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Protein

Envelope glycoprotein

Gene

GP

Organism
Lake Victoria marburgvirus (strain Musoke-80) (MARV) (Marburg virus (strain Kenya/Musoke/1980))
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GP1 is responsible for binding to the receptor(s) on target cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as cofactors for virus entry into the host cell. Binding to CD209 and CLEC4M, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses, facilitate infection of macrophages and endothelial cells. These interactions not only facilitate virus cell entry, but also allow capture of viral particles by DCs and subsequent transmission to susceptible cells without DCs infection (trans infection) (By similarity).By similarity
GP2 acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in GP2, releasing the fusion hydrophobic peptide (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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 entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein
Alternative name(s):
GP1,2
Short name:
GP
Virion spike glycoprotein
Cleaved into the following 2 chains:
Gene namesi
Name:GP
OrganismiLake Victoria marburgvirus (strain Musoke-80) (MARV) (Marburg virus (strain Kenya/Musoke/1980))
Taxonomic identifieri33727 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesFiloviridaeMarburgvirus
Virus hostiChlorocebus aethiops (Green monkey) (Cercopithecus aethiops) [TaxID: 9534]
Homo sapiens (Human) [TaxID: 9606]
Rousettus aegyptiacus (Egyptian rousette) (Egyptian fruit bat) [TaxID: 9407]
Proteomesi
  • UP000007771 Componenti: Genome

Subcellular locationi

GP2 :
  • Virion membrane By similarity; Single-pass type I membrane protein Sequence analysis
  • Host cell membrane By similarity; Single-pass type I membrane protein Sequence analysis

  • Note: In the cell, localizes to the plasma membrane lipid rafts, which probably represent the assembly and budding site.By similarity
GP1 :
  • Virion membrane By similarity; Peripheral membrane protein By similarity
  • Host cell membrane By similarity; Peripheral membrane protein By similarity

  • Note: GP1 is not anchored to the viral envelope, but forms a disulfid-linked complex with the extravirion surface GP2. In the cell, both GP1 and GP2 localize to the plasma membrane lipid rafts, which probably represent the assembly and budding site. GP1 can also be shed after proteolytic processing.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 648ExtracellularSequence analysisAdd BLAST630
Transmembranei649 – 669HelicalSequence analysisAdd BLAST21
Topological domaini670 – 681CytoplasmicSequence analysisAdd BLAST12

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi434K → M: Partial loss of cleavage between GP1 and GP2. 1 Publication1
Mutagenesisi435R → L: Complete loss of cleavage between GP1 and GP2. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 181 PublicationAdd BLAST18
ChainiPRO_000003751519 – 681Envelope glycoproteinAdd BLAST663
ChainiPRO_000031497933 – 435GP1By similarityAdd BLAST403
ChainiPRO_0000314980436 – 681GP2By similarityAdd BLAST246

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi37 ↔ 610Interchain (between GP1 and GP2 chains)By similarity
Disulfide bondi92 ↔ 119Sequence analysis
Glycosylationi94N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi171N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi190N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi202N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi207N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi211 ↔ 226Sequence analysis
Glycosylationi219N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi223N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi255N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi310N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi313N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi325N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi326N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi337N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi344N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi345N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi350N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi360N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi408N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi487N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi512 ↔ 557Sequence analysis
Glycosylationi564N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi602 ↔ 609By similarity
Glycosylationi619N-linked (GlcNAc...); by hostSequence analysis1
Lipidationi671S-palmitoyl cysteine; by host1 Publication1
Lipidationi673S-palmitoyl cysteine; by host1 Publication1

Post-translational modificationi

N-glycosylated.
O-glycosylated in the mucin-like region.Curated
Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into GP1 and GP2 by host cell furin in the trans Golgi, and maybe by other host proteases, to yield the mature GP1 and GP2 proteins. The cleavage site corresponds to the furin optimal cleavage sequence [KR]-X-[KR]-R.1 Publication
GP1 is phosphorylated on serine residues between residues 260 and 273.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei435 – 436Cleavage; by host furinBy similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

PTM databases

UniCarbKBiP35253.

Interactioni

Subunit structurei

Homotrimer; each monomer consists of a GP1 and a GP2 subunit linked by disulfide bonds. The resulting peplomers (GP1,2) protrude from the virus surface as spikes. GP1,2 interacts with human CD209 and CLEC4M (collectively referred to as DC-SIGN(R)). Asialoglycoprotein receptor (ASGP-R) may be a liver-specific receptor for GP1,2. Members of the Tyro3 receptor tyrosine kinase family may be cell entry factors interacting with GP1,2.3 Publications

Structurei

3D structure databases

ProteinModelPortaliP35253.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni38 – 188Receptor-bindingAdd BLAST151
Regioni277 – 455Mucin-like regionBy similarityAdd BLAST179
Regioni529 – 549Fusion peptideBy similarityAdd BLAST21

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi192 – 424Thr-richAdd BLAST233
Compositional biasi471 – 474Poly-Ser4

Domaini

The coiled coil regions play a role in oligomerization and fusion activity.By similarity
The transmembrane domain is essential and sufficient for recruitment envelope glycoproteins into VP40-enriched multivesicular bodies.

Sequence similaritiesi

Belongs to the filoviruses glycoprotein family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR014625. GPC_FiloV.
IPR002561. GPC_filovir-type_extra_dom.
[Graphical view]
PfamiPF01611. Filo_glycop. 1 hit.
[Graphical view]
PIRSFiPIRSF036874. GPC_FiloV. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P35253-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTTCFLISL ILIQGTKNLP ILEIASNNQP QNVDSVCSGT LQKTEDVHLM
60 70 80 90 100
GFTLSGQKVA DSPLEASKRW AFRTGVPPKN VEYTEGEEAK TCYNISVTDP
110 120 130 140 150
SGKSLLLDPP TNIRDYPKCK TIHHIQGQNP HAQGIALHLW GAFFLYDRIA
160 170 180 190 200
STTMYRGKVF TEGNIAAMIV NKTVHKMIFS RQGQGYRHMN LTSTNKYWTS
210 220 230 240 250
SNGTQTNDTG CFGALQEYNS TKNQTCAPSK IPPPLPTARP EIKLTSTPTD
260 270 280 290 300
ATKLNTTDPS SDDEDLATSG SGSGEREPHT TSDAVTKQGL SSTMPPTPSP
310 320 330 340 350
QPSTPQQGGN NTNHSQDAVT ELDKNNTTAQ PSMPPHNTTT ISTNNTSKHN
360 370 380 390 400
FSTLSAPLQN TTNDNTQSTI TENEQTSAPS ITTLPPTGNP TTAKSTSSKK
410 420 430 440 450
GPATTAPNTT NEHFTSPPPT PSSTAQHLVY FRRKRSILWR EGDMFPFLDG
460 470 480 490 500
LINAPIDFDP VPNTKTIFDE SSSSGASAEE DQHASPNISL TLSYFPNINE
510 520 530 540 550
NTAYSGENEN DCDAELRIWS VQEDDLAAGL SWIPFFGPGI EGLYTAVLIK
560 570 580 590 600
NQNNLVCRLR RLANQTAKSL ELLLRVTTEE RTFSLINRHA IDFLLTRWGG
610 620 630 640 650
TCKVLGPDCC IGIEDLSKNI SEQIDQIKKD EQKEGTGWGL GGKWWTSDWG
660 670 680
VLTNLGILLL LSIAVLIALS CICRIFTKYI G
Length:681
Mass (Da):74,376
Last modified:February 1, 1994 - v1
Checksum:iCC89305C64D34B0B
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti547V → G in strain: pp3/guinea pig lethal and pp4/guinea pig nonlethal. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12132 mRNA. Translation: CAA78117.1.
AY430365 Genomic RNA. Translation: AAR85463.1.
AY430366 Genomic RNA. Translation: AAR85456.1.
DQ217792 Genomic RNA. Translation: ABA87127.1.
PIRiA45705.
RefSeqiYP_001531156.1. NC_001608.3.

Genome annotation databases

GeneIDi920945.
KEGGivg:920945.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12132 mRNA. Translation: CAA78117.1.
AY430365 Genomic RNA. Translation: AAR85463.1.
AY430366 Genomic RNA. Translation: AAR85456.1.
DQ217792 Genomic RNA. Translation: ABA87127.1.
PIRiA45705.
RefSeqiYP_001531156.1. NC_001608.3.

3D structure databases

ProteinModelPortaliP35253.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

UniCarbKBiP35253.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi920945.
KEGGivg:920945.

Family and domain databases

InterProiIPR014625. GPC_FiloV.
IPR002561. GPC_filovir-type_extra_dom.
[Graphical view]
PfamiPF01611. Filo_glycop. 1 hit.
[Graphical view]
PIRSFiPIRSF036874. GPC_FiloV. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiVGP_MABVM
AccessioniPrimary (citable) accession number: P35253
Secondary accession number(s): Q38L42, Q6T6U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: October 5, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

Filoviruses entry requires functional lipid rafts at the host cell surface.By similarity
Essential for infectivity, as it is the sole viral protein expressed at the virion surface.By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.