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P21284

- VP4_ROTHL

UniProt

P21284 - VP4_ROTHL

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Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A (strain Human/Philippines/L26/1987 G12-P1B[4]-I2-R2-C2-M1/M2-A2-N1-T2-E2-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/Philippines/L26/1987 G12-P1B[4]-I2-R2-C2-M1/M2-A2-N1-T2-E2-H1) (RV-A)
Taxonomic identifieri10953 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000001459: 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_0000041063Add
BLAST
Chaini1 – 230230Outer capsid protein VP8*Sequence AnalysisPRO_0000041064Add
BLAST
Chaini247 – 775529Outer capsid protein VP5*Sequence AnalysisPRO_0000041065Add
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
Glycosylationi132 – 1321N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi150 – 1501N-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
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

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

ProteinModelPortaliP21284.
SMRiP21284. Positions 60-223, 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.

P21284-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASLIYRQLL TNSYSVDLHD EIEQIGSEKT QNVTINPGPF AQTRYAPVNW
60 70 80 90 100
RHGEINDSTT VEPVLDGPYQ PTTFKPPNDY WLLISSNTDG VVYESTNNSD
110 120 130 140 150
FWTAVIAVEP RVSQTNRQYI LFGENKQFNI ENNSDKWKFF EMFKGSSQSN
160 170 180 190 200
FSNRRTLTSN NRLVGMLKYG GRVWTFHGET PRATTDSSNT ADLNNISIVI
210 220 230 240 250
HSEFYIIPRS QESKCNEYIN NGLPPIQNTR NVVPLSLSSR SIQYRRAQVN
260 270 280 290 300
EDITISKTSL WKEMQYNRDI IIRFKFGNSV IKLGGLGYKW SEISYKAANY
310 320 330 340 350
QYSYSRDGEQ VTAHTTCSVN GVNNFSYNGG SLPTDFSISR YEVIKENSYV
360 370 380 390 400
YIDYWDDSKA FRNMVYVRSL AANLNSVKCA GGSYNFRLPV GEWPIMNGGA
410 420 430 440 450
VSLHFAGVTL STQFTNFVSL NSLRFRFSLT VDEPSFSIIR TRTVNLYGLP
460 470 480 490 500
AANPNNGNEY YEMSGRFSLI SLVPTNDDYQ TPIMNSVTVR QDLERQLSDL
510 520 530 540 550
REEFNSLSQE IAMSQLIDLA LLPLDMFSMF SGIKSTIDLT KSMATSVMKK
560 570 580 590 600
FRKSKLATSI SEMTNSLSDA ASSASRSASV RSNLSVISNW TDASKSTSNI
610 620 630 640 650
TDLVNDVSTQ TSTISKKLRL KEMITQTEGM SFDDISAAVL KTKIDMSTQI
660 670 680 690 700
GKNTLPDIVT EASEKFIPKR SYRVLKDNEV MEINTEGKFF AYKVDTLNEI
710 720 730 740 750
PFDINKFAEL VTDSPVISAI IDFKTLKNLN DNYGITRMEA LNLIKSNPNV
760 770
LRNFINQNNP IIRNRIEQLI LQCKL
Length:775
Mass (Da):87,651
Last modified:May 1, 1991 - v1
Checksum:i40CA498305DECD63
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501N → D in ABV53268. (PubMed:18786998)Curated
Sequence conflicti416 – 4161N → D in ABV53268. (PubMed:18786998)Curated
Sequence conflicti479 – 4791Y → H in ABV53268. (PubMed:18786998)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511R → G in strain: L27.
Natural varianti392 – 3921E → K in strain: L27.
Natural varianti405 – 4051F → C in strain: L27.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58292 Genomic RNA. Translation: AAA47335.1.
EF672591 Genomic RNA. Translation: ABV53268.1.
PIRiA36410. VPXRWL.
C36410. VPXRWM.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58292 Genomic RNA. Translation: AAA47335.1 .
EF672591 Genomic RNA. Translation: ABV53268.1 .
PIRi A36410. VPXRWL.
C36410. VPXRWM.

3D structure databases

ProteinModelPortali P21284.
SMRi P21284. Positions 60-223, 252-521.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi 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. "Nucleotide sequence of VP4 and VP7 genes of human rotaviruses with subgroup I specificity and long RNA pattern: implication for new G serotype specificity."
    Taniguchi K., Urasawa T., Kobayashi N., Gorziglia M., Urasawa S.
    J. Virol. 64:5640-5644(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: L26 and L27.
  2. "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].

Entry informationi

Entry nameiVP4_ROTHL
AccessioniPrimary (citable) accession number: P21284
Secondary accession number(s): B3SRU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: October 29, 2014
This is version 90 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

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3