Detail Information for IndEnz0002006387
IED ID IndEnz0002006387
Enzyme Type ID protease006387
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 Tacaribe virus (strain TRVL 11598) (TCRV)
Taxonomic Lineage Viruses Riboviria Orthornavirae Negarnaviricota Polyploviricotina Ellioviricetes Bunyavirales Arenaviridae Mammarenavirus Tacaribe virus (TCRV) Tacaribe virus (strain TRVL 11598) (TCRV)
Enzyme Sequence MGQFISFMQEIPIFLQEALNIALVAVSLICIVKGLVNLYRCGLFQLMVFLVLAGRSCSEETFKIGMHTQFQEVSLSLSALLTNQSHELPMLCLANKTHLYLKSGRSSFKINIDSVTVLTRSADVFVHSPKLGSCFESDEEWVVAWWIEAIGHRWDQDPGLLCRNKTKTEGKLIQINISRADGNVHYGWRLKNGLDHIYRGREEPCFEGEQCLIKIQPEDWPTDCKADHTNTFRFLSRSQKSIAVGRTLKAFFSWSLTDPLGNEAPGGYCLEKWMLVASELKCFGNTAIAKCNQNHDSEFCDMLRLFDYNKNAIKTLNEETKTRVNVLSHTINALISDNLLMKNKIRELMSVPYCNYTRFWYVNHTLSGQHSLPRCWMIRNNSYLNSSEFRNEWILESDFLISEMLSKEYSERQGRTPITLVDICFWSTVFFTSTLFLHLIGFPTHEHIRGEGCPLPHRLNSMGGCRCGKYLPLKKPTIWHRRH
Enzyme Length 483
Uniprot Accession Number P31840
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. {ECO:0000255|HAMAP-Rule:MF_04084}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (4); Disulfide bond (6); Glycosylation (8); Initiator methionine (1); Lipidation (1); Metal binding (8); Site (2); Topological domain (5); Transmembrane (3)
Keywords 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}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 55,602
Kinetics
Metal Binding METAL 57; /note=Zinc 1; /evidence=ECO:0000255|HAMAP-Rule:MF_04084; METAL 445; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_04084; METAL 447; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_04084; METAL 453; /note=Zinc 2; /evidence=ECO:0000255|HAMAP-Rule:MF_04084; METAL 457; /note=Zinc 1; via pros nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_04084; METAL 465; /note=Zinc 1; /evidence=ECO:0000255|HAMAP-Rule:MF_04084; METAL 467; /note=Zinc 1; /evidence=ECO:0000255|HAMAP-Rule:MF_04084; METAL 483; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_04084
Rhea ID
Cross Reference Brenda