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Protein

Pre-glycoprotein polyprotein GP complex

Gene

GPC

Organism
Lymphocytic choriomeningitis virus (strain WE) (LCMV)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The stable signal peptide (SSP) is cleaved and functions as a signal peptide. In addition, it is apparently 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 (By similarity).By similarity
Glycoprotein G1 mediates virus attachment to host receptor alpha-dystroglycan DAG1. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis (By similarity).By similarity
Glycoprotein G2 is a viral fusion protein. Membrane fusion is mediated by conformational changes induced upon acidification in the endosome (Potential).Curated

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Clathrin- and caveolin-independent endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus endocytosis by host, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-glycoprotein polyprotein GP complex
Short name:
Pre-GP-C
Cleaved into the following 3 chains:
Stable signal peptide
Short name:
SSP
Glycoprotein G1
Short name:
GP1
Glycoprotein G2
Short name:
GP2
Gene namesi
Name:GPC
Synonyms:GP-C
OrganismiLymphocytic choriomeningitis virus (strain WE) (LCMV)
Taxonomic identifieri11627 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesArenaviridaeMammarenavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Mesocricetus auratus (Golden hamster) [TaxID: 10036]
Mus musculus (Mouse) [TaxID: 10090]

Subcellular locationi

Glycoprotein G2 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1716ExtracellularSequence analysisAdd
BLAST
Transmembranei18 – 3215HelicalSequence analysisAdd
BLAST
Topological domaini33 – 331CytoplasmicSequence analysis
Transmembranei34 – 5320HelicalSequence analysisAdd
BLAST
Topological domaini54 – 585ExtracellularSequence analysis
Topological domaini59 – 438380ExtracellularSequence analysisAdd
BLAST
Transmembranei439 – 45921HelicalSequence analysisAdd
BLAST
Topological domaini460 – 49839CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host endoplasmic reticulum, Host Golgi apparatus, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedSequence analysis
Chaini2 – 498497Pre-glycoprotein polyprotein GP complexPRO_0000353858Add
BLAST
Chaini2 – 5857Stable signal peptideBy similarityPRO_0000353859Add
BLAST
Chaini59 – 265207Glycoprotein G1By similarityPRO_0000036605Add
BLAST
Chaini266 – 498233Glycoprotein G2By similarityPRO_0000036606Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
Glycosylationi85 – 851N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi95 – 951N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi114 – 1141N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi124 – 1241N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi171 – 1711N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi232 – 2321N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi371 – 3711N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi396 – 3961N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi401 – 4011N-linked (GlcNAc...); by hostSequence analysis

Post-translational modificationi

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.By similarity
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei58 – 592Cleavage; by host signal peptidaseBy similarity
Sitei265 – 2662Cleavage; by host MBTPS1By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Myristate

Interactioni

Subunit structurei

Glycoprotein G1 is a homotetramer; disulfide-linked (Potential). Glycoprotein G2 is a homotetramer (Potential). GP2 homotetramers bind through ionic interactions with GP1 homotetramers to form, with the stable signal peptide, the GP complex. The GP-C polyprotein interacts with host protease MBTPS1/SKI-1; this results in polyprotein processing (By similarity).By similarityCurated

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S7QX-ray1.99C33-41[»]
1S7RX-ray2.95C/F33-41[»]
1S7SX-ray1.99C33-41[»]
1S7TX-ray2.30C/F33-41[»]
1S7UX-ray2.20C/F/I/L33-41[»]
1S7VX-ray2.20C/F33-41[»]
1S7WX-ray2.40C/F/I/L33-41[»]
1S7XX-ray2.41C/F/I/L33-41[»]
3QUKX-ray2.41C/F33-41[»]
3QULX-ray2.00C/F/I/L33-41[»]
3ROLX-ray2.60E/F34-41[»]
3ROOX-ray2.00E/F34-41[»]
3TBSX-ray2.49C/F33-41[»]
3TBTX-ray2.30C/F/I/L33-41[»]
3TBVX-ray2.10I/J/K/L33-41[»]
3TBWX-ray2.15I/J/K/L33-41[»]
3TBYX-ray2.50C/F/I/L1-9[»]
4NSKX-ray2.60C33-40[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07399.

Family & Domainsi

Domaini

The cytoplasmic domain of GP2 plays a role in ER location and binds to the SSP.

Sequence similaritiesi

Belongs to the arenaviridae GPC protein family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR001535. Arena_glycoprot.
[Graphical view]
PfamiPF00798. Arena_glycoprot. 1 hit.
[Graphical view]
PIRSFiPIRSF004028. GPC_ArenaV. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07399-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:498
Mass (Da):56,281
Last modified:April 1, 1988 - v1
Checksum:i576A8DC2C26BF160
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22138 Genomic RNA. Translation: AAA46265.1.
PIRiA23481. VGXPLC.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22138 Genomic RNA. Translation: AAA46265.1.
PIRiA23481. VGXPLC.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S7QX-ray1.99C33-41[»]
1S7RX-ray2.95C/F33-41[»]
1S7SX-ray1.99C33-41[»]
1S7TX-ray2.30C/F33-41[»]
1S7UX-ray2.20C/F/I/L33-41[»]
1S7VX-ray2.20C/F33-41[»]
1S7WX-ray2.40C/F/I/L33-41[»]
1S7XX-ray2.41C/F/I/L33-41[»]
3QUKX-ray2.41C/F33-41[»]
3QULX-ray2.00C/F/I/L33-41[»]
3ROLX-ray2.60E/F34-41[»]
3ROOX-ray2.00E/F34-41[»]
3TBSX-ray2.49C/F33-41[»]
3TBTX-ray2.30C/F/I/L33-41[»]
3TBVX-ray2.10I/J/K/L33-41[»]
3TBWX-ray2.15I/J/K/L33-41[»]
3TBYX-ray2.50C/F/I/L1-9[»]
4NSKX-ray2.60C33-40[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP07399.

Family and domain databases

InterProiIPR001535. Arena_glycoprot.
[Graphical view]
PfamiPF00798. Arena_glycoprot. 1 hit.
[Graphical view]
PIRSFiPIRSF004028. GPC_ArenaV. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of the S RNA of lymphocytic choriomeningitis virus (WE strain) compared to that of Pichinde arenavirus."
    Romanowski V., Matsuura Y., Bishop D.H.L.
    Virus Res. 3:101-114(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Determination of structural principles underlying three different modes of lymphocytic choriomeningitis virus escape from CTL recognition."
    Velloso L.M., Michaelsson J., Ljunggren H.G., Schneider G., Achour A.
    J. Immunol. 172:5504-5511(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 33-40.

Entry informationi

Entry nameiGLYC_LYCVW
AccessioniPrimary (citable) accession number: P07399
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: May 11, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.