P52549 · GO_HHV6Z

Function

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 Componenthost cell plasma membrane
Cellular Componentmembrane
Cellular Componentvirion component

Names & Taxonomy

Protein names

  • Recommended name
    130 kDa Glycoprotein O
  • Short names
    gO-130K
  • Alternative names
    • Glycoprotein U47
  • Cleaved into 1 chains

Gene names

    • Name
      U47
    • Synonyms
      KA8L

Organism names

Accessions

  • Primary accession
    P52549

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-23
ChainPRO_000044535924-?80 kDa Glycoprotein O
ChainPRO_000003831724-738130 kDa Glycoprotein O
Glycosylation41N-linked (GlcNAc...) asparagine; by host
Glycosylation64N-linked (GlcNAc...) asparagine; by host
Glycosylation114N-linked (GlcNAc...) asparagine; by host
Glycosylation175N-linked (GlcNAc...) asparagine; by host
Glycosylation190N-linked (GlcNAc...) asparagine; by host
Glycosylation201N-linked (GlcNAc...) asparagine; by host
Glycosylation221N-linked (GlcNAc...) asparagine; by host
Glycosylation273N-linked (GlcNAc...) asparagine; by host
Glycosylation326N-linked (GlcNAc...) asparagine; by host
Glycosylation353N-linked (GlcNAc...) asparagine; by host
Glycosylation370N-linked (GlcNAc...) asparagine; by host
Glycosylation445N-linked (GlcNAc...) asparagine; by host
Glycosylation477N-linked (GlcNAc...) asparagine; by host
Glycosylation483N-linked (GlcNAc...) asparagine; by host
Glycosylation529N-linked (GlcNAc...) asparagine; by host
Glycosylation547N-linked (GlcNAc...) asparagine; by host
Glycosylation573N-linked (GlcNAc...) asparagine; by host
Glycosylation629N-linked (GlcNAc...) asparagine; by host
Glycosylation646N-linked (GlcNAc...) asparagine; by host
Glycosylation689N-linked (GlcNAc...) asparagine; by host
Glycosylation710N-linked (GlcNAc...) asparagine; by host
Glycosylation720N-linked (GlcNAc...) asparagine; by host
Glycosylation733N-linked (GlcNAc...) asparagine; by host

Post-translational modification

120 kDa Glycoprotein O: A shorter mature protein, gO-80K, is produced probably by proteolytic cleavage.
120 kDa Glycoprotein O: Modified with high mannose-oligosaccharides.

80 kDa Glycoprotein O

N-glycosylated with complex glycans.

Keywords

PTM databases

Interaction

Subunit

80 kDa Glycoprotein O

Part of a gH-gL-gO complex.

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias240-259Polar residues
Region240-272Disordered
Region330-351Disordered
Region541-568Disordered
Region667-712Disordered

Sequence similarities

Belongs to the herpesviridae U47 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    738
  • Mass (Da)
    82,991
  • Last updated
    1996-10-01 v1
  • Checksum
    EA6BCE87D45BE77A
MLHISRLGLFLALFAIVMHSVNLIKYTSDPLEAFKTVNRHNWSDEQREHFYDLRNLYTTFCQRNLSLDCFTQILTNVFSWNIRDLQCKSAVNLSPLQNLPRAETKIVLSSTAANKSIVASSFSLFYLLFATLSTYTADPPCVELLPFKILGTQLFDIKLTDESLQMAISKFSNSNLTRSLTPFTPEIFFNYTSFVYFLLYNTTSCIRSNDQYFEHSPKPINVTTSFGRAIVNFHSILTTTPSSTPSSTSASITSPHIPSTNTPTPEPSPVTKNFTELQTDTIKVTPNTPTITAQTTESIKKVVKRSDFPRPMYTPTDIPTLTIRRNATIKTEQNTENPTENPKSPPKPTNFENTTIRIPETFESTTVATNTTQKLESTTFATTIGIEEISDNIYSSPKNSIYLKSKSQQSTTKFTDTEHTTPILKFTTWQDAARTYMSHNTEVQNMTENFIKISLGETMGITPKEPTNPTQLLNVKNQTEYANETHSTEVQTVKTFKEDRFQRTTLKSSSEPPTVQTLSVTPKKKLPSNVTAKTEVQVTNNALPSSNSSHSITKVTEEPKQNRMSASTHGEINHTEIPRMTPILNAHTWEKSTTPQWPFTAETSLTTSSKSAILTWSNLLTTPKEPLTNTSLRSTNHITTQLTTSNRTQSAKLTKAHVSSQTTNIYPQTITERSTDVKKKSSTESREANKTLPGNDYRVTDKNSHNHPDNLTTKAYSTQNATHYTYNERHDLNNTDST

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias240-259Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF157706
EMBL· GenBank· DDBJ
AAB06345.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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