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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.
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei443 – 4442Cleavage; by host By similarity
Sitei623 – 6242Cleavage; by viral protease p14 By 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; 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.
R-peptide : Host cell membrane; 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 domaini33 – 584552Extracellular Reviewed predictionAdd
BLAST
Transmembranei585 – 60521Helical; Reviewed predictionAdd
BLAST
Topological domaini606 – 64035Cytoplasmic Reviewed predictionAdd
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 – 3232 Reviewed predictionAdd
BLAST
Chaini33 – 640608Envelope glycoproteinPRO_0000239598Add
BLAST
Chaini33 – 443411Surface protein By similarityPRO_0000040792Add
BLAST
Chaini444 – 623180Transmembrane protein By similarityPRO_0000040793Add
BLAST
Peptidei624 – 64017R-peptide By similarityPRO_0000040794Add
BLAST

Amino acid modifications

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

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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 236205Receptor-binding domain (RBD) Reviewed predictionAdd
BLAST
Regioni446 – 46621Fusion peptide By similarityAdd
BLAST
Regioni512 – 52817Immunosuppression By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili477 – 51135 Reviewed predictionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi310 – 3134CXXC
Motifi529 – 5379CX6CC
Motifi629 – 6324YXXL motif; contains endocytosis signal By 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.
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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MACSTFSKPL KDKINPWGPL IILGILIRAG VSVQHDSPHK VFNVTWRVTN    50
LMTGQTANAT SLLGTMTDAF PKLYFDLCDL VGDYWDDPEP DIGDGCRTPG 100
GRRRTRLYDF YVCPGHTVPI GCGGPGEGYC GKWGCETTGQ AYWKPSSSWD 150
LISLKRGNTP KDQGPCYDSS VSSDIKGATP GGRCNPLVLE FTDAGKKASW 200
DGPKVWGLRL YRSTGTDPVT RFSLTRRVLN IGPRVPIGPN PVIIDQLPPS 250
RPVQIMLPRP PQPPPPGAAS IVPETAPPSQ QPGTGDRLLN LVDGAYQALN 300
LTSPDKTQEC WLCLVAEPPY YEGVAVLGTY SNHTSAPTNC SVASQHKLTL 350
SEVTGQGLCI GTVPKTHQAL CNTTLKTNKG SYYLVAPAGT TWACNTGLTP 400
CLSATVLNRT TDYCVLVELW PRVTYHPPSY VYSQFEKSYR HKREPVSLTL 450
ALLLGGLTMG GIAAGVGTGT TALVATQQFQ QLHAAVQDDL KEVEKSITNL 500
EKSLTSLSEV VLQNRRGLDL LFLKEGGLCA ALKEECCFYA DHTGLVRDSM 550
AKLRERLTQR QKLFESSQGW FEGLFNRSPW FTTLISTIMG PLIILLLILL 600
FGPCILNRLV QFVKDRISVV QALVLTQQYH QLKPLEYEPQ 640
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: September 3, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

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