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Q82040

- VP4_ROTHC

UniProt

Q82040 - VP4_ROTHC

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Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus C (isolate Human/United Kingdom/Bristol/1989) (RV-C)
Status
Reviewed - Annotation score: 3 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 (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 (By similarity).By similarity
VP8* forms the head of the spikes. It is the viral hemagglutinin and an important target of neutralizing antibodies (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei231 – 2322CleavageSequence Analysis
Sitei247 – 2482CleavageSequence Analysis

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 C (isolate Human/United Kingdom/Bristol/1989) (RV-C)
Taxonomic identifieri31567 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007664: Genome

Subcellular locationi

Chain Outer capsid protein VP4 : Virion. 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 By similarity
Note: Outer capsid protein.By similarity
Chain Outer capsid protein VP5* : Virion By similarity
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 – 744744Outer capsid protein VP4PRO_0000369876Add
BLAST
Chaini1 – 231231Outer capsid protein VP8*By similarityPRO_0000369877Add
BLAST
Chaini248 – 744497Outer capsid protein VP5*By similarityPRO_0000369878Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi39 – 391N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi135 – 1351N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi176 – 1761N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi192 – 1921N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi261 – 2611N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi310 – 3101N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi597 – 5971N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi601 – 6011N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi639 – 6391N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi647 – 6471N-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

Glycoprotein

Interactioni

Subunit structurei

VP4 is a homotrimer.Curated

Structurei

3D structure databases

ProteinModelPortaliQ82040.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni401 – 42121Hydrophobic; possible role in virus entry into host cellSequence AnalysisAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili496 – 53035Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the rotavirus VP4 family.Curated

Keywords - Domaini

Coiled coil

Family and domain databases

InterProiIPR000416. Haemagglutinin_VP4.
[Graphical view]
PfamiPF00426. VP4_haemagglut. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q82040-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASSLYAQLI SQNYYSLGNE ILSDQQTNKV VSDYVDAGNY TYAQLPPTTW
60 70 80 90 100
GSGSILKSAF STPEITGPHT NTVIEWSNLI NTNTWLLYQK PLNSVRLLKH
110 120 130 140 150
GPDTYNSNLA AFELWYGKSG TTITSVYYNT INNQNKTHDA NSDCLILFWN
160 170 180 190 200
EGSTQLEKQV VTFNWNVGGI LIKPINSSRM RICMSGMENF NNDSFNWENW
210 220 230 240 250
NHEFPRSNPG ININMYTEYF LASSDPYTYL KNLQQPTAKT VDMKMMKKMN
260 270 280 290 300
DNSKLGDGPI NVSNIISKDS LWQEVQYVRD ITLQCKILSE IVKGGGWGYD
310 320 330 340 350
YTSVTFKTVN HTYSYTRAGE NVNAHVTISF NNVKERAYGG SLPTDFKIGR
360 370 380 390 400
FDILDTDSYV YIDYWDDSEI FKNMVYVRDV RADIGGFQYS YSSEMSYYFQ
410 420 430 440 450
IPVGSYPGLH SSRLQLVYDR CLLSQQFTDY AALNSLRFVF RVVSTSGWFI
460 470 480 490 500
TTGDINTRRV ASGTGFAYSD GHVANTVGTI SFISLIPSNP NYQTPIASSS
510 520 530 540 550
TVRMDLERKI NDLRDDFNAL ASSVALSDIL SLAMSPLTFS NLLESVPAIT
560 570 580 590 600
SSVKDVAASV MKKFRSTKMF KKAAKQNYRE FVIGDLLEDV TNVARNNNSL
610 620 630 640 650
NYSDITSAMM VSTTNRLQIT DVDTFSEIVS RSADNFISNR SYRMIENNTV
660 670 680 690 700
HEITPTRRFS YDIKTLQQRN FDIDKFSKLA SQSPVISAIV DFATIKAIRD
710 720 730 740
TYGISDDIIY KLVASDAPTI LSFINQNNPL IRNRITNLIN QCKL
Length:744
Mass (Da):84,081
Last modified:November 1, 1996 - v1
Checksum:i96A9DBACBB7CD449
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X79442 Genomic RNA. Translation: CAA55958.1.
PIRiS45061.
RefSeqiYP_392514.1. NC_007572.1.

Genome annotation databases

GeneIDi3773132.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X79442 Genomic RNA. Translation: CAA55958.1 .
PIRi S45061.
RefSeqi YP_392514.1. NC_007572.1.

3D structure databases

ProteinModelPortali Q82040.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3773132.

Family and domain databases

InterProi IPR000416. Haemagglutinin_VP4.
[Graphical view ]
Pfami PF00426. VP4_haemagglut. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular characterization of the outer capsid spike protein (VP4) gene from human group C rotavirus."
    Fielding P.A., Lambden P.R., Caul E.O., Clarke I.N.
    Virology 204:442-446(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Whole genomic characterization of a human rotavirus strain B219 belonging to a novel group of the genus Rotavirus."
    Nagashima S., Kobayashi N., Ishino M., Alam M.M., Ahmed M.U., Paul S.K., Ganesh B., Chawla-Sarkar M., Krishnan T., Naik T.N., Wang Y.-H.
    J. Med. Virol. 80:2023-2033(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PUTATIVE CLEAVAGE SITES.

Entry informationi

Entry nameiVP4_ROTHC
AccessioniPrimary (citable) accession number: Q82040
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3