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Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A
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 AImported
Taxonomic identifieri28875 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus

Subcellular locationi

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

GO - Cellular componenti

Keywords - Cellular componenti

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

PTM / Processingi

Keywords - PTMi

Disulfide bondSAAS annotation

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
Domaini65 – 224VP4_haemagglutInterPro annotationAdd BLAST160
Domaini250 – 474Rota_VP4_MIDInterPro annotationAdd BLAST225
Domaini485 – 776VP4_helicalInterPro annotationAdd BLAST292

Sequence similaritiesi

Belongs to the rotavirus VP4 family.UniRule annotationSAAS annotation

Keywords - Domaini

Coiled coilSAAS annotation

Family and domain databases

InterProiView protein in InterPro
IPR013320. ConA-like_dom_sf.
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: Complete.

A0A1V0FUK0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLIYRQLL TNSYSVDLSD EIQKIGSTKT QNVTVNPGPF AQTGYAPVNW
60 70 80 90 100
GPGEINDSTT VEPVLDGPYQ PTTFNPPVDY WMLLAPTIAG VVVEGTNNTD
110 120 130 140 150
RWLATILVEP NVTSEVRSYT LFGVQEQITI ANTSQTQWKF IDVVKTTQNG
160 170 180 190 200
SYSQYGPLQS SPKLYAVMKH NGKIYTYNGE TPNATTGYCS TTNYDSVNMT
210 220 230 240 250
AFCDFYIIPR AEESTCTEYI NNGLPPIQNT RNIVPLALSA RKIISHRAQA
260 270 280 290 300
NEDIVVSETS LWKEMQYNRD ITIRFKFANS IVKSGGLGYK WSEISFKPAN
310 320 330 340 350
YQYTYIRDGE EVTAHTTCSV NGVNDFSFNG GSLPTDFVIS RYEVIKENSY
360 370 380 390 400
VYVDYWDDSQ AFRNMVYVRS LAANLNSVMC TDGDYSFALP VGQWPVMNGG
410 420 430 440 450
AVSLHSAGVT LSTEFTDFVS LNSLRFRFRL ADEEPSFSIT RTSVSSLYGL
460 470 480 490 500
PAANPNNGKE YYEIAGRFSL ISLVPSNDDY QTPIANSVTV RQDLERQLGE
510 520 530 540 550
LRGEFNALSQ EIAMSQLIDL ALLPLDMFSM FSGIKSTIDA AKSMATSVMK
560 570 580 590 600
KFKKSGLASS VSTLTDSLSD AASSVSRSSS IRSVGSSASA WTDVSNQITD
610 620 630 640 650
ETSSVSTIST QTSTISRSLR LKEIATQTEG MNFDDISAAV LKTKIDRSTE
660 670 680 690 700
ISPNTLPDII SEASEKFIPN RAYRVINNNE VLEAGTDGRF FAYRVDTFEE
710 720 730 740 750
IPFDVQKFAD LVTDSPVISA IIDFKTLKNL NDNYGITRKQ ALNLLSSDPR
760 770
VLREFINQDN PIIRNRIEQL IMQSRL
Length:776
Mass (Da):86,082
Last modified:June 7, 2017 - v1
Checksum:i8DFF08581210A8E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KX814943 Genomic RNA. Translation: ARB49195.1.

Similar proteinsi

Entry informationi

Entry nameiA0A1V0FUK0_9REOV
AccessioniPrimary (citable) accession number: A0A1V0FUK0
Entry historyiIntegrated into UniProtKB/TrEMBL: June 7, 2017
Last sequence update: June 7, 2017
Last modified: November 22, 2017
This is version 5 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)