Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Envelope glycoprotein gp130

Gene

env

Organism
Feline foamy virus (FFV) (Feline syncytial virus)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei12Required for Gag-Env interaction1
Sitei15Required for Gag-Env interaction1

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:env
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiFeline foamy virus (FFV) (Feline syncytial virus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri53182 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesOrterviralesRetroviridaeSpumaretrovirinaeFelispumavirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiFelis catus (Cat) (Felis silvestris catus) [TaxID: 9685]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000008763 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome
  • UP000201849 Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 63CytoplasmicSequence analysisAdd BLAST63
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei64 – 86Helical; Signal-anchor for type III membrane proteinSequence analysisAdd BLAST23
Topological domaini87 – 953LumenalSequence analysisAdd BLAST867
Transmembranei954 – 974HelicalSequence analysisAdd BLAST21
Topological domaini975 – 982CytoplasmicSequence analysis8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti

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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

Protein-protein interaction databases

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
O56861

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
O56861

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni569 – 591Fusion peptideBy similarityAdd BLAST23

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi978 – 980Endoplasmic reticulum retention signalBy similarity3

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005070 Foamy_env

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03408 Foamy_virus_ENV, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i1D6DB3D5B2F56FB3
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Y08851 Genomic DNA Translation: CAA70076.1
AJ223851 Genomic RNA Translation: CAA11582.1

NCBI Reference Sequences

More...
RefSeqi
NP_056915.1, NC_001871.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

SMRiO56861
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

ELMiO56861

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiENV_FFV
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O56861
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: June 1, 1998
Last modified: January 16, 2019
This is version 78 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again