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P11194

- VP4_ROTHV

UniProt

P11194 - VP4_ROTHV

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Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A (isolate Human/Italy/VA70/1975 G4-P1A[8]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-E1-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).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
Sitei230 – 2312CleavageBy similarity
Sitei246 – 2472CleavageBy 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 Human/Italy/VA70/1975 G4-P1A[8]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-E1-Hx) (RV-A)
Taxonomic identifieri10961 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiHomo sapiens (Human) [TaxID: 9606]

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 – 775775Outer capsid protein VP4PRO_0000041087Add
BLAST
Chaini1 – 230230Outer capsid protein VP8*Sequence AnalysisPRO_0000041088Add
BLAST
Chaini247 – 775529Outer capsid protein VP5*Sequence AnalysisPRO_0000041089Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi32 – 321N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi56 – 561N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi97 – 971N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi129 – 1291N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi132 – 1321N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi195 – 1951N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi317 ↔ 379Sequence Analysis
Glycosylationi324 – 3241N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi577 – 5771N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi583 – 5831N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi589 – 5891N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi592 – 5921N-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

ProteinModelPortaliP11194.
SMRiP11194. Positions 64-223, 252-521.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni247 – 479233Antigen domainBy similarityAdd
BLAST
Regioni307 – 3093DGE motif; interaction with ITGA2/ITGB1 heterodimerBy similarity
Regioni388 – 40821Hydrophobic; possible role in virus entry into host cellSequence AnalysisAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili483 – 51735Sequence AnalysisAdd
BLAST

Compositional bias

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

P11194-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASLIYRQLL TNSYSVDLHD EIEQIGSEKT QNVTINPGPF AQTRYAPVNW
60 70 80 90 100
GHGEINDSTT LEPILDGPYQ PTTFTPPNDY WILINSNTNG VVYESTNNSD
110 120 130 140 150
FWTAVVAIEP HVNPVDRQYT IFGESKQFNV SNNTNKWKFF EMFISSSQNE
160 170 180 190 200
FYNRRTLTSD TRLVGILKYG GRVWTFHGET PRATTDSSST ANLNNISITI
210 220 230 240 250
HSEFYIIPRS QESKCNEYIN NGLPPIQNTR NVVPLPLSSR SIQYKRAQVN
260 270 280 290 300
EDIIVSKTSL WKEMQYYRDI IIRFKFGNSI VKVGGLGYKW SEISYKAANY
310 320 330 340 350
QYNYLRDGEQ VTAHTTCSVN GVNNFSYNGG SLPTDFGISR YEVIKENSYV
360 370 380 390 400
YVDYWDDSKA FRNMVYVRSL AANLNSVKCT GGSYDFSIPV GAWPVMNGGA
410 420 430 440 450
VSLHFDGVTL STQFTDFVSL NSLRFRLSLT VDEPSFSIMR TRIVNLFGFP
460 470 480 490 500
AANPNNGNEY YEISGRFSLI SLVPTNDDYQ TPIMNSVTVR QDLERQLTDL
510 520 530 540 550
REEFNSLSQE IAMAQLIDLA LLPSDMFSMF SGIKSTIDLT KSMATSVMKK
560 570 580 590 600
FRKSKLATSI SEMTNSLSDA ASSASRNVSI RSNLSAISNW TNVSNDVSNV
610 620 630 640 650
ADSLNDVSTQ TSTISKKLRL KEMITQTEGM SFDDISAAVL KTKIDMSTQI
660 670 680 690 700
GKNTLPDIVT EASEKFIPKR SYRILKDDEV MEINTEGKFF AYKINTFDEV
710 720 730 740 750
PFDVNKFAEL VTDSPVISAI IDFKTLKNLN DNYGITRTEA FNLIKSNPTM
760 770
LRNFINQNHP IIRNRIEQLI LQCRL
Length:775
Mass (Da):87,610
Last modified:November 1, 1990 - v2
Checksum:i0ACFB59F31C728A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ540229 Genomic RNA. Translation: CAD62682.1.
PIRiD28839. VPXRW6.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ540229 Genomic RNA. Translation: CAD62682.1 .
PIRi D28839. VPXRW6.

3D structure databases

ProteinModelPortali P11194.
SMRi P11194. Positions 64-223, 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 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. "Sequence of the fourth gene of human rotaviruses recovered from asymptomatic or symptomatic infections."
    Gorziglia M., Green K.Y., Nishikawa K., Taniguchi K., Jones R.W., Kapikian A.Z., Chanock R.M.
    J. Virol. 62:2978-2984(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. Gentsch J.R.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "Conservation of amino acid sequence of VP8 and cleavage region of 84-kDa outer capsid protein among rotaviruses recovered from asymptomatic neonatal infection."
    Gorziglia M., Hoshino Y., Buckler-White A., Blumentals I., Glass R., Flores J., Kapikian A.Z., Chanock R.M.
    Proc. Natl. Acad. Sci. U.S.A. 83:7039-7043(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-280.

Entry informationi

Entry nameiVP4_ROTHV
AccessioniPrimary (citable) accession number: P11194
Secondary accession number(s): Q70UN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1990
Last modified: October 29, 2014
This is version 92 of the entry and version 2 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.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3