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P39034

- VP4_ROTF1

UniProt

P39034 - VP4_ROTF1

Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A (isolate Cat/Japan/FRV-1/1986 G3-P3[9]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-E3-Hx) (RV-A) (Rotavirus A (isolate FRV1))
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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 (isolate Cat/Japan/FRV-1/1986 G3-P3[9]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-E3-Hx) (RV-A) (Rotavirus A (isolate FRV1))
    Taxonomic identifieri39009 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusunclassified rotaviruses
    Virus hostiFelis catus (Cat) (Felis silvestris catus) [TaxID: 9685]

    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_0000041036Add
    BLAST
    Chaini1 – 231231Outer capsid protein VP8*Sequence AnalysisPRO_0000041037Add
    BLAST
    Chaini248 – 775528Outer capsid protein VP5*Sequence AnalysisPRO_0000041038Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi17 – 171N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi32 – 321N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi97 – 971N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi132 – 1321N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi183 – 1831N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi198 – 1981N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi318 ↔ 380Sequence Analysis
    Glycosylationi567 – 5671N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi613 – 6131N-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

    ProteinModelPortaliP39034.
    SMRiP39034. Positions 65-224, 253-521.
    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 – 61556Ser-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.

    P39034-1 [UniParc]FASTAAdd to Basket

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    MASLIYRQLL SNSYVTNISD EVNEIGTKKT TNVTVNPGPF AQTGYAPVDW    50
    GHGELPDSTL VQPTLDGPYQ PTSLNLPVDY WMLIAPTREG RVAEGTNTTD 100
    RWFACVLVEP NVQNTQRQYV LDGQNVQLQV SNDSSTSWKF ILFIKLTPDG 150
    TYTQYSTLST PHKLCSWMKR DNRVYWYQGS SPNASESYYL TINNDNSNVS 200
    SDAEFYLIPQ SQTAMCTQYI NNGLPPIQNT RNIVPVNIAS RQIKDIRAQM 250
    NEDIVISKTS LWKEMQYNRD IIIRFKFANS IIKSGGLGYK WSEISFKPMN 300
    YQYTYTRDGE EVTAHTTCSV NGVNDFNYNG GTLPTDFAIS RFEVIKENSY 350
    VYVDYWDDSQ AFRNMVYVRS LAANLNDVVC SGGSYSFALP VGNHPVMSGG 400
    AVTLTSAGVT LSTQYTDYVS LNSLRFRFRL AVSEPSFSIS RTRMSGIYGL 450
    PAVNPNNNAE YYEIAGRFSL ISLVPTNDDY QTPIANSVTV RQDLERQLGE 500
    LREEFNSLSQ EIAVSQLIDL ATLPLDMFSM FSGIKSTVEA VKSMTTNVMK 550
    RFKTSSLANA ISDLTSNMSE AASSVRLTSV RSIGTVTLPR ARVSLQVSDD 600
    LRSMQDVSTQ VSNVSRNLRL KEFTTQTDTL SFDDISAAVL KTKLDKSTQI 650
    SQQTMPDIIA ESSEKFIPKR SYRIVDEDTA FETGIDGTFY AYKVDTFNEI 700
    PFDMERFNKL ITDSPVLSAI IDFKTLKNLN DNYGITKKQA MELLHSNPKT 750
    LKEFINNNNP IIRNRIENLI SQCRL 775
    Length:775
    Mass (Da):87,139
    Last modified:February 1, 1995 - v1
    Checksum:i8C22E881D82F2823
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10971 mRNA. Translation: BAA01748.1.
    PIRiJQ1639.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10971 mRNA. Translation: BAA01748.1 .
    PIRi JQ1639.

    3D structure databases

    ProteinModelPortali P39034.
    SMRi P39034. Positions 65-224, 253-521.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi 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 VP4 sequence highly conserved in human rotavirus strain AU-1 and feline rotavirus strain FRV-1."
      Isegawa Y., Nakagomi O., Nakagomi T., Ueda S.
      J. Gen. Virol. 73:1939-1946(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiVP4_ROTF1
    AccessioniPrimary (citable) accession number: P39034
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 78 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-independent in cell culture conditions.By similarity

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3