P10228 · GC_HHV11

Function

function

Major attachment protein that mediates binding of the virus to cell surface heparan sulfate or chondroitin sulfate. Also plays several roles in host immune evasion by inhibiting the host complement cascade activation, and by providing a shield against neutralizing antibodies that interfere with gB-gD, gB-gH/gL or gD-gH/gL interactions (By similarity).

Miscellaneous

There are seven external glycoproteins in HSV-1 and 2: gH, gB, gC, gG, gD, gI, and gE.

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 Componentmembrane
Cellular Componentvirion membrane
Molecular Functioncomplement binding
Biological Processadhesion receptor-mediated virion attachment to host cell
Biological Processsymbiont entry into host cell
Biological Processsymbiont-mediated suppression of host complement activation
Biological Processvirus-mediated perturbation of host defense response

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Envelope glycoprotein C

Gene names

    • Name
      gC
    • Synonyms
      UL44

Organism names

Accessions

  • Primary accession
    P10228

Proteomes

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain25-480Virion surface
Transmembrane481-497Helical
Topological domain498-511Cytoplasmic

Keywords

Phenotypes & Variants

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-24
ChainPRO_000003819725-511Envelope glycoprotein C
Glycosylation42N-linked (GlcNAc...) asparagine; by host
Glycosylation70N-linked (GlcNAc...) asparagine; by host
Glycosylation74N-linked (GlcNAc...) asparagine; by host
Glycosylation108N-linked (GlcNAc...) asparagine; by host
Disulfide bond127↔144
Glycosylation148N-linked (GlcNAc...) asparagine; by host
Glycosylation181N-linked (GlcNAc...) asparagine; by host
Glycosylation197N-linked (GlcNAc...) asparagine; by host
Disulfide bond286↔347
Glycosylation362N-linked (GlcNAc...) asparagine; by host
Disulfide bond386↔442
Disulfide bond390↔419

Keywords

PTM databases

Interaction

Subunit

Interacts with host complement component C3b; this interaction inhibits host immune response by disregulating complement cascade.

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias42-80Polar residues
Region42-130Disordered
Compositional bias81-105Pro residues
Region137-151Heparin-binding domain
Domain267-359Ig-like

Sequence similarities

Keywords

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing & Alternative initiation.

P10228-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    gC
  • Note
    Membrane-bound gC.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    511
  • Mass (Da)
    54,998
  • Last updated
    1989-07-01 v1
  • Checksum
    874BE474DC7D71C5
MAPGRVGLAVVLWSLLWLGAGVSGGSETASTGPTITAGAVTNASEAPTSGSPGSAASPEVTPTSTPNPNNVTQNKTTPTEPASPPTTPKPTSTPKSPPTSTPDPKPKNNTTPAKSGRPTKPPGPVWCDRRDPLARYGSRVQIRCRFRNSTRMEFRLQIWRYSMGPSPPIAPAPDLEEVLTNITAPPGGLLVYDSAPNLTDPHVLWAEGAGPGADPPLYSVTGPLPTQRLIIGEVTPATQGMYYLAWGRMDSPHEYGTWVRVRMFRPPSLTLQPHAVMEGQPFKATCTAAAYYPRNPVEFVWFEDDHQVFNPGQIDTQTHEHPDGFTTVSTVTSEAVGGQVPPRTFTCQMTWHRDSVTFSRRNATGLALVLPRPTITMEFGVRIVVCTAGCVPEGVTFAWFLGDDPSPAAKSAVTAQESCDHPGLATVRSTLPISYDYSEYICRLTGYPAGIPVLEHHGSHQPPPRDPTERQVIEAIEWVGIGIGVLAAGVLVVTAIVYVVRTSQSRQRHRR

P10228-2

  • Name
    gCsec
  • Note
    Secreted.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 472-511: VIEAIEWVGIGIGVLAAGVLVVTAIVYVVRTSQSRQRHRR → VILGRSRTTHGVEQNASP

Features

Showing features for compositional bias, alternative sequence.

TypeIDPosition(s)Description
Compositional bias42-80Polar residues
Compositional bias81-105Pro residues
Alternative sequenceVSP_040892472-511in isoform gCsec

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X14112
EMBL· GenBank· DDBJ
CAA32294.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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