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P21436 (ENV_MLVHO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 89. 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 76
    Short name=gp76
  2. Transmembrane protein
    Short name=TM
    Alternative name(s):
    Envelope protein p15E
  3. R-peptide
    Alternative name(s):
    p2E
Gene names
Name:env
OrganismHortulanus murine leukemia virus (HoMuLV) (Mus hortulanus virus)
Taxonomic identifier11799 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostMus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length666 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 666633Envelope glycoprotein
PRO_0000239585
Chain34 – 466433Surface protein By similarity
PRO_0000040760
Chain467 – 646180Transmembrane protein By similarity
PRO_0000040761
Peptide647 – 66620R-peptide By similarity
PRO_0000239586

Regions

Topological domain34 – 607574Extracellular Potential
Transmembrane608 – 62821Helical; Potential
Topological domain629 – 66638Cytoplasmic Potential
Region31 – 264234Receptor-binding domain (RBD) Potential
Region469 – 48921Fusion peptide By similarity
Region535 – 55117Immunosuppression By similarity
Coiled coil500 – 53435 Potential
Motif334 – 3374CXXC
Motif552 – 5609CX6CC
Motif652 – 6554YXXL motif; contains endocytosis signal By similarity
Compositional bias261 – 30444Pro-rich

Sites

Metal binding1151Zinc By similarity
Site466 – 4672Cleavage; by host By similarity
Site646 – 6472Cleavage; by viral protease p14 By similarity

Amino acid modifications

Lipidation6271S-palmitoyl cysteine; by host By similarity
Glycosylation421N-linked (GlcNAc...); by host By similarity
Glycosylation1971N-linked (GlcNAc...); by host Potential
Glycosylation2901N-linked (GlcNAc...); by host Potential
Glycosylation3241N-linked (GlcNAc...); by host By similarity
Glycosylation3561N-linked (GlcNAc...); by host Potential
Glycosylation3631N-linked (GlcNAc...); by host Potential
Glycosylation4311N-linked (GlcNAc...); by host Potential
Disulfide bond76 ↔ 127 By similarity
Disulfide bond102 ↔ 116 By similarity
Disulfide bond103 ↔ 112 By similarity
Disulfide bond150 ↔ 170 By similarity
Disulfide bond162 ↔ 175 By similarity
Disulfide bond207 ↔ 213 By similarity
Disulfide bond334 ↔ 560Interchain (between SU and TM chains, or C-337 with C-560); alternate
Disulfide bond334 ↔ 337Alternate
Disulfide bond364 ↔ 417 By similarity
Disulfide bond424 ↔ 437 By similarity
Disulfide bond552 ↔ 560 By similarity

Sequences

Sequence LengthMass (Da)Tools
P21436 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: FDC77956E4B213D1

FASTA66673,035
        10         20         30         40         50         60 
MDRPALPKSI KDKTNPWGPI ILGILIMLGG ALGKGSPHKV FNLTWEVYNQ EYETVWATSG 

        70         80         90        100        110        120 
SHPLWTWWPT LTPDLCMLAQ LAKPSWGLSD YPPYSKPPGP PCCTTDNNPP GCSRDCNGPL 

       130        140        150        160        170        180 
TYLTPRCSTA WNRLKLVLTT HHLNQGFYVC PGPHRPRHAR NCGGPDDFYC AHWGCETTGQ 

       190        200        210        220        230        240 
AYWKPSSSWD YIRVSNNASS SDATTACKNN NWCSPLAISF TDPGKRATSW TSGFTWGLRL 

       250        260        270        280        290        300 
YISGHPGLIF GVRLKISDLG PRVPIGPNPV LSEQRPPSQP EPARLPPSSN LTQGGTPSAP 

       310        320        330        340        350        360 
TGPPQEGTGD RLLDLVQGAY QALNATSPDK TQECWLCLVS SPPYYEGVAV VGPYSNHTTA 

       370        380        390        400        410        420 
PANCSADSQH KLTLSEVTGK PLPRKGSQDP PGPVQYHSGA RQKYSLSGGS RGTMWACNTG 

       430        440        450        460        470        480 
LTPCLSTAVL NLTTDYCVLV ELWPRVTYHS LDFVYRQVEG RTRYQREPVS LTLALLLGGL 

       490        500        510        520        530        540 
TMGGIAAGVG TGTSALVKTQ QFEQLHAAIQ ADLKEVESSI TNLEKSLTSL SEVVLQNRRG 

       550        560        570        580        590        600 
LDLLFLEKGG LCAALKEECC FYADHTGLVR DSMAKLRERL NQRQKLFEAG QGWFEGLFNR 

       610        620        630        640        650        660 
SPWLTTLIST IMGPLIILLL ILMFGPCILN RLVQFVKDRI SVVQALVLTQ QYHQLKPLEH 


GRAIVK 

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References

[1]"Nucleotide sequence and mode of transmission of the wild mouse ecotropic virus, HoMuLV."
Voytek P., Kozak C.A.
Virology 173:58-67(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26527 Genomic RNA. No translation available.
PIRVCMVHL. B32594.

3D structure databases

ProteinModelPortalP21436.
SMRP21436. Positions 39-263, 512-564.
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_MLVHO
AccessionPrimary (citable) accession number: P21436
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: February 19, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program