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P03385

- ENV_MLVMS

UniProt

P03385 - ENV_MLVMS

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Protein

Envelope glycoprotein

Gene
env
Organism
Moloney murine leukemia virus (isolate Shinnick) (MoMLV)
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. Interaction with HECT ubiquitin ligases activates a thiol in a CXXC motif of the C-terminal domain, where the other Cys residue participates in the formation of the intersubunit disulfide. The activated thiol will attack the disulfide and cause its isomerization into a disulfide isomer within the motif. This leads to SU displacement and TM refolding, and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane.1 Publication
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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi117 – 1171Zinc By similarity
Sitei469 – 4702Cleavage; by host
Sitei649 – 6502Cleavage; by viral protease p14 Reviewed prediction

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. metal ion binding Source: UniProtKB-KW
  3. structural molecule activity Source: InterPro

GO - Biological processi

  1. fusion of virus membrane with host plasma membrane Source: UniProtKB-KW
  2. 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, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus entry into host cell

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein
Short name:
Pr80env
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
OrganismiMoloney murine leukemia virus (isolate Shinnick) (MoMLV)
Taxonomic identifieri928306 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
ProteomesiUP000006625: Genome

Subcellular locationi

Chain Transmembrane protein : Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity 1 Publication
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.1 Publication
R-peptide : Host cell membrane; Peripheral membrane protein
Note: The R-peptide is membrane-associated through its palmitate.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 610577Extracellular Reviewed predictionAdd
BLAST
Transmembranei611 – 63121Helical; Reviewed predictionAdd
BLAST
Topological domaini632 – 66534Cytoplasmic Reviewed predictionAdd
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 – 3333 Reviewed predictionAdd
BLAST
Chaini34 – 665632Envelope glycoproteinPRO_0000239588Add
BLAST
Chaini34 – 469436Surface protein By similarityPRO_0000040765Add
BLAST
Chaini470 – 649180Transmembrane proteinPRO_0000040766Add
BLAST
Peptidei650 – 66516R-peptidePRO_0000040767Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi45 – 451N-linked (GlcNAc...); by host By similarity
Disulfide bondi79 ↔ 129 By similarity
Disulfide bondi105 ↔ 118 By similarity
Disulfide bondi106 ↔ 114 By similarity
Disulfide bondi152 ↔ 172 By similarity
Disulfide bondi164 ↔ 177 By similarity
Glycosylationi199 – 1991N-linked (GlcNAc...); by host By similarity
Disulfide bondi209 ↔ 215 By similarity
Glycosylationi326 – 3261N-linked (GlcNAc...); by host By similarity
Disulfide bondi336 ↔ 563Interchain (between SU and TM chains, or C-339 with C-563); in linked form1 Publication
Disulfide bondi336 ↔ 339
Glycosylationi358 – 3581N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi365 – 3651N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi366 ↔ 420 By similarity
Disulfide bondi385 ↔ 397 By similarity
Glycosylationi398 – 3981N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi427 ↔ 440 By similarity
Glycosylationi434 – 4341N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi555 ↔ 562 By similarity
Lipidationi630 – 6301S-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.1 Publication
The R-peptide is palmitoylated.1 Publication

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. The activated Env consists of SU monomers and TM trimers.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-8074066,EBI-8074066

Protein-protein interaction databases

MINTiMINT-7304679.

Structurei

Secondary structure

1
665
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi516 – 54732
Helixi549 – 5513
Helixi554 – 5585

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MOFX-ray1.70A514-567[»]
ProteinModelPortaliP03385.
SMRiP03385. Positions 42-266, 515-567.

Miscellaneous databases

EvolutionaryTraceiP03385.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 267234Receptor-binding domain (RBD) Reviewed predictionAdd
BLAST
Regioni472 – 49221Fusion peptide By similarityAdd
BLAST
Regioni538 – 55417Immunosuppression By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili500 – 53738 Reviewed predictionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi336 – 3394CXXC
Motifi555 – 5639CX6CC
Motifi655 – 6584YXXL motif; contains endocytosis signal By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi264 – 30744Pro-richAdd
BLAST

Domaini

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.
The YXXL motif is involved in determining the exact site of viral release at the surface of infected mononuclear cells and promotes endocytosis.

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.

P03385-1 [UniParc]FASTAAdd to Basket

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MARSTLSKPL KNKVNPRGPL IPLILLMLRG VSTASPGSSP HQVYNITWEV    50
TNGDRETVWA TSGNHPLWTW WPDLTPDLCM LAHHGPSYWG LEYQSPFSSP 100
PGPPCCSGGS SPGCSRDCEE PLTSLTPRCN TAWNRLKLDQ TTHKSNEGFY 150
VCPGPHRPRE SKSCGGPDSF YCAYWGCETT GRAYWKPSSS WDFITVNNNL 200
TSDQAVQVCK DNKWCNPLVI RFTDAGRRVT SWTTGHYWGL RLYVSGQDPG 250
LTFGIRLRYQ NLGPRVPIGP NPVLADQQPL SKPKPVKSPS VTKPPSGTPL 300
SPTQLPPAGT ENRLLNLVDG AYQALNLTSP DKTQECWLCL VAGPPYYEGV 350
AVLGTYSNHT SAPANCSVAS QHKLTLSEVT GQGLCIGAVP KTHQALCNTT 400
QTSSRGSYYL VAPTGTMWAC STGLTPCIST TILNLTTDYC VLVELWPRVT 450
YHSPSYVYGL FERSNRHKRE PVSLTLALLL GGLTMGGIAA GIGTGTTALM 500
ATQQFQQLQA AVQDDLREVE KSISNLEKSL TSLSEVVLQN RRGLDLLFLK 550
EGGLCAALKE ECCFYADHTG LVRDSMAKLR ERLNQRQKLF ESTQGWFEGL 600
FNRSPWFTTL ISTIMGPLIV LLMILLFGPC ILNRLVQFVK DRISVVQALV 650
LTQQYHQLKP IEYEP 665
Length:665
Mass (Da):73,302
Last modified:July 21, 1986 - v1
Checksum:i12EBA09C8FB93FE2
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti655 – 6551Y → F1 Publication
Sequence conflicti663 – 6631Y → C1 Publication
Sequence conflicti663 – 6631Y → C1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02255 Genomic RNA. Translation: AAB59943.1.
AF033811 Genomic RNA. Translation: AAC82567.1.
PIRiA93265. VCVWEM.
RefSeqiNP_057935.1. NC_001501.1.

Genome annotation databases

GeneIDi2193424.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02255 Genomic RNA. Translation: AAB59943.1 .
AF033811 Genomic RNA. Translation: AAC82567.1 .
PIRi A93265. VCVWEM.
RefSeqi NP_057935.1. NC_001501.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MOF X-ray 1.70 A 514-567 [» ]
ProteinModelPortali P03385.
SMRi P03385. Positions 42-266, 515-567.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-7304679.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2193424.

Miscellaneous databases

EvolutionaryTracei P03385.

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. "Nucleotide sequence of Moloney murine leukaemia virus."
    Shinnick T.M., Lerner R.A., Sutcliffe J.G.
    Nature 293:543-548(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Clone pMLV-1.
  2. Chappey C.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "Chemical synthesis of a polypeptide predicted from nucleotide sequence allows detection of a new retroviral gene product."
    Sutcliffe J.G., Shinnick T.M., Green N., Liu F.-T., Niman H.L., Lerner R.A.
    Nature 287:801-805(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 496-665.
  4. "Nucleotide sequence of Moloney leukemia virus: 3' end reveals details of replications, analogy to bacterial transposons, and an unexpected gene."
    Sutcliffe J.G., Shinnick T.M., Verma I.M., Lerner R.A.
    Proc. Natl. Acad. Sci. U.S.A. 77:3302-3306(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 484-665.
    Strain: Clone pMLV-201.
  5. "Sequence-specific antibodies show that maturation of Moloney leukemia virus envelope polyprotein involves removal of a COOH-terminal peptide."
    Green N., Shinnick T.M., Witte O., Ponticelli A., Sutcliffe J.G., Lerner R.A.
    Proc. Natl. Acad. Sci. U.S.A. 78:6023-6027(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 470-489 AND 598-665.
  6. "Inhibition of lymphocyte proliferation by a synthetic peptide homologous to retroviral envelope proteins."
    Cianciolo G.J., Copeland T.D., Oroszlan S., Snyderman R.
    Science 230:453-455(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: IMMUNOSUPPRESSIVE REGION.
  7. "Palmitoylation of the intracytoplasmic R peptide of the transmembrane envelope protein in Moloney murine leukemia virus."
    Olsen K.E., Andersen K.B.
    J. Virol. 73:8975-8981(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION OF THE R-PEPTIDE, PALMITOYLATION OF THE R-PEPTIDE.
  8. "Mutational analysis of the R peptide cleavage site of Moloney murine leukaemia virus envelope protein."
    Kubo Y., Amanuma H.
    J. Gen. Virol. 84:2253-2257(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF THE R-PEPTIDE.
  9. "Isomerization of the intersubunit disulphide-bond in Env controls retrovirus fusion."
    Wallin M., Ekstroem M., Garoff H.
    EMBO J. 23:54-65(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERCHAIN DISULFIDE BOND.
  10. "Turning of the receptor-binding domains opens up the murine leukaemia virus Env for membrane fusion."
    Wu S.-R., Sjoeberg M., Wallin M., Lindqvist B., Ekstroem M., Hebert H., Koeck P.J., Garoff H.
    EMBO J. 27:2799-2808(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Stabilization of TM trimer interactions during activation of moloney murine leukemia virus Env."
    Sjoberg M., Lindqvist B., Garoff H.
    J. Virol. 82:2358-2366(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  12. "Retrovirus envelope domain at 1.7-A resolution."
    Fass D., Harrison S.C., Kim P.S.
    Nat. Struct. Biol. 3:465-469(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 514-567.

Entry informationi

Entry nameiENV_MLVMS
AccessioniPrimary (citable) accession number: P03385
Secondary accession number(s): Q77YG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 3, 2014
This is version 115 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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