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P03386 (ENV_MLVAV) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Envelope glycoprotein
Alternative name(s):
Env polyprotein

Cleaved into the following 3 chains:

  1. Surface protein
    Short name=SU
    Alternative name(s):
    Glycoprotein 70
    Short name=gp70
  2. Transmembrane protein
    Short name=TM
    Alternative name(s):
    Envelope protein p15E
  3. R-peptide
    Alternative name(s):
    p2E
Gene names
Name:env
OrganismAKV murine leukemia virus (AKR (endogenous) murine leukemia virus) [Complete proteome]
Taxonomic identifier11791 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostMus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length669 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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

Subcellular location

Transmembrane protein: Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity.

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.

Domain

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.

Post-translational modification

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.

Sequence caution

The sequence CAA24493.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 669638Envelope glycoprotein
PRO_0000239579
Chain32 – 470439Surface protein By similarity
PRO_0000040745
Chain471 – 650180Transmembrane protein By similarity
PRO_0000040746
Peptide651 – 66919R-peptide By similarity
PRO_0000040747

Regions

Topological domain32 – 611580Extracellular Potential
Transmembrane612 – 63221Helical; Potential
Topological domain633 – 66937Cytoplasmic Potential
Region32 – 267236Receptor-binding domain (RBD) Potential
Region473 – 49321Fusion peptide By similarity
Region539 – 55517Immunosuppression By similarity
Coiled coil502 – 53837 Potential
Motif337 – 3404CXXC
Motif556 – 5649CX6CC
Motif656 – 6594YXXL motif; contains endocytosis signal By similarity
Compositional bias264 – 30845Pro-rich

Sites

Metal binding1171Zinc By similarity
Site470 – 4712Cleavage; by host By similarity
Site650 – 6512Cleavage; by viral protease p14 By similarity

Amino acid modifications

Lipidation6311S-palmitoyl cysteine; by host By similarity
Glycosylation431N-linked (GlcNAc...); by host By similarity
Glycosylation1991N-linked (GlcNAc...); by host By similarity
Glycosylation2931N-linked (GlcNAc...); by host Potential
Glycosylation3271N-linked (GlcNAc...); by host By similarity
Glycosylation3591N-linked (GlcNAc...); by host Potential
Glycosylation3661N-linked (GlcNAc...); by host Potential
Glycosylation3991N-linked (GlcNAc...); by host Potential
Disulfide bond77 ↔ 129 By similarity
Disulfide bond103 ↔ 118 By similarity
Disulfide bond104 ↔ 114 By similarity
Disulfide bond152 ↔ 172 By similarity
Disulfide bond164 ↔ 177 By similarity
Disulfide bond209 ↔ 215 By similarity
Disulfide bond337 ↔ 564Interchain (between SU and TM chains, or C-340 with C-564); alternate
Disulfide bond337 ↔ 340Alternate
Disulfide bond367 ↔ 421 By similarity
Disulfide bond386 ↔ 398 By similarity
Disulfide bond428 ↔ 441 By similarity
Disulfide bond556 ↔ 563 By similarity

Experimental info

Sequence conflict351G → R Ref.2
Sequence conflict4631E → K Ref.2
Sequence conflict5921E → K Ref.2

Sequences

Sequence LengthMass (Da)Tools
P03386 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 3A6C3845208A13F2

FASTA66973,756
        10         20         30         40         50         60 
MESTTLSKPF KNQVNPWGPL IVLLILGGVN PVTLGNSPHQ VFNLTWEVTN GDRETVWAIT 

        70         80         90        100        110        120 
GNHPLWTWWP DLTPDLCMLA LHGPSYWGLE YRAPFSPPPG PPCCSGSSDS TPGCSRDCEE 

       130        140        150        160        170        180 
PLTSYTPRCN TAWNRLKLSK VTHAHNGGFY VCPGPHRPRW ARSCGGPESF YCASWGCETT 

       190        200        210        220        230        240 
GRASWKPSSS WDYITVSNNL TSDQATPVCK GNEWCNSLTI RFTSFGKQAT SWVTGHWWGL 

       250        260        270        280        290        300 
RLYVSGHDPG LIFGIRLKIT DSGPRVPIGP NPVLSDRRPP SRPRPTRSPP PSNSTPTETP 

       310        320        330        340        350        360 
LTLPEPPPAG VENRLLNLVK GAYQALNLTS PDKTQECWLC LVSGPPYYEG VAVLGTYSNH 

       370        380        390        400        410        420 
TSAPANCSVA SQHKLTLSEV TGQGLCIGAV PKTHQVLCNT TQKTSDGSYY LAAPTGTTWA 

       430        440        450        460        470        480 
CSTGLTPCIS TTILDLTTDY CVLVELWPRV TYHSPSYVYH QFERRAKYKR EPVSLTLALL 

       490        500        510        520        530        540 
LGGLTMGGIA AGVGTGTTAL VATQQFQQLQ AAMHDDLKEV EKSITNLEKS LTSLSEVVLQ 

       550        560        570        580        590        600 
NRRGLDLLFL KEGGLCAALK EECCFYADHT GLVRDSMAKL RERLSQRQKL FESQQGWFEG 

       610        620        630        640        650        660 
LFNKSPWFTT LISTIMGPLI ILLLILLFGP CILNRLVQFI KDRISVVQAL VLTQQYHQLK 


TIEDCKSRE 

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References

[1]"Nucleotide sequence of AKV murine leukemia virus."
Herr W.
J. Virol. 49:471-478(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Nucleotide sequence of the 3' half of AKV."
Herr W., Corbin V., Gilbert W.
Nucleic Acids Res. 10:6931-6944(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"Nucleotide sequence of the Akv env gene."
Lenz J., Crowther R., Straceski A., Haseltine W.
J. Virol. 42:519-529(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01998 Genomic RNA. Translation: AAB03092.1.
V01164 Genomic DNA. Translation: CAA24493.1. Different initiation.
PIRVCVWEK. A92995.

3D structure databases

ProteinModelPortalP03386.
SMRP03386. Positions 40-266, 516-568.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.90.310.10. 1 hit.
InterProIPR008981. FMuLV_rcpt-bd.
IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERPTHR10424. PTHR10424. 1 hit.
PfamPF00429. TLV_coat. 1 hit.
[Graphical view]
SUPFAMSSF49830. SSF49830. 1 hit.
ProtoNetSearch...

Entry information

Entry nameENV_MLVAV
AccessionPrimary (citable) accession number: P03386
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program