HAMAP rule MF_04084
General rule information
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| Accession | MF_04084 |
| Dates | 12-JAN-2018 (Created)
4-JUL-2023 (Last updated, Version 10) |
| Name | ARENA_GPC |
| Scope(s) |
Viruses Arenaviridae |
| Template(s) | P19240 (GLYC_MOPEI); P08669 (GLYC_LASSJ); P26313 (GLYC_JUNIN); P09991 (GLYC_LYCVA); [ Recover all ] |
| Triggered by |
HAMAP; MF_04084 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | GLYC |
| Protein name | RecName: Full=Pre-glycoprotein polyprotein GP complex; Short=Pre-GP-C; Contains: RecName: Full=Stable signal peptide; Short=SSP; Contains: RecName: Full=Glycoprotein G1; Short=GP1; Contains: RecName: Full=Glycoprotein G2; Short=GP2; |
| Gene name | Name=GPC; |
Comments
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| FUNCTION | [Stable signal peptide]: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP- C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post- translational maturation cleavage of G1 and G2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion. |
| case <OS:Mammarenavirus lassaense> | |
| FUNCTION | [Glycoprotein G1]: Forms the virion spikes together with glycoprotein G2. The glycoprotein spike trimers are connected to the underlying matrix. Interacts with the host receptor. Mediates virus attachment to the host primary receptor alpha-dystroglycan DAG1 (alpha- DG) at the cell surface. This attachment induces virion internalization apparently through macropinocytosis. Following endocytosis, there is a pH-dependent switch from binding DAG1 to the host lysosomal receptor LAMP1. This latter binding triggers the dissociation of GP1, exposing the fusion subunit, GP2, such that fusion can occur. Down-modulates host DAG1. |
| else | |
| FUNCTION | [Glycoprotein G1]: Forms the virion spikes together with glycoprotein G2. The glycoprotein spike trimers are connected to the underlying matrix. Interacts with the host receptor leading to virus endocytosis. |
| end case | |
| FUNCTION | [Glycoprotein G2]: Forms the virion spikes together with glycoprotein G1. The glycoprotein spike trimers are connected to the underlying matrix. Class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced by acidification. |
| SUBUNIT | [Stable signal peptide]: Interacts with glycoprotein G2. Part of the GP complex (GP-C) together with glycoprotein G1 and glycoprotein G2. The GP-complex interacts with protein Z, which interacts with ribonucleocapsid; these interactions may induce virion budding. |
| case <OS:Mammarenavirus lassaense> | |
| SUBUNIT | [Glycoprotein G1]: Homotrimer; disulfide-linked. In pre-fusion state, G1 homotrimers bind G2 homotrimers via ionic interactions. Part of the GP complex (GP-C) together with glycoprotein G2 and the stable signal peptide. Interacts with the primary host receptor DAG1 on the cell surface; this interaction occurs at pH 8.0 but not at pH 6.0 and below. Upon virus internalization and at endosomal pH, interacts with the host lysosomal protein LAMP1; this interaction mediates G1 dissociation from GP-C and membrane fusion. The GP-complex interacts with protein Z, which interacts with ribonucleocapsid; these interactions may induce virion budding. |
| else | |
| SUBUNIT | [Glycoprotein G1]: Homotrimer; disulfide-linked. In pre-fusion state, G1 homotrimers bind G2 homotrimers via ionic interactions. Part of the GP complex (GP-C) together with glycoprotein G2 and the stable signal peptide. The GP-complex interacts with protein Z, which interacts with ribonucleocapsid; these interactions may induce virion budding. |
| end case | |
| SUBUNIT | [Glycoprotein G2]: Homotrimer. Interacts with the stable signal peptide. In pre-fusion state, G2 homotrimers bind G1 homotrimers via ionic interactions. Part of the GP complex (GP-C) together with glycoprotein G1 and the stable signal peptide. Acidification in the endosome triggers rearrangements, which ultimately leads to a 6 helix bundle formed by the two heptad repeat domains (HR1 and HR2) in post- fusion state. The GP-complex interacts with protein Z, which interacts with ribonucleocapsid; these interactions may induce virion budding. |
| SUBCELLULAR LOCATION | [Stable signal peptide]: Virion membrane; Single- pass type II membrane protein. Host endoplasmic reticulum membrane; Single-pass type II membrane protein. Host Golgi apparatus membrane; Single-pass type II membrane protein. Host cell membrane ; Single-pass type II membrane protein. |
| SUBCELLULAR LOCATION | [Glycoprotein G1]: Virion membrane; Peripheral membrane protein. Host endoplasmic reticulum membrane; Peripheral membrane protein. Host Golgi apparatus membrane; Peripheral membrane protein. Host cell membrane; Peripheral membrane protein. |
| SUBCELLULAR LOCATION | [Glycoprotein G2]: Virion membrane; Single-pass membrane protein. Host endoplasmic reticulum membrane; Single-pass membrane protein. Host Golgi apparatus membrane; Single-pass membrane protein. Host cell membrane; Single-pass membrane protein. Note=Binding to the stable signal peptide masks endogenous ER localization signals in the cytoplasmic domain of G2 to ensure that only the fully assembled, tripartite GP complex is transported for virion assembly. |
| DOMAIN | [Stable signal peptide]: The N-terminus is localized at the extracellular side of the GP-C, with a part embedded in the membrane probably. |
| case <OS:Mammarenavirus lassaense> and <FTGroup:1> | |
| DOMAIN | [Glycoprotein G1]: Upon protonation in a weak acidic environment, the histidine triad involved in host LAMP1 binding inhibits pre-mature triggering of the spike, an inhibition that LAMP1 overrides. |
| end case | |
| DOMAIN | [Glycoprotein G2]: Contains 1 fusion peptide at the N-terminus, 2 heptad repeats domains HR1 and HR2 and, at the C-terminus, a cytoplasmic domain that plays a role in ER location. Also contains a zinc-binding domain that allows SSP retention in the GPC complex by accepting a cysteine from SSP as the fourth ligand. |
| PTM | [Pre-glycoprotein polyprotein GP complex]: Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions. The SSP remains stably associated with the GP complex following cleavage by signal peptidase. |
| SIMILARITY | Belongs to the arenaviridae GPC protein family. |
Keywords
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Gene Ontology
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| GO:0020002; Cellular component:host cell plasma membrane |
| GO:0016020; Cellular component:membrane |
| GO:0019031; Cellular component:viral envelope |
| GO:0055036; Cellular component:virion membrane |
| GO:0039654; Biological process:fusion of virus membrane with host endosome membrane |
| GO:0019065; Biological process:receptor-mediated endocytosis of virus by host cell |
| GO:0019062; Biological process:virion attachment to host cell |
Cross-references
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| Pfam | PF00798; Arena_glycoprot; 1; |
| PIRSF | PIRSF004028; GPC_ArenaV; 1; |
| General | Transmembrane; -; 3; |
Features
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| From: GLYC_LASSJ (P08669) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| INIT_MET | 1 | 1 | /note="Removed; by host" | M | ||||||||
| CHAIN | 2 | Cter | /note="Pre-glycoprotein polyprotein GP complex" | |||||||||
| CHAIN | 2 | 58 | /note="Stable signal peptide" | |||||||||
| CHAIN | 59 | 259 | /note="Glycoprotein G1" | |||||||||
| CHAIN | 260 | Cter | /note="Glycoprotein G2" | |||||||||
| TOPO_DOM | 2 | 17 | /note="Extracellular" | |||||||||
| TRANSMEM | 18 | 33 | /note="Helical" | |||||||||
| TOPO_DOM | 34 | 58 | /note="Cytoplasmic" | |||||||||
| TOPO_DOM | 59 | 432 | /note="Extracellular" | |||||||||
| TRANSMEM | 433 | 453 | /note="Helical" | |||||||||
| TOPO_DOM | 454 | Cter | /note="Cytoplasmic" | |||||||||
| SITE | 58 | 59 | /note="Cleavage; by host signal peptidase" | |||||||||
| SITE | 259 | 260 | /note="Cleavage; by host MBTPS1" | |||||||||
| LIPID | 2 | 2 | /note="N-myristoyl glycine; by host" | G | ||||||||
| REGION | 258 | 294 | /note="Fusion" /evidence="ECO:0000269|PubMed:28572385, |
|||||||||
| REGION | 295 | 363 | /note="HR1" | |||||||||
| REGION | 368 | 431 | /note="HR2" | |||||||||
| CARBOHYD | 79 | 79 | /note="N-linked (GlcNAc...) asparagine; by host" | N | ||||||||
| CARBOHYD | 89 | 89 | /note="N-linked (GlcNAc...) asparagine; by host" | N | ||||||||
| CARBOHYD | 99 | 99 | /note="N-linked (GlcNAc...) asparagine; by host" | N | ||||||||
| CARBOHYD | 109 | 109 | /note="N-linked (GlcNAc...) asparagine; by host" | N | ||||||||
| CARBOHYD | 119 | 119 | /note="N-linked (GlcNAc...) asparagine; by host" | N | ||||||||
| CARBOHYD | 167 | 167 | /note="N-linked (GlcNAc...) asparagine; by host" | N | ||||||||
| CARBOHYD | 224 | 224 | /note="N-linked (GlcNAc...) asparagine; by host" | N | ||||||||
| CARBOHYD | 365 | 365 | /note="N-linked (GlcNAc...) asparagine; by host" | N | ||||||||
| CARBOHYD | 373 | 373 | /note="N-linked (GlcNAc...) asparagine; by host" | N | ||||||||
| CARBOHYD | 390 | 390 | /note="N-linked (GlcNAc...) asparagine; by host" | N | ||||||||
| CARBOHYD | 395 | 395 | /note="N-linked (GlcNAc...) asparagine; by host" | N | ||||||||
| DISULFID | 86 | 231 | C-x*-C | |||||||||
| DISULFID | 118 | 155 | C-x*-C | |||||||||
| DISULFID | 180 | 212 | C-x*-C | |||||||||
| DISULFID | 180 | 212 | C-x*-C | |||||||||
| DISULFID | 279 | 292 | C-x*-C | |||||||||
| DISULFID | 301 | 310 | C-x*-C | |||||||||
| DISULFID | 364 | 385 | C-x*-C | |||||||||
| case <OS:Mammarenavirus lassaense> | ||||||||||||
| REGION | 188 | 216 | /note="Binding to the host receptor LAMP1" | |||||||||
| SITE | 92 | 92 | /note="Binding to the host receptor LAMP1" | H | 1 | |||||||
| SITE | 93 | 93 | /note="Binding to the host receptor LAMP1" | H | 1 | |||||||
| SITE | 230 | 230 | /note="Binding to the host receptor LAMP1" | H | 1 | |||||||
| end case | ||||||||||||
| From: GLYC_JUNIN (P26313) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 57 | 57 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" |
C | ||||||||
| BINDING | 447 | 447 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" |
H | ||||||||
| BINDING | 449 | 449 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" |
H | ||||||||
| BINDING | 455 | 455 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" |
C | ||||||||
| BINDING | 459 | 459 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" |
H | ||||||||
| BINDING | 467 | 467 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" |
C | ||||||||
| BINDING | 469 | 469 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" |
C | ||||||||
| BINDING | 485 | 485 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" |
H | ||||||||
Additional information
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| Size range | 479-518 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |