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Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus G3
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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.SAAS annotation
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.SAAS annotation

GO - Biological processi

Keywordsi

Molecular functionHemagglutininSAAS annotation
Biological processHost-virus interaction, Viral attachment to host cellSAAS annotation, Viral penetration into host cytoplasm, Viral penetration via permeabilization of host membraneSAAS annotation, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Outer capsid protein VP4UniRule annotationSAAS annotation
OrganismiRotavirus G3Imported
Taxonomic identifieri73036 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A

Subcellular locationi

A0A168GWW3:
  • Host rough endoplasmic reticulum SAAS annotation
A0A168GWW3:
  • Virion UniRule annotationSAAS annotation

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host endoplasmic reticulumSAAS annotation, Outer capsid proteinSAAS annotation, Virion

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.SAAS annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini49 – 208VP4_haemagglutInterPro annotationAdd BLAST160
Domaini234 – 458Rota_VP4_MIDInterPro annotationAdd BLAST225
Domaini469 – 708VP4_helicalInterPro annotationAdd BLAST240

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili468 – 495Sequence analysisAdd BLAST28

Sequence similaritiesi

Belongs to the rotavirus VP4 family.UniRule annotationSAAS annotation

Keywords - Domaini

Coiled coilSequence analysisSAAS annotation

Family and domain databases

InterProiView protein in InterPro
IPR013320. ConA-like_dom.
IPR035330. Rota_VP4_MID.
IPR000416. VP4_concanavalin-like.
IPR035329. VP4_helical.
PfamiView protein in Pfam
PF17477. Rota_VP4_MID. 1 hit.
PF00426. VP4_haemagglut. 1 hit.
PF17478. VP4_helical. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Fragment.

A0A168GWW3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VVLSDDTRIG STKTQNVTIN PGPFAQTGYA PVNWGPGETN DSTTVEPVLD
60 70 80 90 100
GPYQPTTFNP PVDYWMLLAP TAPGVVVEGT NNTDRWLATI LVEPSVPSEI
110 120 130 140 150
RSYTIFGIQE QITVANTSQT QWKFIDVVKT AQGGSYSQYG PLQSTPKLYA
160 170 180 190 200
VMKHNGKIYT YNGETPNATT GYYSTTNYDS VNMTAFCDFY IIPRAEESTC
210 220 230 240 250
TEYINNGLPP IQNTRNIVPL ALSARSIISP RAQANEDIVV SKTSLWKEMQ
260 270 280 290 300
YNRDITIRFK FANSIIKSGG LGYKWSEISF KPANYQYTYT RDGEEVTAHT
310 320 330 340 350
TCSVNGMNDF NFNGGSLPTD FVISRYEVIK ENSFVYVDYW DDSQAFKNMV
360 370 380 390 400
YVRSLAANLN SVMCTGGDYS FALPVGQWPV MTGGAVSLHS AGVTLSTQFT
410 420 430 440 450
DFVSLNSLRF RFRLTVEEPS FSITRTRVSR LYGLPAANPN NGKEYYEVAG
460 470 480 490 500
RFSLISLVPS NDDYQTPIAN SVTVRQDLER QLGELREEFN ALSQEIAMSQ
510 520 530 540 550
LIDLALLPLD MFSMFSGIKS TIDAAKSMAT SVMKKFKKSS LASSVSTLTD
560 570 580 590 600
SLSDAASSIS RGSSIRSIGS SVSAWTDVST QITDVSSSVS SISTQTSTIS
610 620 630 640 650
RRLRLKEMAT QTEGMNFDDI SAAVLKTKID RSTQISPNTL PDIVTEASEK
660 670 680 690 700
FIPNRAYRVI NNDEVFEAGT DGRFFAYRVE TFDEIPFDVQ KFADLVTDSP

VISAIMDLE
Length:709
Mass (Da):78,300
Last modified:July 6, 2016 - v1
Checksum:iEF6582EBE2BFE0C0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei1Imported1
Non-terminal residuei709Imported1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KU243624 Genomic RNA. Translation: ANC33770.1.

Similar proteinsi

Entry informationi

Entry nameiA0A168GWW3_9REOV
AccessioniPrimary (citable) accession number: A0A168GWW3
Entry historyiIntegrated into UniProtKB/TrEMBL: July 6, 2016
Last sequence update: July 6, 2016
Last modified: September 27, 2017
This is version 8 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)