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Protein

Outer capsid protein VP4

Gene
N/A
Organism
Rotavirus A
Status
Unreviewed-Annotation score: -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 VP4SAAS annotation
OrganismiRotavirus AImported
Taxonomic identifieri28875 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
Proteomesi
  • UP000122618 Componenti: Genome

Subcellular locationi

  • Host rough endoplasmic reticulum SAAS annotation
  • Virion SAAS 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
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.SAAS annotation

Keywords - Domaini

Coiled coilSequence analysisSAAS annotation

Family and domain databases

InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR035330 Rota_VP4_MID
IPR038017 Rota_VP4_MID_sf
IPR035329 VP4_helical
PfamiView protein in Pfam
PF17477 Rota_VP4_MID, 1 hit
PF17478 VP4_helical, 1 hit
SUPFAMiSSF111379 SSF111379, 1 hit
SSF49899 SSF49899, 1 hit

Sequencei

Sequence statusi: Complete.

A0A060NED7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLIYRQLL SNSYVTNISD EVSEIGARKT ANVTVNPGPF AQTGYAPVNW
60 70 80 90 100
GHGELSDSTL VQPTLDGPYQ PTTFNLPIDY WMLIAPTQAG RVAEGTNTTD
110 120 130 140 150
RWFACVLVEP NVQNTQREYI LDGQTVQLQV SNDSSTLWKF ILFIKLEKNG
160 170 180 190 200
NYSQYSALST SNKLCAWMKR EGRVYWYEGI TPNASESYYL TINNDNSNVS
210 220 230 240 250
CDAEFYLIPR SQTELCAQYI NNGLPPIQNT RNVVPVRLTS REIRHTRAQM
260 270 280 290 300
NEDIVVSKTS LWKEMQYNRD ITIRFKFANS IVKSGGLGYK WSEISFKPMN
310 320 330 340 350
YQYTYTRDGE EITAHTTCSV NGVNDFSYNG GTLPTDFAIS RFEVIKENSY
360 370 380 390 400
VYIDYWDDSQ AFKNMVYVRS LSANLNDVVC SGGDYSFALP VGAYPVMSGG
410 420 430 440 450
AVTLSPAGVT LSTQFTDYVS LNSLRFRFRL AVSEPSFSIS RTRLSGIYGL
460 470 480 490 500
PAANPNNNVE YYEIAGRFSL ISLVPTNDDY QTPIANSVTV RQDLERQLGE
510 520 530 540 550
LREEFNSLSQ EIALSQLIDL ATLPLDMFSM FSGIKSTVEA VKSMTTNIMK
560 570 580 590 600
KFKTSNLANA ISDLTNSMSD AASSISRSAS VRSIGSNTTM RISTVIQTGE
610 620 630 640 650
DLRTVADAST QISNVSRSLR LREFTTQTDN LSFDDISAAV LKTKLDKSTQ
660 670 680 690 700
ISQNTIPDII SESSERFIPM RTYRVIDNDT AFETGIDGTF YAYRVDTFDE
710 720 730 740 750
VPFDIEKFNR LITDSPVLSA IIDFKTLKNL NDNYGITKTQ AMELLQSNPR
760 770
TLKEFINNNN PIIRNRIENL IAQCRL
Length:776
Mass (Da):87,088
Last modified:September 3, 2014 - v1
Checksum:i09AD391622B9DB0D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB853893 Genomic RNA Translation: BAO77766.1

Similar proteinsi

Entry informationi

Entry nameiA0A060NED7_9REOV
AccessioniPrimary (citable) accession number: A0A060NED7
Entry historyiIntegrated into UniProtKB/TrEMBL: September 3, 2014
Last sequence update: September 3, 2014
Last modified: February 28, 2018
This is version 23 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported
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Main funding by: National Institutes of Health