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A9Q1L0

- VP4_ROTB2

UniProt

A9Q1L0 - VP4_ROTB2

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Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus (isolate Human/Bangladesh/ADRV-N B219/2002) (RV ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-B219))
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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei249 – 2502CleavageSequence Analysis
Sitei262 – 2632CleavageSequence 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 (isolate Human/Bangladesh/ADRV-N B219/2002) (RV ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-B219))
Taxonomic identifieri348136 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusunclassified rotaviruses
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000008656: 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 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 – 826826Outer capsid protein VP4PRO_0000369842Add
BLAST
Chaini1 – 249249Outer capsid protein VP8*Sequence AnalysisPRO_0000369843Add
BLAST
Chaini263 – 826564Outer capsid protein VP5*Sequence AnalysisPRO_0000369844Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi143 – 1431N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi153 – 1531N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi198 – 1981N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi333 – 3331N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi487 – 4871N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi494 – 4941N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi514 – 5141N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi561 – 5611N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi804 – 8041N-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

Cleavage on pair of basic residues, Glycoprotein

Interactioni

Subunit structurei

VP4 is a homotrimer.Curated

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi260 – 2634Poly-Lys

Sequence similaritiesi

Belongs to the rotavirus VP4 family.Curated

Family and domain databases

InterProiIPR000416. Haemagglutinin_VP4.
[Graphical view]
PfamiPF00426. VP4_haemagglut. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A9Q1L0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLRSLLITT EAVGETTQTS DHQTSFSTRT YNEINDRPSL RVEKDGEKAY
60 70 80 90 100
CFKNLDPVRY DTRMGEYPFD YGGQSTENNQ LQFDLFTKDL MADTDIGLSD
110 120 130 140 150
DVRDDLKRQI KEYYQQGYRA IFLIRPQNQE QQYIASYSST NLNFTSQLSV
160 170 180 190 200
GVNLSVLNKI QENKLHIYST QPHIPSVGCE MITKIFRTDV DNENSLINYS
210 220 230 240 250
VPVTVTISVT KATFEDTFVW NQNNDYPNMN YKDLIPAVTK NSIYHDVKRI
260 270 280 290 300
TKIHEYINSK KKKNGVGKIG GIQIAESKDG FWKILTKNYQ IKLKFGIEGY
310 320 330 340 350
GVMGGTFGNW LIDSGFKTVE TNYEYQRNGK TINATTVASV KPSRKCGTRS
360 370 380 390 400
PVFGQLQFSG EMMVLSHNDI LTVFYTEREW ALSNAIYAKN FATDFKRQFE
410 420 430 440 450
VTAQSDELLV RTNVVPHTIK NTPGKALMEY SHGGFGQIDT SDYTGMALTF
460 470 480 490 500
RFRCVSEDLP EGYYDKDKAL TFANVGLTSF QDRQETNGTY WVYNTSTVGF
510 520 530 540 550
GSCYPKKEFE YDINVTYTTL LPSDPEFTTG GTNYAQSVTA VLEESFINLQ
560 570 580 590 600
NQVNEMLTRM NISDLTSGVM SVFSVATSFP QILDGISDLL KAASSAFKKV
610 620 630 640 650
KGKVGNVAKR LRGKRYVRLF DEDISIEETP RFLDSIRSSR RPSILSNMFN
660 670 680 690 700
DDETFTALHT LASRTNSVAS DVTYIQPIIT TRIANSTPPV IAPASSVTYA
710 720 730 740 750
KLKDISKIIN AEIDPKSIME FNQVSNTISI LDSTKKLAQY AVDPDVIDGI
760 770 780 790 800
LNKMVGGHAR SLFSLKVRKH LLDAVEKDAF VKYNYHDLMG KLLNDRELLD
810 820
ITNNLSSQKQ FELAKEFRDL LINALA
Length:826
Mass (Da):93,311
Last modified:February 5, 2008 - v1
Checksum:iB8CC3EDD7D540505
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EF453358 mRNA. Translation: ABR32125.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EF453358 mRNA. Translation: ABR32125.1 .

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR000416. Haemagglutinin_VP4.
[Graphical view ]
Pfami PF00426. VP4_haemagglut. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "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: NUCLEOTIDE SEQUENCE [MRNA], PUTATIVE CLEAVAGE SITES.

Entry informationi

Entry nameiVP4_ROTB2
AccessioniPrimary (citable) accession number: A9Q1L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: October 29, 2014
This is version 30 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3