P18551 · GB_EHV1A
- ProteinEnvelope glycoprotein B
- GenegB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids980 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | host cell endosome membrane | |
Cellular Component | host cell Golgi membrane | |
Cellular Component | host cell plasma membrane | |
Cellular Component | membrane | |
Cellular Component | viral envelope | |
Cellular Component | virion membrane | |
Biological Process | symbiont entry into host cell | |
Biological Process | virion attachment to host cell |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameEnvelope glycoprotein B
- Short namesgB
Gene names
Organism names
- Taxonomic lineageViruses > Duplodnaviria > Heunggongvirae > Peploviricota > Herviviricetes > Herpesvirales > Orthoherpesviridae > Alphaherpesvirinae > Varicellovirus > Varicellovirus equidalpha1 > Equid alphaherpesvirus 1
- Virus hosts
Accessions
- Primary accessionP18551
Subcellular Location
UniProt Annotation
GO Annotation
Virion membrane ; Single-pass type I membrane protein
Host cell membrane ; Single-pass type I membrane protein
Host endosome membrane ; Single-pass type I membrane protein
Host Golgi apparatus membrane ; Single-pass type I membrane protein
Note: During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 87-849 | Virion surface | ||||
Sequence: PTTPSPPTSTPTSMSTHSHGTVDPTLLPTETPDPLRLAVRESGILAEDGDFYTCPPPTGSTVVRIEPPRTCPKFDLGRNFTEGIAVIFKENIAPYKFRANVYYKDIVVTRVWKGYSHTSLSDRYNDRVPVSVEEIFGLIDSKGKCSSKAEYLRDNIMHHAYHDDEDEVELDLVPSKFATPGARAWQTTNDTTSYVGWMPWRHYTSTSVNCIVEEVEARSVYPYDSFALSTGDIVYASPFYGLRAAARIEHNSYAQDSFRQVEGYRPRDLDSKLQAEEPVTKNFITTPHVTVSWNWTEKKVEACTLTKWKEVDELVRDEFRGSYRFTIRSISSTFISNTTQFKLESAPLTECVSKEAKEAIDSIYKKQYESTHVFSGDVEYYLARGGFLIAFRPMLSNELARLYLNELVRSNRTYDLKNLLNPNANNNNNTTRRRRSLLSVPEPQPTQDGVHREQILHRLHKRAVEATAGTDSSNVTAKQLELIKTTSSIEFAMLQFAYDHIQSHVNEMLSRIATAWCTLQNKERTLWNEMVKINPSAIVSATLDERVAARVLGDVIAITHCAKIEGNVYLQNSMRSMDSNTCYSRPPVTFTITKNANNRGSIEGQLGEENEIFTERKLIEPCALNQKRYFKFGKEYVYYENYTFVRKVPPTEIEVISTYVELNLTLLEDREFLPLEVYTRAELEDTGLLDYSEIQRRNQLHALRFYDIDSVVNVDNTAVIMQGIASFFKGLGKVGEAVGTLVLAAAGAVVSTVSGIASFLNNP | ||||||
Transmembrane | 850-870 | Helical | ||||
Sequence: FGGLAIGLLVIAGLVAAFFAY | ||||||
Topological domain | 871-980 | Intravirion | ||||
Sequence: RYVMQIRSNPMKALYPITTKALKNKAKTSYGQNEEDDGSDFDEAKLEEAREMIKYMSMVSALEKQEKKAIKKNSGVGLIASNVSKLALRRRGPKYTRLQQNDTMENEKMV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-86 | |||||
Sequence: MSSGCRSVGGSTWGNWRGDGGDLRQRRVLSPVCSAPAAGSWIGSQLGNVGNLLATPHPLGKPASSRVGTIVLACLLLFGSCVVRAV | ||||||
Chain | PRO_0000038171 | 87-980 | Envelope glycoprotein B | |||
Sequence: PTTPSPPTSTPTSMSTHSHGTVDPTLLPTETPDPLRLAVRESGILAEDGDFYTCPPPTGSTVVRIEPPRTCPKFDLGRNFTEGIAVIFKENIAPYKFRANVYYKDIVVTRVWKGYSHTSLSDRYNDRVPVSVEEIFGLIDSKGKCSSKAEYLRDNIMHHAYHDDEDEVELDLVPSKFATPGARAWQTTNDTTSYVGWMPWRHYTSTSVNCIVEEVEARSVYPYDSFALSTGDIVYASPFYGLRAAARIEHNSYAQDSFRQVEGYRPRDLDSKLQAEEPVTKNFITTPHVTVSWNWTEKKVEACTLTKWKEVDELVRDEFRGSYRFTIRSISSTFISNTTQFKLESAPLTECVSKEAKEAIDSIYKKQYESTHVFSGDVEYYLARGGFLIAFRPMLSNELARLYLNELVRSNRTYDLKNLLNPNANNNNNTTRRRRSLLSVPEPQPTQDGVHREQILHRLHKRAVEATAGTDSSNVTAKQLELIKTTSSIEFAMLQFAYDHIQSHVNEMLSRIATAWCTLQNKERTLWNEMVKINPSAIVSATLDERVAARVLGDVIAITHCAKIEGNVYLQNSMRSMDSNTCYSRPPVTFTITKNANNRGSIEGQLGEENEIFTERKLIEPCALNQKRYFKFGKEYVYYENYTFVRKVPPTEIEVISTYVELNLTLLEDREFLPLEVYTRAELEDTGLLDYSEIQRRNQLHALRFYDIDSVVNVDNTAVIMQGIASFFKGLGKVGEAVGTLVLAAAGAVVSTVSGIASFLNNPFGGLAIGLLVIAGLVAAFFAYRYVMQIRSNPMKALYPITTKALKNKAKTSYGQNEEDDGSDFDEAKLEEAREMIKYMSMVSALEKQEKKAIKKNSGVGLIASNVSKLALRRRGPKYTRLQQNDTMENEKMV | ||||||
Disulfide bond | 140↔647 | |||||
Sequence: CPPPTGSTVVRIEPPRTCPKFDLGRNFTEGIAVIFKENIAPYKFRANVYYKDIVVTRVWKGYSHTSLSDRYNDRVPVSVEEIFGLIDSKGKCSSKAEYLRDNIMHHAYHDDEDEVELDLVPSKFATPGARAWQTTNDTTSYVGWMPWRHYTSTSVNCIVEEVEARSVYPYDSFALSTGDIVYASPFYGLRAAARIEHNSYAQDSFRQVEGYRPRDLDSKLQAEEPVTKNFITTPHVTVSWNWTEKKVEACTLTKWKEVDELVRDEFRGSYRFTIRSISSTFISNTTQFKLESAPLTECVSKEAKEAIDSIYKKQYESTHVFSGDVEYYLARGGFLIAFRPMLSNELARLYLNELVRSNRTYDLKNLLNPNANNNNNTTRRRRSLLSVPEPQPTQDGVHREQILHRLHKRAVEATAGTDSSNVTAKQLELIKTTSSIEFAMLQFAYDHIQSHVNEMLSRIATAWCTLQNKERTLWNEMVKINPSAIVSATLDERVAARVLGDVIAITHC | ||||||
Disulfide bond | 157↔603 | |||||
Sequence: CPKFDLGRNFTEGIAVIFKENIAPYKFRANVYYKDIVVTRVWKGYSHTSLSDRYNDRVPVSVEEIFGLIDSKGKCSSKAEYLRDNIMHHAYHDDEDEVELDLVPSKFATPGARAWQTTNDTTSYVGWMPWRHYTSTSVNCIVEEVEARSVYPYDSFALSTGDIVYASPFYGLRAAARIEHNSYAQDSFRQVEGYRPRDLDSKLQAEEPVTKNFITTPHVTVSWNWTEKKVEACTLTKWKEVDELVRDEFRGSYRFTIRSISSTFISNTTQFKLESAPLTECVSKEAKEAIDSIYKKQYESTHVFSGDVEYYLARGGFLIAFRPMLSNELARLYLNELVRSNRTYDLKNLLNPNANNNNNTTRRRRSLLSVPEPQPTQDGVHREQILHRLHKRAVEATAGTDSSNVTAKQLELIKTTSSIEFAMLQFAYDHIQSHVNEMLSRIATAWC | ||||||
Glycosylation | 165 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 231↔296 | |||||
Sequence: CSSKAEYLRDNIMHHAYHDDEDEVELDLVPSKFATPGARAWQTTNDTTSYVGWMPWRHYTSTSVNC | ||||||
Glycosylation | 275 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 380 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 389↔437 | |||||
Sequence: CTLTKWKEVDELVRDEFRGSYRFTIRSISSTFISNTTQFKLESAPLTEC | ||||||
Glycosylation | 423 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 497 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 514 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 515 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 560 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 668↔708 | |||||
Sequence: CYSRPPVTFTITKNANNRGSIEGQLGEENEIFTERKLIEPC | ||||||
Glycosylation | 727 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 749 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N |
Post-translational modification
A proteolytic cleavage by host furin generates two subunits that remain linked by disulfide bonds.
Keywords
- PTM
PTM databases
Interaction
Subunit
Homotrimer; disulfide-linked. Binds to heparan sulfate proteoglycans. Interacts with gH/gL heterodimer.
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MSSGCRSVGGSTWGNWRGDG | ||||||
Region | 88-118 | Disordered | ||||
Sequence: TTPSPPTSTPTSMSTHSHGTVDPTLLPTETP | ||||||
Compositional bias | 95-111 | Polar residues | ||||
Sequence: STPTSMSTHSHGTVDPT | ||||||
Region | 197-203 | Involved in fusion and/or binding to host membrane | ||||
Sequence: VWKGYSH | ||||||
Region | 282-290 | Involved in fusion and/or binding to host membrane | ||||
Sequence: GWMPWRHYT | ||||||
Compositional bias | 505-529 | Polar residues | ||||
Sequence: LLNPNANNNNNTTRRRRSLLSVPEP | ||||||
Region | 505-535 | Disordered | ||||
Sequence: LLNPNANNNNNTTRRRRSLLSVPEPQPTQDG | ||||||
Region | 794-847 | Hydrophobic membrane proximal region | ||||
Sequence: IDSVVNVDNTAVIMQGIASFFKGLGKVGEAVGTLVLAAAGAVVSTVSGIASFLN | ||||||
Region | 823-843 | Hydrophobic membrane proximal region | ||||
Sequence: AVGTLVLAAAGAVVSTVSGIA | ||||||
Motif | 925-928 | Golgi targeting | ||||
Sequence: YMSM | ||||||
Motif | 965-968 | Internalization motif | ||||
Sequence: YTRL |
Sequence similarities
Belongs to the herpesviridae glycoprotein B family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length980
- Mass (Da)109,736
- Last updated1990-11-01 v1
- Checksum264D273CED70E5A1
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 95-111 | Polar residues | ||||
Sequence: STPTSMSTHSHGTVDPT | ||||||
Compositional bias | 505-529 | Polar residues | ||||
Sequence: LLNPNANNNNNTTRRRRSLLSVPEP |