UniProtKB - P26313 (GLYC_JUNIN)
Pre-glycoprotein polyprotein GP complex
GPC
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 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 annotationInteracts with the host receptor (By similarity).
Mediates virus attachment to host TFRC. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis (PubMed:17287727).
UniRule annotation2 PublicationsSites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 57 | Zinc 1UniRule annotation1 Publication | 1 | |
Metal bindingi | 447 | Zinc 2; via tele nitrogenUniRule annotation1 Publication | 1 | |
Metal bindingi | 449 | Zinc 2; via tele nitrogenUniRule annotation1 Publication | 1 | |
Metal bindingi | 455 | Zinc 2UniRule annotation1 Publication | 1 | |
Metal bindingi | 459 | Zinc 1; via pros nitrogenUniRule annotation1 Publication | 1 | |
Metal bindingi | 467 | Zinc 1UniRule annotation1 Publication | 1 | |
Metal bindingi | 469 | Zinc 1UniRule annotation1 Publication | 1 | |
Metal bindingi | 485 | Zinc 2; via tele nitrogenUniRule annotation1 Publication | 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
Protein family/group databases
TCDBi | 1.G.8.1.2, the arenavirus fusion protein (av-fp) family |
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 | Junin mammarenavirus (JUNV) (Junn mammarenavirus) |
Taxonomic identifieri | 2169991 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Negarnaviricota › Polyploviricotina › Ellioviricetes › Bunyavirales › Arenaviridae › Mammarenavirus |
Virus hosti | Akodon azarae (Azara's grass mouse) [TaxID: 29095] Bolomys [TaxID: 10080] Calomys laucha (Small vesper mouse) [TaxID: 56211] Calomys musculinus (Drylands vesper mouse) [TaxID: 56212] Homo sapiens (Human) [TaxID: 9606] |
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 – 424 | ExtracellularUniRule annotationAdd BLAST | 366 | |
Transmembranei | 425 – 445 | HelicalUniRule annotationAdd BLAST | 21 | |
Topological domaini | 446 – 485 | CytoplasmicUniRule annotationAdd BLAST | 40 |
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 | 2 | G → A: Reduces membrane fusion activity. No effect on GP complex formation. 1 Publication | 1 | |
Mutagenesisi | 476 – 477 | KK → AA: Induces transport to the cell surface in the absence of SSP. No effect on SSP binding. 1 Publication | 2 | |
Mutagenesisi | 482 – 483 | RR → AA: Induces transport to the cell surface in the absence of SSP. No effect on SSP binding. 1 Publication | 2 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed; by hostUniRule annotation1 Publication | |||
ChainiPRO_0000353850 | 2 – 485 | Pre-glycoprotein polyprotein GP complexUniRule annotationAdd BLAST | 484 | |
ChainiPRO_0000353851 | 2 – 58 | Stable signal peptideUniRule annotationAdd BLAST | 57 | |
ChainiPRO_0000036597 | 59 – 251 | Glycoprotein G1UniRule annotationAdd BLAST | 193 | |
ChainiPRO_0000036598 | 252 – 485 | Glycoprotein G2UniRule annotationAdd BLAST | 234 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 2 | N-myristoyl glycine; by hostUniRule annotation1 Publication | 1 | |
Disulfide bondi | 92 ↔ 226 | UniRule annotation1 Publication | ||
Glycosylationi | 95 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 105 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication | 1 | |
Disulfide bondi | 135 ↔ 164 | UniRule annotation1 Publication | ||
Glycosylationi | 166 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication | 1 | |
Glycosylationi | 178 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication | 1 | |
Disulfide bondi | 207 ↔ 213 | UniRule annotation1 Publication | ||
Disulfide bondi | 271 ↔ 284 | UniRule annotation | ||
Disulfide bondi | 293 ↔ 302 | UniRule annotation | ||
Disulfide bondi | 356 ↔ 377 | UniRule annotation | ||
Glycosylationi | 357 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 365 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 382 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 387 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 58 – 59 | Cleavage; by host signal peptidaseUniRule annotation | 2 | |
Sitei | 251 – 252 | Cleavage; by host MBTPS1UniRule annotation | 2 |
Keywords - PTMi
Disulfide bond, Glycoprotein, Lipoprotein, MyristatePTM databases
iPTMneti | P26313 |
Interactioni
Subunit structurei
Homotetramer; disulfide-linked (By similarity).
Interacts with host TFRC (PubMed:17287727).
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 annotation1 PublicationStructurei
Secondary structure
3D structure databases
SMRi | P26313 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P26313 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 476 – 477 | Involved in ER localization | 2 | |
Regioni | 482 – 483 | Involved in ER localization | 2 |
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, 2 hits |
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
MGQFISFMQE IPTFLQEALN IALVAVSLIA IIKGVVNLYK SGLFQFFVFL
60 70 80 90 100
ALAGRSCTEE AFKIGLHTEF QTVSFSMVGL FSNNPHDLPL LCTLNKSHLY
110 120 130 140 150
IKGGNASFKI SFDDIAVLLP EYDVIIQHPA DMSWCSKSDD QIWLSQWFMN
160 170 180 190 200
AVGHDWYLDP PFLCRNRTKT EGFIFQVNTS KTGINENYAK KFKTGMHHLY
210 220 230 240 250
REYPDSCLDG KLCLMKAQPT SWPLQCPLDH VNTLHFLTRG KNIQLPRRSL
260 270 280 290 300
KAFFSWSLTD SSGKDTPGGY CLEEWMLVAA KMKCFGNTAV AKCNLNHDSE
310 320 330 340 350
FCDMLRLFDY NKNAIKTLND ETKKQVNLMG QTINALISDN LLMKNKIREL
360 370 380 390 400
MSVPYCNYTK FWYVNHTLSG QHSLPRCWLI KNNSYLNISD FRNDWILESD
410 420 430 440 450
FLISEMLSKE YSDRQGKTPL TLVDICFWST VFFTASLFLH LVGIPTHRHI
460 470 480
RGEACPLPHR LNSLGGCRCG KYPNLKKPTV WRRGH
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D10072 Genomic RNA Translation: BAA00964.2 |
PIRi | JT0978, VGXPJV |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D10072 Genomic RNA Translation: BAA00964.2 |
PIRi | JT0978, VGXPJV |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2L0Z | NMR | - | A | 445-485 | [»] | |
5EN2 | X-ray | 1.82 | C | 87-227 | [»] | |
5W1K | X-ray | 3.99 | E/J/P/R | 87-228 | [»] | |
SMRi | P26313 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
TCDBi | 1.G.8.1.2, the arenavirus fusion protein (av-fp) family |
PTM databases
iPTMneti | P26313 |
Protocols and materials databases
ABCDi | P26313, 5 sequenced antibodies |
Miscellaneous databases
EvolutionaryTracei | P26313 |
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, 2 hits |
PIRSFi | PIRSF004028, GPC_ArenaV, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | GLYC_JUNIN | |
Accessioni | P26313Primary (citable) accession number: P26313 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 1, 1992 |
Last sequence update: | July 19, 2004 | |
Last modified: | February 23, 2022 | |
This is version 105 of the entry and version 2 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