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Protein

Outer capsid protein VP4

Gene

VP4

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
Gene namesi
Name:VP4Imported
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

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili484 – 511Sequence 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_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.

A0A1Q2TSK9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLIYRQLL TNSYTVDLSD EIQEIGSTKS QNVTINPGPF AQTGYAPVNW
60 70 80 90 100
GPGEINDSTT VGPLLDGPYQ PTTFNPPVDY WMLLAPTTPG VIVEGTNNTD
110 120 130 140 150
RWLATILIEP NVQSENRTYT IFGIQEQLTV SNTSQDQWKF IDVVKTTANG
160 170 180 190 200
SIGQYGPLLS SPKLYAVMKH NEKLYTYEGQ TPNARTAHYS TTNYDSVNMT
210 220 230 240 250
AFCDFYIIPR SEESKCTEYI NNGLPPIQNT RNVVPLSLTA RDVIHYRAQA
260 270 280 290 300
NEDIVISKTS LWKEMQYNRD ITIRFKFANT IIKSGGLGYK WSEISFKPAN
310 320 330 340 350
YQYTYTRDGE EVTAHTTCSV NGVNDFSFNG GYLPTDFVVS KFEVIKENSY
360 370 380 390 400
VYIDYWDDSQ AFRNVVYVRS LAANLNSVMC TGGSYNFSLP VGQWPVLTGG
410 420 430 440 450
AVSLHSAGVT LSTQFTDFVS LNSLRFRFRL AVEEPHFKLT RTRLDRLYGL
460 470 480 490 500
PAADPNNGKE YYEIAGRFSL ISLVPSNDDY QTPIANSVTV RQDLERQLGE
510 520 530 540 550
LREEFNALSQ EIAMSQLIDL ALLPLDMFSM FSGIKSTIDA AKSMATNVMK
560 570 580 590 600
KFKKSGLANS VSTLTDSLSD AASSISRGSS IRSIGSSASA WTDVSTQITD
610 620 630 640 650
ISSSVSSVST QTSTISRRLR LKEMATQTEG MNFDDISAAV LKTKIDKSTQ
660 670 680 690 700
ISPNTIPDIV TEASEKFIPN RAYRVINNDD VFEAGIDGKF FAYKVDTFEE
710 720 730 740 750
IPFDVQKFAD LVTDSPVISA IIDFKTLKNL NDNYGITKQQ AFNLLRSDPR
760 770
VLREFINQDN PIIRNRIEQL IMQCRL
Length:776
Mass (Da):86,703
Last modified:April 12, 2017 - v1
Checksum:iA4CF0AA10DBAE1F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
LC178567 Genomic RNA. Translation: BAW94614.1.

Similar proteinsi

Entry informationi

Entry nameiA0A1Q2TSK9_9REOV
AccessioniPrimary (citable) accession number: A0A1Q2TSK9
Entry historyiIntegrated into UniProtKB/TrEMBL: April 12, 2017
Last sequence update: April 12, 2017
Last modified: November 22, 2017
This is version 7 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)