ENV_FFV
ID ENV_FFV Reviewed; 982 AA.
AC O56861;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 23-FEB-2022, entry version 85.
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 Feline foamy virus (FFV) (Feline syncytial virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Spumaretrovirinae; Felispumavirus.
OX NCBI_TaxID=53182;
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9261397; DOI=10.1128/jvi.71.9.6727-6741.1997;
RA Winkler I., Bodem J., Haas L., Zemba M., Delius H., Flower R.,
RA Fluegel R.M., Loechelt M.;
RT "Characterization of the genome of feline foamy virus and its proteins
RT shows distinct features different from those of primate Spumaviruses.";
RL J. Virol. 71:6727-6741(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate FUV;
RX PubMed=9601510; DOI=10.1006/viro.1998.9113;
RA Bodem J., Loechelt M., Delius H., Fluegel R.M.;
RT "Detection of subgenomic cDNAs and mapping of feline foamy virus mRNAs
RT reveals complex patterns of transcription.";
RL Virology 244:417-426(1998).
RN [3]
RP INTERACTION OF ENV LEADER PEPTIDE WITH GAG PROTEIN N-TERMINUS.
RC STRAIN=Isolate FUV;
RX PubMed=11483744; DOI=10.1128/jvi.75.17.7995-8007.2001;
RA Wilk T., Geiselhart V., Frech M., Fuller S.D., Fluegel R.M., Loechelt M.;
RT "Specific interaction of a novel foamy virus Env leader protein with the N-
RT terminal Gag domain.";
RL J. Virol. 75:7995-8007(2001).
RN [4]
RP SUBCELLULAR LOCATION OF ENV LEADER PEPTIDE, AND INTERACTION OF ENV LEADER
RP PEPTIDE WITH GAG PROTEIN N-TERMINUS.
RX PubMed=12781711; DOI=10.1016/s0042-6822(03)00125-9;
RA Geiselhart V., Schwantes A., Bastone P., Frech M., Loechelt M.;
RT "Features of the Env leader protein and the N-terminal Gag domain of feline
RT foamy virus important for virus morphogenesis.";
RL Virology 310:235-244(2003).
RN [5]
RP TOPOLOGY OF ENVELOPE GLYCOPROTEIN GP130, CLEAVAGE OF LEADER PEPTIDE BY A
RP HOST FURIN-LIKE PROTEASE, AND LOW EFFICIENCY OF SIGNAL CLEAVAGE BY SIGNAL
RP PEPTIDASE.
RX PubMed=15564468; DOI=10.1128/jvi.78.24.13573-13581.2004;
RA Geiselhart V., Bastone P., Kempf T., Schnoelzer M., Loechelt M.;
RT "Furin-mediated cleavage of the feline foamy virus Env leader protein.";
RL J. Virol. 78:13573-13581(2004).
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 transmembrane protein (TM) and is thought to activate its
CC fusogenic potential by unmasking its fusion peptide (By similarity).
CC {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.
CC -!- SUBUNIT: The mature envelope protein consists of a trimer of SU-TM
CC heterodimers (By similarity). The N-terminus of leader peptide
CC specifically interacts with Gag protein. This specific interaction
CC between Gag protein and Env glycoprotein may allow particle egress.
CC {ECO:0000250, ECO:0000269|PubMed:11483744,
CC ECO:0000269|PubMed:12781711}.
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.
CC -!- SUBCELLULAR LOCATION: [Leader peptide]: Virion membrane {ECO:0000305};
CC Single-pass type II membrane protein {ECO:0000305}. Host endoplasmic
CC reticulum membrane {ECO:0000305}; Single-pass type II membrane protein
CC {ECO:0000305}. Note=Its N-terminus is located inside the viral
CC particle. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Host
CC endoplasmic reticulum membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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. A 9 kDa protein corresponding to
CC the N-terminus of the leader peptide may arise through low efficient
CC cleavage by host signal peptidase. {ECO:0000269|PubMed:15564468}.
CC -!- PTM: The transmembrane protein and the surface protein are N-
CC glycosylated. {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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y08851; CAA70076.1; -; Genomic_DNA.
DR EMBL; AJ223851; CAA11582.1; -; Genomic_RNA.
DR RefSeq; NP_056915.1; NC_001871.1.
DR ELM; O56861; -.
DR Proteomes; UP000008763; Genome.
DR Proteomes; UP000201849; 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 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Glycoprotein;
KW Host endoplasmic reticulum; Host membrane; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Viral envelope protein;
KW Virion.
FT CHAIN 1..982
FT /note="Envelope glycoprotein gp130"
FT /evidence="ECO:0000250"
FT /id="PRO_0000244973"
FT CHAIN 1..127
FT /note="Leader peptide"
FT /id="PRO_0000244974"
FT CHAIN 128..563
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000244975"
FT CHAIN 564..982
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000244976"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..86
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..953
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 954..974
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 975..982
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 548..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..591
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT MOTIF 978..980
FT /note="Endoplasmic reticulum retention signal"
FT /evidence="ECO:0000250"
FT SITE 12
FT /note="Required for Gag-Env interaction"
FT SITE 15
FT /note="Required for Gag-Env interaction"
FT SITE 127..128
FT /note="Cleavage; by host"
FT SITE 563..564
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000305"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000305"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
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 409
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 775
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 800
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 825
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 982 AA; 113715 MW; 1D6DB3D5B2F56FB3 CRC64;
MEQEHVMTLK EWMEWNAHKQ LQKLQSTHPE LHVDIPEDIP LVPEKVPLKM RMRYRCYTLC
ATSTRIMFWI LFFLLCFSIV TLSTIISILR YQWKEAITHP GPVLSWQVTN SHVTMGGNTS
SSSRRRRDIQ YHKLPVEVNI SGIPQGLFFA PQPKPIFHKE RTLGLSQVIL IDSDTITQGH
IKQQKAYLVS TINEEMEQLQ KTVLPFDLPI KDPLTQKEYI EKRCFQKYGH CYVIAFNGNK
VWPSQDLIQD QCPLPPRFGN NLKYRNHTIW KYYIPLPFKV SSNWTRVESY GNIRIGSFKV
PDEFRQNATH GIFCSDALYS NWYPRDLPSS VQQSFAQAYI TKVLMKRKKQ PTLRDIAFPK
ELSPVGSGML FRPINPYDIC NMPRAVLLLN KTYYTFSLWE GDCGYYQHNL TLHPACKNFN
RTRQDHPYAC RFWRNKYDSE SVQCYNNDMC YYRPLYDGTE NTEDWGWLAY TDSFPSPICI
EEKRIWKKNY TLSSVLAECV NQAMEYGIDE VLSKLDLIFG NLTHQSADEA FIPVNNFTWP
RYEKQNKQQK TSCERKKGRR QRRSVSTENL RRIQEAGLGL ANAITTVAKI SDLNDQKLAK
GVHLLRDHVV TLMEANLDDI VSLGEGIQIE HIHNHLTSLK LLTLENRIDW RFINDSWIQE
ELGVSDNIMK VIRKTARCIP YNVKQTRNLN TSTAWEIYLY YEIIIPTTIY TQNWNIKNLG
HLVRNAGYLS KVWIQQPFEV LNQECGTNIY LHMEECVDQD YIICEEVMEL PPCGNGTGSD
CPVLTKPLTD EYLEIEPLKN GSYLVLSSTT DCGIPAYVPV VITVNDTISC FDKEFKRPLK
QELKVTKYAP SVPQLELRVP RLTSLIAKIK GIQIEITSSW ETIKEQVARA KAELLRLDLH
EGDYPEWLQL LGEATKDVWP TISNFVSGIG NFIKDTAGGI FGTAFSFLGY VKPVLLGFVI
IFCIILIIKI IGWLQNTRKK DQ
