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)

P17465

- VP4_ROTBN

UniProt

P17465 - VP4_ROTBN

Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A (strain Cow/United States/NCDV-Lincoln/1969 G6-P6[1]-I2-R2-C2-M2-Ax-N2-T6-E2-Hx) (RV-A) (Rotavirus A (strain Nebraska calf diarrhea virus))
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      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
    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

    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 Cow/United States/NCDV-Lincoln/1969 G6-P6[1]-I2-R2-C2-M2-Ax-N2-T6-E2-Hx) (RV-A) (Rotavirus A (strain Nebraska calf diarrhea virus))
    Taxonomic identifieri36439 [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 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 VP4PRO_0000041123Add
    BLAST
    Chaini1 – 231231Outer capsid protein VP8*Sequence AnalysisPRO_0000041124Add
    BLAST
    Chaini248 – 775528Outer capsid protein VP5*Sequence AnalysisPRO_0000041125Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi56 – 561N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi97 – 971N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi132 – 1321N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi151 – 1511N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi183 – 1831N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi198 – 1981N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi318 ↔ 380Sequence Analysis
    Glycosylationi456 – 4561N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi507 – 5071N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi596 – 5961N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi602 – 6021N-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

    ProteinModelPortaliP17465.
    SMRiP17465. Positions 64-224, 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.
    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.

    P17465-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASLIYRQLL TNSYTVELSD EIQEIGSTKT QDVTVNPGPF AQTNYAPVNW    50
    GPGETNDSTT VEPVLDGPYQ PTTFNPPVSY WMLLAPTNAG VVVEGTNNTN 100
    RWLATILIEP NVQQVERTYT LFGQQVQVTV SNDSQTKWKF VDLSKQTQDG 150
    NYSQHGSLLS TPKLYGVMKH GGKIYTYNGE TPNATTGYYS TTNFDTVNMT 200
    AYCDFYIIPL AQEAKCTEYI NNGLPPIQNT RNIVPVSIVS RNIVYTRAQP 250
    NQDIVVSKTS LWKEMQYNRD IVIRFKFANS IIKSGGLGYK WSEVSFKPAN 300
    YQYTYTRDGE EVTAHTTCSV NGINDFNYNG GSLPTDFVIS KYEVIKENSF 350
    VYIDYWDDSQ AFRNMVNVRS LAADLNSVMC TGGDYSFALP VGNYPVMTGG 400
    AVSLHSAGVT LSTQFTDFVS LNSLRFRFRL SVEEPPFSIL RTRVSGLYGL 450
    PAARPNNSQE YYEIAGRFSL ISLVPSNDDY QTPIINSVTV RQDLERQLGE 500
    LRDEFNNLSQ QIAMSQLIDL ALLPLDMFSM FSGIKSTIDA AKSMATNVMK 550
    RFKKSSLANS VSTLTNSLSD AASSISRSAS VRSVSSTASA WTEVSNITSD 600
    INVTTSSIST QTSTISRRLR LKEMATQTDG MNFDDISAAV LKTKIDKSTQ 650
    LNTNTLPEIV TEASEKFIPN RAYRVKDDEV LEASTDGKYF AYKVETFEEI 700
    PFDVQKFADL VTDSPVISAI IDFKTLKNLN DNYGISRQQA LNLLRSDPRV 750
    LREFINQDNP IIRNRIESLI MQCRL 775
    Length:775
    Mass (Da):86,549
    Last modified:August 1, 1990 - v1
    Checksum:iF5D28332747FD9AB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti676 – 6761K → IK in BAC85485. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB119636 Genomic RNA. Translation: BAC85485.1.
    PIRiC31159. VPXRT2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB119636 Genomic RNA. Translation: BAC85485.1 .
    PIRi C31159. VPXRT2.

    3D structure databases

    ProteinModelPortali P17465.
    SMRi P17465. 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. "Comparative analysis of the VP3 gene of divergent strains of the rotaviruses simian SA11 and bovine Nebraska calf diarrhea virus."
      Nishikawa K., Taniguchi K., Torres A., Hoshino Y., Green K.Y., Kapikian A.Z., Chanock R.M., Gorziglia M.
      J. Virol. 62:4022-4026(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "VP4 gene of bovine rotavirus."
      Homma S., Hoshino Y.
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiVP4_ROTBN
    AccessioniPrimary (citable) accession number: P17465
    Secondary accession number(s): Q75Z90
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 83 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, and integrin-dependent in cell culture conditions.

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3