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P11200

- VP4_ROTHT

UniProt

P11200 - VP4_ROTHT

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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: 3 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.
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 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 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 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
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 VP4 By similarity
PRO_0000368146Add
BLAST
Chaini1 – 230230Outer capsid protein VP8* Reviewed prediction
PRO_0000041082Add
BLAST
Chaini247 – 775529Outer capsid protein VP5* Reviewed prediction
PRO_0000041083Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi32 – 321N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi56 – 561N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi97 – 971N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi111 – 1111N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi114 – 1141N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi132 – 1321N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi192 – 1921N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi277 – 2771N-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
Glycosylationi606 – 6061N-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

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.

Family & Domainsi

Region

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

Coiled coil

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

Compositional bias

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

P11200-1 [UniParc]FASTAAdd to Basket

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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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 535TWSHG → VLESW1 Publication
Sequence conflicti49 – 535TWSHG → VLESW1 Publication
Sequence conflicti70 – 701Q → R in AAA66952. 1 Publication
Sequence conflicti130 – 1301I → V1 Publication
Sequence conflicti130 – 1301I → V1 Publication
Sequence conflicti146 – 1461N → S1 Publication
Sequence conflicti146 – 1461N → S1 Publication
Sequence conflicti175 – 1751T → S1 Publication
Sequence conflicti175 – 1751T → S1 Publication
Sequence conflicti190 – 1901T → A in ABV53292. 1 Publication
Sequence conflicti250 – 2501S → N1 Publication
Sequence conflicti250 – 2501S → N1 Publication
Sequence conflicti316 – 3161T → I in ABV53292. 1 Publication
Sequence conflicti331 – 3311L → S in AAA66952. 1 Publication
Sequence conflicti335 – 3351H → D in ABV53292. 1 Publication
Sequence conflicti338 – 3381I → V1 Publication
Sequence conflicti353 – 3531D → N1 Publication
Sequence conflicti361 – 3611F → L1 Publication
Sequence conflicti388 – 3881M → L1 Publication
Sequence conflicti413 – 4131Q → K1 Publication
Sequence conflicti474 – 4741P → L in AAA66952. 1 Publication
Sequence conflicti565 – 5651G → R1 Publication
Sequence conflicti589 – 5891E → V1 Publication
Sequence conflicti589 – 5891E → V in ABV53292. 1 Publication
Sequence conflicti614 – 6141Missing1 Publication
Sequence conflicti632 – 6321D → I1 Publication
Sequence conflicti732 – 7321N → T in ABV53292. 1 Publication

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: February 19, 2014
This is version 86 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

Similar proteinsi