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Q9TTC0

- ENV_KORV

UniProt

Q9TTC0 - ENV_KORV

Protein

Envelope glycoprotein

Gene

env

Organism
Koala retrovirus (KoRV)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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
    Sitei463 – 4642Cleavage; by hostBy similarity
    Sitei643 – 6442Cleavage; by viral proteaseBy 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

    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
    OrganismiKoala retrovirus (KoRV)
    Taxonomic identifieri394239 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusunclassified Gammaretrovirus
    Virus hostiPhascolarctos cinereus (Koala) [TaxID: 38626]
    ProteomesiUP000007765: 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 extravirion 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-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

    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 – 3535Sequence AnalysisAdd
    BLAST
    Chaini36 – 659624Envelope glycoproteinPRO_0000249423Add
    BLAST
    Chaini36 – 463428Surface proteinBy similarityPRO_0000249424Add
    BLAST
    Chaini464 – 659196Transmembrane proteinBy similarityPRO_0000249425Add
    BLAST
    Peptidei645 – 65915R-peptideBy similarityPRO_0000249426Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi141 ↔ 162By similarity
    Disulfide bondi154 ↔ 167By similarity
    Glycosylationi318 – 3181N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi328 ↔ 558Interchain (between SU and TM chains, or C-357 with C-584); in linked formBy similarity
    Disulfide bondi328 ↔ 331By similarity
    Glycosylationi389 – 3891N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi395 – 3951N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi407 – 4071N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi427 – 4271N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi550 ↔ 557By similarity
    Lipidationi625 – 6251S-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

    ProteinModelPortaliQ9TTC0.
    SMRiQ9TTC0. Positions 510-562.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini36 – 606571ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini628 – 65932CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei607 – 62721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni466 – 48621Fusion peptideBy similarityAdd
    BLAST
    Regioni533 – 54917ImmunosuppressionBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili506 – 53227Sequence AnalysisAdd
    BLAST
    Coiled coili567 – 58721Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi328 – 3314CXXCBy similarity
    Motifi550 – 5589CX6CCBy similarity
    Motifi650 – 6534YXXL motif; contains endocytosis signalBy similarity

    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.

    Q9TTC0-1 [UniParc]FASTAAdd to Basket

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    MLLISNPRHL GHPMSPGNWK RLIILLSCVF GGAEMNQQHN NPHQPMTLTW    50
    QVLSQTGSVV WEKKAVEPPW TWWPSLEPDV CALVAGLESW DIPELTASAS 100
    QQARPPDSNY EHAYNQITWG TLGCSYPRAR TRIARSQFYV CPRDGRSLSE 150
    ARRCGGLESL YCKEWGCETA GTAYWQPRSS WDLITVGQGH PTGTCERTGW 200
    CNPLKIEFTE PGKRFRNWLQ GRTWGLRFYV TGHPGVQLTI RLVITSPPPV 250
    VVGPDPVLAE QGPPRKIPFL PRVPVPTLSP PASPIPTVQA SPPAPSTPSP 300
    TTGDRLFGLV QGAFLALNAT NPEATESCWL CLALGPPYYE GIATPGQVTY 350
    ASTDSQCRWG GKGKLTLTEV SGLGLCIGKV PPTHQHLCNL TIPLNASHTH 400
    KYLLPSNRSW WACNSGLTPC LSTSVFNQSN DFCIQIQLVP RIYYHPDGTL 450
    LQAYESPHSR NKREPVSLTL AVLLGLGVAA GIGTGSTALI KGPIDLQQGL 500
    TSLQIAMDTD LRALQDSISK LEDSLTSLSE VVLQNRRGLD LLFLKEGGLC 550
    AALKEECCFY VDHSGAVRDS MRRLKERLDK RQLEHQKNLS WYEGWFNRSP 600
    WLTTLLSALA GPLLLLLLLL TLGPCVINKL VQFINDRVSA VRILVLRHKY 650
    QTLDNEDNL 659
    Length:659
    Mass (Da):72,860
    Last modified:May 1, 2000 - v1
    Checksum:i68B2220DAA6A2ABA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF151794 Genomic DNA. Translation: AAF15099.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF151794 Genomic DNA. Translation: AAF15099.1 .

    3D structure databases

    ProteinModelPortali Q9TTC0.
    SMRi Q9TTC0. Positions 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. "The nucleotide sequence of koala (Phascolarctos cinereus) retrovirus: a novel type C endogenous virus related to Gibbon ape leukemia virus."
      Hanger J.J., Bromham L.D., McKee J.J., O'Brien T.M., Robinson W.F.
      J. Virol. 74:4264-4272(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiENV_KORV
    AccessioniPrimary (citable) accession number: Q9TTC0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Koala retrovirus is both a circulating virus and an endogenous retrovirus of koala, except in some isolated populations in south Australia.

    Keywords - Technical termi

    Complete proteome

    External Data

    Dasty 3