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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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi117 – 1171ZincBy similarity
Sitei469 – 4702Cleavage; by host
Sitei649 – 6502Cleavage; by viral protease p14Sequence Analysis

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 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 1 Publication; Peripheral membrane protein 1 Publication
Note: The R-peptide is membrane-associated through its palmitate.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 610577ExtracellularSequence AnalysisAdd
BLAST
Transmembranei611 – 63121HelicalSequence AnalysisAdd
BLAST
Topological domaini632 – 66534CytoplasmicSequence 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Sequence AnalysisAdd
BLAST
Chaini34 – 665632Envelope glycoproteinPRO_0000239588Add
BLAST
Chaini34 – 469436Surface proteinBy 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 hostBy similarity
Disulfide bondi79 ↔ 129By similarity
Disulfide bondi105 ↔ 118By similarity
Disulfide bondi106 ↔ 114By similarity
Disulfide bondi152 ↔ 172By similarity
Disulfide bondi164 ↔ 177By similarity
Glycosylationi199 – 1991N-linked (GlcNAc...); by hostBy similarity
Disulfide bondi209 ↔ 215By similarity
Glycosylationi326 – 3261N-linked (GlcNAc...); by hostBy similarity
Disulfide bondi336 ↔ 563Interchain (between SU and TM chains, or C-339 with C-563); in linked form
Disulfide bondi336 ↔ 339
Glycosylationi358 – 3581N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi365 – 3651N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi366 ↔ 420By similarity
Disulfide bondi385 ↔ 397By similarity
Glycosylationi398 – 3981N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi427 ↔ 440By similarity
Glycosylationi434 – 4341N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi555 ↔ 562By similarity
Lipidationi630 – 6301S-palmitoyl cysteine; by hostBy 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).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.By similarity
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 – 54732Combined sources
Helixi549 – 5513Combined sources
Helixi554 – 5585Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MOFX-ray1.70A514-567[»]
ProteinModelPortaliP03385.
SMRiP03385. Positions 42-266, 515-567.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03385.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 267234Receptor-binding domain (RBD)Sequence AnalysisAdd
BLAST
Regioni472 – 49221Fusion peptideBy similarityAdd
BLAST
Regioni538 – 55417ImmunosuppressionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili500 – 53738Sequence AnalysisAdd
BLAST

Motif

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

« Hide

        10         20         30         40         50
MARSTLSKPL KNKVNPRGPL IPLILLMLRG VSTASPGSSP HQVYNITWEV
60 70 80 90 100
TNGDRETVWA TSGNHPLWTW WPDLTPDLCM LAHHGPSYWG LEYQSPFSSP
110 120 130 140 150
PGPPCCSGGS SPGCSRDCEE PLTSLTPRCN TAWNRLKLDQ TTHKSNEGFY
160 170 180 190 200
VCPGPHRPRE SKSCGGPDSF YCAYWGCETT GRAYWKPSSS WDFITVNNNL
210 220 230 240 250
TSDQAVQVCK DNKWCNPLVI RFTDAGRRVT SWTTGHYWGL RLYVSGQDPG
260 270 280 290 300
LTFGIRLRYQ NLGPRVPIGP NPVLADQQPL SKPKPVKSPS VTKPPSGTPL
310 320 330 340 350
SPTQLPPAGT ENRLLNLVDG AYQALNLTSP DKTQECWLCL VAGPPYYEGV
360 370 380 390 400
AVLGTYSNHT SAPANCSVAS QHKLTLSEVT GQGLCIGAVP KTHQALCNTT
410 420 430 440 450
QTSSRGSYYL VAPTGTMWAC STGLTPCIST TILNLTTDYC VLVELWPRVT
460 470 480 490 500
YHSPSYVYGL FERSNRHKRE PVSLTLALLL GGLTMGGIAA GIGTGTTALM
510 520 530 540 550
ATQQFQQLQA AVQDDLREVE KSISNLEKSL TSLSEVVLQN RRGLDLLFLK
560 570 580 590 600
EGGLCAALKE ECCFYADHTG LVRDSMAKLR ERLNQRQKLF ESTQGWFEGL
610 620 630 640 650
FNRSPWFTTL ISTIMGPLIV LLMILLFGPC ILNRLVQFVK DRISVVQALV
660
LTQQYHQLKP IEYEP
Length:665
Mass (Da):73,302
Last modified:July 21, 1986 - v1
Checksum:i12EBA09C8FB93FE2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti655 – 6551Y → F(PubMed:6251454)Curated
Sequence conflicti663 – 6631Y → C(PubMed:6251454)Curated
Sequence conflicti663 – 6631Y → C(PubMed:6947213)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 118 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