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P12474

- VP4_ROTBU

UniProt

P12474 - VP4_ROTBU

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Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A (strain Cow/United Kingdom/UK/1975 G6-P7[5]-I2-R2-C2-M2-A3-N2-T7-E2-H3) (RV-A)
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. According to the considered strain, VP4 seems to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1 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. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment By similarity.
VP8* forms the head of the spikes. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei231 – 2322Cleavage By similarity
Sitei247 – 2482Cleavage Reviewed prediction

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 A (strain Cow/United Kingdom/UK/1975 G6-P7[5]-I2-R2-C2-M2-A3-N2-T7-E2-H3) (RV-A)
Taxonomic identifieri10934 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiBos taurus (Bovine) [TaxID: 9913]
ProteomesiUP000008657: Genome

Subcellular locationi

Chain Outer capsid protein VP4 : Virion By similarity. Host rough endoplasmic reticulum Reviewed prediction
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.
Chain Outer capsid protein VP8* : Virion
Note: Outer capsid protein By similarity.
Chain Outer capsid protein VP5* : Virion
Note: Outer capsid protein By similarity.

GO - Cellular componenti

  1. host cell rough endoplasmic reticulum Source: UniProtKB-SubCell
  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 – 776776Outer capsid protein VP4PRO_0000041030Add
BLAST
Chaini1 – 231231Outer capsid protein VP8* Reviewed predictionPRO_0000041031Add
BLAST
Chaini248 – 776529Outer capsid protein VP5* Reviewed predictionPRO_0000041032Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi17 – 171N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi56 – 561N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi132 – 1321N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi183 – 1831N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi318 ↔ 380 Reviewed prediction
Glycosylationi507 – 5071N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi593 – 5931N-linked (GlcNAc...); by host Reviewed prediction

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.

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

VP4 is a homotrimer Reviewed prediction. VP4 adopts a dimeric appearance above the capsid surface, while forming a trimeric base anchored inside the capsid layer. Only hints of the third molecule are observed above the capsid surface. It probably performs a series of molecular rearrangements during viral entry. Prior to trypsin cleavage, it is flexible. The priming trypsin cleavage triggers its rearrangement into rigid spikes with approximate two-fold symmetry of their protruding parts. After an unknown second triggering event, cleaved VP4 may undergo another rearrangement, in which two VP5* subunits fold back on themselves and join a third subunit to form a tightly associated trimer, shaped like a folded umbrella. VP5* is a homotrimer Reviewed prediction. The trimer is coiled-coil stabilized by its C-terminus, however, its N-terminus, known as antigen domain or "body", seems to be flexible allowing it to self-associate either as a dimer or a trimer. The two- to three-fold reorganization and fold-back of VP5* may be linked to membrane penetration, by exposing its hydrophobic region. Interacts with host ITGA2 (via ITAG2 I-domain); this interaction occurs when ITGA2 is part of the integrin heterodimer ITGA2/ITGB1. Interacts with host integrin heterodimer ITGA4/ITGB1 and ITGA4/ITGB7 By similarity.

Structurei

3D structure databases

ProteinModelPortaliP12474.
SMRiP12474. Positions 65-224, 253-522.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni248 – 480233Antigen domain By similarityAdd
BLAST
Regioni308 – 3103DGE motif; interaction with ITGA2/ITGB1 heterodimer By similarity
Regioni389 – 40921Hydrophobic; possible role in virus entry into host cell Reviewed predictionAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili484 – 51835 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi560 – 61657Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the rotavirus VP4 family.

Keywords - Domaini

Coiled coil

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000416. Haemagglutinin_VP4.
[Graphical view]
PfamiPF00426. VP4_haemagglut. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P12474-1 [UniParc]FASTAAdd to Basket

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MASLIYRQLL ANSYAVNLSD EIQSVGSGKN QRVTVNPGPF AQTGYAPVNW    50
GPGEVNDSTV VQPVLDGPYQ PAPFDLPVGN WMLLAPTRPG VVVEGTDNSG 100
RWLSVILIEP GVASETRTYM MFGSSKQVVV SNVSDTKWKF VEMVKTAVDG 150
DYAEWGTLLS DTKLYGMMKY GRRLFIYEGE TPNATTKGYF ITNYASAEVR 200
PYSDFYIISR SQESACTEYI NNGLPPIQNT RNVVPVAISS RSIKPREVQA 250
NEDIVVSKTS LWKEMQYNRD IIIRFKFDNS IIKSGGLGYK WAEISFKAAN 300
YQYNYMRDGE EVTAHTTCSV NGVNDFSFNG GSLPTDFAIS RYEVIKENSY 350
VYVDYWDDSQ AFRNMVYVRS LAANLNDVMC SGGHYSFALP VGQWPVMKGG 400
AVTLHTAGVT LSTQFTDFVS LNSLRFRFRL AVEEPSFTIT RTRVSKLYGL 450
PAANPNGGKE YYEVAGRFSF ISLVPSNDDY QTPIMNSVTV RQDLERRLNE 500
LREEFNNLSQ EIAVSQLIDL AMLPLDMFSM FSGIESTVNA AKSMATNVMR 550
KFKSSKLASS VSMLTDSLSD AASSIARSTS VRSIGSTASA WANISEQTQD 600
AVSEVATISS QVSQISGRLR LKEITTQTEG MNFDDISAAV LKAKIDRSIQ 650
VDQNALPDVI TEASEKFIRN RAYRVIDGDE AFEAGTDGRF FAYKVETLEE 700
MPFNMEKFAD LVTNSPVISA IIDFKTLKNL NDNYGITREQ AFNLLRSDPK 750
VLRGFIDQNN PIIKNRIEQL IMQCRL 776
Length:776
Mass (Da):86,466
Last modified:October 1, 1989 - v1
Checksum:iE8BB6975CC3BA13A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M22306 Genomic RNA. Translation: AAA47318.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M22306 Genomic RNA. Translation: AAA47318.1 .

3D structure databases

ProteinModelPortali P12474.
SMRi P12474. Positions 65-224, 253-522.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000416. Haemagglutinin_VP4.
[Graphical view ]
Pfami PF00426. VP4_haemagglut. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of UK bovine rotavirus segment 4: possible host restriction of VP3 genes."
    Kantharidis P., Dyall-Smith M.L., Tregear G.W., Holmes I.H.
    Virology 166:308-315(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiVP4_ROTBU
AccessioniPrimary (citable) accession number: P12474
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: February 19, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

In group A rotaviruses, VP4 defines the P serotype.
This strain has been shown to be sialic acid-independent in cell culture conditions.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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