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Q06894

- VP4_ROTD9

UniProt

Q06894 - VP4_ROTD9

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Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A (isolate Dog/United States/K9/1981 G3-P5A[3]-I3-R3-C2-M3-A9-N2-T3-E3-H6) (RV-A)
Status
Reviewed - 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. 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 (isolate Dog/United States/K9/1981 G3-P5A[3]-I3-R3-C2-M3-A9-N2-T3-E3-H6) (RV-A)
Taxonomic identifieri557232 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiCanis familiaris (Dog) (Canis lupus familiaris) [TaxID: 9615]

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_0000041033Add
BLAST
Chaini1 – 231231Outer capsid protein VP8* Reviewed predictionPRO_0000041034Add
BLAST
Chaini248 – 776529Outer capsid protein VP5* Reviewed predictionPRO_0000041035Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi17 – 171N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi32 – 321N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi56 – 561N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi97 – 971N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi111 – 1111N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi132 – 1321N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi151 – 1511N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi183 – 1831N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi198 – 1981N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi318 ↔ 380 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

ProteinModelPortaliQ06894.
SMRiQ06894. Positions 64-224, 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.

Q06894-1 [UniParc]FASTAAdd to Basket

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MASLIYRQLL TNSYTVNLSD EIQEIGSTKT QNTTINPGPF AQTGYAPVNW    50
GPGETNDSTT IEPVLDGPYQ PTSFNPPVGY WMLLSPTAAG VIVEGTNNTD 100
RWLATILIEP NVTSQQRTYT IFGVQEQITV ENTSQTQWRF VDVSKTTQNG 150
NYSQHGPLLS TPKLYAVMKY GGRIHTYSGQ TPNATTGYYS ATNYDSVNMT 200
TFCDFYIIPR SEESKCTEYI NNRLPPIQNT RNIVPLALSA RNVISLKAQS 250
NEDIVVSKTS LWKEMQYNRD ITIRFKFANS IVKSGGLGYK WSEISFKPAN 300
YQYTYMRDGE EVTAHTTCSV NGMNDFSFNG GSLPTDFVIS RYEVIKENSY 350
VYIDYWDDSQ AFRNMVYVRS LAANLNSVIC TGGDYNFALP VGQWPYMTGG 400
AVSLHSAGVT LSTQFTDFVS LNSLRFRFRL AVEEPSFAIM RTRVSGLYGL 450
PAANPNNGRE YYEIAGRFSL ISLVPSNDNY QTPIANSVTV RQDLERQLGE 500
LREEFNALSQ EIAMSQLIDL ALLPLDMFSM FSGIKSTIDA AKSIATNVMK 550
KFKKSSLASS VSTLTDSLSD AASSVSRGSS IRSVGSSVSA WTDVSTQITD 600
VSSSVSSIST QTSTISRRLR LKEMATQTEG MNFDDISAAV LKTKIDKSIQ 650
ISPNTLPDIV TEASEKFIPN RAYRVINNDE VLEAGTDGKF FAYRVDTFEE 700
IPFDVQKFAD LVTDSPVISA IIDFKTLKNL NDNYGIGKQQ AFNLLRSDPR 750
VLREFINQNN PIIRNRIEQL IMQCRL 776
Length:776
Mass (Da):86,469
Last modified:October 1, 1996 - v1
Checksum:iEBD22430F21D5F5F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171N → D in BAA02664. 1 Publication
Sequence conflicti73 – 731S → T in BAA02664. 1 Publication
Sequence conflicti381 – 3811T → A in BAA02664. 1 Publication
Sequence conflicti384 – 3896DYNFAL → HYHFAH in BAA02664. 1 Publication
Sequence conflicti486 – 4861N → Y in BAA02664. 1 Publication
Sequence conflicti682 – 6821L → F in BAA02664. 1 Publication
Sequence conflicti685 – 6851G → S in BAA02664. 1 Publication
Sequence conflicti689 – 6891K → R in BAA02664. 1 Publication
Sequence conflicti751 – 7511V → E in BAA02664. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D14725 mRNA. Translation: BAA03545.1.
D13400 mRNA. Translation: BAA02664.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D14725 mRNA. Translation: BAA03545.1 .
D13400 mRNA. Translation: BAA02664.1 .

3D structure databases

ProteinModelPortali Q06894.
SMRi Q06894. Positions 64-224, 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. "A new serotype of the outer capsid protein VP4 shared by an unusual human rotavirus strain Ro1845 and canine rotaviruses."
    Isegawa Y., Nakagomi O., Hoshino Y., Aboudy Y., Shif I., Silberstein I., Nakagomi T., Ueda S., Sears J., Flores J.
    J. Gen. Virol. 74:2771-2774(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Species specificity and interspecies relatedness in VP4 genotypes demonstrated by VP4 sequence analysis of equine, feline, and canine rotavirus strains."
    Taniguchi K., Urasawa T., Urasawa S.
    Virology 200:390-400(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiVP4_ROTD9
AccessioniPrimary (citable) accession number: Q06894
Secondary accession number(s): Q86179
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 79 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-dependent in cell culture conditions By similarity.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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