IED ID | IndEnz0002016004 |
Enzyme Type ID | protease016004 |
Protein Name |
Envelope glycoprotein B gB |
Gene Name | gB |
Organism | Suid herpesvirus 1 (strain Indiana-Funkhauser / Becker) (SuHV-1) (Pseudorabies virus (strain Indiana-Funkhauser / Becker)) |
Taxonomic Lineage | Viruses Duplodnaviria Heunggongvirae Peploviricota Herviviricetes Herpesvirales Herpesviridae Alphaherpesvirinae Varicellovirus Suid alphaherpesvirus 1 Suid herpesvirus 1 (strain Indiana-Funkhauser / Becker) (SuHV-1) (Pseudorabies virus (strain Indiana-Funkhauser / Becker)) |
Enzyme Sequence | MPAGGGLWRGPRGHRPGHHGGAGLGRLWPAPHHAAAARGAVALALLLLALAAAPPCGAAAVTRAASASPTPGTGATPNDVSAEASLEEIEAFSPGPSEAPDGEYGDLDARTAVRAAATERDRFYVCPPPSGSTVVRLEPEQACPEYSQGRNFTEGIAVLFKENIAPHKFKAHIYYKNVIVTTVWSGSTYAAITNRFTDRVPVPVQEITDVIDRRGKCVSKAEYVRNNHKVTAFDRDENPVEVDLRPSRLNALGTRGWHTTNDTYTKIGAAGFYHTGTSVNCIVEEVEARSVYPYDSFALSTGDIVYMSPFYGLREGAHGEHIGYAPGRFQQVEHYYPIDLDSRLRASESVTRNFLRTPHFTVAWDWAPKTRRVCSLAKWREAEEMTRDETRDGSFRFTSRALGASFVSDVTQLDLQRVHLGDCVLREASEAIDAIYRRRYNSTHVLAGDRPEVYLARGGFVVAFRPLISNELAQLYARELERLGLAGVVGPAAPAAARRARRSPGPAGTPEPPAVNGTGHLRITTGSAEFARLQFTYDHIQAHVNDMLGRIAAAWCELQNKDRTLWSEMSRLNPSAVATAALGQRVSARMLGDVMAISRCVEVRGGVYVQNSMRVPGERGTCYSRPLVTFEHNGTGVIEGQLGDDNELLISRDLIEPCTGNHRRYFKLGSGYVYYEDYNYVRMVEVPETISTRVTLNLTLLEDREFLPLEVYTREELADTGLLDYSEIQRRNQLHALKFYDIDRVVKVDHNVVLLRGIANFFQGLGDVGAAVGKVVLGATGAVISAVGGMVSFLSNPFGALAIGLLVLAGLVAAFLAYRHISRLRRNPMKALYPVTTKTLKEDGVDEGDVDEAKLDQARDMIRYMSIVSALEQQEHKARKKNSGPALLASRVGAMATRRRHYQRLESEDPDAL |
Enzyme Length | 913 |
Uniprot Accession Number | P08355 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme 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. {ECO:0000255|HAMAP-Rule:MF_04032}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (5); Glycosylation (6); Motif (1); Region (6); Signal peptide (1); Topological domain (2); Transmembrane (1) |
Keywords | Disulfide bond;Glycoprotein;Host Golgi apparatus;Host cell membrane;Host endosome;Host membrane;Host-virus interaction;Membrane;Signal;Transmembrane;Transmembrane helix;Viral attachment to host cell;Viral envelope protein;Virion;Virus entry into host cell |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. 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). {ECO:0000255|HAMAP-Rule:MF_04032}. |
Modified Residue | |
Post Translational Modification | PTM: A proteolytic cleavage by host furin generates two subunits that remain linked by disulfide bonds. {ECO:0000305}. |
Signal Peptide | SIGNAL 1..59; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 902..905; /note=Internalization motif; /evidence=ECO:0000255|HAMAP-Rule:MF_04032 |
Gene Encoded By | |
Mass | 100,234 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |