P16832 · GL_HCMVA

Function

function

The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH (By similarity).
In human cytomegalovirus, forms two distincts complexes to mediate viral entry, a trimer and a pentamer at the surface of the virion envelope. The gH-gL-gO trimer is required for infection in fibroblasts by interacting with host PDGFRA. The gH-gL-UL128-UL130-UL131A pentamer is essential for viral entry in epithelial, endothelial and myeloid cells via interaction with host NRP2 (By similarity).

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 Golgi apparatus
Cellular Componenthost cell plasma membrane
Cellular Componentmembrane
Cellular Componentviral envelope
Cellular Componentvirion membrane
Biological Processentry receptor-mediated virion attachment to host cell
Biological Processfusion of virus membrane with host plasma membrane
Biological Processsymbiont entry into host cell

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Envelope glycoprotein L
  • Short names
    gL

Gene names

    • Name
      gL
    • Synonyms
      UL115

Organism names

Accessions

  • Primary accession
    P16832
  • Secondary accessions
    • Q7M6S9

Proteomes

Subcellular Location

Virion membrane
; Peripheral membrane protein
Host cell membrane
; Peripheral membrane protein
Host Golgi apparatus, host trans-Golgi network
Note: gL associates with the extravirion surface through its binding to gH. During virion morphogenesis, this protein probably accumulates in the host trans-Golgi where secondary envelopment occurs.

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-30
ChainPRO_000003827831-278Envelope glycoprotein L
Disulfide bond47Interchain
Disulfide bond54Interchain
Disulfide bond144Interchain
Disulfide bond154↔159

Keywords

Interaction

Subunit

Interacts with glycoprotein H (gH); this interaction is necessary for the correct processing and cell surface expression of gH (By similarity).
Forms the envelope pentamer complex (PC) composed of gH, gL, UL128, UL130, and UL131A. The pentamer interacts with host NRP2. Forms the envelope trimer complex composed of gH, gL, and gO. The trimer interacts with host PDGFRA (By similarity) (PubMed:21880752, PubMed:9733861).

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain43-256gL betaherpesvirus-type

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    278
  • Mass (Da)
    30,913
  • Last updated
    1997-11-01 v2
  • Checksum
    9DD91A50BE0C25E5
MCRRPDCGFSFSPGPVVLLWCCLLLPIVSSVAVSVAPTAAEKVPAECPELTRRCLLGEVFQGDKYESWLRPLVNVTRRDGPLSQLIRYRPVTPEAANSVLLDDAFLDTLALLYNNPDQLRALLTLLSSDTAPRWMTVMRGYSECGDGSPAVYTCVDDLCRGYDLTRLSYGRSIFTEHVLGFELVPPSLFNVVVAIRNEATRTNRAVRLPVSTAAAPEGITLFYGLYNAVKEFCLRHQLDPPLLRHLDKYYAGLPPELKQTRVNLPAHSRYGPQAVDAR

Sequence caution

The sequence CAA35317.1 differs from that shown. Reason: Erroneous initiation

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X17403
EMBL· GenBank· DDBJ
CAA35317.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
AF530171
EMBL· GenBank· DDBJ
AAM96168.1
EMBL· GenBank· DDBJ
Genomic DNA
AF530172
EMBL· GenBank· DDBJ
AAM96169.1
EMBL· GenBank· DDBJ
Genomic DNA
AF530173
EMBL· GenBank· DDBJ
AAM96170.1
EMBL· GenBank· DDBJ
Genomic DNA
BK000394
EMBL· GenBank· DDBJ
DAA00105.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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