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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.

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 lineageiVirusesRetro-transcribing virusesRetroviridaeSpumaretrovirinaeSpumavirus
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 :
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

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...); by hostCurated1
Glycosylationi139N-linked (GlcNAc...); by hostCurated1
Glycosylationi266N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi283N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi307N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi390N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi409N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi420N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi489N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi521N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi536N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi654N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi690N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi775N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi800N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi825N-linked (GlcNAc...); 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

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

Family and domain databases

InterProiIPR005070. Foamy_env.
[Graphical view]
PfamiPF03408. Foamy_virus_ENV. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGivg:4405350.

Family and domain databases

InterProiIPR005070. Foamy_env.
[Graphical view]
PfamiPF03408. Foamy_virus_ENV. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

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.