Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P11200

- VP4_ROTHT

UniProt

P11200 - VP4_ROTHT

Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A (strain Human/United Kingdom/ST3/1975 G4-P2A[6]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A) (Rotavirus A (strain St. Thomas 3))
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 3 (14 Apr 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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 Human/United Kingdom/ST3/1975 G4-P2A[6]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A) (Rotavirus A (strain St. Thomas 3))
    Taxonomic identifieri10960 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007048: Genome

    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 rough endoplasmic reticulum Source: UniProtKB-SubCell
    2. viral outer capsid Source: UniProtKB-KW

    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 VP4By similarityPRO_0000368146Add
    BLAST
    Chaini1 – 230230Outer capsid protein VP8*Sequence AnalysisPRO_0000041082Add
    BLAST
    Chaini247 – 775529Outer capsid protein VP5*Sequence AnalysisPRO_0000041083Add
    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
    Glycosylationi111 – 1111N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi114 – 1141N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi132 – 1321N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi192 – 1921N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi277 – 2771N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi317 ↔ 379Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi583 – 5831N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi606 – 6061N-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

    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.
    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.

    P11200-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASLIYRQLL TNSYTVELSD EINTIGSEKS QNITINPGPF AQTNYAPVTW    50
    SHGEVNDSTT IEPVLDGPYQ PTSFKPPSDY WILLNPTNQQ VVLEGTNKTD 100
    IWIALLLVEP NVTNQSRQYT LFGETKQITI ENNTNKWKFF EMFRSNVSSE 150
    FQHKRTLTSD TKLAGFLKHY NSVWTFHGET PHATTDYSST SNLSEVETTI 200
    HVEFYIISRS QESKCVEYIN TGLPPMQNTR NIVPVALSSR SVTYQRAQVS 250
    EDIIISKTSL WKEMQYNRDI IIRFKFNNSI IKLGGLGYKW SEISFKAANY 300
    QYNYLRDGEQ VTAHTTCSVN GVNNFSYNGG LLPTHFSISR YEVIKENSYV 350
    YVDYWDDSQA FRNMVYVRSL AANLNSVKCS GGNYNFQMPV GAWPVMSGGA 400
    VSLHFAGVTL STQFTDFVSL NSLRFRFSLT VEEPPFSILR TRVSGLYGLP 450
    ASNPNSGHEY YEIAGRFSLI SLVPSNDDYQ TPIMNSITVR QDLERQLGDL 500
    REEFNSLSQE IAITQLIDLA LLPLDMFSMF SGIKSTIDAA KSMATKVMKK 550
    FKRSGLATSI SELTGSLSNA ASSVSRSSSI RSNISSISEW TDVSEQIAGS 600
    SDSVRNISTQ TSAISRRLRL REITTQTEGM NDIDISAAVL KTKIDRSTHI 650
    RPDTLPDIIT ESSEKFIPKR AYRVLKDDEV MEADVDGKFF AYKVDTFEEV 700
    PFDVDKFVDL VTDSPVISAI IDFKTLKNLN DNYGITRSQA LDLIRSDPRV 750
    LRDFINQNNP IIKNRIEQLI LQCRL 775
    Length:775
    Mass (Da):87,487
    Last modified:April 14, 2009 - v3
    Checksum:i1F9E5AA8C35BE7DD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti49 – 535TWSHG → VLESW(PubMed:2839714)Curated
    Sequence conflicti49 – 535TWSHG → VLESW(PubMed:3018754)Curated
    Sequence conflicti70 – 701Q → R in AAA66952. (PubMed:7530390)Curated
    Sequence conflicti130 – 1301I → V(PubMed:2839714)Curated
    Sequence conflicti130 – 1301I → V(PubMed:3018754)Curated
    Sequence conflicti146 – 1461N → S(PubMed:2839714)Curated
    Sequence conflicti146 – 1461N → S(PubMed:3018754)Curated
    Sequence conflicti175 – 1751T → S(PubMed:2839714)Curated
    Sequence conflicti175 – 1751T → S(PubMed:3018754)Curated
    Sequence conflicti190 – 1901T → A in ABV53292. (PubMed:18786998)Curated
    Sequence conflicti250 – 2501S → N(PubMed:2839714)Curated
    Sequence conflicti250 – 2501S → N(PubMed:3018754)Curated
    Sequence conflicti316 – 3161T → I in ABV53292. (PubMed:18786998)Curated
    Sequence conflicti331 – 3311L → S in AAA66952. (PubMed:7530390)Curated
    Sequence conflicti335 – 3351H → D in ABV53292. (PubMed:18786998)Curated
    Sequence conflicti338 – 3381I → V(PubMed:2839714)Curated
    Sequence conflicti353 – 3531D → N(PubMed:2839714)Curated
    Sequence conflicti361 – 3611F → L(PubMed:2839714)Curated
    Sequence conflicti388 – 3881M → L(PubMed:2839714)Curated
    Sequence conflicti413 – 4131Q → K(PubMed:2839714)Curated
    Sequence conflicti474 – 4741P → L in AAA66952. (PubMed:7530390)Curated
    Sequence conflicti565 – 5651G → R(PubMed:2839714)Curated
    Sequence conflicti589 – 5891E → V(PubMed:7530390)Curated
    Sequence conflicti589 – 5891E → V in ABV53292. (PubMed:18786998)Curated
    Sequence conflicti614 – 6141Missing(PubMed:2839714)Curated
    Sequence conflicti632 – 6321D → I(PubMed:2839714)Curated
    Sequence conflicti732 – 7321N → T in ABV53292. (PubMed:18786998)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33895 Genomic RNA. Translation: AAA66952.1.
    EF672612 Genomic RNA. Translation: ABV53292.1.
    PIRiH28839. VPXRWT.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33895 Genomic RNA. Translation: AAA66952.1 .
    EF672612 Genomic RNA. Translation: ABV53292.1 .
    PIRi H28839. VPXRWT.

    3D structure databases

    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. "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. "Identification of two independent neutralization domains on the VP4 trypsin cleavage products VP5* and VP8* of human rotavirus ST3."
      Padilla-Noriega L., Dunn S.J., Lopez S., Greenberg H.B., Arias C.F.
      Virology 206:148-154(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Group A human rotavirus genomics: evidence that gene constellations are influenced by viral protein interactions."
      Heiman E.M., McDonald S.M., Barro M., Taraporewala Z.F., Bar-Magen T., Patton J.T.
      J. Virol. 82:11106-11116(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    4. "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_ROTHT
    AccessioniPrimary (citable) accession number: P11200
    Secondary accession number(s): B3SRW7, Q86201
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: April 14, 2009
    Last modified: October 1, 2014
    This is version 87 of the entry and version 3 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