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Envelope glycoprotein gp130 (Env polyprotein) [Cleaved into: Leader peptide (LP) (Env leader protein) (Elp) (gp18LP); Surface protein (SU) (Glycoprotein 80) (gp80); Transmembrane protein (TM) (Glycoprotein 48) (gp48)]

 ENV_FFV                 Reviewed;         982 AA.
O56861;
11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
25-OCT-2017, entry version 76.
RecName: Full=Envelope glycoprotein gp130;
AltName: Full=Env polyprotein;
Contains:
RecName: Full=Leader peptide;
Short=LP;
AltName: Full=Env leader protein;
Short=Elp;
AltName: Full=gp18LP;
Contains:
RecName: Full=Surface protein;
Short=SU;
AltName: Full=Glycoprotein 80;
Short=gp80;
Contains:
RecName: Full=Transmembrane protein;
Short=TM;
AltName: Full=Glycoprotein 48;
Short=gp48;
Name=env;
Feline foamy virus (FFV) (Feline syncytial virus).
Viruses; Retro-transcribing viruses; Retroviridae; Spumaretrovirinae;
Spumavirus.
NCBI_TaxID=53182;
NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9261397;
Winkler I., Bodem J., Haas L., Zemba M., Delius H., Flower R.,
Fluegel R.M., Loechelt M.;
"Characterization of the genome of feline foamy virus and its proteins
shows distinct features different from those of primate
Spumaviruses.";
J. Virol. 71:6727-6741(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate FUV;
PubMed=9601510; DOI=10.1006/viro.1998.9113;
Bodem J., Loechelt M., Delius H., Fluegel R.M.;
"Detection of subgenomic cDNAs and mapping of feline foamy virus mRNAs
reveals complex patterns of transcription.";
Virology 244:417-426(1998).
[3]
INTERACTION OF ENV LEADER PEPTIDE WITH GAG PROTEIN N-TERMINUS.
STRAIN=Isolate FUV;
PubMed=11483744; DOI=10.1128/JVI.75.17.7995-8007.2001;
Wilk T., Geiselhart V., Frech M., Fuller S.D., Fluegel R.M.,
Loechelt M.;
"Specific interaction of a novel foamy virus Env leader protein with
the N-terminal Gag domain.";
J. Virol. 75:7995-8007(2001).
[4]
SUBCELLULAR LOCATION OF ENV LEADER PEPTIDE, AND INTERACTION OF ENV
LEADER PEPTIDE WITH GAG PROTEIN N-TERMINUS.
PubMed=12781711; DOI=10.1016/S0042-6822(03)00125-9;
Geiselhart V., Schwantes A., Bastone P., Frech M., Loechelt M.;
"Features of the Env leader protein and the N-terminal Gag domain of
feline foamy virus important for virus morphogenesis.";
Virology 310:235-244(2003).
[5]
TOPOLOGY OF ENVELOPE GLYCOPROTEIN GP130, CLEAVAGE OF LEADER PEPTIDE BY
A HOST FURIN-LIKE PROTEASE, AND LOW EFFICIENCY OF SIGNAL CLEAVAGE BY
SIGNAL PEPTIDASE.
PubMed=15564468; DOI=10.1128/JVI.78.24.13573-13581.2004;
Geiselhart V., Bastone P., Kempf T., Schnoelzer M., Loechelt M.;
"Furin-mediated cleavage of the feline foamy virus Env leader
protein.";
J. Virol. 78:13573-13581(2004).
-!- FUNCTION: The surface protein (SU) attaches the virus to the host
cell by binding to the cell receptor. This interaction triggers
the refolding of transmembrane protein (TM) and is thought to
activate its fusogenic potential by unmasking its fusion peptide
(By similarity). {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: The leader peptide is a component of released,
infectious virions and is required for particle budding.
-!- SUBUNIT: The mature envelope protein consists of a trimer of SU-TM
heterodimers (By similarity). The N-terminus of leader peptide
specifically interacts with Gag protein. This specific interaction
between Gag protein and Env glycoprotein may allow particle
egress. {ECO:0000250, ECO:0000269|PubMed:11483744,
ECO:0000269|PubMed:12781711}.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein gp130: Host
endoplasmic reticulum membrane. Note=The polyprotein has a highly
unusual biosynthesis for a retroviral glycoprotein. It is
translated as a full-length precursor protein into the rough
endoplasmic reticulum and initially has a type III protein
configuration with both its N and C-termini located
intracytoplasmically.
-!- SUBCELLULAR LOCATION: Leader peptide: Virion membrane
{ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass
type II membrane protein {ECO:0000305}. Note=Its N-terminus is
located inside the viral particle. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Transmembrane protein: Virion membrane
{ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Host endoplasmic reticulum membrane {ECO:0000305}; Single-pass
type I membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Surface protein: Virion membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host
endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane
protein {ECO:0000250}. Note=The surface protein is not anchored to
the viral envelope, but associates with the extravirion surface
through its binding to TM. {ECO:0000250}.
-!- DOMAIN: The ER retention signal plays an important role in
establishing the intracellular site of budding. {ECO:0000250}.
-!- PTM: Envelope glycoproteins are synthesized as a inactive
precursor that is processed by host furin or a furin-like protease
to yield a functional hetero-oligomeric complex. A 9 kDa protein
corresponding to the N-terminus of the leader peptide may arise
through low efficient cleavage by host signal peptidase.
{ECO:0000269|PubMed:15564468}.
-!- PTM: The transmembrane protein and the surface protein are N-
glycosylated. {ECO:0000250}.
-!- MISCELLANEOUS: Foamy viruses are distinct from other retroviruses
in many respects. Their protease is active as an uncleaved Pro-Pol
protein. Mature particles do not include the usual processed
retroviral structural protein (MA, CA and NC), but instead contain
two large Gag proteins. Their functional nucleic acid appears to
be either RNA or dsDNA (up to 20% of extracellular particles),
because they probably proceed either to an early (before
integration) or late reverse transcription (after assembly). Foamy
viruses have the ability to retrotranspose intracellularly with
high efficiency. They bud predominantly into the endoplasmic
reticulum (ER) and occasionally at the plasma membrane. Budding
requires the presence of Env proteins. Most viral particles
probably remain within the infected cell.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y08851; CAA70076.1; -; Genomic_DNA.
EMBL; AJ223851; CAA11582.1; -; Genomic_RNA.
RefSeq; NP_056915.1; NC_001871.1.
SMR; O56861; -.
ELM; O56861; -.
KEGG; vg:4405350; -.
OrthoDB; VOG0900001C; -.
Proteomes; UP000008763; Genome.
Proteomes; UP000201849; Genome.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
InterPro; IPR005070; Foamy_env.
Pfam; PF03408; Foamy_virus_ENV; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Complete proteome; Glycoprotein;
Host endoplasmic reticulum; Host membrane; Membrane;
Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
Viral envelope protein; Virion.
CHAIN 1 982 Envelope glycoprotein gp130.
{ECO:0000250}.
/FTId=PRO_0000244973.
CHAIN 1 127 Leader peptide.
/FTId=PRO_0000244974.
CHAIN 128 563 Surface protein. {ECO:0000250}.
/FTId=PRO_0000244975.
CHAIN 564 982 Transmembrane protein. {ECO:0000250}.
/FTId=PRO_0000244976.
TOPO_DOM 1 63 Cytoplasmic. {ECO:0000255}.
TRANSMEM 64 86 Helical; Signal-anchor for type III
membrane protein. {ECO:0000255}.
TOPO_DOM 87 953 Lumenal. {ECO:0000255}.
TRANSMEM 954 974 Helical. {ECO:0000255}.
TOPO_DOM 975 982 Cytoplasmic. {ECO:0000255}.
REGION 569 591 Fusion peptide. {ECO:0000250}.
MOTIF 978 980 Endoplasmic reticulum retention signal.
{ECO:0000250}.
SITE 12 12 Required for Gag-Env interaction.
SITE 15 15 Required for Gag-Env interaction.
SITE 127 128 Cleavage; by host.
SITE 563 564 Cleavage; by host. {ECO:0000250}.
CARBOHYD 118 118 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000305}.
CARBOHYD 139 139 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000305}.
CARBOHYD 266 266 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 283 283 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 390 390 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 409 409 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 420 420 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 489 489 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 521 521 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 536 536 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 654 654 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 690 690 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 775 775 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 800 800 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 825 825 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
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


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