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Q27ID8

- ENV_XMRV6

UniProt

Q27ID8 - ENV_XMRV6

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Protein

Envelope glycoprotein

Gene

env

Organism
Xenotropic MuLV-related virus (isolate VP62) (XMRV)
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 activates a thiol in a CXXC motif of the C-terminal domain, where the other Cys residue participates in the formation of the intersubunit disulfide. The activated thiol will attack the disulfide and cause its isomerization into a disulfide isomer within the motif. This leads to SU displacement and TM refolding, 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
Sitei444 – 4452Cleavage; by hostBy similarity
Sitei624 – 6252Cleavage; 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:
Gene namesi
Name:env
OrganismiXenotropic MuLV-related virus (isolate VP62) (XMRV)
Taxonomic identifieri373193 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusunclassified Gammaretrovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000002240: Genome

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; Peripheral membrane protein
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 – 3333Sequence AnalysisAdd
BLAST
Chaini34 – 645612Envelope glycoproteinBy similarityPRO_0000390831Add
BLAST
Chaini34 – 444411Surface proteinBy similarityPRO_0000390832Add
BLAST
Chaini445 – 645201Transmembrane proteinBy similarityPRO_0000390833Add
BLAST
Peptidei625 – 64521R-peptideBy similarityPRO_0000390834Add
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
Glycosylationi301 – 3011N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi311 ↔ 538Interchain (between SU and TM chains, or C-314 with C-538); in linked formBy similarity
Disulfide bondi311 ↔ 314By similarity
Glycosylationi333 – 3331N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi340 – 3401N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi341 ↔ 395By similarity
Disulfide bondi360 ↔ 372By similarity
Glycosylationi373 – 3731N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi402 ↔ 415By similarity
Glycosylationi409 – 4091N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi530 ↔ 537By similarity
Lipidationi605 – 6051S-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.

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. The activated Env consists of SU monomers and TM trimers (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ27ID8.
SMRiQ27ID8. Positions 38-234, 490-542.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 585552ExtracellularSequence AnalysisAdd
BLAST
Topological domaini607 – 64034CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei586 – 60621HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 237206Receptor-binding domain (RBD)Sequence AnalysisAdd
BLAST
Regioni447 – 46721Fusion peptideBy similarityAdd
BLAST
Regioni513 – 52917ImmunosuppressionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili490 – 51021Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi311 – 3144CXXCBy similarity
Motifi530 – 5389CX6CCBy similarity
Motifi630 – 6334YXXL motif; contains endocytosis signalBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi234 – 28350Pro-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.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.

Q27ID8-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MESPAFSKPL KDKINPWGPL IIMGILVRAG ASVQRDSPHQ VFNVTWKITN
60 70 80 90 100
LMTGQTANAT SLLGTMTDTF PKLYFDLCDL VGDNWDDPEP DIGDGCRSPG
110 120 130 140 150
GRKRTRLYDF YVCPGHTVLT GCGGPREGYC GKWGCETTGQ AYWKPSSSWD
160 170 180 190 200
LISLKRGNTP KGQGPCFDSS VGSGSIQGAT PGGRCNPLVL EFTDAGKRAS
210 220 230 240 250
WDAPKTWGLR LYRSTGADPV TLFSLTRQVL NVGPRVPIGP NPVITEQLPP
260 270 280 290 300
SQPVQIMLPR TPRPPPSGAA SMVPGAPPPS QQPGTGDRLL NLVEGAYLAL
310 320 330 340 350
NLTSPDKTQE CWLCLVSGPP YYEGVAVLGT YSNHTSAPAN CSVTSQHKLT
360 370 380 390 400
LSEVTGQGLC IGAVPKTHQA LCNTTQKTSD GSYYLASPAG TIWACSTGLT
410 420 430 440 450
PCLSTTVLNL TTDYCVLVEL WPKVTYHSPN YVYGQFEKKT KYKREPVSLT
460 470 480 490 500
LALLLGGLTM GGIAAGVGTG TTALVATKQF EQLQAAIHTD LGALEKSVSA
510 520 530 540 550
LEKSLTSLSE VVLQNRRGLD LLFLKEGGLC AALKEECCFY ADHTGVVRDS
560 570 580 590 600
MAKLRERLNQ RQKLFESGQG WFEGLFNRSP WFTTLISTIM GPLIVLLLIL
610 620 630 640
LFGPCILNRL VQFVKDRISV VQALVLTQQY HQLKSIDPEE VESRE
Length:645
Mass (Da):69,876
Last modified:April 4, 2006 - v1
Checksum:i19ACC5E3EAF9AEC3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti261 – 2611T → P in ABM47429. (PubMed:16609730)Curated
Sequence conflicti298 – 2981L → Q in ABM47429. (PubMed:16609730)Curated
Sequence conflicti568 – 5681G → R in ABM47429. (PubMed:16609730)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ399707 Genomic RNA. Translation: ABD49688.1.
EF185282 Genomic RNA. Translation: ABM47429.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ399707 Genomic RNA. Translation: ABD49688.1 .
EF185282 Genomic RNA. Translation: ABM47429.1 .

3D structure databases

ProteinModelPortali Q27ID8.
SMRi Q27ID8. Positions 38-234, 490-542.
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. "Identification of a novel Gammaretrovirus in prostate tumors of patients homozygous for R462Q RNASEL variant."
    Urisman A., Molinaro R.J., Fischer N., Plummer S.J., Casey G., Klein E.A., Malathi K., Magi-Galluzzi C., Tubbs R.R., Ganem D., Silverman R.H., DeRisi J.L.
    PLoS Pathog. 2:E25-E25(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "An infectious retrovirus susceptible to an IFN antiviral pathway from human prostate tumors."
    Dong B., Kim S., Hong S., Das Gupta J., Malathi K., Klein E.A., Ganem D., Derisi J.L., Chow S.A., Silverman R.H.
    Proc. Natl. Acad. Sci. U.S.A. 104:1655-1660(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiENV_XMRV6
AccessioniPrimary (citable) accession number: Q27ID8
Secondary accession number(s): A1Z653
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: April 4, 2006
Last modified: October 29, 2014
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

External Data

Dasty 3