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P11195

- VP4_ROTHP

UniProt

P11195 - VP4_ROTHP

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Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A (strain Human/United States/P/1974 G3-P1A[8]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A)
Status
Reviewed - Annotation score: 4 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.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
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/P/1974 G3-P1A[8]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A)
Taxonomic identifieri10957 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007047: 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 endoplasmic reticulum Source: UniProtKB-KW
  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_0000041072Add
BLAST
Chaini1 – 230230Outer capsid protein VP8*Sequence AnalysisPRO_0000041073Add
BLAST
Chaini247 – 775529Outer capsid protein VP5*Sequence AnalysisPRO_0000041074Add
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
Glycosylationi129 – 1291N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi132 – 1321N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi195 – 1951N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi317 ↔ 379Sequence Analysis
Glycosylationi324 – 3241N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi583 – 5831N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi589 – 5891N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi592 – 5921N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi599 – 5991N-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

Proteomic databases

PRIDEiP11195.

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

ProteinModelPortaliP11195.
SMRiP11195. Positions 64-223, 252-521.
ModBaseiSearch...
MobiDBiSearch...

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.
InterProiIPR013320. ConA-like_dom.
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.

P11195-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASLIYRQLL TNSYSVDLHD EIEQIGSEKT QNVTVNPGPF AQTRYAPVNW
60 70 80 90 100
GHGEINDSTT VELILDGPYQ PTTFTPPTDY WILINSNTNG VVYESTNNSD
110 120 130 140 150
FWTAVVAVEP HVNPVDRQYL IFGENKQFNV SNDSDKWKFL EMFRSSSQNE
160 170 180 190 200
FYNRRTLTSD TRLVGILKYG GRVWTFHGET PRATTDSSNT ANLNNISITI
210 220 230 240 250
HSEFYIIPRS QESKCNEYIN NGLPPIQNTR NVVPLSLSSR SIQYKRAQVN
260 270 280 290 300
EDITISKTSL WKEMQYNGDI IIRFKFGNSI IKPGGLGYKW SEISFKAANY
310 320 330 340 350
QYNYLRDGEQ VTAHTTCSVN GINNFSYNGG YLPTDFSVLR YEVIKENSYV
360 370 380 390 400
YVDYWDDSKA FRNMVYVRSL AANLNSVKCT GGSYDFSIPV GAWPVMNGGA
410 420 430 440 450
VSLHFAGVTL STQFTDFVSL NSLRFRFSLT VDEPSFSILR TRTVNLYGLP
460 470 480 490 500
AANPNNGNEY YEISGRFSLI SLVPTNDDYQ TPIMNSVTVR QDLERQLTDL
510 520 530 540 550
REEFNSLSQE IAMSQLIDLA LLPLDMFSMF SGIKSTIHLT KSMATSVMKK
560 570 580 590 600
FRKSKLATSV SEMTNSLSDA ASSASRSVSV RSNISAISNW TNVSDDVSNV
610 620 630 640 650
TDSVNDVSTQ TSTISKKLRL KEMITQTEGM SFDDISAAVL KTKIDKSTQI
660 670 680 690 700
RKNTLPDIVE EASEKFIPKR SYRILKDDEV MEINTEGKFF AYKIDTLNEV
710 720 730 740 750
PFDVNKFTEL VTNTPVISAI IDFKTLKNLN DNYGITRTEA FNLIKSNPNV
760 770
LRNFINQNHP IIRNRIEQLI LQCRL
Length:775
Mass (Da):87,688
Last modified:November 1, 1990 - v2
Checksum:i6B431C8A5D3FDB38
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311Q → K in ABV53276. (PubMed:18786998)Curated
Sequence conflicti35 – 351V → I(PubMed:3018754)Curated
Sequence conflicti120 – 1212LI → TV in ABV53276. (PubMed:18786998)Curated
Sequence conflicti131 – 1311S → R in ABV53276. (PubMed:18786998)Curated
Sequence conflicti192 – 1921Missing(PubMed:3018754)Curated
Sequence conflicti236 – 2372SL → PS(PubMed:3018754)Curated
Sequence conflicti283 – 2831P → L in ABV53276. (PubMed:18786998)Curated
Sequence conflicti331 – 3311Y → S in ABV53276. (PubMed:18786998)Curated
Sequence conflicti339 – 3391L → S in ABV53276. (PubMed:18786998)Curated
Sequence conflicti385 – 3851D → N in ABV53276. (PubMed:18786998)Curated
Sequence conflicti471 – 4711S → C in ABV53276. (PubMed:18786998)Curated
Sequence conflicti538 – 5381H → D in ABV53276. (PubMed:18786998)Curated
Sequence conflicti602 – 6076DSVNDV → NSLNDI in ABV53276. (PubMed:18786998)Curated
Sequence conflicti617 – 6171K → N in ABV53276. (PubMed:18786998)Curated
Sequence conflicti646 – 6461K → M in ABV53276. (PubMed:18786998)Curated
Sequence conflicti651 – 6511R → G in ABV53276. (PubMed:18786998)Curated
Sequence conflicti660 – 6601E → T in ABV53276. (PubMed:18786998)Curated
Sequence conflicti714 – 7141T → S in ABV53276. (PubMed:18786998)Curated
Sequence conflicti741 – 7411F → L in ABV53276. (PubMed:18786998)Curated
Sequence conflicti759 – 7591H → N in ABV53276. (PubMed:18786998)Curated
Sequence conflicti774 – 7741R → K in ABV53276. (PubMed:18786998)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ540228 Genomic RNA. Translation: CAD62681.1.
EF672598 Genomic RNA. Translation: ABV53276.1.
PIRiC28839. VPXRW5.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ540228 Genomic RNA. Translation: CAD62681.1 .
EF672598 Genomic RNA. Translation: ABV53276.1 .
PIRi C28839. VPXRW5.

3D structure databases

ProteinModelPortali P11195.
SMRi P11195. Positions 64-223, 252-521.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P11195.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR013320. ConA-like_dom.
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.

Entry informationi

Entry nameiVP4_ROTHP
AccessioniPrimary (citable) accession number: P11195
Secondary accession number(s): B3SRV1, Q70UN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1990
Last modified: October 29, 2014
This is version 95 of the entry and version 2 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

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3