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P06445

- ENV_RMCFV

UniProt

P06445 - ENV_RMCFV

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Protein

Envelope glycoprotein

Gene

env

Organism
Rauscher mink cell focus-inducing virus
Status
Reviewed - 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
Sitei443 – 4442Cleavage; by hostBy similarity
Sitei623 – 6242Cleavage; by viral protease p14By 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
OrganismiRauscher mink cell focus-inducing virus
Taxonomic identifieri11784 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostiMus musculus (Mouse) [TaxID: 10090]

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

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. viral capsid Source: InterPro
  4. viral envelope Source: UniProtKB-KW
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 – 3232Sequence AnalysisAdd
BLAST
Chaini33 – 640608Envelope glycoproteinPRO_0000239598Add
BLAST
Chaini33 – 443411Surface proteinBy similarityPRO_0000040792Add
BLAST
Chaini444 – 623180Transmembrane proteinBy similarityPRO_0000040793Add
BLAST
Peptidei624 – 64017R-peptideBy similarityPRO_0000040794Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi58 – 581N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi113 ↔ 130By similarity
Disulfide bondi122 ↔ 135By similarity
Glycosylationi300 – 3001N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi310 ↔ 537Interchain (between SU and TM chains, or C-310 with C-535); in linked formBy similarity
Disulfide bondi310 ↔ 313By similarity
Glycosylationi332 – 3321N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi339 – 3391N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi372 – 3721N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi408 – 4081N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi529 ↔ 536By similarity
Lipidationi604 – 6041S-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

ProteinModelPortaliP06445.
SMRiP06445. Positions 38-233, 489-541.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 584552ExtracellularSequence AnalysisAdd
BLAST
Topological domaini606 – 64035CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei585 – 60521HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 236205Receptor-binding domain (RBD)Sequence AnalysisAdd
BLAST
Regioni446 – 46621Fusion peptideBy similarityAdd
BLAST
Regioni512 – 52817ImmunosuppressionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili477 – 51135Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi310 – 3134CXXC
Motifi529 – 5379CX6CC
Motifi629 – 6324YXXL motif; contains endocytosis signalBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi233 – 28250Pro-richAdd
BLAST

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
The YXXL motif is involved in determining the exact site of viral release at the surface of infected mononuclear cells and promotes endocytosis.

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.

P06445-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MACSTFSKPL KDKINPWGPL IILGILIRAG VSVQHDSPHK VFNVTWRVTN
60 70 80 90 100
LMTGQTANAT SLLGTMTDAF PKLYFDLCDL VGDYWDDPEP DIGDGCRTPG
110 120 130 140 150
GRRRTRLYDF YVCPGHTVPI GCGGPGEGYC GKWGCETTGQ AYWKPSSSWD
160 170 180 190 200
LISLKRGNTP KDQGPCYDSS VSSDIKGATP GGRCNPLVLE FTDAGKKASW
210 220 230 240 250
DGPKVWGLRL YRSTGTDPVT RFSLTRRVLN IGPRVPIGPN PVIIDQLPPS
260 270 280 290 300
RPVQIMLPRP PQPPPPGAAS IVPETAPPSQ QPGTGDRLLN LVDGAYQALN
310 320 330 340 350
LTSPDKTQEC WLCLVAEPPY YEGVAVLGTY SNHTSAPTNC SVASQHKLTL
360 370 380 390 400
SEVTGQGLCI GTVPKTHQAL CNTTLKTNKG SYYLVAPAGT TWACNTGLTP
410 420 430 440 450
CLSATVLNRT TDYCVLVELW PRVTYHPPSY VYSQFEKSYR HKREPVSLTL
460 470 480 490 500
ALLLGGLTMG GIAAGVGTGT TALVATQQFQ QLHAAVQDDL KEVEKSITNL
510 520 530 540 550
EKSLTSLSEV VLQNRRGLDL LFLKEGGLCA ALKEECCFYA DHTGLVRDSM
560 570 580 590 600
AKLRERLTQR QKLFESSQGW FEGLFNRSPW FTTLISTIMG PLIILLLILL
610 620 630 640
FGPCILNRLV QFVKDRISVV QALVLTQQYH QLKPLEYEPQ
Length:640
Mass (Da):70,072
Last modified:January 1, 1988 - v1
Checksum:i1E4450343643D799
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M10100 Genomic RNA. Translation: AAA46528.1.
PIRiA03990. VCMVRV.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M10100 Genomic RNA. Translation: AAA46528.1 .
PIRi A03990. VCMVRV.

3D structure databases

ProteinModelPortali P06445.
SMRi P06445. Positions 38-233, 489-541.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.90.310.10. 1 hit.
InterProi IPR008981. FMuLV_rcpt-bd.
IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view ]
PANTHERi PTHR10424. PTHR10424. 1 hit.
Pfami PF00429. TLV_coat. 1 hit.
[Graphical view ]
SUPFAMi SSF49830. SSF49830. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Envelope gene and long terminal repeat determine the different biological properties of Rauscher, Friend, and Moloney mink cell focus-inducing viruses."
    Vogt M., Haggblom C., Swift S., Haas M.
    J. Virol. 55:184-192(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiENV_RMCFV
AccessioniPrimary (citable) accession number: P06445
Secondary accession number(s): Q85628, Q85629, Q89529
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: October 29, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program