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Protein

Envelope glycoprotein

Gene

env

Organism
Cas-Br-E murine leukemia virus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
Metal bindingi86ZincBy similarity1
Metal bindingi117ZincBy similarity1

GO - Molecular functioni

GO - Biological processi

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

Keywords - Ligandi

Metal-binding, Zinc

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
OrganismiCas-Br-E murine leukemia virus
Taxonomic identifieri11792 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostiMus musculus (Mouse) [TaxID: 10090]

Subcellular locationi

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 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).By similarity
Peptide R-peptide :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini34 – 606ExtracellularSequence analysisAdd BLAST573
Transmembranei607 – 627HelicalSequence analysisAdd BLAST21
Topological domaini628 – 661CytoplasmicSequence analysisAdd BLAST34

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Sequence analysisAdd BLAST33
ChainiPRO_000023958034 – 661Envelope glycoproteinAdd BLAST628
ChainiPRO_000004074834 – 465Surface proteinBy similarityAdd BLAST432
ChainiPRO_0000040749466 – 645Transmembrane proteinBy similarityAdd BLAST180
PeptideiPRO_0000040750646 – 661R-peptideAdd BLAST16

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi43N-linked (GlcNAc...); by hostBy similarity1
Disulfide bondi77 ↔ 129By similarity
Disulfide bondi103 ↔ 118By similarity
Disulfide bondi104 ↔ 114By similarity
Disulfide bondi152 ↔ 172By similarity
Disulfide bondi164 ↔ 177By similarity
Glycosylationi199N-linked (GlcNAc...); by hostBy similarity1
Disulfide bondi209 ↔ 215By similarity
Glycosylationi322N-linked (GlcNAc...); by hostBy similarity1
Disulfide bondi332 ↔ 559Interchain (between SU and TM chains, or C-335 with C-559); in linked form
Disulfide bondi332 ↔ 335
Glycosylationi361N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi362 ↔ 416By similarity
Disulfide bondi381 ↔ 393By similarity
Glycosylationi394N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi423 ↔ 436By similarity
Glycosylationi430N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi551 ↔ 558By similarity
Lipidationi626S-palmitoyl cysteine; by hostBy similarity1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei465 – 466Cleavage; by hostBy similarity2
Sitei645 – 646Cleavage; by viral protease p142

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

ProteinModelPortaliP08360.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 267Receptor-binding domain (RBD)Sequence analysisAdd BLAST236
Regioni468 – 488Fusion peptideBy similarityAdd BLAST21
Regioni534 – 550ImmunosuppressionBy similarityAdd BLAST17

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili497 – 533Sequence analysisAdd BLAST37

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi332 – 335CXXC4
Motifi551 – 559CX6CC9
Motifi651 – 654YXXL motif; contains endocytosis signalBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi264 – 302Pro-richAdd BLAST39

Domaini

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).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. 2 hits.
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.

P08360-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGPAFSKSP KDKTIERAFL GVLGILFVTG GLASRDNPHQ VYNITWEVTN
60 70 80 90 100
GEQDTVWAVT GNHPLWTWWP DLTPDLCMLA LHGPTHWGLD NHPPYSSPPG
110 120 130 140 150
PPCCSGDAGA VSGCARDCDE PLTSYSPRCN TAWNRLKLAR VTHAPKEGFY
160 170 180 190 200
ICPGSHRPRW ARSCGGLDAY YCASWGCETT GRAAWNPTSS WDYITVSNNL
210 220 230 240 250
TSSQATKACK NNGWCNPLVI RFTGPGKRAT SWTTGHFWGL RLYISGHDPG
260 270 280 290 300
LTFGIRLKVT DLGPRVPIGP NPVLSDQRPP SRPVPARPPP PSASPSTPTI
310 320 330 340 350
PPQQGTGDRL LNLVQGAYLT LNMTDPTRTQ ECWLCLVSEP PYYEGVAVLR
360 370 380 390 400
EYTSHETAPA NCSSGSQHKL TLSEVTGQGR CLGTVPKTHQ ALCNRTEPTV
410 420 430 440 450
SGSNYLVAPE GTLWACSTGL TPCLSTTVLN LTTDYCVLVE LWPKVTYHSP
460 470 480 490 500
DYVYTQFEPG ARFRREPVSL TLALLPEGLT MGGIAAGVGT GTTALVATQQ
510 520 530 540 550
FQQLQAAMHN DLKEVEKSIT NLEKSLTSLS EVVLQNRRGL DLLFLKEGGL
560 570 580 590 600
CAALKEECCF YADHTGLVRD SMAKLRERLN QRQKLFESGQ GWFEGLFNRS
610 620 630 640 650
PWFTTLISTI MGPLIVLLLI LLFGPCILNR LVQFVKDRIS VVQALVLTQQ
660
YHQLKPIEYE P
Length:661
Mass (Da):72,625
Last modified:August 1, 1988 - v1
Checksum:i255BEE3AF62FB9FF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti476 – 477PE → LG (PubMed:1840655).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14702 Genomic DNA. Translation: AAA46512.1.
X57540 Genomic DNA. No translation available.
PIRiB26103. VCMVCB.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14702 Genomic DNA. Translation: AAA46512.1.
X57540 Genomic DNA. No translation available.
PIRiB26103. VCMVCB.

3D structure databases

ProteinModelPortaliP08360.
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. 2 hits.
PfamiPF00429. TLV_coat. 1 hit.
[Graphical view]
SUPFAMiSSF49830. SSF49830. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiENV_MLVCB
AccessioniPrimary (citable) accession number: P08360
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 5, 2016
This is version 100 of the entry and version 1 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 one 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.