Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P15155

- VP4_ROTGI

UniProt

P15155 - VP4_ROTGI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus B (isolate Rat/United States/IDIR/1984) (RV-B) (Rotavirus B (isolate infectious diarrhea of infant rats))
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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei207 – 2082CleavageSequence Analysis
Sitei214 – 2152CleavageSequence 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 B (isolate Rat/United States/IDIR/1984) (RV-B) (Rotavirus B (isolate infectious diarrhea of infant rats))
Taxonomic identifieri28877 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Rattus norvegicus (Rat) [TaxID: 10116]

Subcellular locationi

Chain 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
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 – 751751Outer capsid protein VP4PRO_0000149539Add
BLAST
Chaini1 – 207207Outer capsid protein VP8*Sequence AnalysisPRO_0000369840Add
BLAST
Chaini215 – 751537Outer capsid protein VP5*Sequence AnalysisPRO_0000369841Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi23 – 231N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi141 – 1411N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi211 – 2111N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi276 – 2761N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi292 – 2921N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi528 – 5281N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi678 – 6781N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi699 – 6991N-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

Structurei

3D structure databases

ProteinModelPortaliP15155.
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.

P15155-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLAYLRREWQ SYGETVIAEG TFNSTSSDSS QSEKPIKTDG RYCYQAEIGR
60 70 80 90 100
NAYSMDARGF MLGESDRHVD TTQFLPYTGY ITDGIKYCNI EPPCGTLLRM
110 120 130 140 150
HFDVSGDVSV DMHRVASIYV EVDSVTYDGS QYTIRGYRDR NLTATETQKK
160 170 180 190 200
LIFYGFRKLG MIGMTGNGRV MLTSTIIQKI SYKHQFTFQM HSESYVWGPC
210 220 230 240 250
SGRIKTRVQG NDSRIIIYEQ EDGFWKILKE TLWIKLKPYF KPYGTMGGAF
260 270 280 290 300
KNWLIDSGFE KHEYTYSYER DGQVVNATTV TYVKPTGKAG INQSWRPATD
310 320 330 340 350
YNGQFTVLQP EDEFSVWYFE DKWQISQAIY AKNFQSDSQV EGELTNNGAL
360 370 380 390 400
IFKMNYIPSL AGITNKGGKV KYRYISGGFA QIDTSRHTGL AIILNFKCYG
410 420 430 440 450
KKFYADNNNY PVDNALNPYI CYIGDSYTLS GGTHYRQGAC AGFAAGYDDE
460 470 480 490 500
ITEHDMTISY TVMKPSDPDF VTGGDNYGQT VTSDIERSIR DLQDQINSIL
510 520 530 540 550
AEMNIQQVTS AVFTAITNLG ELPSLFSNIT KVFNRAKDNI KKLRSRSNSD
560 570 580 590 600
ISPIGATKII DKTTLETPQL SVINRMPEEY ELGIIYNSMR TRKLIDERKH
610 620 630 640 650
DFDTFAVATE MELPYISKVN TLTKEFKDYL KKPGLLSNDD VAVQIDPMNN
660 670 680 690 700
RLSVLRRKYA DIIEYKIDPE LAHEVLSNMS NSATRSLFSL NVRKQIAMNN
710 720 730 740 750
SFSEPTFSQI IDRMFDDGQL IDVLNNLNRE TATELFDEFL TRIKSMLVKM

S
Length:751
Mass (Da):85,558
Last modified:April 1, 1990 - v1
Checksum:i756A33227C065709
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16949 Genomic RNA. Translation: CAA34823.1.
PIRiA33093. WMXRGB.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16949 Genomic RNA. Translation: CAA34823.1 .
PIRi A33093. WMXRGB.

3D structure databases

ProteinModelPortali P15155.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

ProtoNeti Search...

Publicationsi

  1. "The complete nucleic acid sequence of gene segment 3 of the IDIR strain of group B rotavirus."
    Sato S., Yolken R.H., Eiden J.J.
    Nucleic Acids Res. 17:10113-10113(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiVP4_ROTGI
AccessioniPrimary (citable) accession number: P15155
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 29, 2014
This is version 69 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