SubmitCancel

Skip Header

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

Q83440

- VP4_ROTMB

UniProt

Q83440 - VP4_ROTMB

(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 A (isolate Mouse/United States/Eb/1982 G16-P10[16]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-E7-Hx) (RV-A)
Status
Reviewed - Annotation score: 4 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
Sitei230 – 2312Cleavage By similarity
Sitei246 – 2472Cleavage By similarity

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 (isolate Mouse/United States/Eb/1982 G16-P10[16]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-E7-Hx) (RV-A)
Taxonomic identifieri578842 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiMus musculus musculus (eastern European house mouse) [TaxID: 39442]

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 – 775775Outer capsid protein VP4PRO_0000368125Add
BLAST
Chaini1 – 230230Outer capsid protein VP8*PRO_0000368126Add
BLAST
Chaini247 – 775529Outer capsid protein VP5*PRO_0000368127Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi32 – 321N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi57 – 571N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi111 – 1111N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi149 – 1491N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi197 – 1971N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi317 ↔ 379 Reviewed prediction
Glycosylationi669 – 6691N-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

ProteinModelPortaliQ83440.
SMRiQ83440. Positions 65-223, 252-521.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni247 – 479233Antigen domain By similarityAdd
BLAST
Regioni307 – 3093DGE motif; interaction with ITGA2/ITGB1 heterodimer By similarity
Regioni388 – 40821Hydrophobic; possible role in virus entry into host cell Reviewed predictionAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili483 – 51735 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi559 – 61557Ser-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.

Q83440-1 [UniParc]FASTAAdd to Basket

« Hide

MASLIYRQLL TNSFTVDLSD EIETIGAEKT KNVTVNPGPF AQTGYAPVNW    50
GPGETSNSTT VEPVLDGPYQ PIAFSPPSEY YILLSPTVPG VVVECTNTVD 100
RWIATIAIEP NVSKTKRTYT LFGITEQLTV ENSYADKWKF IDFLKASTNG 150
SYARYNILLS STKLCAVAKH TDRLYSYIRE TPNAGQAYYA FSHNIFNLTA 200
HCDFYIIPWA QQSLCTQYIN TGLPPIQNTR NVVARHLSAR SIITRRAQAN 250
EDIVVSKTSL WKEMQFNRDI TIRFKFANAI IKSGGLGYKW SEISFKPANY 300
QYTYTRDGEE VTAHTTCSVN GVNNFDFFGG SLPTDFGISR YEVLKENSFV 350
YIDYWDDSQA FRNMVYVRSL AADLNTIECT GGTYEFSLPV GQWPAMTGGA 400
VSLRVAGVTL STQYTDFVSL NSLRFRFRLS VEEPPFSITR TRVSGLYGLP 450
AANPNNGKEY YELAGRFSLI SLVPSNDNYQ TPIMNSVTVR QDLERQLGEL 500
REEFNALSQE IALSQLVDLA LLPLDMFSMF SGIKATLDVA KSMATNVMKK 550
FKSSGLATSV SAMTESLSDA ASSVSRSNTI RSISSTSSAW TDVSSRVADL 600
DNAASTVSTQ TATISRRLRL KEITTQTEGM NFDDISAAVL KIKLDKSAQI 650
APNTLPDIVT EASEKFIPNR SYRIINNNEA FEAGTDGRFF AYRVDTLEEL 700
PFDVQKFANL VTESPVISAI IDFKTLRNLN DNYGISKEQA FNLLRSDPRV 750
LREFINQGNP IIRNRIEQLI MQCKL 775
Length:775
Mass (Da):86,493
Last modified:November 1, 1996 - v1
Checksum:i5162D98EB313BD54
GO

Sequence cautioni

The sequence AAA47356.1 differs from that shown. Reason: Frameshift at position 88.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461A → P in AAA47356. 1 Publication
Sequence conflicti218 – 2181Y → S in AAA47356. 1 Publication
Sequence conflicti234 – 2341A → S in AAA47356. 1 Publication
Sequence conflicti253 – 2542IV → RC in AAA47356. 1 Publication
Sequence conflicti269 – 2691D → N in AAA47356. 1 Publication
Sequence conflicti504 – 5041F → C in AAA47356. 1 Publication
Sequence conflicti537 – 5371L → F in AAA47356. 1 Publication
Sequence conflicti558 – 5581T → A in AAA47356. 1 Publication
Sequence conflicti615 – 6162SR → RQ in AAA47356. 1 Publication
Sequence conflicti666 – 6661F → L in AAA47356. 1 Publication
Sequence conflicti674 – 6752II → TT in AAA47356. 1 Publication
Sequence conflicti749 – 7491R → G in AAA47356. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U08419 Genomic RNA. Translation: AAA50482.1.
L18992 Genomic DNA. Translation: AAA47356.1. Frameshift.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U08419 Genomic RNA. Translation: AAA50482.1 .
L18992 Genomic DNA. Translation: AAA47356.1 . Frameshift.

3D structure databases

ProteinModelPortali Q83440.
SMRi Q83440. Positions 65-223, 252-521.
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. "Comparison of VP4 and VP7 of five murine rotavirus strains."
    Dunn S.J., Burns J.W., Cross T.L., Vo P.T., Ward R.L., Bremont M., Greenberg H.B.
    Virology 203:250-259(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "The outer capsid protein VP4 of murine rotavirus strain Eb represents a tentative new P type."
    Sereno M.M., Gorziglia M.I.
    Virology 199:500-504(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiVP4_ROTMB
AccessioniPrimary (citable) accession number: Q83440
Secondary accession number(s): Q86227
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 72 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 By similarity.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi