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P03390

- ENV_MLVF5

UniProt

P03390 - ENV_MLVF5

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Protein

Envelope glycoprotein

Gene

env

Organism
Friend murine leukemia virus (isolate 57) (FrMLV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).By similarity
The transmembrane protein (TM) 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. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi89 – 891Zinc
Metal bindingi120 – 1201Zinc
Sitei479 – 4802Cleavage; by hostBy similarity
Sitei659 – 6602Cleavage; by viral protease p14By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. structural molecule activity Source: InterPro

GO - Biological processi

  1. fusion of virus membrane with host plasma membrane Source: UniProtKB-KW
  2. suppression by virus of host adaptive immune response Source: UniProtKB-KW
  3. suppression by virus of host antigen processing and presentation Source: UniProtKB-KW
  4. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Fusion of virus membrane with host cell membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host adaptive immune response by virus, Inhibition of host proteasome antigen processing by virus, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Virus entry into host cell

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein
Alternative name(s):
Env polyprotein
Cleaved into the following 3 chains:
Surface protein
Short name:
SU
Alternative name(s):
Glycoprotein 70
Short name:
gp70
Transmembrane protein
Short name:
TM
Alternative name(s):
Envelope protein p15E
Alternative name(s):
p2E
Gene namesi
Name:env
OrganismiFriend murine leukemia virus (isolate 57) (FrMLV)
Taxonomic identifieri11796 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
ProteomesiUP000007776: Genome

Subcellular locationi

Chain Surface protein : Virion membrane; Peripheral membrane protein. Host cell membrane By similarity; Peripheral membrane protein By similarity
Note: The surface protein is not anchored to the viral envelope, but associates with the virion surface through its binding to TM. Both proteins are thought to be concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity).By similarity
R-peptide : Host cell membrane By similarity; Peripheral membrane protein By similarity
Note: The R-peptide is membrane-associated through its palmitate.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini35 – 620586ExtracellularSequence AnalysisAdd
BLAST
Transmembranei621 – 64121HelicalSequence AnalysisAdd
BLAST
Topological domaini642 – 67534CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. viral capsid Source: InterPro
  4. viral envelope Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi640 – 6401C → S: Complete loss of palmitoylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434Sequence AnalysisAdd
BLAST
Chaini35 – 675641Envelope glycoproteinPRO_0000239581Add
BLAST
Chaini35 – 479445Surface proteinBy similarityPRO_0000040751Add
BLAST
Chaini480 – 659180Transmembrane proteinBy similarityPRO_0000040752Add
BLAST
Peptidei660 – 67516R-peptideBy similarityPRO_0000040753Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...); by host
Disulfide bondi80 ↔ 132
Disulfide bondi106 ↔ 121
Disulfide bondi107 ↔ 117
Disulfide bondi155 ↔ 175
Disulfide bondi167 ↔ 180
Glycosylationi202 – 2021N-linked (GlcNAc...); by host
Disulfide bondi212 ↔ 218
Glycosylationi336 – 3361N-linked (GlcNAc...); by hostBy similarity
Disulfide bondi346 ↔ 573Interchain (between SU and TM chains, or C-349 with C-573); in linked form
Disulfide bondi346 ↔ 349
Glycosylationi368 – 3681N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi375 – 3751N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi376 ↔ 430By similarity
Disulfide bondi395 ↔ 407By similarity
Glycosylationi408 – 4081N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi437 ↔ 450By similarity
Glycosylationi444 – 4441N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi565 ↔ 572By similarity
Lipidationi640 – 6401S-palmitoyl cysteine; by host1 Publication

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as a inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. The R-peptide is released from the C-terminus of the cytoplasmic tail of the TM protein upon particle formation as a result of proteolytic cleavage by the viral protease. Cleavage of this peptide is required for TM to become fusogenic (By similarity).By similarity
The CXXC motif is highly conserved across a broad range of retroviral envelope proteins. It is thought to participate in the formation of a labile disulfide bond possibly with the CX6CC motif present in the transmembrane protein. Isomerization of the intersubunit disulfide bond to an SU intrachain disulfide bond is thought to occur upon receptor recognition in order to allow membrane fusion (By similarity).By similarity
The transmembrane protein is palmitoylated.1 Publication
The R-peptide is palmitoylated.By similarity

Keywords - PTMi

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

Interactioni

Subunit structurei

The mature envelope protein (Env) consists of a trimer of SU-TM heterodimers attached by a labile interchain disulfide bond.By similarity

Structurei

Secondary structure

1
675
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 529Combined sources
Beta strandi58 – 6710Combined sources
Helixi79 – 835Combined sources
Helixi88 – 903Combined sources
Helixi119 – 1224Combined sources
Beta strandi130 – 1345Combined sources
Helixi135 – 14612Combined sources
Beta strandi152 – 1565Combined sources
Helixi164 – 1674Combined sources
Helixi170 – 1723Combined sources
Beta strandi183 – 1864Combined sources
Beta strandi196 – 2038Combined sources
Helixi205 – 2139Combined sources
Beta strandi220 – 2256Combined sources
Helixi227 – 2315Combined sources
Helixi234 – 2363Combined sources
Beta strandi239 – 2457Combined sources
Turni248 – 2503Combined sources
Beta strandi253 – 26311Combined sources
Helixi266 – 2683Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOLX-ray2.00A43-270[»]
ProteinModelPortaliP03390.
SMRiP03390. Positions 43-269, 525-577.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03390.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 270236Receptor-binding domain (RBD)Sequence AnalysisAdd
BLAST
Regioni482 – 50221Fusion peptideBy similarityAdd
BLAST
Regioni548 – 56417ImmunosuppressionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili513 – 54735Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi346 – 3494CXXC
Motifi565 – 5739CX6CC
Motifi665 – 6684YXXL motif; contains endocytosis signalBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi267 – 31751Pro-richAdd
BLAST

Domaini

The YXXL motif is involved in determining the exact site of viral release at the surface of infected mononuclear cells and promotes endocytosis.
The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo (By similarity).By similarity

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di3.90.310.10. 1 hit.
InterProiIPR008981. FMuLV_rcpt-bd.
IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERiPTHR10424. PTHR10424. 1 hit.
PfamiPF00429. TLV_coat. 1 hit.
[Graphical view]
SUPFAMiSSF49830. SSF49830. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P03390-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MACSTLPKSP KDKIDPRDLL IPLILFLSLK GARSAAPGSS PHQVYNITWE
60 70 80 90 100
VTNGDRETVW AISGNHPLWT WWPVLTPDLC MLALSGPPHW GLEYQAPYSS
110 120 130 140 150
PPGPPCCSGS SGSSAGCSRD CDEPLTSLTP RCNTAWNRLK LDQVTHKSSE
160 170 180 190 200
GFYVCPGSHR PREAKSCGGP DSFYCASWGC ETTGRVYWKP SSSWDYITVD
210 220 230 240 250
NNLTTSQAVQ VCKDNKWCNP LAIQFTNAGK QVTSWTTGHY WGLRLYVSGR
260 270 280 290 300
DPGLTFGIRL RYQNLGPRVP IGPNPVLADQ LSLPRPNPLP KPAKSPPASN
310 320 330 340 350
STPTLISPSP TPTQPPPAGT GDRLLNLVQG AYQALNLTNP DKTQECWLCL
360 370 380 390 400
VSGPPYYEGV AVLGTYSNHT SAPANCSVAS QHKLTLSEVT GRGLCIGTVP
410 420 430 440 450
KTHQALCNTT LKIDKGSYYL VAPTGTTWAC NTGLTPCLSA TVLNRTTDYC
460 470 480 490 500
VLVELWPRVT YHPPSYVYSQ FEKSYRHKRE PVSLTLALLL GGLTMGGIAA
510 520 530 540 550
GVGTGTTALV ATQQFQQLHA AVQDDLKEVE KSITNLEKSL TSLSEVVLQN
560 570 580 590 600
RRGLDLLFLK EGGLCAALKE ECCFYADHTG LVRDSMAKLR ERLTQRQKLF
610 620 630 640 650
ESSQGWFEGL FNRSPWFTTL ISTIMGPLII LLLILLFGPC ILNRLVQFVK
660 670
DRISVVQALV LTQQYHQLKP LEYEP
Length:675
Mass (Da):74,025
Last modified:August 1, 1992 - v3
Checksum:iA097038E422BB3D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02794 Genomic RNA. Translation: CAA26561.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02794 Genomic RNA. Translation: CAA26561.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AOL X-ray 2.00 A 43-270 [» ]
ProteinModelPortali P03390.
SMRi P03390. Positions 43-269, 525-577.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P03390.

Family and domain databases

Gene3Di 3.90.310.10. 1 hit.
InterProi IPR008981. FMuLV_rcpt-bd.
IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view ]
PANTHERi PTHR10424. PTHR10424. 1 hit.
Pfami PF00429. TLV_coat. 1 hit.
[Graphical view ]
SUPFAMi SSF49830. SSF49830. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Friedrich R.W., Koch W., von Maydell-Livonius U., Schrewe H., Zimmermann W.
    Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Molecular analysis of the envelope gene and long terminal repeat of Friend mink cell focus-inducing virus: implications for the functions of these sequences."
    Koch W., Zimmermann W., Oliff A., Friedrich R.W.
    J. Virol. 49:828-840(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE.
  3. "Palmitoylation of the murine leukemia virus envelope glycoprotein transmembrane subunits."
    Yang C., Compans R.W.
    Virology 221:87-97(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION OF THE TRANSMEMBRANE PROTEIN, MUTAGENESIS OF CYS-640.
  4. "Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0-A resolution."
    Fass D., Davey R.A., Hamson C.A., Kim P.S., Cunningham J.M., Berger J.M.
    Science 277:1662-1666(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 43-270.

Entry informationi

Entry nameiENV_MLVF5
AccessioniPrimary (citable) accession number: P03390
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1992
Last modified: November 26, 2014
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3