UniProtKB - P07399 (GLYC_LYCVW)
Protein
Pre-glycoprotein polyprotein GP complex
Gene
GPC
Organism
Lymphocytic choriomeningitis virus (strain WE) (LCMV)
Status
Functioni
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.UniRule annotation
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.UniRule annotation
interacts with the host receptor.UniRule annotation
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 57 | Zinc 1UniRule annotation | 1 | |
Metal bindingi | 461 | Zinc 2; via tele nitrogenUniRule annotation | 1 | |
Metal bindingi | 463 | Zinc 2; via tele nitrogenUniRule annotation | 1 | |
Metal bindingi | 469 | Zinc 2UniRule annotation | 1 | |
Metal bindingi | 473 | Zinc 1; via pros nitrogenUniRule annotation | 1 | |
Metal bindingi | 481 | Zinc 1UniRule annotation | 1 | |
Metal bindingi | 483 | Zinc 1UniRule annotation | 1 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- fusion of virus membrane with host endosome membrane Source: UniProtKB-UniRule
- receptor-mediated endocytosis of virus by host cell Source: UniProtKB-UniRule
- virion attachment to host cell Source: UniProtKB-UniRule
Keywordsi
Names & Taxonomyi
Protein namesi | Recommended name: Pre-glycoprotein polyprotein GP complexUniRule annotationShort name: Pre-GP-CUniRule annotation Cleaved into the following 3 chains: |
Gene namesi | Name:GPCUniRule annotation Synonyms:GP-C |
Organismi | Lymphocytic choriomeningitis virus (strain WE) (LCMV) |
Taxonomic identifieri | 11627 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Negarnaviricota › Polyploviricotina › Ellioviricetes › Bunyavirales › Arenaviridae › Mammarenavirus › |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] Mesocricetus auratus (Golden hamster) [TaxID: 10036] Mus musculus (Mouse) [TaxID: 10090] |
Subcellular locationi
- Virion membrane UniRule annotation; Peripheral membrane protein UniRule annotation
- Host endoplasmic reticulum membrane UniRule annotation; Peripheral membrane protein UniRule annotation
- Host Golgi apparatus membrane UniRule annotation; Peripheral membrane protein UniRule annotation
- Host cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation
- Virion membrane UniRule annotation; Single-pass membrane protein UniRule annotation
- Host endoplasmic reticulum membrane UniRule annotation; Single-pass membrane protein UniRule annotation
- Host Golgi apparatus membrane UniRule annotation; Single-pass membrane protein UniRule annotation
- Host cell membrane UniRule annotation; Single-pass membrane protein UniRule annotation 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.UniRule annotation
- Virion membrane UniRule annotation; Multi-pass membrane protein UniRule annotation
- Host endoplasmic reticulum membrane UniRule annotation; Multi-pass membrane protein UniRule annotation
- Host Golgi apparatus membrane UniRule annotation; Multi-pass membrane protein UniRule annotation
- Host cell membrane UniRule annotation; Multi-pass membrane protein UniRule annotation
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 2 – 17 | ExtracellularUniRule annotationAdd BLAST | 16 | |
Transmembranei | 18 – 32 | HelicalUniRule annotationAdd BLAST | 15 | |
Topological domaini | 33 | CytoplasmicUniRule annotation | 1 | |
Transmembranei | 34 – 53 | HelicalUniRule annotationAdd BLAST | 20 | |
Topological domaini | 54 – 58 | ExtracellularUniRule annotation | 5 | |
Topological domaini | 59 – 438 | ExtracellularUniRule annotationAdd BLAST | 380 | |
Transmembranei | 439 – 459 | HelicalUniRule annotationAdd BLAST | 21 | |
Topological domaini | 460 – 498 | CytoplasmicUniRule annotationAdd BLAST | 39 |
GO - Cellular componenti
- host cell endoplasmic reticulum membrane Source: UniProtKB-SubCell
- host cell Golgi membrane Source: UniProtKB-SubCell
- host cell plasma membrane Source: UniProtKB-SubCell
- integral component of membrane Source: UniProtKB-UniRule
- viral envelope Source: UniProtKB-UniRule
- virion membrane Source: UniProtKB-SubCell
Keywords - Cellular componenti
Host cell membrane, Host endoplasmic reticulum, Host Golgi apparatus, Host membrane, Membrane, Viral envelope protein, VirionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed; by hostUniRule annotation | |||
ChainiPRO_0000353858 | 2 – 498 | Pre-glycoprotein polyprotein GP complexUniRule annotationAdd BLAST | 497 | |
ChainiPRO_0000353859 | 2 – 58 | Stable signal peptideUniRule annotationAdd BLAST | 57 | |
ChainiPRO_0000036605 | 59 – 265 | Glycoprotein G1UniRule annotationAdd BLAST | 207 | |
ChainiPRO_0000036606 | 266 – 498 | Glycoprotein G2UniRule annotationAdd BLAST | 233 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 2 | N-myristoyl glycine; by hostUniRule annotation | 1 | |
Glycosylationi | 85 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Disulfide bondi | 92 ↔ 239 | UniRule annotation | ||
Glycosylationi | 95 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 114 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Disulfide bondi | 123 ↔ 160 | UniRule annotation | ||
Glycosylationi | 124 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 171 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Disulfide bondi | 184 ↔ 220 | UniRule annotation | ||
Glycosylationi | 232 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Disulfide bondi | 285 ↔ 298 | UniRule annotation | ||
Disulfide bondi | 307 ↔ 316 | UniRule annotation | ||
Disulfide bondi | 370 ↔ 391 | UniRule annotation | ||
Glycosylationi | 371 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 396 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 401 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 |
Post-translational modificationi
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.UniRule annotation
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.UniRule annotation
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 58 – 59 | Cleavage; by host signal peptidaseUniRule annotation | 2 | |
Sitei | 265 – 266 | Cleavage; by host MBTPS1UniRule annotation | 2 |
Keywords - PTMi
Disulfide bond, Glycoprotein, Lipoprotein, MyristateInteractioni
Subunit structurei
homotetramer. GP2 homotetramers bind through ionic interactions with GP1 homotetramers to form the GP complex together with the stable signal peptide. The GP-C polyprotein interacts with the host protease MBTPS1/SKI-1 resulting in the polyprotein processing.
UniRule annotationStructurei
3D structure databases
SMRi | P07399 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P07399 |
Family & Domainsi
Domaini
The cytoplasmic domain of GP2 plays a role in ER location. It also contains a zinc-binding domain that allows SSP retention in the GPC complex by accepting a cysteine from SSP as the fourth ligand.UniRule annotation
Sequence similaritiesi
Belongs to the arenaviridae GPC protein family.UniRule annotation
Keywords - Domaini
Transmembrane, Transmembrane helixFamily and domain databases
Gene3Di | 2.20.28.180, 1 hit |
HAMAPi | MF_04084, ARENA_GPC, 1 hit |
InterProi | View protein in InterPro IPR001535, Arena_glycoprot IPR043015, Arena_glycoprot_zinc-bd |
Pfami | View protein in Pfam PF00798, Arena_glycoprot, 1 hit |
PIRSFi | PIRSF004028, GPC_ArenaV, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P07399-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGQIVTMFEA LPHIIDEVIN IVIIVLIIIT SIKAVYNFAT CGILALVSFL
60 70 80 90 100
FLAGRSCGMY GLNGPDIYKG VYQFKSVEFD MSHLNLTMPN ACSVNNSHHY
110 120 130 140 150
ISMGSSGLEP TFTNDSILNH NFCNLTSALN KKSFDHTLMS IVSSLHLSIR
160 170 180 190 200
GNSNYKAVSC DFNNGITIQY NLSSSDPQSA MSQCRTFRGR VLDMFRTAFG
210 220 230 240 250
GKYMRSGWGW TGSDGKTTWC SQTSYQYLII QNRTWENHCR YAGPFGMSRI
260 270 280 290 300
LFAQEKTKFL TRRLSGTFTW TLSDSSGVEN PGGYCLTKWM ILAAELKCFG
310 320 330 340 350
NTAVAKCNVN HDEEFCDMLR LIDYNKAALS KFKQDVESAL HVFKTTLNSL
360 370 380 390 400
ISDQLLMRNH LRDLMGVPYC NYSKFWYLEH AKTGETSVPK CWLVTNGSYL
410 420 430 440 450
NETHFSDQIE QEADNMITEM LRKDYIKRQG STPLALMDLL MFSTSAYLIS
460 470 480 490
IFLHFVRIPT HRHIKGGSCP KPHRLTNKGI CSCGAFKVPG VKTIWKRR
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M22138 Genomic RNA Translation: AAA46265.1 |
PIRi | A23481, VGXPLC |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M22138 Genomic RNA Translation: AAA46265.1 |
PIRi | A23481, VGXPLC |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1S7Q | X-ray | 1.99 | C | 33-41 | [»] | |
1S7R | X-ray | 2.95 | C/F | 33-41 | [»] | |
1S7S | X-ray | 1.99 | C | 33-41 | [»] | |
1S7T | X-ray | 2.30 | C/F | 33-41 | [»] | |
1S7U | X-ray | 2.20 | C/F/I/L | 33-41 | [»] | |
1S7V | X-ray | 2.20 | C/F | 33-41 | [»] | |
1S7W | X-ray | 2.40 | C/F/I/L | 33-41 | [»] | |
1S7X | X-ray | 2.41 | C/F/I/L | 33-41 | [»] | |
3QUK | X-ray | 2.41 | C/F | 33-41 | [»] | |
3QUL | X-ray | 2.00 | C/F/I/L | 33-41 | [»] | |
3ROL | X-ray | 2.60 | E/F | 34-41 | [»] | |
3ROO | X-ray | 2.00 | E/F | 34-41 | [»] | |
3TBS | X-ray | 2.49 | C/F | 33-41 | [»] | |
3TBT | X-ray | 2.30 | C/F/I/L | 33-41 | [»] | |
3TBV | X-ray | 2.10 | I/J/K/L | 33-41 | [»] | |
3TBW | X-ray | 2.15 | I/J/K/L | 33-41 | [»] | |
3TBY | X-ray | 2.50 | C/F/I/L | 1-9 | [»] | |
4NSK | X-ray | 2.60 | C | 33-40 | [»] | |
SMRi | P07399 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P07399 |
Family and domain databases
Gene3Di | 2.20.28.180, 1 hit |
HAMAPi | MF_04084, ARENA_GPC, 1 hit |
InterProi | View protein in InterPro IPR001535, Arena_glycoprot IPR043015, Arena_glycoprot_zinc-bd |
Pfami | View protein in Pfam PF00798, Arena_glycoprot, 1 hit |
PIRSFi | PIRSF004028, GPC_ArenaV, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | GLYC_LYCVW | |
Accessioni | P07399Primary (citable) accession number: P07399 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1988 |
Last sequence update: | April 1, 1988 | |
Last modified: | December 2, 2020 | |
This is version 97 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families