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Envelope glycoprotein (GP1,2) (GP) (Virion spike glycoprotein) [Cleaved into: GP1; GP2]

 VGP_MABVM               Reviewed;         681 AA.
P35253; Q38L42; Q6T6U0;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
18-JUL-2018, entry version 95.
RecName: Full=Envelope glycoprotein;
AltName: Full=GP1,2;
Short=GP;
AltName: Full=Virion spike glycoprotein;
Contains:
RecName: Full=GP1;
Contains:
RecName: Full=GP2;
Flags: Precursor;
Name=GP;
Lake Victoria marburgvirus (strain Musoke-80) (MARV) (Marburg virus
(strain Kenya/Musoke/1980)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Filoviridae; Marburgvirus.
NCBI_TaxID=33727;
NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9407; Rousettus aegyptiacus (Egyptian rousette) (Egyptian fruit bat).
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-37.
PubMed=8437211;
Will C., Muehlberger E., Linder D., Slenczka W., Klenk H.-D.,
Feldmann H.;
"Marburg virus gene 4 encodes the virion membrane protein, a type I
transmembrane glycoprotein.";
J. Virol. 67:1203-1210(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=pp3/guinea pig lethal, and pp4/guinea pig nonlethal;
Chain P.S.G., Malfatti S.A., Hajjaj A., Vergez L.M., Do L.H.,
Smith K.L., McCready P.M.;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=pp3/guinea pig lethal, and pp4/guinea pig nonlethal;
Ichou M.A., Paragas J., Jahrling P.B., Ibrahim M.S., Lofts L.,
Hevey M., Schmaljohn A.;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16379005; DOI=10.1128/JVI.80.2.1038-1043.2006;
Enterlein S., Volchkov V., Weik M., Kolesnikova L., Volchkova V.,
Klenk H.-D., Muehlberger E.;
"Rescue of recombinant Marburg virus from cDNA is dependent on
nucleocapsid protein VP30.";
J. Virol. 80:1038-1043(2006).
[5]
SUBUNIT, AND GLYCOSYLATION.
PubMed=2024471; DOI=10.1016/0042-6822(91)90680-A;
Feldmann H., Will C., Schikore M., Slenczka W., Klenk H.-D.;
"Glycosylation and oligomerization of the spike protein of Marburg
virus.";
Virology 182:353-356(1991).
[6]
PALMITOYLATION AT CYS-671 AND CYS-673.
PubMed=11831710; DOI=10.1006/viro.1995.1151;
Funke C., Becker S., Dartsch H., Klenk H.-D., Muehlberger E.;
"Acylation of the Marburg virus glycoprotein.";
Virology 208:289-297(1995).
[7]
GLYCOSYLATION.
PubMed=1421752; DOI=10.1093/glycob/2.4.299;
Geyer H., Will C., Feldmann H., Klenk H.-D., Geyer R.;
"Carbohydrate structure of Marburg virus glycoprotein.";
Glycobiology 2:299-312(1992).
[8]
INTERACTION WITH HUMAN ASIALOGLYCOPROTEIN RECEPTOR.
PubMed=7844558; DOI=10.1099/0022-1317-76-2-393;
Becker S., Spiess M., Klenk H.-D.;
"The asialoglycoprotein receptor is a potential liver-specific
receptor for Marburg virus.";
J. Gen. Virol. 76:393-399(1995).
[9]
PROTEOLYTIC PROCESSING OF ENVELOPE GLYCOPROTEIN, AND MUTAGENESIS OF
LYS-434 AND ARG-435.
PubMed=10683320; DOI=10.1006/viro.1999.0110;
Volchkov V.E., Volchkova V.A., Stroeher U., Becker S., Dolnik O.,
Cieplik M., Garten W., Klenk H.-D., Feldmann H.;
"Proteolytic processing of Marburg virus glycoprotein.";
Virology 268:1-6(2000).
[10]
PHOSPHORYLATION.
PubMed=12033762; DOI=10.1006/viro.2002.1374;
Saenger C., Muehlberger E., Loetfering B., Klenk H.-D., Becker S.;
"The Marburg virus surface protein GP is phosphorylated at its
ectodomain.";
Virology 295:20-29(2002).
[11]
INTERACTION WITH HUMAN CD209 AND CLEC4M.
PubMed=15479853; DOI=10.1128/JVI.78.21.12090-12095.2004;
Marzi A., Gramberg T., Simmons G., Moeller P., Rennekamp A.J.,
Krumbiegel M., Geier M., Eisemann J., Turza N., Saunier B.,
Steinkasserer A., Becker S., Bates P., Hofmann H., Poehlmann S.;
"DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus
and the S protein of severe acute respiratory syndrome coronavirus.";
J. Virol. 78:12090-12095(2004).
[12]
FUNCTION.
PubMed=17005688; DOI=10.1128/JVI.01157-06;
Shimojima M., Takada A., Ebihara H., Neumann G., Fujioka K.,
Irimura T., Jones S., Feldmann H., Kawaoka Y.;
"Tyro3 family-mediated cell entry of Ebola and Marburg viruses.";
J. Virol. 80:10109-10116(2006).
[13]
RECEPTOR-BINDING REGION.
PubMed=16595665; DOI=10.1074/jbc.M601796200;
Kuhn J.H., Radoshitzky S.R., Guth A.C., Warfield K.L., Li W.,
Vincent M.J., Towner J.S., Nichol S.T., Bavari S., Choe H., Aman M.J.,
Farzan M.;
"Conserved receptor-binding domains of Lake Victoria marburgvirus and
Zaire ebolavirus bind a common receptor.";
J. Biol. Chem. 281:15951-15958(2006).
[14]
TRANSMEMBRANE DOMAIN.
PubMed=17267489; DOI=10.1128/JVI.02263-06;
Mittler E., Kolesnikova L., Strecker T., Garten W., Becker S.;
"Role of the transmembrane domain of marburg virus surface protein GP
in assembly of the viral envelope.";
J. Virol. 81:3942-3948(2007).
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:15479853, ECO:0000269|PubMed:2024471,
ECO:0000269|PubMed:7844558}.
-!- SUBCELLULAR LOCATION: GP2: Virion membrane
{ECO:0000250|UniProtKB:Q05320}; Single-pass type I membrane
protein {ECO:0000255}. Host cell membrane
{ECO:0000250|UniProtKB:Q05320}; Single-pass type I membrane
protein {ECO:0000255}. Note=In the cell, localizes to the plasma
membrane lipid rafts, which probably represent the assembly and
budding site. {ECO:0000250|UniProtKB:Q05320}.
-!- SUBCELLULAR LOCATION: GP1: Virion membrane
{ECO:0000250|UniProtKB:Q05320}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q05320}. Host cell membrane
{ECO:0000250|UniProtKB:Q05320}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q05320}. 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. {ECO:0000250|UniProtKB:Q05320}.
-!- DOMAIN: The coiled coil regions play a role in oligomerization and
fusion activity. {ECO:0000250}.
-!- DOMAIN: The transmembrane domain is essential and sufficient for
recruitment envelope glycoproteins into VP40-enriched
multivesicular bodies.
-!- PTM: N-glycosylated.
-!- PTM: O-glycosylated in the mucin-like region. {ECO:0000305}.
-!- PTM: 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.
{ECO:0000269|PubMed:10683320}.
-!- PTM: GP1 is phosphorylated on serine residues between residues 260
and 273. {ECO:0000269|PubMed:12033762}.
-!- MISCELLANEOUS: Filoviruses entry requires functional lipid rafts
at the host cell surface. {ECO:0000250}.
-!- MISCELLANEOUS: Essential for infectivity, as it is the sole viral
protein expressed at the virion surface. {ECO:0000250}.
-!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z12132; CAA78117.1; -; mRNA.
EMBL; AY430365; AAR85463.1; -; Genomic_RNA.
EMBL; AY430366; AAR85456.1; -; Genomic_RNA.
EMBL; DQ217792; ABA87127.1; -; Genomic_RNA.
PIR; A45705; A45705.
RefSeq; YP_001531156.1; NC_001608.3.
ProteinModelPortal; P35253; -.
SMR; P35253; -.
GlyConnect; 579; -.
UniCarbKB; P35253; -.
PRIDE; P35253; -.
GeneID; 920945; -.
KEGG; vg:920945; -.
OrthoDB; VOG09000092; -.
Proteomes; UP000007771; Genome.
Proteomes; UP000137266; Genome.
Proteomes; UP000160614; Genome.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR014625; GPC_FiloV.
InterPro; IPR002561; GPC_filovir-type_extra_dom.
InterPro; IPR018154; TLV/ENV_coat_polyprotein.
PANTHER; PTHR10424; PTHR10424; 1.
Pfam; PF01611; Filo_glycop; 1.
PIRSF; PIRSF036874; GPC_FiloV; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host membrane; Host-virus interaction;
Lipoprotein; Membrane; Palmitate; Reference proteome; Signal;
Transmembrane; Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Viral penetration into host cytoplasm; Virion;
Virus entry into host cell.
SIGNAL 1 18 {ECO:0000269|PubMed:8437211}.
CHAIN 19 681 Envelope glycoprotein.
/FTId=PRO_0000037515.
CHAIN 33 435 GP1. {ECO:0000250}.
/FTId=PRO_0000314979.
CHAIN 436 681 GP2. {ECO:0000250}.
/FTId=PRO_0000314980.
TOPO_DOM 19 648 Extracellular. {ECO:0000255}.
TRANSMEM 649 669 Helical. {ECO:0000255}.
TOPO_DOM 670 681 Cytoplasmic. {ECO:0000255}.
REGION 38 188 Receptor-binding.
REGION 277 455 Mucin-like region. {ECO:0000250}.
REGION 529 549 Fusion peptide. {ECO:0000250}.
COMPBIAS 192 424 Thr-rich.
COMPBIAS 471 474 Poly-Ser.
SITE 435 436 Cleavage; by host furin. {ECO:0000250}.
LIPID 671 671 S-palmitoyl cysteine; by host.
{ECO:0000305|PubMed:11831710}.
LIPID 673 673 S-palmitoyl cysteine; by host.
{ECO:0000305|PubMed:11831710}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 171 171 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 190 190 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 202 202 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 223 223 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 255 255 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 310 310 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 313 313 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 325 325 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 326 326 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 337 337 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 344 344 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 360 360 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 487 487 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 564 564 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 619 619 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 37 610 Interchain (between GP1 and GP2 chains).
{ECO:0000250}.
DISULFID 92 119 {ECO:0000255}.
DISULFID 211 226 {ECO:0000255}.
DISULFID 512 557 {ECO:0000255}.
DISULFID 602 609 {ECO:0000250}.
VARIANT 547 547 V -> G (in strain: pp3/guinea pig lethal
and pp4/guinea pig nonlethal).
MUTAGEN 434 434 K->M: Partial loss of cleavage between
GP1 and GP2.
{ECO:0000269|PubMed:10683320}.
MUTAGEN 435 435 R->L: Complete loss of cleavage between
GP1 and GP2.
{ECO:0000269|PubMed:10683320}.
SEQUENCE 681 AA; 74376 MW; CC89305C64D34B0B CRC64;
MKTTCFLISL ILIQGTKNLP ILEIASNNQP QNVDSVCSGT LQKTEDVHLM GFTLSGQKVA
DSPLEASKRW AFRTGVPPKN VEYTEGEEAK TCYNISVTDP SGKSLLLDPP TNIRDYPKCK
TIHHIQGQNP HAQGIALHLW GAFFLYDRIA STTMYRGKVF TEGNIAAMIV NKTVHKMIFS
RQGQGYRHMN LTSTNKYWTS SNGTQTNDTG CFGALQEYNS TKNQTCAPSK IPPPLPTARP
EIKLTSTPTD ATKLNTTDPS SDDEDLATSG SGSGEREPHT TSDAVTKQGL SSTMPPTPSP
QPSTPQQGGN NTNHSQDAVT ELDKNNTTAQ PSMPPHNTTT ISTNNTSKHN FSTLSAPLQN
TTNDNTQSTI TENEQTSAPS ITTLPPTGNP TTAKSTSSKK GPATTAPNTT NEHFTSPPPT
PSSTAQHLVY FRRKRSILWR EGDMFPFLDG LINAPIDFDP VPNTKTIFDE SSSSGASAEE
DQHASPNISL TLSYFPNINE NTAYSGENEN DCDAELRIWS VQEDDLAAGL SWIPFFGPGI
EGLYTAVLIK NQNNLVCRLR RLANQTAKSL ELLLRVTTEE RTFSLINRHA IDFLLTRWGG
TCKVLGPDCC IGIEDLSKNI SEQIDQIKKD EQKEGTGWGL GGKWWTSDWG VLTNLGILLL
LSIAVLIALS CICRIFTKYI G


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