| IED ID | IndEnz0002003815 |
| Enzyme Type ID | protease003815 |
| Protein Name |
Pre-glycoprotein polyprotein GP complex Pre-GP-C Cleaved into: Stable signal peptide SSP ; Glycoprotein G1 GP1 ; Glycoprotein G2 GP2 |
| Gene Name | GPC GP-C |
| Organism | Junin mammarenavirus (JUNV) (Junn mammarenavirus) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Negarnaviricota Polyploviricotina Ellioviricetes Bunyavirales Arenaviridae Mammarenavirus Junin mammarenavirus (JUNV) (Junn mammarenavirus) |
| Enzyme Sequence | MGQFISFMQEIPTFLQEALNIALVAVSLIAIIKGVVNLYKSGLFQFFVFLALAGRSCTEEAFKIGLHTEFQTVSFSMVGLFSNNPHDLPLLCTLNKSHLYIKGGNASFKISFDDIAVLLPEYDVIIQHPADMSWCSKSDDQIWLSQWFMNAVGHDWYLDPPFLCRNRTKTEGFIFQVNTSKTGINENYAKKFKTGMHHLYREYPDSCLDGKLCLMKAQPTSWPLQCPLDHVNTLHFLTRGKNIQLPRRSLKAFFSWSLTDSSGKDTPGGYCLEEWMLVAAKMKCFGNTAVAKCNLNHDSEFCDMLRLFDYNKNAIKTLNDETKKQVNLMGQTINALISDNLLMKNKIRELMSVPYCNYTKFWYVNHTLSGQHSLPRCWLIKNNSYLNISDFRNDWILESDFLISEMLSKEYSDRQGKTPLTLVDICFWSTVFFTASLFLHLVGIPTHRHIRGEACPLPHRLNSLGGCRCGKYPNLKKPTVWRRGH |
| Enzyme Length | 485 |
| Uniprot Accession Number | P26313 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: [Glycoprotein G2]: 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 upon acidification in the endosome. {ECO:0000255|HAMAP-Rule:MF_04084}.; FUNCTION: Stable signal peptide (SSP): cleaved and functions as a signal peptide. In addition, it is also retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion. {ECO:0000255|HAMAP-Rule:MF_04084}.; FUNCTION: [Glycoprotein G1]: Interacts with the host receptor (By similarity). Mediates virus attachment to host TFRC. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis (PubMed:17287727). {ECO:0000255|HAMAP-Rule:MF_04084, ECO:0000269|PubMed:17287727, ECO:0000269|PubMed:19548229}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (11); Chain (4); Disulfide bond (6); Glycosylation (8); Helix (4); Initiator methionine (1); Lipidation (1); Metal binding (8); Mutagenesis (3); Region (2); Site (2); Topological domain (5); Transmembrane (3); Turn (4) |
| Keywords | 3D-structure;Disulfide bond;Fusion of virus membrane with host endosomal membrane;Fusion of virus membrane with host membrane;Glycoprotein;Host Golgi apparatus;Host cell membrane;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Lipoprotein;Membrane;Metal-binding;Myristate;Transmembrane;Transmembrane helix;Viral attachment to host cell;Viral envelope protein;Viral penetration into host cytoplasm;Virion;Virus endocytosis by host;Virus entry into host cell;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Glycoprotein G1]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}.; SUBCELLULAR LOCATION: [Glycoprotein G2]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. 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. {ECO:0000255|HAMAP-Rule:MF_04084}.; SUBCELLULAR LOCATION: [Stable signal peptide]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. |
| Modified Residue | |
| Post Translational Modification | PTM: 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. {ECO:0000255|HAMAP-Rule:MF_04084}.; PTM: The SSP remains stably associated with the GP complex following cleavage by signal peptidase and plays crucial roles in the trafficking of GP through the secretory pathway. {ECO:0000255|HAMAP-Rule:MF_04084, ECO:0000269|PubMed:18400865}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1); X-ray crystallography (2) |
| Cross Reference PDB | 2L0Z; 5EN2; 5W1K; |
| Mapped Pubmed ID | 29760382; |
| Motif | |
| Gene Encoded By | |
| Mass | 55,607 |
| Kinetics | |
| Metal Binding | METAL 57; /note="Zinc 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_04084, ECO:0000269|PubMed:21068387"; METAL 447; /note="Zinc 2; via tele nitrogen"; /evidence="ECO:0000255|HAMAP-Rule:MF_04084, ECO:0000269|PubMed:21068387"; METAL 449; /note="Zinc 2; via tele nitrogen"; /evidence="ECO:0000255|HAMAP-Rule:MF_04084, ECO:0000269|PubMed:21068387"; METAL 455; /note="Zinc 2"; /evidence="ECO:0000255|HAMAP-Rule:MF_04084, ECO:0000269|PubMed:21068387"; METAL 459; /note="Zinc 1; via pros nitrogen"; /evidence="ECO:0000255|HAMAP-Rule:MF_04084, ECO:0000269|PubMed:21068387"; METAL 467; /note="Zinc 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_04084, ECO:0000269|PubMed:21068387"; METAL 469; /note="Zinc 1"; /evidence="ECO:0000255|HAMAP-Rule:MF_04084, ECO:0000269|PubMed:21068387"; METAL 485; /note="Zinc 2; via tele nitrogen"; /evidence="ECO:0000255|HAMAP-Rule:MF_04084, ECO:0000269|PubMed:21068387" |
| Rhea ID | |
| Cross Reference Brenda |