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P31794

- ENV_MLVRK

UniProt

P31794 - ENV_MLVRK

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Protein

Envelope glycoprotein

Gene
env
Organism
Radiation murine leukemia virus (strain Kaplan)
Status
Reviewed - 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.
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
Metal bindingi117 – 1171Zinc By similarity
Sitei467 – 4682Cleavage; by host By similarity
Sitei644 – 6452Cleavage; by viral protease p14 By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. 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

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 76
Short name:
gp76
Transmembrane protein
Short name:
TM
Alternative name(s):
Envelope protein p15E
Alternative name(s):
p2E
Gene namesi
Name:env
OrganismiRadiation murine leukemia virus (strain Kaplan)
Taxonomic identifieri31689 [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 domaini32 – 605574Extracellular Reviewed predictionAdd
BLAST
Transmembranei606 – 62621Helical; Reviewed predictionAdd
BLAST
Topological domaini627 – 66539Cytoplasmic 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 – 3131 Reviewed predictionAdd
BLAST
Chaini32 – 665634Envelope glycoproteinPRO_0000239589Add
BLAST
Chaini32 – 467436Surface protein By similarityPRO_0000040768Add
BLAST
Chaini468 – 644177Transmembrane protein By similarityPRO_0000040769Add
BLAST
Peptidei645 – 66521R-peptide By similarityPRO_0000040770Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...); by host By similarity
Disulfide bondi77 ↔ 129 By similarity
Disulfide bondi103 ↔ 118 By similarity
Disulfide bondi104 ↔ 114 By similarity
Disulfide bondi152 ↔ 172 By similarity
Disulfide bondi164 ↔ 177 By similarity
Glycosylationi199 – 1991N-linked (GlcNAc...); by host By similarity
Disulfide bondi209 ↔ 215 By similarity
Glycosylationi211 – 2111N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi324 – 3241N-linked (GlcNAc...); by host By similarity
Disulfide bondi334 ↔ 558Interchain (between SU and TM chains, or C-337 with C-558); in linked form
Disulfide bondi334 ↔ 337
Glycosylationi356 – 3561N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi363 – 3631N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi364 ↔ 418 By similarity
Disulfide bondi383 ↔ 395 By similarity
Glycosylationi396 – 3961N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi400 – 4001N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi425 ↔ 438 By similarity
Glycosylationi432 – 4321N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi550 ↔ 557 By similarity
Lipidationi625 – 6251S-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

ProteinModelPortaliP31794.
SMRiP31794. Positions 40-266, 510-562.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 267236Receptor-binding domain (RBD) Reviewed predictionAdd
BLAST
Regioni470 – 49021Fusion peptide By similarityAdd
BLAST
Regioni533 – 54917Immunosuppression By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili505 – 53228 Reviewed predictionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi334 – 3374CXXC
Motifi550 – 5589CX6CC
Motifi650 – 6534YXXL motif; contains endocytosis signal By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi264 – 30542Pro-richAdd
BLAST

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.

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.

P31794-1 [UniParc]FASTAAdd to Basket

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MESTTLSKPF KNQVNPWGPL IVLLILGRVN PVALGNSPHQ VFNLSWEVTN    50
EDRETVWAIT GNHPLWTWWP DLTPDLCMLA LHGPSYWGLE YQAPFSPPPG 100
PPCCSRSSGS TPGCSRDCEE PLTSYTPRCN TAWNRLKLSK VTHAHNEGFY 150
VCPGPHRPRW ARSCGGPESF YCASWGCETT GRASWKPSSS WDYITVSNNL 200
TSGQATPVCK NNTWCNSLTI RFTSLGKQAT SWVTGHWWGL RLYVSGHDPG 250
LIFGIRLKIT DSGPRVPIGP NPVLSDQRPP SQPRSPPHSN STPTETPLTL 300
PEPPPAGVEN RLLNLVKGAY QALNLTSPDR TQECWLCLVS GPPYYEGVAV 350
LGTYSNHTSA PANCSVASQH KLTLSEVTGR GLCVGAVPKT HQALCNTTQN 400
TSGGSYYLAA PAGTIWACNT GLTPCLSTTV LNLTTDYCVL VELWPRVTYH 450
SPSYVYHQFE GRAKYKREPV SLTLALLLGG LTMGGIAAGV GTGTTALVAT 500
QQLQAAVHDD LKEVEKSITN LEKSLTSLSE VVLQNRRGLD LLFLKEGGLC 550
AALKEECCFY ADHTGVVRDS MAKLRERLNQ RQKLFESGQG WFERLFNGSP 600
WFTTLISTIM GPLIVLLLIL LLGPCILNRL VQFVKDRISV VQALVLTQQY 650
HQLKSIDPEE MESRE 665
Length:665
Mass (Da):73,085
Last modified:July 1, 1993 - v1
Checksum:iFA15AB6B0C63F0AA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M93052 Genomic DNA. Translation: AAA46526.1.
PIRiB42743. VCMVKA.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M93052 Genomic DNA. Translation: AAA46526.1 .
PIRi B42743. VCMVKA.

3D structure databases

ProteinModelPortali P31794.
SMRi P31794. Positions 40-266, 510-562.
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. "Determinants of thymotropism in Kaplan radiation leukemia virus and nucleotide sequence of its envelope region."
    Poliquin L., Bergeron D., Fortier J.L., Paquette Y., Bergeron R., Rassart E.
    J. Virol. 66:5141-5146(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiENV_MLVRK
AccessioniPrimary (citable) accession number: P31794
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: September 3, 2014
This is version 89 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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