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P31791 (ENV_FENV1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. 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
OrganismFeline endogenous virus ECE1
Taxonomic identifier11766 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusunclassified Gammaretrovirus
Virus hostFelidae (cat family) [TaxID: 9681]

Protein attributes

Sequence length671 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 noncovalent interactions or 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 extravirion 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 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 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 – 2222 Potential
Chain23 – 671649Envelope glycoprotein
PRO_0000239558
Chain23 – 470448Surface protein By similarity
PRO_0000040703
Chain471 – 650180Transmembrane protein By similarity
PRO_0000040704
Peptide651 – 67121R-peptide By similarity
PRO_0000239559

Regions

Topological domain23 – 611589Extracellular Potential
Transmembrane612 – 63221Helical; Potential
Topological domain633 – 67139Cytoplasmic Potential
Region473 – 49321Fusion peptide Potential
Region539 – 55517Immunosuppression By similarity
Coiled coil501 – 55050 Potential
Coiled coil560 – 59637 Potential
Motif336 – 3394CXXC
Motif556 – 5649CX6CC
Motif656 – 6594YXXL motif; contains endocytosis signal By similarity

Sites

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

Amino acid modifications

Lipidation6311S-palmitoyl cysteine; by host By similarity
Glycosylation1691N-linked (GlcNAc...); by host Potential
Glycosylation2811N-linked (GlcNAc...); by host Potential
Glycosylation3261N-linked (GlcNAc...); by host Potential
Glycosylation3311N-linked (GlcNAc...); by host Potential
Glycosylation3551N-linked (GlcNAc...); by host Potential
Glycosylation3581N-linked (GlcNAc...); by host Potential
Glycosylation4151N-linked (GlcNAc...); by host Potential
Glycosylation4351N-linked (GlcNAc...); by host Potential
Disulfide bond121 ↔ 142 By similarity
Disulfide bond134 ↔ 147 By similarity

Sequences

Sequence LengthMass (Da)Tools
P31791 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: EA9847024EF794A0

FASTA67175,152
        10         20         30         40         50         60 
MKPPAGMVFL WVLTSLGAGI GAKIVKEGNP HQVYTLTWQI YSQSGEVVWE VQGNHALNTW 

        70         80         90        100        110        120 
WPALTPDFCQ LAAGLDTWDI PDRSPKNLET SMEGTSQQLT PQGCSKPWKR CALTERDFYV 

       130        140        150        160        170        180 
CPRDNRDRAT AHRCGGYEEY FCSAWGCETT GDAYWQPTST WDLITITRNY TKPDSCDDRV 

       190        200        210        220        230        240 
ERERKTSRHW RDPLSLPLKI TFTDSGKRAL GWQTGYTWGL RWYLPGKDRG IILKIKLKID 

       250        260        270        280        290        300 
TITQTVGPNL VLADQKTPVQ LAIPVQPPRA PTQTPRVNPV NSTLSPSLGY PAPAPGPRPP 

       310        320        330        340        350        360 
YPTSPSRPGT GDRLLNLVQG VYLTLNLTAP NQTQDCWLCL TAKPPYYQGV AIIGNFTNHT 

       370        380        390        400        410        420 
NAPLRCSTTP RHGLTLTEVT GYGLCIGKIP PSHQNLCSQT VPSVGQGPYY LTAPNGTYWV 

       430        440        450        460        470        480 
CNTGLTPCIS LQILNDTADY CILIELWPKI FYHDSEYIYG HYEPGGRFRR DPVSLTVALL 

       490        500        510        520        530        540 
LGGLTMGSLA AGIGTGTAAL IETNQFKQLQ IAMHSDIQAL EESISALERS LISLSEVVLQ 

       550        560        570        580        590        600 
NRRGLDLLFL QEGGLCAALK EECCFYADHT GIVRDSMAKL RERFKQRQKL FESQQGWFEG 

       610        620        630        640        650        660 
WYNKSPWFTT LVSSLMVPLI LLLLILMFGP CILNHLLQFI RERLSVIQAL VLTQQYHQLR 

       670 
QFDAERPDAI E 

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References

[1]"The exogenous RD-114 and the related endogenous proviral element ECE1 of domestic cat differ in their env genes."
Moehring R., Drescher B., Riedel H., Bauer D., Rohde K., Beyer W., Rosenthal S.
Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51929 Genomic DNA. Translation: CAB38567.1.
PIRVCMVCE. S12815.

3D structure databases

ProteinModelPortalP31791.
SMRP31791. Positions 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_FENV1
AccessionPrimary (citable) accession number: P31791
Secondary accession number(s): Q28416
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: February 19, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program