATSIID KTTVDVPNLT IVNKMPEEYE LGIIYNSMRT KKLIEQKKHD
610 620 630 640 650
FSTFTVATEV KLPYISKATN FSDQFMTSIS SRGITIGKSD IIQYDPMNNI
660 670 680 690 700
LSAMNRKNAQ IINYKIDPDL AHEVLSQMST NATRSLFSLN VRKQLHINNS
710 720 730 740
FDTPTYGQLV ERILDDGQLL DILGKLNPNS VEELFSEFLH RIQHQLREY
Length:749
Mass (Da):84,362
Last modified:June 1, 1994 - v1
Checksum:iD1223527DEAE0F21
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91434 mRNA. Translation: AAA47338.1.
PIRiA45687.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91434 mRNA. Translation: AAA47338.1.
PIRiA45687.

3D structure databases

ProteinModelPortaliQ04916.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiVP4_ROTGA
AccessioniPrimary (citable) accession number: Q04916
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 30, 2016
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.