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Q65525

- VP4_ROTBS

UniProt

Q65525 - VP4_ROTBS

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Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus C (isolate Cow/Japan/Shintoku/1991) (RV-C)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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. It is the viral hemagglutinin and an important target of neutralizing antibodies (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei228 – 2292CleavageSequence Analysis
Sitei244 – 2452CleavageSequence Analysis

GO - Biological processi

  1. permeabilization of host organelle membrane involved in viral entry into host cell Source: UniProtKB-KW
  2. virion attachment to host cell Source: UniProtKB-KW
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 C (isolate Cow/Japan/Shintoku/1991) (RV-C)
Taxonomic identifieri33723 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]

Subcellular locationi

Chain Outer capsid protein VP4 : Virion. 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
Chain Outer capsid protein VP8* : Virion By similarity
Note: Outer capsid protein.By similarity
Chain Outer capsid protein VP5* : Virion By similarity
Note: Outer capsid protein.By similarity

GO - Cellular componenti

  1. host cell endoplasmic reticulum Source: UniProtKB-KW
  2. viral outer capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 733733Outer capsid protein VP4PRO_0000369873Add
BLAST
Chaini1 – 228228Outer capsid protein VP8*By similarityPRO_0000369874Add
BLAST
Chaini229 – 733505Outer capsid protein VP5*By similarityPRO_0000369875Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi28 – 281N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi39 – 391N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi120 – 1201N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi162 – 1621N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi189 – 1891N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi301 – 3011N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi379 – 3791N-linked (GlcNAc...); by hostSequence Analysis

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

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

VP4 is a homotrimer.Curated

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni390 – 41021Hydrophobic; possible role in virus entry into host cellSequence AnalysisAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili485 – 51935Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi714 – 7174Poly-Asn

Sequence similaritiesi

Belongs to the rotavirus VP4 family.Curated

Keywords - Domaini

Coiled coil

Family and domain databases

InterProiIPR000416. Haemagglutinin_VP4.
[Graphical view]
PfamiPF00426. VP4_haemagglut. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q65525-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASSLYRQLI SQNYYSTGNE ILLDQQTNKT TVDYVDAGNY TYAQLPPTTW
60 70 80 90 100
GAESTYESAF SAPEITGPYT NTVIKLSDLS DSNVWVLYQK PTSTVKLLKN
110 120 130 140 150
GPESYSWNLA AFELWYGKAN TTVTSDYYSG MTNSEKSVEV DHDSLVLFWN
160 170 180 190 200
EGSTALSNKV INFSWNVGGV LIKLTSNTRI DICMANMDNF TSDSFNWEEW
210 220 230 240 250
THNFPRSASM NIYTDYYLAS VDPYSQIRAL QQPIITTVEM KMVKVKREGS
260 270 280 290 300
INVDEVVSKD SLWQEVRYVR DITLQCKIES EVVKGGGWGY DYTSVAFKTI
310 320 330 340 350
NHTYSYTRAG EAVNAHVTIS FNNLKERSYG GSLPTDFKIG RFDIIDVDTY
360 370 380 390 400
MYIDYWDDSE IFKNMVYVRD LRADMGGFNY SSAMSYYFRI PVGQYPGLHS
410 420 430 440 450
SGVRFTYERS LLSQQFTDQV ALNSMRFVFR ATSSDGWFMT AGNINARRIA
460 470 480 490 500
SGTGFAYSDG YVTETVGTVS FISLIPSNPN YQTPIASSST VRMDLERKIN
510 520 530 540 550
DLRNDFNELA SSVALGDILS LAMSPLTFAN LLESVPAIAS SVKDVAANVM
560 570 580 590 600
KKFKTTKMFK KAAKPKYKEY IIGDLLEDVT NLPRSTTAMD FDDITSAVMV
610 620 630 640 650
STTNRLQLTD VETLSEIVAR SADDFIPNRA YRMIEDGMVH EATPNGVFSY
660 670 680 690 700
DLATLQQRNF DMEKFMQLAS KSPVISAIVD FATLKAMRDT YGVSTDIMYK
710 720 730
LVASDAPTIV SFINNNNPLI RNRIEGLLRQ CRI
Length:733
Mass (Da):82,495
Last modified:November 1, 1996 - v1
Checksum:i67C1B19AFCD1631C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26551 Genomic DNA. Translation: AAB01672.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26551 Genomic DNA. Translation: AAB01672.1 .

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR000416. Haemagglutinin_VP4.
[Graphical view ]
Pfami PF00426. VP4_haemagglut. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Sequence analysis of VP3 and VP4 genes of a bovine group C rotavirus: molecular evidence for a new P type."
    Jiang B., Gentsch J.R., Tsunemitsu H., Saif L.J., Glass R.I.
    Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiVP4_ROTBS
AccessioniPrimary (citable) accession number: Q65525
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 58 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

External Data

Dasty 3