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P21415 (ENV_GALV) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 95. 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
OrganismGibbon ape leukemia virus (GALV) [Complete proteome]
Taxonomic identifier11840 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostHylobatidae (gibbons) [TaxID: 9577]

Protein attributes

Sequence length685 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 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.

The YXXL motif is involved in determining the exact site of viral release at the surface of infected mononuclear cells and promotes endocytosis 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 AAA46811.1 differs from that shown. Reason: Frameshift at positions 667 and 674.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141 Potential
Chain42 – 685644Envelope glycoprotein
PRO_0000239575
Chain42 – 489448Surface protein By similarity
PRO_0000040731
Chain490 – 670181Transmembrane protein By similarity
PRO_0000040732
Peptide671 – 68515R-peptide By similarity
PRO_0000239576

Regions

Topological domain42 – 632591Extracellular Potential
Transmembrane633 – 65321Helical; Potential
Topological domain654 – 68532Cytoplasmic Potential
Region492 – 51221Fusion peptide By similarity
Region559 – 57517Immunosuppression By similarity
Coiled coil520 – 57051 Potential
Coiled coil580 – 61637 Potential
Motif354 – 3574CXXC
Motif576 – 5849CX6CC
Motif676 – 6794YXXL motif; contains endocytosis signal By similarity

Sites

Site489 – 4902Cleavage; by host By similarity
Site669 – 6702Cleavage; by viral protease By similarity

Amino acid modifications

Lipidation6511S-palmitoyl cysteine; by host By similarity
Glycosylation3011N-linked (GlcNAc...); by host Potential
Glycosylation3441N-linked (GlcNAc...); by host Potential
Glycosylation4151N-linked (GlcNAc...); by host Potential
Glycosylation4211N-linked (GlcNAc...); by host Potential
Glycosylation4331N-linked (GlcNAc...); by host Potential
Glycosylation4531N-linked (GlcNAc...); by host Potential
Disulfide bond148 ↔ 169 By similarity
Disulfide bond161 ↔ 174 By similarity
Disulfide bond354 ↔ 584Interchain (between SU and TM chains, or C-357 with C-584); alternate By similarity
Disulfide bond354 ↔ 357Alternate By similarity
Disulfide bond576 ↔ 583 By similarity

Sequences

Sequence LengthMass (Da)Tools
P21415 [UniParc].

Last modified June 13, 2006. Version 2.
Checksum: D13AB40C5F3A1721

FASTA68575,837
        10         20         30         40         50         60 
MVLLPGSMLL TSNLHHLRHQ MSPGSWKRLI ILLSCVFGGG GTSLQNKNPH QPMTLTWQVL 

        70         80         90        100        110        120 
SQTGDVVWDT KAVQPPWTWW PTLKPDVCAL AASLESWDIP GTDVSSSKRV RPPDSDYTAA 

       130        140        150        160        170        180 
YKQITWGAIG CSYPRARTRM ASSTFYVCPR DGRTLSEARR CGGLESLYCK EWDCETTGTG 

       190        200        210        220        230        240 
YWLSKSSKDL ITVKWDQNSE WTQKFQQCHQ TGWCNPLKID FTDKGKLSKD WITGKTWGLR 

       250        260        270        280        290        300 
FYVSGHPGVQ FTIRLKITNM PAVAVGPDLV LVEQGPPRTS LALPPPLPPR EAPPPSLPDS 

       310        320        330        340        350        360 
NSTALATSAQ TPTVRKTIVT LNTPPPTTGD RLFDLVQGAF LTLNATNPGA TESCWLCLAM 

       370        380        390        400        410        420 
GPPYYEAIAS SGEVAYSTDL DRCRWGTQGK LTLTEVSGHG LCIGKVPFTH QHLCNQTLSI 

       430        440        450        460        470        480 
NSSGDHQYLL PSNHSWWACS TGLTPCLSTS VFNQTRDFCI QVQLIPRIYY YPEEVLLQAY 

       490        500        510        520        530        540 
DNSHPRTKRE AVSLTLAVLL GLGITAGIGT GSTALIKGPI DLQQGLTSLQ IAIDADLRAL 

       550        560        570        580        590        600 
QDSVSKLEDS LTSLSEVVLQ NRRGLDLLFL KEGGLCAALK EECCFYIDHS GAVRDSMKKL 

       610        620        630        640        650        660 
KEKLDKRQLE RQKSQNWYEG WFNNSPWFTT LLSTIAGPLL LLLLLLILGP CIINKLVQFI 

       670        680 
NDRISAVKIL VLRQKYQALE NEGNL 

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References

[1]"Genetic organization of gibbon ape leukemia virus."
Delassus S., Sonigo P., Wain-Hobson S.
Virology 173:205-213(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Simian sarcoma-associated virus fails to infect Chinese hamster cells despite the presence of functional gibbon ape leukemia virus receptors."
Ting Y.T., Wilson C.A., Farrell K.B., Chaudry G.J., Eiden M.V.
J. Virol. 72:9453-9458(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: SEATO.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26927 Genomic RNA. Translation: AAA46811.1. Frameshift.
AF055060 mRNA. Translation: AAC96083.1.
PIRVCLJGL. C32595.
RefSeqNP_056791.2. NC_001885.2.

3D structure databases

ProteinModelPortalP21415.
SMRP21415. Positions 536-588.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1491895.

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_GALV
AccessionPrimary (citable) accession number: P21415
Secondary accession number(s): Q9YWM3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: June 13, 2006
Last modified: February 19, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program