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Protein

Envelope glycoprotein

Gene

env

Organism
Feline sarcoma virus (strain SM) (Sm-FeSV)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

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).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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei448 – 4492Cleavage; by hostBy similarity
Sitei628 – 6292Cleavage; by viral proteaseBy similarity

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. fusion of virus membrane with host plasma membrane Source: UniProtKB-KW
  2. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Fusion of virus membrane with host cell membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein
Alternative name(s):
Env polyprotein
Cleaved into the following 3 chains:
Surface protein
Short name:
SU
Alternative name(s):
Glycoprotein 70
Short name:
gp70
Transmembrane protein
Short name:
TM
Alternative name(s):
Envelope protein p15E
Alternative name(s):
p2E
Gene namesi
Name:env
OrganismiFeline sarcoma virus (strain SM) (Sm-FeSV)
Taxonomic identifieri11779 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostiFelidae (cat family) [TaxID: 9681]

Subcellular locationi

Chain Surface protein : Virion membrane; Peripheral membrane protein. Host cell membrane By similarity; 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).By similarity
R-peptide : Host cell membrane By similarity; Peripheral membrane protein By similarity
Note: The R-peptide is membrane-associated through its palmitate.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini37 – 589553ExtracellularSequence AnalysisAdd
BLAST
Transmembranei590 – 61021HelicalSequence AnalysisAdd
BLAST
Topological domaini611 – 64535CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. viral capsid Source: InterPro
  4. viral envelope Source: UniProtKB-KW
  5. virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3636Sequence AnalysisAdd
BLAST
Chaini37 – 645609Envelope glycoproteinPRO_0000239572Add
BLAST
Chaini37 – 448412Surface proteinBy similarityPRO_0000040727Add
BLAST
Chaini449 – 628180Transmembrane proteinBy similarityPRO_0000040728Add
BLAST
Peptidei629 – 64517R-peptideBy similarityPRO_0000239573Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi61 – 611N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi128 ↔ 150By similarity
Disulfide bondi142 ↔ 155By similarity
Glycosylationi270 – 2701N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi305 – 3051N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi310 – 3101N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi315 ↔ 542Interchain (between SU and TM chains, or C-318 with C-542); in linked formBy similarity
Disulfide bondi315 ↔ 318By similarity
Glycosylationi334 – 3341N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi337 – 3371N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi377 – 3771N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi393 – 3931N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi413 – 4131N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi534 ↔ 541By similarity
Lipidationi609 – 6091S-palmitoyl cysteine; by hostBy similarity

Post-translational modificationi

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).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).By similarity
The transmembrane protein is palmitoylated.By similarity
The R-peptide is palmitoylated.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP21445.
SMRiP21445. Positions 41-236, 494-546.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni451 – 47121Fusion peptideSequence AnalysisAdd
BLAST
Regioni517 – 53317ImmunosuppressionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili479 – 52850Sequence AnalysisAdd
BLAST
Coiled coili538 – 57437Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi315 – 3184CXXC
Motifi534 – 5429CX6CC

Domaini

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).By similarity

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di3.90.310.10. 1 hit.
InterProiIPR008981. FMuLV_rcpt-bd.
IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERiPTHR10424. PTHR10424. 1 hit.
PfamiPF00429. TLV_coat. 1 hit.
[Graphical view]
SUPFAMiSSF49830. SSF49830. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21445-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEGPTHPKPF KDKTFSWDLI ILVGVVRVLL RLDVGMANPS PHQVYNVTWV
60 70 80 90 100
ITNVQTNSQA NATSMLGTLT DAYPTLHVDL CDLVGDTWEP IVLDPSNVKH
110 120 130 140 150
GARYSSSKYG CKTTDRKKQQ QTYPFYVCPG HAPSMGPKGT HCGGAHDGFC
160 170 180 190 200
AAWGCETTGE AWWKPTSSWD YITVKRGSSQ DTSCDKNCNP LVLQFTQKGR
210 220 230 240 250
QASWDGPKLW GLRLYRTGYD PIALFSVSRQ VSTIMPPQAM GPNLVLPEQK
260 270 280 290 300
PPSRQSQTKS KVATQKPQTN GTTPRSVAPA TMSPKRIGTR DRLINLVQGT
310 320 330 340 350
YLALNATDPN KTKDCWLCLV SRPPYYEGIA ILGNYSNQTN PPPSCLSTPQ
360 370 380 390 400
HKLTISEVSG QGLCIGTVPR THQALCNKTQ QGHTGAHYLA APNGTYWACN
410 420 430 440 450
TGLTPCISMA VLNWTSDFCV LIELWPRVTY HQPEYIYTHF DKAVRFRREP
460 470 480 490 500
ISLTVALMLG GLTVGGIAAG VGTGTKALLE TAQFRQLQIA MHTDIQALEE
510 520 530 540 550
SISALEKSLT SLSEVVLQNR RGLDILFLQG GGLCAALKEE CCFYADHTGL
560 570 580 590 600
VRDNMAKLRE RLKQRQQLFD SQQGWFEGWF NKSPWFTTLI SSIMGPLLIL
610 620 630 640
LLILLFGPCI LNRLVQFVKD RISVVQALIL TQQYQQIQQY DPDRP
Length:645
Mass (Da):71,594
Last modified:February 1, 1996 - v2
Checksum:i4E6DB90A00A43B21
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23025 Genomic DNA. Translation: AAA74004.1.
PIRiA33741. VCMVSS.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23025 Genomic DNA. Translation: AAA74004.1.
PIRiA33741. VCMVSS.

3D structure databases

ProteinModelPortaliP21445.
SMRiP21445. Positions 41-236, 494-546.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.90.310.10. 1 hit.
InterProiIPR008981. FMuLV_rcpt-bd.
IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERiPTHR10424. PTHR10424. 1 hit.
PfamiPF00429. TLV_coat. 1 hit.
[Graphical view]
SUPFAMiSSF49830. SSF49830. 1 hit.
ProtoNetiSearch...

Publicationsi

  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].

Entry informationi

Entry nameiENV_FSVSM
AccessioniPrimary (citable) accession number: P21445
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: February 1, 1996
Last modified: January 7, 2015
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.