ENV_KORV
ID ENV_KORV Reviewed; 659 AA.
AC Q9TTC0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 70;
DE Short=gp70;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Envelope protein p15E;
DE Contains:
DE RecName: Full=R-peptide;
DE AltName: Full=p2E;
DE Flags: Precursor;
GN Name=env;
OS Koala retrovirus (KoRV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=394239;
OH NCBI_TaxID=38626; Phascolarctos cinereus (Koala).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10756041; DOI=10.1128/jvi.74.9.4264-4272.2000;
RA Hanger J.J., Bromham L.D., McKee J.J., O'Brien T.M., Robinson W.F.;
RT "The nucleotide sequence of koala (Phascolarctos cinereus) retrovirus: a
RT novel type C endogenous virus related to Gibbon ape leukemia virus.";
RL J. Virol. 74:4264-4272(2000).
CC -!- FUNCTION: The surface protein (SU) attaches the virus to the host cell
CC by binding to its receptor. This interaction triggers the refolding of
CC the transmembrane protein (TM) and is thought to activate its fusogenic
CC potential by unmasking its fusion peptide. Fusion occurs at the host
CC cell plasma membrane (By similarity). {ECO:0000250}.
CC -!- FUNCTION: The transmembrane protein (TM) acts as a class I viral fusion
CC protein. Under the current model, the protein has at least 3
CC conformational states: pre-fusion native state, pre-hairpin
CC intermediate state, and post-fusion hairpin state. During viral and
CC target cell membrane fusion, the coiled coil regions (heptad repeats)
CC assume a trimer-of-hairpins structure, positioning the fusion peptide
CC in close proximity to the C-terminal region of the ectodomain. The
CC formation of this structure appears to drive apposition and subsequent
CC fusion of viral and target cell membranes. Membranes fusion leads to
CC delivery of the nucleocapsid into the cytoplasm (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of SU-
CC TM heterodimers attached by a labile interchain disulfide bond.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host
CC cell membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral
CC membrane protein. Host cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Note=The surface protein is not anchored to the
CC viral envelope, but associates with the extravirion surface through its
CC binding to TM. Both proteins are thought to be concentrated at the site
CC of budding and incorporated into the virions possibly by contacts
CC between the cytoplasmic tail of Env and the N-terminus of Gag (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [R-peptide]: Host cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=The R-peptide is
CC membrane-associated through its palmitate. {ECO:0000250}.
CC -!- DOMAIN: The 17 amino acids long immunosuppressive region is present in
CC many retroviral envelope proteins. Synthetic peptides derived from this
CC relatively conserved sequence inhibit immune function in vitro and in
CC vivo (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The YXXL motif is involved in determining the exact site of
CC viral release at the surface of infected mononuclear cells and promotes
CC endocytosis. {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC Envelope glycoproteins are synthesized as an inactive precursor that is
CC N-glycosylated and processed likely by host cell furin or by a furin-
CC like protease in the Golgi to yield the mature SU and TM proteins. The
CC cleavage site between SU and TM requires the minimal sequence [KR]-X-
CC [KR]-R. The R-peptide is released from the C-terminus of the
CC cytoplasmic tail of the TM protein upon particle formation as a result
CC of proteolytic cleavage by the viral protease. Cleavage of this peptide
CC is required for TM to become fusogenic (By similarity). {ECO:0000250}.
CC -!- PTM: The CXXC motif is highly conserved across a broad range of
CC retroviral envelope proteins. It is thought to participate in the
CC formation of a labile disulfide bond possibly with the CX6CC motif
CC present in the transmembrane protein. Isomerization of the intersubunit
CC disulfide bond to an SU intrachain disulfide bond is thought to occur
CC upon receptor recognition in order to allow membrane fusion (By
CC similarity). {ECO:0000250}.
CC -!- PTM: The transmembrane protein is palmitoylated. {ECO:0000250}.
CC -!- PTM: The R-peptide is palmitoylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: Koala retrovirus is both a circulating virus and an
CC endogenous retrovirus of koala, except in some isolated populations in
CC south Australia.
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DR EMBL; AF151794; AAF15099.1; -; Genomic_DNA.
DR SMR; Q9TTC0; -.
DR Proteomes; UP000007765; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 3.90.310.10; -; 1.
DR InterPro; IPR008981; FMuLV_rcpt-bd.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF00429; TLV_coat; 1.
DR SUPFAM; SSF49830; SSF49830; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
KW Fusion of virus membrane with host cell membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW Membrane; Palmitate; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..659
FT /note="Envelope glycoprotein"
FT /id="PRO_0000249423"
FT CHAIN 36..463
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000249424"
FT CHAIN 464..659
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000249425"
FT PEPTIDE 645..659
FT /note="R-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000249426"
FT TOPO_DOM 36..606
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 607..627
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 628..659
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 278..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..486
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT REGION 533..549
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 506..532
FT /evidence="ECO:0000255"
FT COILED 567..587
FT /evidence="ECO:0000255"
FT MOTIF 328..331
FT /note="CXXC"
FT /evidence="ECO:0000250"
FT MOTIF 550..558
FT /note="CX6CC"
FT /evidence="ECO:0000250"
FT MOTIF 650..653
FT /note="YXXL motif; contains endocytosis signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 278..299
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 463..464
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 643..644
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT LIPID 625
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 141..162
FT /evidence="ECO:0000250"
FT DISULFID 154..167
FT /evidence="ECO:0000250"
FT DISULFID 328..558
FT /note="Interchain (between SU and TM chains, or C-357 with
FT C-584); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 328..331
FT /evidence="ECO:0000250"
FT DISULFID 550..557
FT /evidence="ECO:0000250"
SQ SEQUENCE 659 AA; 72860 MW; 68B2220DAA6A2ABA CRC64;
MLLISNPRHL GHPMSPGNWK RLIILLSCVF GGAEMNQQHN NPHQPMTLTW QVLSQTGSVV
WEKKAVEPPW TWWPSLEPDV CALVAGLESW DIPELTASAS QQARPPDSNY EHAYNQITWG
TLGCSYPRAR TRIARSQFYV CPRDGRSLSE ARRCGGLESL YCKEWGCETA GTAYWQPRSS
WDLITVGQGH PTGTCERTGW CNPLKIEFTE PGKRFRNWLQ GRTWGLRFYV TGHPGVQLTI
RLVITSPPPV VVGPDPVLAE QGPPRKIPFL PRVPVPTLSP PASPIPTVQA SPPAPSTPSP
TTGDRLFGLV QGAFLALNAT NPEATESCWL CLALGPPYYE GIATPGQVTY ASTDSQCRWG
GKGKLTLTEV SGLGLCIGKV PPTHQHLCNL TIPLNASHTH KYLLPSNRSW WACNSGLTPC
LSTSVFNQSN DFCIQIQLVP RIYYHPDGTL LQAYESPHSR NKREPVSLTL AVLLGLGVAA
GIGTGSTALI KGPIDLQQGL TSLQIAMDTD LRALQDSISK LEDSLTSLSE VVLQNRRGLD
LLFLKEGGLC AALKEECCFY VDHSGAVRDS MRRLKERLDK RQLEHQKNLS WYEGWFNRSP
WLTTLLSALA GPLLLLLLLL TLGPCVINKL VQFINDRVSA VRILVLRHKY QTLDNEDNL
