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A0A977MCS3 · A0A977MCS3_9PICO

Function

function

Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.
Plays a role in the assembly of the 12 pentamers into an icosahedral structure. Has not been detected in mature virions, supposedly owing to its small size.
Precursor component of immature procapsids that corresponds to an extended form of the structural protein VP1. After maturation, possibly by the host Cathepsin L, the assembly signal 2A is cleaved to give rise to the mature VP1 protein.
VP0 precursor is a component of the immature procapsids.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasmic vesicle membrane
Cellular Componenthost cell cytoplasmic vesicle membrane
Cellular Componenthost multivesicular body
Cellular ComponentT=pseudo3 icosahedral viral capsid
Molecular FunctionATP binding
Molecular Functionchannel activity
Molecular Functioncysteine-type endopeptidase activity
Molecular FunctionRNA binding
Molecular FunctionRNA helicase activity
Molecular FunctionRNA-dependent RNA polymerase activity
Molecular Functionstructural molecule activity
Biological ProcessDNA-templated transcription
Biological Processmonoatomic ion transmembrane transport
Biological Processproteolysis
Biological ProcessRNA-protein covalent cross-linking
Biological Processsymbiont entry into host cell
Biological Processviral RNA genome replication
Biological Processvirion attachment to host cell
Biological Processvirus-mediated perturbation of host defense response

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Genome polyprotein

Organism names

  • Taxonomic identifier
  • Strain
    • 15893
  • Taxonomic lineage
    Viruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Picornavirales > Picornaviridae > Heptrevirinae > Hepatovirus

Accessions

  • Primary accession
    A0A977MCS3

Subcellular Location

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Homopentamer. Homooligomer.
Interacts with capsid protein VP1. Interacts with capsid protein VP2.
Interacts with capsid protein VP1. Interacts with capsid protein VP3.
Interacts with capsid protein VP2. Interacts with capsid protein VP3.

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias495-521Polar residues
Region495-526Disordered
Domain1161-1327SF3 helicase
Domain1483-1696Peptidase C3
Domain1946-2067RdRp catalytic

Sequence similarities

Belongs to the picornaviridae polyprotein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,153
  • Mass (Da)
    242,310
  • Last updated
    2023-02-22 v1
  • MD5 Checksum
    56A1504AF402DB2191915BECE5496C41
MIFMMSSNKKDGLFQTIGSGLDKVLSLADIEEEQTMQTPDRVVVGGASYFTSVDQSSVHSSVSGKHQEEKLLTSVDLPGTKRTQGEKFFLIHTAEWNTTDALFHEVAKLDVVKLLYDQQFAVDGLLRYHTYARFGVEVQIQINPTTFQQGGLICAMVPADQGYGSIACLTVYPHGLLNCNINNVVRIRVPFVYTRGAYNLRDPLYTIWELTIRVWNRLYIGTGTTPFTTVNVLARLVDLELHGLTPIFTQMMRNEFRISTTENVVNLANFEDSRAKISLALDQEDWRKDASEAGGLEIKSFTTWTSIPTLATQFAFNDSATVGTQIKVIPVDPYYYQMTNSSPDQKCVTSLASVAQMYCFWRGDLVFDFQAFPTKYHSGRLLFCFVPGNENMDVSKITLKQATTGPCAVMDITGVNSTLRFRVPWISDTPYRVNRYTKSSHVKGEYTAIGKIIVFVYNRLSNPNNVAGHVYFNVYTSAVNLELFGPVYSVMSNTSSQAGEDEEGFSSTSETQQNQPDPCGGITTPKQLKGRANQGKLDLAAGKVPTGAITILEDPILAKKIPETFPEKKPGVSRHTSDHMDIYKYMGRAHFLGTFTFTTNNKEYTFPISLSSSANPPGGLPSTLRWFFNMFHLYRGPLDLTIIVAGATDVDGLVWFTPVGMAADPSFQEASSNLSVDYKTSLGAVRFNTRRTGNIQMRLPWYSYLYAISGVLDGDGDKSDSTFGTLSIQITNYTRADEYLSFSLYLALTEQSQCLFPRAPLNNNAIMDTPNSHNIMARIAAGDLESCVDEFEVWTEMGAVDPVNFSIMSRLDTSTNKILKGFFYNDMVYRLSIANWFENLVPIQSGNFVAEKPNEWRVEILKPVIVPLLETMVAIPDWEKTKFPCKLTDKKKFIDSIVKTEVFKTILNHHDPEDVLEMFEILKPGDVTMLDRAIDKTGVTKVTSSAEKLVEECRTFLQTIKDSIKRFAMGFHRNKGIAWLKACLEISKIAVNIYICHRSNWDPMVVWPITLVLGLENIIKATDLFSAVSAHLAARLTDDDDEEEKIKTESGNWLRDICSGITIFKTVKDVFLWLIDKLKNFYDRKFGEASKKIQLIKEHQDEIENTLEEADMYCVSLVQDVTKEEQYNKGISLITSLRTVSSLAESDPSLRKFSQPLRDAIQRVHNKIKSLGAINQNVVTRPEPVVCYLYGRRGGGKSLTSMAIATKICKQYGVDPKKNIYTKPVSSDYWDGYSNQLVCVIDDIGQCTDDEDWADFCQLVSGCPLRLNMASLEEKGKHFSSPFIICTSNQDDPAPKTVYVKEAIQRRLHYKVKVEPEAYYSVNSMLNVSLAKKDGVIKDMRCVNMTSDGSKIDINTLVDNLVATVQVRQQNMDDFMDLWTESWSDVKDAIGDEFRRLMRFDCMKQSTKQRLREFFRKVNSNKLLIFGTALGFLGLATGLFYGFKAIKKIYKEEHENKEEDSLTSGVYHGVTRPKNVVKLDSLTPESQSIVEISAVVHKNLVRFGIGEKGGCVNWLMNGLGIKDEWLLLPSHAYIFEPDLQNKEFYFQRNNTYYSVNSGSVQILTLDTGFQDVVLMKVPQMPKFKDIIHHFIKKKDLDQASNRLATLVTMNSGVYQMVSEGQLQLEEHSTYSHKTDTGEIKELTISQAWRGKGMSSPGMCGGALVSSNSKLQNPIIGIHVAGGKGHMISKVVYQEMLEQINAKVDTNQRISKVEFTQSCVNVGSKTLFEKSPIHDFVEPEMINYPAALPFGRNNEIDPIQVMLSKYDIPIAEEPDAYFMSYDYYIEKIQGLPYVIEEQISLKQAIEGVEGMDALNMKTSAGLPYTLYNMSKEELIWKDDDGSFIGINPYLKNRIDLNMLCMDAGNQMDVIYMTCPKDELRPLEKVLSSKTRAIEACPLDFTIICRMMWAPAISYFQLNPGFHTGVAVGMDPDSDWDSLFKAMMKFGDFGLDLDFSSFDASLSPFMISYGCDVLSSISGLSEGQSRALSNAISFSRHQILNMIYTVSGSMPSGTPCTSLLNSIINNINLIYVFSLVLNKPPNLVFDYLKMICYGDDVLIVFNRKIPKEKLELICPKVVKQFSKLHMTVTSSSKGIPEIKKISELTFLKREFNLDFPRVKPAISDKTIWSLVSWQISAELRQISKSIHTSLYATLK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias495-521Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
OM302498
EMBL· GenBank· DDBJ
UXK63025.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

Disclaimer

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