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UniProtKB - O56861 (ENV_FFV)

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Protein

Envelope glycoprotein gp130

Gene

env

Organism
Feline foamy virus (FFV) (Feline syncytial virus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).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
The leader peptide is a component of released, infectious virions and is required for particle budding.

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei12Required for Gag-Env interaction1
Sitei15Required for Gag-Env interaction1

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein gp130
Alternative name(s):
Env polyprotein
Cleaved into the following 3 chains:
Leader peptide
Short name:
LP
Alternative name(s):
Env leader protein
Short name:
Elp
gp18LP
Surface protein
Short name:
SU
Alternative name(s):
Glycoprotein 80
Short name:
gp80
Transmembrane protein
Short name:
TM
Alternative name(s):
Glycoprotein 48
Short name:
gp48
Gene namesi
Name:env
OrganismiFeline foamy virus (FFV) (Feline syncytial virus)
Taxonomic identifieri53182 [NCBI]
Taxonomic lineageiViruses › Retro-transcribing viruses › Retroviridae › Spumaretrovirinae › Spumavirus
Virus hostiFelis catus (Cat) (Felis silvestris catus) [TaxID: 9685]
Proteomesi
  • UP000008763 Componenti: Genome

Subcellular locationi

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.
Leader peptide :
Transmembrane protein :
Surface protein :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 63CytoplasmicSequence analysisAdd BLAST63
Transmembranei64 – 86Helical; Signal-anchor for type III membrane proteinSequence analysisAdd BLAST23
Topological domaini87 – 953LumenalSequence analysisAdd BLAST867
Transmembranei954 – 974HelicalSequence analysisAdd BLAST21
Topological domaini975 – 982CytoplasmicSequence analysis8

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host endoplasmic reticulum, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002449731 – 982Envelope glycoprotein gp130By similarityAdd BLAST982
ChainiPRO_00002449741 – 127Leader peptideAdd BLAST127
ChainiPRO_0000244975128 – 563Surface proteinBy similarityAdd BLAST436
ChainiPRO_0000244976564 – 982Transmembrane proteinBy similarityAdd BLAST419

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi118N-linked (GlcNAc...) asparagine; by hostCurated1
Glycosylationi139N-linked (GlcNAc...) asparagine; by hostCurated1
Glycosylationi266N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi283N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi307N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi390N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi409N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi420N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi489N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi521N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi536N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi654N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi690N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi775N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi800N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi825N-linked (GlcNAc...) asparagine; by hostSequence analysis1

Post-translational modificationi

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.1 Publication
The transmembrane protein and the surface protein are N-glycosylated.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei127 – 128Cleavage; by host2
Sitei563 – 564Cleavage; by hostBy similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein

Interactioni

Subunit structurei

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.By similarity2 Publications

Structurei

3D structure databases

SMRiO56861.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni569 – 591Fusion peptideBy similarityAdd BLAST23

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi978 – 980Endoplasmic reticulum retention signalBy similarity3

Domaini

The ER retention signal plays an important role in establishing the intracellular site of budding.By similarity

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

OrthoDBiVOG0900001C.

Family and domain databases

InterProiView protein in InterPro
IPR005070. Foamy_env.
PfamiView protein in Pfam
PF03408. Foamy_virus_ENV. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O56861-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQEHVMTLK EWMEWNAHKQ LQKLQSTHPE LHVDIPEDIP LVPEKVPLKM 
        60         70         80         90        100
RMRYRCYTLC ATSTRIMFWI LFFLLCFSIV TLSTIISILR YQWKEAITHP 
       110        120        130        140        150
GPVLSWQVTN SHVTMGGNTS SSSRRRRDIQ YHKLPVEVNI SGIPQGLFFA 
       160        170        180        190        200
PQPKPIFHKE RTLGLSQVIL IDSDTITQGH IKQQKAYLVS TINEEMEQLQ 
       210        220        230        240        250
KTVLPFDLPI KDPLTQKEYI EKRCFQKYGH CYVIAFNGNK VWPSQDLIQD 
       260        270        280        290        300
QCPLPPRFGN NLKYRNHTIW KYYIPLPFKV SSNWTRVESY GNIRIGSFKV 
       310        320        330        340        350
PDEFRQNATH GIFCSDALYS NWYPRDLPSS VQQSFAQAYI TKVLMKRKKQ 
       360        370        380        390        400
PTLRDIAFPK ELSPVGSGML FRPINPYDIC NMPRAVLLLN KTYYTFSLWE 
       410        420        430        440        450
GDCGYYQHNL TLHPACKNFN RTRQDHPYAC RFWRNKYDSE SVQCYNNDMC 
       460        470        480        490        500
YYRPLYDGTE NTEDWGWLAY TDSFPSPICI EEKRIWKKNY TLSSVLAECV 
       510        520        530        540        550
NQAMEYGIDE VLSKLDLIFG NLTHQSADEA FIPVNNFTWP RYEKQNKQQK 
       560        570        580        590        600
TSCERKKGRR QRRSVSTENL RRIQEAGLGL ANAITTVAKI SDLNDQKLAK 
       610        620        630        640        650
GVHLLRDHVV TLMEANLDDI VSLGEGIQIE HIHNHLTSLK LLTLENRIDW 
       660        670        680        690        700
RFINDSWIQE ELGVSDNIMK VIRKTARCIP YNVKQTRNLN TSTAWEIYLY 
       710        720        730        740        750
YEIIIPTTIY TQNWNIKNLG HLVRNAGYLS KVWIQQPFEV LNQECGTNIY 
       760        770        780        790        800
LHMEECVDQD YIICEEVMEL PPCGNGTGSD CPVLTKPLTD EYLEIEPLKN 
       810        820        830        840        850
GSYLVLSSTT DCGIPAYVPV VITVNDTISC FDKEFKRPLK QELKVTKYAP 
       860        870        880        890        900
SVPQLELRVP RLTSLIAKIK GIQIEITSSW ETIKEQVARA KAELLRLDLH 
       910        920        930        940        950
EGDYPEWLQL LGEATKDVWP TISNFVSGIG NFIKDTAGGI FGTAFSFLGY 
       960        970        980 
VKPVLLGFVI IFCIILIIKI IGWLQNTRKK DQ
Length:982
Mass (Da):113,715
Last modified:June 1, 1998 - v1
Checksum:i1D6DB3D5B2F56FB3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08851 Genomic DNA. Translation: CAA70076.1.
AJ223851 Genomic RNA. Translation: CAA11582.1.
RefSeqiNP_056915.1. NC_001871.1.

Genome annotation databases

KEGGivg:4405350.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiENV_FFV
AccessioniPrimary (citable) accession number: O56861
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: June 1, 1998
Last modified: May 10, 2017
This is version 74 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome