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VGP_MABVO
ID   VGP_MABVO               Reviewed;         681 AA.
AC   Q6UY66; O36428;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Envelope glycoprotein;
DE   AltName: Full=GP1,2;
DE            Short=GP;
DE   AltName: Full=Virion spike glycoprotein;
DE   Contains:
DE     RecName: Full=GP1;
DE   Contains:
DE     RecName: Full=GP2;
DE   Flags: Precursor;
GN   Name=GP;
OS   Lake Victoria marburgvirus (strain Ozolin-75) (MARV) (Marburg virus (strain
OS   South Africa/Ozolin/1975)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX   NCBI_TaxID=482820;
OH   NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9407; Rousettus aegyptiacus (Egyptian rousette) (Egyptian fruit bat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Sanchez;
RX   PubMed=9448698; DOI=10.1006/viro.1997.8902;
RA   Sanchez A., Trappier S.G., Stroeher U., Nichol S.T., Bowen M.D.,
RA   Feldmann H.;
RT   "Variation in the glycoprotein and VP35 genes of Marburg virus strains.";
RL   Virology 240:138-146(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Bowen M.D., Thurman K., Minor E., Ibrahim M.S., Meyer R.F., Malfatti S.A.,
RA   Do L.H., Smith K.L., McCready P.M., Chain P.S.G.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GP1 is responsible for binding to the receptor(s) on target
CC       cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as
CC       cofactors for virus entry into the host cell. Binding to CD209 and
CC       CLEC4M, which are respectively found on dendritic cells (DCs), and on
CC       endothelial cells of liver sinusoids and lymph node sinuses, facilitate
CC       infection of macrophages and endothelial cells. These interactions not
CC       only facilitate virus cell entry, but also allow capture of viral
CC       particles by DCs and subsequent transmission to susceptible cells
CC       without DCs infection (trans infection) (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: GP2 acts as a class I viral fusion protein. Under the current
CC       model, the protein has at least 3 conformational states: pre-fusion
CC       native state, pre-hairpin intermediate state, and post-fusion hairpin
CC       state. During viral and target cell membrane fusion, the coiled coil
CC       regions (heptad repeats) assume a trimer-of-hairpins structure,
CC       positioning the fusion peptide in close proximity to the C-terminal
CC       region of the ectodomain. The formation of this structure appears to
CC       drive apposition and subsequent fusion of viral and target cell
CC       membranes. Responsible for penetration of the virus into the cell
CC       cytoplasm by mediating the fusion of the membrane of the endocytosed
CC       virus particle with the endosomal membrane. Low pH in endosomes induces
CC       an irreversible conformational change in GP2, releasing the fusion
CC       hydrophobic peptide (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer; each monomer consists of a GP1 and a GP2 subunit
CC       linked by disulfide bonds. The resulting peplomers (GP1,2) protrude
CC       from the virus surface as spikes. GP1,2 interacts with human CD209 and
CC       CLEC4M (collectively referred to as DC-SIGN(R)). Asialoglycoprotein
CC       receptor (ASGP-R) may be a liver-specific receptor for GP1,2. Members
CC       of the Tyro3 receptor tyrosine kinase family may be cell entry factors
CC       interacting with GP1,2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [GP2]: Virion membrane
CC       {ECO:0000250|UniProtKB:Q05320}; Single-pass type I membrane protein
CC       {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:Q05320};
CC       Single-pass type I membrane protein {ECO:0000255}. Note=In the cell,
CC       localizes to the plasma membrane lipid rafts, which probably represent
CC       the assembly and budding site. {ECO:0000250|UniProtKB:Q05320}.
CC   -!- SUBCELLULAR LOCATION: [GP1]: Virion membrane
CC       {ECO:0000250|UniProtKB:Q05320}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q05320}. Host cell membrane
CC       {ECO:0000250|UniProtKB:Q05320}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q05320}. Note=GP1 is not anchored to the viral
CC       envelope, but forms a disulfid-linked complex with the extravirion
CC       surface GP2. In the cell, both GP1 and GP2 localize to the plasma
CC       membrane lipid rafts, which probably represent the assembly and budding
CC       site. GP1 can also be shed after proteolytic processing.
CC       {ECO:0000250|UniProtKB:Q05320}.
CC   -!- DOMAIN: The coiled coil regions play a role in oligomerization and
CC       fusion activity. {ECO:0000250}.
CC   -!- DOMAIN: The transmembrane domain is essential and sufficient for
CC       recruitment envelope glycoproteins into VP40-enriched multivesicular
CC       bodies. {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- PTM: O-glycosylated in the mucin-like region. {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC       precursor is processed into GP1 and GP2 by host cell furin in the trans
CC       Golgi, and maybe by other host proteases, to yield the mature GP1 and
CC       GP2 proteins. The cleavage site corresponds to the furin optimal
CC       cleavage sequence [KR]-X-[KR]-R (By similarity). {ECO:0000250}.
CC   -!- PTM: GP1 is phosphorylated on serine residues between residues 260 and
CC       273. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Filoviruses entry requires functional lipid rafts at the
CC       host cell surface. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Essential for infectivity, as it is the sole viral
CC       protein expressed at the virion surface. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AY358025; AAQ55258.1; -; Genomic_RNA.
DR   EMBL; AF005733; AAC40458.1; -; Genomic_RNA.
DR   SMR; Q6UY66; -.
DR   Proteomes; UP000000838; Genome.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR014625; GPC_FiloV.
DR   InterPro; IPR002561; GPC_filovir-type_extra_dom.
DR   Pfam; PF01611; Filo_glycop; 1.
DR   PIRSF; PIRSF036874; GPC_FiloV; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein;
KW   Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW   Membrane; Palmitate; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..681
FT                   /note="Envelope glycoprotein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000314981"
FT   CHAIN           33..435
FT                   /note="GP1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000314982"
FT   CHAIN           436..681
FT                   /note="GP2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000314983"
FT   TOPO_DOM        19..648
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        649..669
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        670..681
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          38..188
FT                   /note="Receptor-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          221..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..455
FT                   /note="Mucin-like region"
FT                   /evidence="ECO:0000250"
FT   REGION          529..549
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        228..242
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            435..436
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000250"
FT   LIPID           671
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P35253"
FT   LIPID           673
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P35253"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        337
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        344
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        360
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        422
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        487
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        564
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        619
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   VARIANT         212
FT                   /note="F -> L (in strain: Isolate Sanchez)"
FT   VARIANT         370
FT                   /note="A -> V (in strain: Isolate Sanchez)"
FT   VARIANT         405
FT                   /note="M -> L (in strain: Isolate Sanchez)"
FT   VARIANT         535
FT                   /note="F -> L (in strain: Isolate Sanchez)"
SQ   SEQUENCE   681 AA;  74481 MW;  325815B750EDBA93 CRC64;
     MRTTCLFISL ILIQGIKTLP ILEIASNDQP QNVDSVCSGT LQKTEDVHLM GFTLSGQKVA
     DSPLEASKRW AFRTGVPPKN VEYTEGEEAK TCYNISVTDP SGKSLLLDPP TNVRDYPKCK
     TIHHIQGQNP HAQGIALHLW GAFFLYDRIA STTMYRGKVF TEGNIAAMIV NKTVHKMIFS
     RQGQGYRHMN LTSTNKYWTS SNGTQTNDTG CFGTLHEYNS TKNQTCAPSK TPPPPPTARP
     EIKPTSTPTD ATRLNTTNPN SDDEDLTTSG SGSGEQELYT TSDAVTKQGL SSTMPPTPSP
     QPGTPQQGGN NTNHSQDATT ELDNTNTTAQ PPTPSHNTTT ISTNNTSKHN LSTLSAPPQN
     TTNPNTQSMA TENEKTSAPP KATLPPTENP TTEKSTNNTK SPTTMEPNTT NGHFTSPSST
     PNSTTQHLIY FRRKRSILWR EGDMFPFLDG LINAPIDFDP VPNTKTIFDE SSSSGASTEE
     DQHASSNISL TLSYLPHTSG NTAYSGENEN DCDAELRIWS VQEDDLAAGL SWIPFFGPGI
     EGLYTAGLIK NQNNLVCRLR RLANQTAKSL ELLLRVTTEE RTFSLINRHA IDFLLTRWGG
     TCKVLGPDCC IGIEDLSRNI SEQIDQIKKD EQKEGTGWGL GGKWWTSDWG VLTNLGILLL
     LSIAVLIALS CICRIFTKYI G
 
 
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