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Q96642

- VP4_ROTBV

UniProt

Q96642 - VP4_ROTBV

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Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A (isolate Cow/United States/VMRI/1988 G6-Px[5]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-H3) (RV-A)
Status
Reviewed - Annotation score: 4 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.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.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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei231 – 2322CleavageBy similarity
Sitei247 – 2482CleavageBy 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 Cow/United States/VMRI/1988 G6-Px[5]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-H3) (RV-A)
Taxonomic identifieri10935 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiBos taurus (Bovine) [TaxID: 9913]

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
Note: Outer capsid protein.By similarity
Chain Outer capsid protein VP5* : Virion
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 – 776776Outer capsid protein VP4PRO_0000368095Add
BLAST
Chaini1 – 231231Outer capsid protein VP8*PRO_0000368096Add
BLAST
Chaini248 – 776529Outer capsid protein VP5*PRO_0000368097Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi56 – 561N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi132 – 1321N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi183 – 1831N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi318 ↔ 380Sequence Analysis
Glycosylationi507 – 5071N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi593 – 5931N-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

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

VP4 is a homotrimer Potential. 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 Potential. 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.By similarityCurated

Structurei

3D structure databases

ProteinModelPortaliQ96642.
SMRiQ96642. Positions 65-224, 253-522.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni248 – 480233Antigen domainBy similarityAdd
BLAST
Regioni308 – 3103DGE motif; interaction with ITGA2/ITGB1 heterodimerBy similarity
Regioni389 – 40921Hydrophobic; possible role in virus entry into host cellSequence AnalysisAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili484 – 51835Sequence AnalysisAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Belongs to the rotavirus VP4 family.Curated

Keywords - Domaini

Coiled coil

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
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.

Q96642-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASLIYRQLL ANSYAVDLSD EIQSVGSEKN QRVTVNPGPF AQTGYAPVNW
60 70 80 90 100
GPGEVNDSTV VQPVLDGPYQ PASFDLPVGN WMLLAPTGPG VVVEGTDNSG
110 120 130 140 150
RWLSVILIEP GVTSETRTYT MFGSSKQVLV SNASDTKWKF VEMMKTAVDG
160 170 180 190 200
DYAEWGTLLS DTKLYGMMKY GERLFIYEGE TPNATTKGYI VTNYASVEVR
210 220 230 240 250
PYSDFYIISR SQESACTEYI NNGLPPIQNT RNVVPVAISS RSIEPRRVQA
260 270 280 290 300
NEDIVVSKTS LWKEMQYNRD IIIRFRFDNS IIKSGGLAYK WAEISFKAAN
310 320 330 340 350
YQYNYMKDGE EVTAHTTCSV NGVNDFSFNG GSLPTDFAIS RYEVIKENSY
360 370 380 390 400
VYVDYWDDSQ TFRNMVYVRS LAANLNDVMC SGGDYSFALP AGQWPVMKGG
410 420 430 440 450
AATLHTAGVT LSTQFTDYVS LNSLRFRFRL AVEEPSFTIT RTRVSKLYGL
460 470 480 490 500
PAANPNGGRE YYEVAGRFSL ISLVPSNDDY QAPIMNSVTV RQDLERRLNE
510 520 530 540 550
LREEFNNLSQ EIAVSQLIDL AMLPLDMFSM FSGIEGTVNA PQSMATNVMR
560 570 580 590 600
KFKSSKLASS VSMLTDSLSD AASSIARSTS IRSIGSAASA WANISEQTQD
610 620 630 640 650
AVNEVATISS QVSQISGKLR LKEITTPTEG MNFDDISAAV LKAKIDRSIQ
660 670 680 690 700
VDPNALPDVI TEASEKFIRN RAYRVIDGDE SFEAGTGGRF FANKVETLEE
710 720 730 740 750
MPFNIEKFAD LVTHSPVISA IIDFKTLKNL NDNYGITREQ AFNLLRSNPK
760 770
VLRGFIDPNN PIIKNRIEQL IMQCRL
Length:776
Mass (Da):86,173
Last modified:February 1, 1997 - v1
Checksum:i861E97A2AFEFDEAB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U53923 mRNA. Translation: AAB18952.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U53923 mRNA. Translation: AAB18952.1 .

3D structure databases

ProteinModelPortali Q96642.
SMRi Q96642. 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 IPR013320. ConA-like_dom.
IPR000416. Haemagglutinin_VP4.
[Graphical view ]
Pfami PF00426. VP4_haemagglut. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The VP4 and VP7 of bovine rotavirus VMRI are antigenically and genetically closely related to P-type 5, G-type 6 strains."
    Mummidi S., Brooks M.A., Paul P.S., Lyoo Y.S., Zaberezhny A.D.
    Vet. Microbiol. 51:241-255(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiVP4_ROTBV
AccessioniPrimary (citable) accession number: Q96642
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 1, 1997
Last modified: October 29, 2014
This is version 74 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.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3