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P11196

- VP4_ROTHD

UniProt

P11196 - VP4_ROTHD

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Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A (strain Human/United States/DS-1/1976 G2-P1B[4]-I2-R2-C2-M2-A2-N2-T2-E2-H2) (RV-A) (Rotavirus A (strain DS1))
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein 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.
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.
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei230 – 2312Cleavage By similarity
Sitei246 – 2472Cleavage By 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 (strain Human/United States/DS-1/1976 G2-P1B[4]-I2-R2-C2-M2-A2-N2-T2-E2-H2) (RV-A) (Rotavirus A (strain DS1))
Taxonomic identifieri10950 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000001457: Genome

Subcellular locationi

Chain Outer capsid protein VP4 : Virion. Host rough endoplasmic reticulum Reviewed prediction
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.
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
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_0000041054Add
BLAST
Chaini1 – 230230Outer capsid protein VP8* By similarityPRO_0000041055Add
BLAST
Chaini247 – 775529Outer capsid protein VP5* By similarityPRO_0000041056Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi56 – 561N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi132 – 1321N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi150 – 1501N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi195 – 1951N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi317 ↔ 379 Reviewed prediction
Glycosylationi324 – 3241N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi583 – 5831N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi589 – 5891N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi592 – 5921N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi599 – 5991N-linked (GlcNAc...); by host Reviewed prediction

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.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

VP4 is a homotrimer Reviewed prediction. 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 Reviewed prediction. 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.

Structurei

Secondary structure

1
775
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi66 – 694
Beta strandi71 – 744
Beta strandi80 – 856
Beta strandi88 – 969
Beta strandi98 – 1003
Beta strandi102 – 1087
Beta strandi110 – 12112
Beta strandi124 – 1329
Beta strandi134 – 14613
Beta strandi152 – 16110
Beta strandi163 – 1697
Beta strandi172 – 1798
Beta strandi184 – 1896
Beta strandi197 – 2004
Beta strandi204 – 2085
Helixi209 – 2113
Helixi212 – 22110

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AENX-ray1.60A/B/C/D/E/F/G/H60-223[»]

Miscellaneous databases

EvolutionaryTraceiP11196.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni247 – 479233Antigen domain By similarityAdd
BLAST
Regioni307 – 3093DGE motif; interaction with ITGA2/ITGB1 heterodimer By similarity
Regioni388 – 40821Hydrophobic; possible role in virus entry into host cell Reviewed predictionAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili483 – 51735 Reviewed predictionAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Belongs to the rotavirus VP4 family.

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.

P11196-1 [UniParc]FASTAAdd to Basket

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MASLIYRQLL TNSYSVDLHD EIEQIGSEKT QSVTVNPGPF AQTRYAPVNW    50
GSWEINDSTT VEPVLDGPYQ PTTFKPPNDY WLLISSNTNG VVYESTNNND 100
FWTAVSSVEP HVSQTNRQYI LFGENKQFNV ENNSDKWKFF ETFTGSSQGN 150
FSNRRTLTSS NRLVGMLKYG GRVWTFHGET PRATTDSSNT ADLNNISIII 200
HSEFYIIPRS QESKCNEYIN NGLPPIQNTR NVVPLSLSSR SIQYKRAQVN 250
EDITISKTSL WKEMQYNRDI IIRFKFGNSI IKLGGLGYKW SEISYKAANY 300
QYSYSRDGEQ VTAHTTCSVN GVNNFSYNGG SLPTDFSISR YEVIKENSYV 350
YIDYWDDSKA FRNMVYVRSL AANLNSVKCT GGSYNFRLPV GKWPIMNGGA 400
VSLHFAGVTL STQFTDFVSL NSLRFRFSLT VDEPSFSIIR TRTINLYGLP 450
AANPNNGNEY YEMSGRFSLI SLVQTNDDYQ TPIMNSVTVR QDLERQLNDL 500
REEFNSLSQE IAMSQLIDLA LLPLDMFSMF SGIKSTIDLT KSMATSVMKK 550
FRKSKLATSI SEMTNSLSDA ASSASRSASI RSNLSTISNW TNTSKSVSNV 600
TDSVNDVSTQ TSTISKKLRL REMITQTEGL SFDDISAAVL KTKIDMSTQI 650
GKNTLPDIVT EASEKFIPKR SYRVLKDDEV MEINTEGKFF AYKVDTLNEI 700
PFDINKFAEL VTDSPVISAI IDFKTLKNLN DNYGITRIEA FNLIKSNPNV 750
LRNFINQNNP IIRNRIEQLI LQCKL 775
Length:775
Mass (Da):87,590
Last modified:April 14, 2009 - v3
Checksum:iA3A11BAFF15EC7C8
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 532SW → HG1 Publication
Sequence conflicti52 – 532SW → HG in ABV53252. 1 Publication
Sequence conflicti106 – 1072SS → IA1 Publication
Sequence conflicti106 – 1072SS → IA in ABV53252. 1 Publication
Sequence conflicti142 – 1443TFT → MFK1 Publication
Sequence conflicti142 – 1443TFT → MFK in ABV53252. 1 Publication
Sequence conflicti150 – 1501N → D in ABV53252. 1 Publication
Sequence conflicti230 – 2301R → S in ABV53252. 1 Publication
Sequence conflicti245 – 2451K → R1 Publication
Sequence conflicti245 – 2451K → R in ABV53252. 1 Publication
Sequence conflicti280 – 2801I → V1 Publication
Sequence conflicti280 – 2801I → V in ABV53252. 1 Publication
Sequence conflicti380 – 3801T → I in ABV53252. 1 Publication
Sequence conflicti397 – 3971N → D in CAD62680. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ540227 Genomic RNA. Translation: CAD62680.1.
EF672577 Genomic RNA. Translation: ABV53252.1.
PIRiB28839. VPXRW4.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ540227 Genomic RNA. Translation: CAD62680.1 .
EF672577 Genomic RNA. Translation: ABV53252.1 .
PIRi B28839. VPXRW4.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2AEN X-ray 1.60 A/B/C/D/E/F/G/H 60-223 [» ]
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P11196.

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. Gentsch J.R.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    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.
  5. "High-resolution molecular and antigen structure of the VP8* core of a sialic acid-independent human rotavirus strain."
    Monnier N., Higo-Moriguchi K., Sun Z.Y., Prasad B.V.V., Taniguchi K., Dormitzer P.R.
    J. Virol. 80:1513-1523(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 60-223.

Entry informationi

Entry nameiVP4_ROTHD
AccessioniPrimary (citable) accession number: P11196
Secondary accession number(s): B3SRS7, Q80P75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 14, 2009
Last modified: February 19, 2014
This is version 97 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

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi