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P26804

- ENV_MLVFF

UniProt

P26804 - ENV_MLVFF

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Protein
Envelope glycoprotein
Gene
env
Organism
Friend murine leukemia virus (isolate FB29) (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.
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi89 – 891Zinc By similarity
Metal bindingi120 – 1201Zinc By similarity
Sitei479 – 4802Cleavage; by host By similarity
Sitei659 – 6602Cleavage; by viral protease p14 By similarity

GO - Molecular functioni

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

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 FB29) (FrMLV)
Taxonomic identifieri11797 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
ProteomesiUP000008877: Genome

Subcellular locationi

Chain Surface protein : Virion membrane; Peripheral membrane protein. Host cell membrane; 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.
R-peptide : Host cell membrane; 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 – 620586Extracellular Reviewed prediction
Add
BLAST
Transmembranei621 – 64121Helical; Reviewed prediction
Add
BLAST
Topological domaini642 – 67635Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434 Reviewed prediction
Add
BLAST
Chaini35 – 676642Envelope glycoprotein
PRO_0000239582Add
BLAST
Chaini35 – 479445Surface protein By similarity
PRO_0000040754Add
BLAST
Chaini480 – 659180Transmembrane protein By similarity
PRO_0000040755Add
BLAST
Peptidei660 – 67617R-peptide By similarity
PRO_0000040756Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...); by host By similarity
Disulfide bondi80 ↔ 132 By similarity
Disulfide bondi106 ↔ 121 By similarity
Disulfide bondi107 ↔ 117 By similarity
Disulfide bondi155 ↔ 175 By similarity
Disulfide bondi167 ↔ 180 By similarity
Glycosylationi202 – 2021N-linked (GlcNAc...); by host By similarity
Disulfide bondi212 ↔ 218 By similarity
Glycosylationi336 – 3361N-linked (GlcNAc...); by host By 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 host Reviewed prediction
Glycosylationi375 – 3751N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi376 ↔ 430 By similarity
Disulfide bondi395 ↔ 407 By similarity
Glycosylationi408 – 4081N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi437 ↔ 450 By similarity
Glycosylationi444 – 4441N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi565 ↔ 572 By similarity
Lipidationi640 – 6401S-palmitoyl cysteine; by host By similarity

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.
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.
The transmembrane protein is palmitoylated By similarity.
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

3D structure databases

ProteinModelPortaliP26804.
SMRiP26804. Positions 43-269, 525-577.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 270236Receptor-binding domain (RBD) Reviewed prediction
Add
BLAST
Regioni482 – 50221Fusion peptide By similarity
Add
BLAST
Regioni548 – 56417Immunosuppression By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili513 – 54735 Reviewed prediction
Add
BLAST

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi267 – 31751Pro-rich
Add
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.

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.

P26804-1 [UniParc]FASTAAdd to Basket

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MACSTLSKSP KDKIDPRDLL IPLILFLSLK GARSAAPGSS PHQVYNITWE    50
VTNGDRETVW AISGNHPLWT WWPVLTPDLC MLALSGPPHW GLEYQAPYSS 100
PPGPPCCSGS SGNVAGCARD CNEPLTSLTP RCNTAWNRLK LDQVTHKSSE 150
GFYVCPGSHR PREAKSCGGP DSFYCASWGC ETTGRVYWKP SSSWDYITVD 200
NNLTSNQAVQ VCKDNKWCNP LAIRFTNAGK QVTSWTTGHY WGLRLYVSGQ 250
DPGLTFGIRL SYQNLGPRIP IGPNPVLADQ LSFPLPNPLP KPAKSPPASS 300
STPTLISPSP TPTQPPPAGT GDRLLNLVQG AYQALNLTNP DKTQECWLCL 350
VSGPPYYEGV AVLGTYSNHT SAPANCSVAS QHKLTLSEVT GRGLCIGTVP 400
KTHQALCNTT LKAGKGSYYL VAPTGTMWAC NTGLTPCLSA TVLNRTTDYC 450
VLVELWPRVT YHPPSYVYSQ FEKSHRHKRE PVSLTLALLL GGLTMGGIAA 500
GVGTGTTALV ATQQFQQLHA AVQDDLKEVE KSITNLEKSL TSLSEVVLQN 550
RRGLDLLFLK EGGLCAALKE ECCFYADHTG LVRDSMAKLR ERLSQRQKLF 600
ESSQGWFEGW FNRSPWFTTL ISTIMGPLII LLLILLFGPC ILNRLVQFVK 650
DRISVVQALV LTQQYHQLKP LEYEPQ 676
Length:676
Mass (Da):74,050
Last modified:August 1, 1992 - v1
Checksum:iE18C44511145188B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11128 Genomic DNA. Translation: CAA77479.1.
PIRiS70395.
RefSeqiNP_040334.1. NC_001362.1.

Genome annotation databases

GeneIDi1491875.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11128 Genomic DNA. Translation: CAA77479.1 .
PIRi S70395.
RefSeqi NP_040334.1. NC_001362.1.

3D structure databases

ProteinModelPortali P26804.
SMRi P26804. Positions 43-269, 525-577.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1491875.

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. "Complete nucleotide sequence of Friend murine leukemia virus, strain FB29."
    Perryman S., Nishio J., Chesebro B.
    Nucleic Acids Res. 19:6950-6950(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiENV_MLVFF
AccessioniPrimary (citable) accession number: P26804
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: September 3, 2014
This is version 98 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

Complete proteome

External Data

Dasty 3

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