ENV_SFV3L
ID ENV_SFV3L Reviewed; 982 AA.
AC P27399;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Envelope glycoprotein gp130;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Leader peptide;
DE Short=LP;
DE AltName: Full=Env leader protein;
DE Short=Elp;
DE AltName: Full=gp18LP;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 80;
DE Short=gp80;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Glycoprotein 48;
DE Short=gp48;
GN Name=env;
OS Simian foamy virus type 3 (strain LK3) (SFVagm) (SFV-3).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Spumaretrovirinae; Spumavirus.
OX NCBI_TaxID=11644;
OH NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1310187; DOI=10.1016/0042-6822(92)90026-l;
RA Renne R., Friedl E., Schweizer M., Fleps U., Turek R., Neumann-Haefelin D.;
RT "Genomic organization and expression of simian foamy virus type 3 (SFV-
RT 3).";
RL Virology 186:597-608(1992).
CC -!- FUNCTION: The surface protein (SU) attaches the virus to the host cell
CC by binding to the cell receptor. This interaction triggers the
CC refolding of TM and is thought to activate its fusogenic potential by
CC unmasking its fusion peptide (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 -!- FUNCTION: The leader peptide is a component of released, infectious
CC virions and is required for particle budding. {ECO:0000250}.
CC -!- SUBUNIT: The mature envelope protein consists of a trimer of SU-TM
CC heterodimers. The N-terminus of leader peptide specifically interacts
CC with Gag protein. This specific interaction between Gag protein and Env
CC glycoprotein may allow particle egress (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Envelope glycoprotein gp130]: Host endoplasmic
CC reticulum membrane. Note=The polyprotein has a highly unusual
CC biosynthesis for a retroviral glycoprotein. It is translated as a full-
CC length precursor protein into the rough endoplasmic reticulum and
CC initially has a type III protein configuration with both its N and C-
CC termini located intracytoplasmically (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Leader peptide]: Virion membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}. Host endoplasmic
CC reticulum membrane {ECO:0000250}; Single-pass type II membrane protein
CC {ECO:0000250}. Note=Its N-terminus is located inside the viral
CC particle. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host
CC endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Virion membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Host endoplasmic reticulum
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=The surface protein is not anchored to the viral envelope, but
CC associates with the extravirion surface through its binding to TM.
CC {ECO:0000250}.
CC -!- DOMAIN: The ER retention signal plays an important role in establishing
CC the intracellular site of budding. {ECO:0000250}.
CC -!- PTM: Envelope glycoproteins are synthesized as an inactive precursor
CC that is processed by host furin or a furin-like protease to yield a
CC functional hetero-oligomeric complex. {ECO:0000250}.
CC -!- PTM: The transmembrane protein and the surface protein are N-
CC glycosylated. {ECO:0000250}.
CC -!- PTM: Mono- and polyubiquitinated leader peptide are found in viral
CC particles. Ubiquitination may be involved in regulating the balance
CC between viral and subviral particles release (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Foamy viruses are distinct from other retroviruses in
CC many respects. Their protease is active as an uncleaved Pro-Pol
CC protein. Mature particles do not include the usual processed retroviral
CC structural protein (MA, CA and NC), but instead contain two large Gag
CC proteins. Their functional nucleic acid appears to be either RNA or
CC dsDNA (up to 20% of extracellular particles), because they probably
CC proceed either to an early (before integration) or late reverse
CC transcription (after assembly). Foamy viruses have the ability to
CC retrotranspose intracellularly with high efficiency. They bud
CC predominantly into the endoplasmic reticulum (ER) and occasionally at
CC the plasma membrane. Budding requires the presence of Env proteins.
CC Most viral particles probably remain within the infected cell.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA47798.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M74895; AAA47798.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_001956723.2; NC_010820.1.
DR GeneID; 6386653; -.
DR KEGG; vg:6386653; -.
DR Proteomes; UP000007217; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum 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 InterPro; IPR005070; Foamy_env.
DR Pfam; PF03408; Foamy_virus_ENV; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues; Glycoprotein;
KW Host endoplasmic reticulum; Host membrane; Isopeptide bond; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Ubl conjugation; Viral envelope protein; Virion.
FT CHAIN 1..982
FT /note="Envelope glycoprotein gp130"
FT /id="PRO_0000125470"
FT CHAIN 1..126
FT /note="Leader peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000245434"
FT CHAIN 127..566
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000245435"
FT CHAIN 567..982
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000245436"
FT TOPO_DOM 1..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..88
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..954
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 955..975
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 976..982
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..15
FT /note="Involved in virion budding"
FT /evidence="ECO:0000255"
FT REGION 570..592
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT MOTIF 978..980
FT /note="Endoplasmic reticulum retention signal"
FT /evidence="ECO:0000250"
FT SITE 126..127
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 566..567
FT /note="Cleavage; by host"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 802
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 827
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 982 AA; 113314 MW; 721F2F8929D604FF CRC64;
MAPPMNLQQW LLWKKMNETH LALENISSLT EEQKQQVIIE IQQEEVIPTR MDRVKYLAYA
CCATSTRVMC WLFLICVLLI IVFVSCFVTV ARIQWNRDIN VFGPVIDWNV THQATYQQLK
AARLTRSLKV EHPHISYISI NMSSIPQGVM YTPHPEPIIL KERVLGISQV LMINSENIAN
VANLSQETKV LLTDMINEEL QDLSNQMIDF ELPLGDPRDQ DQYIHHKCYQ EFAHCYLVKY
KKPSPWISEG IIVDQCPLPR IHDPNYYKYQ PIWDYYLKIQ NIRPQGWTSK SYYGTARMGS
FYIPTFLRNN TVSHVLFCSD QLYGKWYNIE NNIQENEQLL KTKLYNLTTY SKLKARALPK
EWNNQGNARL FRSFNPLDVC NRPEAVLLLN TTYFTYSLWE GDCNYTTALI QNLTECRQPD
RLKLKHPYAC RFWRYKEGQE EVKCLGNEKK KCLYYSEYSS PEAQFDFGFL SYLNAFPGLK
YIENQTVREP EYEVYSLYME CMNSAEKYGI DSVLFALKTF LNFTGTPVNE MSTARAFVGL
TDPKFPPTYP NITKEQKRCN NLKRRKRSTN IEKLRSMGYS LTGAVQTLSQ ISDINDERLQ
QGVSLLRDHV VTLMEAALHD ITIMEGMLAI QHVHTHLNHL KTILLMRKID WTFIKSNWIK
EQLQKTEDEM KIIRRTAKSL VYYVTQTSSS TTATSWEIGI YYEITIPKHI YLNNWQVINI
GHLVESAGHL TLIRVKHPYE VINKECTYEQ YLHLEDCISQ DYVICDTVQI VSPCGNSTTT
SDCPVTAEKV KEPYVQVSAL KNGSYLVLTS RTDCSIPAYV PSIVTVNETV KCFGVEFHKP
LYSESKVSFE PQVPHLKLRL PHLVGIIANL QNLEIEVTST QESIKDQIER AKSQLLRLDI
HEGDFPAWIQ QLASATRDVW PAAARALQGI GNVLSNTAQG IFGTTVSILS YAKPILIGIG
VILLIAFLFK IVSWLPGKKK RN
