UniProtKB - P08669 (GLYC_LASSJ)
Pre-glycoprotein polyprotein GP complex
GPC
Functioni
Interacts with the host receptor (By similarity).
Mediates virus attachment to host receptor alpha-dystroglycan DAG1. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis (PubMed:11967329).
UniRule annotation1 PublicationClass 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 annotationStable 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 annotation1 PublicationSites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 57 | Zinc 1UniRule annotation | 1 | |
Metal bindingi | 455 | Zinc 2; via tele nitrogenUniRule annotation | 1 | |
Metal bindingi | 457 | Zinc 2; via tele nitrogenUniRule annotation | 1 | |
Metal bindingi | 463 | Zinc 2UniRule annotation | 1 | |
Metal bindingi | 467 | Zinc 1; via pros nitrogenUniRule annotation | 1 | |
Metal bindingi | 475 | Zinc 1UniRule annotation | 1 | |
Metal bindingi | 477 | 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 | Lassa virus (strain Mouse/Sierra Leone/Josiah/1976) (LASV) |
Taxonomic identifieri | 11622 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Negarnaviricota › Polyploviricotina › Ellioviricetes › Bunyavirales › Arenaviridae › Mammarenavirus › |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] Mastomys natalensis (African soft-furred rat) (Praomys natalensis) [TaxID: 10112] |
Proteomesi |
|
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 – 432 | ExtracellularUniRule annotationAdd BLAST | 374 | |
Transmembranei | 433 – 453 | HelicalUniRule annotationAdd BLAST | 21 | |
Topological domaini | 454 – 491 | CytoplasmicUniRule annotationAdd BLAST | 38 |
Keywords - Cellular componenti
Host cell membrane, Host endoplasmic reticulum, Host Golgi apparatus, Host membrane, Membrane, Viral envelope protein, VirionPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 54 | G → A: No effect on SSP cleavage. 1 Publication | 1 | |
Mutagenesisi | 56 | S → A: Complete loss of SSP cleavage. 1 Publication | 1 | |
Mutagenesisi | 58 | T → A: Complete loss of SSP cleavage. 1 Publication | 1 | |
Mutagenesisi | 60 | S → A: No effect on SSP cleavage. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed; by hostUniRule annotation | |||
ChainiPRO_0000353854 | 2 – 491 | Pre-glycoprotein polyprotein GP complexUniRule annotationAdd BLAST | 490 | |
ChainiPRO_0000353855 | 2 – 58 | Stable signal peptideUniRule annotationAdd BLAST | 57 | |
ChainiPRO_0000036601 | 59 – 259 | Glycoprotein G1UniRule annotationAdd BLAST | 201 | |
ChainiPRO_0000036602 | 260 – 491 | Glycoprotein G2UniRule annotationAdd BLAST | 232 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 2 | N-myristoyl glycine; by hostUniRule annotation | 1 | |
Glycosylationi | 79 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication | 1 | |
Disulfide bondi | 86 ↔ 231 | UniRule annotation3 Publications | ||
Glycosylationi | 89 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication | 1 | |
Glycosylationi | 99 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication | 1 | |
Glycosylationi | 109 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation3 Publications | 1 | |
Disulfide bondi | 118 ↔ 155 | UniRule annotation3 Publications | ||
Glycosylationi | 119 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation3 Publications | 1 | |
Glycosylationi | 167 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation3 Publications | 1 | |
Disulfide bondi | 180 ↔ 212 | UniRule annotation3 Publications | ||
Glycosylationi | 224 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation3 Publications | 1 | |
Disulfide bondi | 279 ↔ 292 | UniRule annotation1 Publication | ||
Disulfide bondi | 301 ↔ 310 | UniRule annotation1 Publication | ||
Disulfide bondi | 364 ↔ 385 | UniRule annotation1 Publication | ||
Glycosylationi | 365 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication | 1 | |
Glycosylationi | 373 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication | 1 | |
Glycosylationi | 390 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication | 1 | |
Glycosylationi | 395 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 58 – 59 | Cleavage; by host signal peptidaseUniRule annotation | 2 | |
Sitei | 259 – 260 | Cleavage; by host MBTPS1UniRule annotation | 2 |
Keywords - PTMi
Disulfide bond, Glycoprotein, Lipoprotein, MyristatePTM databases
iPTMneti | P08669 |
Interactioni
Subunit structurei
Homotetramer; disulfide-linked (By similarity).
Interacts with host DAG1 (PubMed:11967329).
UniRule annotation1 PublicationHomotetramer. 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 annotation3 PublicationsBinary interactionsi
P08669
With | #Exp. | IntAct |
---|---|---|
LAMP1 [P11279] from Homo sapiens. | 4 | EBI-8411266,EBI-2805407 |
Protein-protein interaction databases
IntActi | P08669, 5 interactors |
MINTi | P08669 |
Structurei
Secondary structure
3D structure databases
SMRi | P08669 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domaini
Sequence similaritiesi
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
10 20 30 40 50
MGQIVTFFQE VPHVIEEVMN IVLIALSVLA VLKGLYNFAT CGLVGLVTFL
60 70 80 90 100
LLCGRSCTTS LYKGVYELQT LELNMETLNM TMPLSCTKNN SHHYIMVGNE
110 120 130 140 150
TGLELTLTNT SIINHKFCNL SDAHKKNLYD HALMSIISTF HLSIPNFNQY
160 170 180 190 200
EAMSCDFNGG KISVQYNLSH SYAGDAANHC GTVANGVLQT FMRMAWGGSY
210 220 230 240 250
IALDSGRGNW DCIMTSYQYL IIQNTTWEDH CQFSRPSPIG YLGLLSQRTR
260 270 280 290 300
DIYISRRLLG TFTWTLSDSE GKDTPGGYCL TRWMLIEAEL KCFGNTAVAK
310 320 330 340 350
CNEKHDEEFC DMLRLFDFNK QAIQRLKAEA QMSIQLINKA VNALINDQLI
360 370 380 390 400
MKNHLRDIMG IPYCNYSKYW YLNHTTTGRT SLPKCWLVSN GSYLNETHFS
410 420 430 440 450
DDIEQQADNM ITEMLQKEYM ERQGKTPLGL VDLFVFSTSF YLISIFLHLV
460 470 480 490
KIPTHRHIVG KSCPKPHRLN HMGICSCGLY KQPGVPVKWK R
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M15076 Genomic RNA Translation: AAA46283.1 J04324 Genomic RNA Translation: AAA46286.1 |
PIRi | A24296, VGXPLV |
RefSeqi | NP_694870.1, NC_004296.1 |
Genome annotation databases
GeneIDi | 956585 |
KEGGi | vg:956585 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M15076 Genomic RNA Translation: AAA46283.1 J04324 Genomic RNA Translation: AAA46286.1 |
PIRi | A24296, VGXPLV |
RefSeqi | NP_694870.1, NC_004296.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4ZJF | X-ray | 2.60 | A/B/C/D | 75-237 | [»] | |
5FT2 | electron microscopy | 16.40 | B | 75-237 | [»] | |
5OMI | X-ray | 2.56 | A/B/C | 306-419 | [»] | |
5VK2 | X-ray | 3.20 | A/B/C | 1-259 | [»] | |
a/b/c | 260-423 | [»] | ||||
6JGY | X-ray | 3.39 | A | 306-432 | [»] | |
SMRi | P08669 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P08669, 5 interactors |
MINTi | P08669 |
PTM databases
iPTMneti | P08669 |
Genome annotation databases
GeneIDi | 956585 |
KEGGi | vg:956585 |
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 |
MobiDBi | Search... |
Entry informationi
Entry namei | GLYC_LASSJ | |
Accessioni | P08669Primary (citable) accession number: P08669 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1988 |
Last sequence update: | January 1, 1988 | |
Last modified: | February 23, 2022 | |
This is version 114 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-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families