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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.
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
Sitei444 – 4452Cleavage; by host By similarity
Sitei624 – 6252Cleavage; by viral protease p14 By similarity

GO - Molecular functioni

  1. structural molecule activity Source: InterPro
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 585552Extracellular Reviewed prediction
Add
BLAST
Transmembranei586 – 60621Helical; Reviewed prediction
Add
BLAST
Topological domaini607 – 64034Cytoplasmic Reviewed prediction
Add
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 – 3333 Reviewed prediction
Add
BLAST
Chaini34 – 645612Envelope glycoprotein By similarity
PRO_0000390831Add
BLAST
Chaini34 – 444411Surface protein By similarity
PRO_0000390832Add
BLAST
Chaini445 – 645201Transmembrane protein By similarity
PRO_0000390833Add
BLAST
Peptidei625 – 64521R-peptide By similarity
PRO_0000390834Add
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
Glycosylationi301 – 3011N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi311 ↔ 538Interchain (between SU and TM chains, or C-314 with C-538); in linked form By similarity
Disulfide bondi311 ↔ 314 By similarity
Glycosylationi333 – 3331N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi340 – 3401N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi341 ↔ 395 By similarity
Disulfide bondi360 ↔ 372 By similarity
Glycosylationi373 – 3731N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi402 ↔ 415 By similarity
Glycosylationi409 – 4091N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi530 ↔ 537 By similarity
Lipidationi605 – 6051S-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.

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.

Structurei

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 237206Receptor-binding domain (RBD) Reviewed prediction
Add
BLAST
Regioni447 – 46721Fusion peptide By similarity
Add
BLAST
Regioni513 – 52917Immunosuppression By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili490 – 51021 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi311 – 3144CXXC By similarity
Motifi530 – 5389CX6CC By similarity
Motifi630 – 6334YXXL motif; contains endocytosis signal By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi234 – 28350Pro-rich
Add
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 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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MESPAFSKPL KDKINPWGPL IIMGILVRAG ASVQRDSPHQ VFNVTWKITN    50
LMTGQTANAT SLLGTMTDTF PKLYFDLCDL VGDNWDDPEP DIGDGCRSPG 100
GRKRTRLYDF YVCPGHTVLT GCGGPREGYC GKWGCETTGQ AYWKPSSSWD 150
LISLKRGNTP KGQGPCFDSS VGSGSIQGAT PGGRCNPLVL EFTDAGKRAS 200
WDAPKTWGLR LYRSTGADPV TLFSLTRQVL NVGPRVPIGP NPVITEQLPP 250
SQPVQIMLPR TPRPPPSGAA SMVPGAPPPS QQPGTGDRLL NLVEGAYLAL 300
NLTSPDKTQE CWLCLVSGPP YYEGVAVLGT YSNHTSAPAN CSVTSQHKLT 350
LSEVTGQGLC IGAVPKTHQA LCNTTQKTSD GSYYLASPAG TIWACSTGLT 400
PCLSTTVLNL TTDYCVLVEL WPKVTYHSPN YVYGQFEKKT KYKREPVSLT 450
LALLLGGLTM GGIAAGVGTG TTALVATKQF EQLQAAIHTD LGALEKSVSA 500
LEKSLTSLSE VVLQNRRGLD LLFLKEGGLC AALKEECCFY ADHTGVVRDS 550
MAKLRERLNQ RQKLFESGQG WFEGLFNRSP WFTTLISTIM GPLIVLLLIL 600
LFGPCILNRL VQFVKDRISV VQALVLTQQY HQLKSIDPEE VESRE 645
Length:645
Mass (Da):69,876
Last modified:April 4, 2006 - v1
Checksum:i19ACC5E3EAF9AEC3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti261 – 2611T → P in ABM47429. 1 Publication
Sequence conflicti298 – 2981L → Q in ABM47429. 1 Publication
Sequence conflicti568 – 5681G → R in ABM47429. 1 Publication

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...

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: September 3, 2014
This is version 41 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

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