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P21445 (ENV_FSVSM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. 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 sarcoma virus (strain SM) (Sm-FeSV)
Taxonomic identifier11779 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostFelidae (cat family) [TaxID: 9681]

Protein attributes

Sequence length645 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 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 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 – 3636 Potential
Chain37 – 645609Envelope glycoprotein
PRO_0000239572
Chain37 – 448412Surface protein By similarity
PRO_0000040727
Chain449 – 628180Transmembrane protein By similarity
PRO_0000040728
Peptide629 – 64517R-peptide By similarity
PRO_0000239573

Regions

Topological domain37 – 589553Extracellular Potential
Transmembrane590 – 61021Helical; Potential
Topological domain611 – 64535Cytoplasmic Potential
Region451 – 47121Fusion peptide Potential
Region517 – 53317Immunosuppression By similarity
Coiled coil479 – 52850 Potential
Coiled coil538 – 57437 Potential
Motif315 – 3184CXXC
Motif534 – 5429CX6CC

Sites

Site448 – 4492Cleavage; by host By similarity
Site628 – 6292Cleavage; by viral protease By similarity

Amino acid modifications

Lipidation6091S-palmitoyl cysteine; by host By similarity
Glycosylation461N-linked (GlcNAc...); by host Potential
Glycosylation611N-linked (GlcNAc...); by host Potential
Glycosylation2701N-linked (GlcNAc...); by host Potential
Glycosylation3051N-linked (GlcNAc...); by host Potential
Glycosylation3101N-linked (GlcNAc...); by host Potential
Glycosylation3341N-linked (GlcNAc...); by host Potential
Glycosylation3371N-linked (GlcNAc...); by host Potential
Glycosylation3771N-linked (GlcNAc...); by host Potential
Glycosylation3931N-linked (GlcNAc...); by host Potential
Glycosylation4131N-linked (GlcNAc...); by host Potential
Disulfide bond128 ↔ 150 By similarity
Disulfide bond142 ↔ 155 By similarity
Disulfide bond315 ↔ 542Interchain (between SU and TM chains, or C-318 with C-542); alternate By similarity
Disulfide bond315 ↔ 318Alternate By similarity
Disulfide bond534 ↔ 541 By similarity

Sequences

Sequence LengthMass (Da)Tools
P21445 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 4E6DB90A00A43B21

FASTA64571,594
        10         20         30         40         50         60 
MEGPTHPKPF KDKTFSWDLI ILVGVVRVLL RLDVGMANPS PHQVYNVTWV ITNVQTNSQA 

        70         80         90        100        110        120 
NATSMLGTLT DAYPTLHVDL CDLVGDTWEP IVLDPSNVKH GARYSSSKYG CKTTDRKKQQ 

       130        140        150        160        170        180 
QTYPFYVCPG HAPSMGPKGT HCGGAHDGFC AAWGCETTGE AWWKPTSSWD YITVKRGSSQ 

       190        200        210        220        230        240 
DTSCDKNCNP LVLQFTQKGR QASWDGPKLW GLRLYRTGYD PIALFSVSRQ VSTIMPPQAM 

       250        260        270        280        290        300 
GPNLVLPEQK PPSRQSQTKS KVATQKPQTN GTTPRSVAPA TMSPKRIGTR DRLINLVQGT 

       310        320        330        340        350        360 
YLALNATDPN KTKDCWLCLV SRPPYYEGIA ILGNYSNQTN PPPSCLSTPQ HKLTISEVSG 

       370        380        390        400        410        420 
QGLCIGTVPR THQALCNKTQ QGHTGAHYLA APNGTYWACN TGLTPCISMA VLNWTSDFCV 

       430        440        450        460        470        480 
LIELWPRVTY HQPEYIYTHF DKAVRFRREP ISLTVALMLG GLTVGGIAAG VGTGTKALLE 

       490        500        510        520        530        540 
TAQFRQLQIA MHTDIQALEE SISALEKSLT SLSEVVLQNR RGLDILFLQG GGLCAALKEE 

       550        560        570        580        590        600 
CCFYADHTGL VRDNMAKLRE RLKQRQQLFD SQQGWFEGWF NKSPWFTTLI SSIMGPLLIL 

       610        620        630        640 
LLILLFGPCI LNRLVQFVKD RISVVQALIL TQQYQQIQQY DPDRP 

« Hide

References

[1]"Nucleotide sequence analysis of the LTRs and env genes of SM-FeSV and GA-FeSV."
Guilhot S., Hampe A., D'Auriol L., Galibert F.
Virology 161:252-258(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23025 Genomic DNA. Translation: AAA74004.1.
PIRVCMVSS. A33741.

3D structure databases

ProteinModelPortalP21445.
SMRP21445. Positions 41-236, 494-546.
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_FSVSM
AccessionPrimary (citable) accession number: P21445
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program