UniProtKB - A0A161I2Q8 (A0A161I2Q8_9REOV)
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Protein
Outer capsid protein VP4
Gene
N/A
Organism
Rotavirus G3
Status
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
- permeabilization of host organelle membrane involved in viral entry into host cell Source: UniProtKB-KW
- viral entry via permeabilization of inner membrane Source: UniProtKB-KW
- virion attachment to host cell Source: UniProtKB-KW
Keywordsi
Molecular function | HemagglutininSAAS annotation |
Biological process | Host-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 |
Organismi | Rotavirus G3Imported |
Taxonomic identifieri | 73036 [NCBI] |
Taxonomic lineagei | Viruses › dsRNA viruses › Reoviridae › Sedoreovirinae › Rotavirus › Rotavirus A |
Subcellular locationi
- Host rough endoplasmic reticulum SAAS annotation
- Virion UniRule annotationSAAS annotation
GO - Cellular componenti
- host cell rough endoplasmic reticulum Source: UniProtKB-SubCell
- viral outer capsid Source: UniProtKB-KW
Keywords - Cellular componenti
Capsid protein, Host endoplasmic reticulumSAAS annotation, Outer capsid proteinSAAS annotation, VirionInteractioni
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 49 – 208 | VP4_haemagglutInterPro annotationAdd BLAST | 160 | |
Domaini | 234 – 458 | Rota_VP4_MIDInterPro annotationAdd BLAST | 225 | |
Domaini | 469 – 708 | VP4_helicalInterPro annotationAdd BLAST | 240 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 468 – 495 | Sequence analysisAdd BLAST | 28 |
Sequence similaritiesi
Keywords - Domaini
Coiled coilSequence analysisSAAS annotationFamily and domain databases
InterProi | View protein in InterPro IPR013320. ConA-like_dom_sf. IPR035330. Rota_VP4_MID. IPR038017. Rota_VP4_MID_sf. IPR000416. VP4_concanavalin-like. IPR035329. VP4_helical. |
Pfami | View protein in Pfam PF17477. Rota_VP4_MID. 1 hit. PF00426. VP4_haemagglut. 1 hit. PF17478. VP4_helical. 1 hit. |
SUPFAMi | SSF111379. SSF111379. 1 hit. SSF49899. SSF49899. 1 hit. |
i Sequence
Sequence statusi: Fragment.
A0A161I2Q8-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Non-terminal residuei | 1 | Imported | 1 | |
Non-terminal residuei | 709 | Imported | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | KU243625 Genomic RNA. Translation: ANC33771.1. |
Similar proteinsi
Entry informationi
Entry namei | A0A161I2Q8_9REOV | |
Accessioni | A0A161I2Q8Primary (citable) accession number: A0A161I2Q8 | |
Entry historyi | Integrated into UniProtKB/TrEMBL: | July 6, 2016 |
Last sequence update: | July 6, 2016 | |
Last modified: | February 28, 2018 | |
This is version 11 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Unreviewed (UniProtKB/TrEMBL) |