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Entry version 140 (29 Sep 2021)
Sequence version 1 (21 Jul 1986)
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Protein

Fusion glycoprotein F0

Gene

F

Organism
Human respiratory syncytial virus A (strain A2)
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

Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins.

1 Publication

Class I viral fusion protein (PubMed:23618766).

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 (PubMed:23618766).

During viral and plasma cell membrane fusion, the coiled coil regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain (PubMed:23618766, PubMed:19966279).

The formation of this structure appears to drive apposition and subsequent fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm (PubMed:23593008, PubMed:23618766).

This fusion is pH independent and occurs at the plasma or endosomal membrane (Probable). The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate (PubMed:10864656).

F protein is involved in the entry into the host cell through the interaction with host IGFR1 (PubMed:32494007).

This interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell surface where it can bind fusion glycoprotein F1 (PubMed:32494007, PubMed:21841784).

Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (PubMed:10438814).

F protein may trigger p53-dependent apoptosis (PubMed:18216092).

2 Publications8 Publications

Major determinant of the species specificity of RSV infection (PubMed:12663767).

The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate (PubMed:10864656).

F protein is involved in the entry into the host cell through the interaction with host IGFR1 (PubMed:32494007).

This interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell surface where it can bind fusion glycoprotein F1 (PubMed:32494007).

Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (PubMed:10438814).

F protein seems to trigger p53-dependent apoptosis (PubMed:18216092).

5 Publications

<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 - Molecular functioni

GO - Biological processi

<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>Keywordsi

Biological processFusion of virus membrane with host cell membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Syncytium formation induced by viral infection, Viral attachment to host cell, Viral attachment to host entry receptor, Viral penetration into host cytoplasm, Virus entry into host cell

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.G.2.1.3, the viral pore-forming membrane fusion protein-2 (vmfp2) family

<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:
Fusion glycoprotein F0
Cleaved into the following 3 chains:
Fusion glycoprotein F21 Publication
Short name:
F2
p271 Publication
Alternative name(s):
Intervening segment
Pep27
Peptide 27
Fusion glycoprotein F11 Publication
Short name:
F1
<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:F
<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>OrganismiHuman respiratory syncytial virus A (strain A2)
<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 identifieri11259 [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 lineageiVirusesRiboviriaOrthornaviraeNegarnaviricotaHaploviricotinaMonjiviricetesMononegaviralesPneumoviridaeOrthopneumovirus
<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 hostiHomo sapiens (Human) [TaxID: 9606]
<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
  • UP000181559 <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
  • UP000181262 Componenti: Genome
  • UP000181145 Componenti: Genome
  • UP000007678 Componenti: Genome
  • UP000134464 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

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 domaini26 – 524Extracellular1 PublicationAdd BLAST499
<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>Transmembranei525 – 550Helical1 PublicationAdd BLAST26
Topological domaini551 – 574Cytoplasmic1 PublicationAdd BLAST24

Keywords - Cellular componenti

Host cell membrane, Host Golgi apparatus, Host membrane, Membrane, Viral envelope protein, Virion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi37C → S: Impairs translation or folding of the F protein. 1 Publication1
Mutagenesisi69C → S: Impairs translation or folding of the F protein. 1 Publication1
Mutagenesisi108 – 109RR → NN: Complete loss of cleavage between F2 and p27. 2 Publications2
Mutagenesisi108R → N: Complete loss of cleavage between F2 and p27. 1 Publication1
Mutagenesisi109R → N: Complete loss of cleavage between F2 and p27. 1 Publication1
Mutagenesisi131K → Q: No effect on cleavage between F2 and p27. 1 Publication1
Mutagenesisi212C → S: No effect on F1 and F2 structure and glycosylation. 1 Publication1
Mutagenesisi313C → S: Impairs translation or folding of the F protein. 1 Publication1
Mutagenesisi322C → S: Impairs translation or folding of the F protein. 1 Publication1
Mutagenesisi333C → S: Impairs translation or folding of the F protein. 1 Publication1
Mutagenesisi343C → S: Impairs translation or folding of the F protein. 1 Publication1
Mutagenesisi358C → S: Impairs translation or folding of the F protein. 1 Publication1
Mutagenesisi367C → S: Impairs translation or folding of the F protein. 1 Publication1
Mutagenesisi382C → S: No effect on F1 and F2 structure and glycosylation. 1 Publication1
Mutagenesisi393C → S: Impairs translation or folding of the F protein. 1 Publication1
Mutagenesisi416C → S: Impairs translation or folding of the F protein. 1 Publication1
Mutagenesisi422C → S: No effect on F1 and F2 structure and glycosylation. 1 Publication1
Mutagenesisi439C → S: Impairs translation or folding of the F protein. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3856166

DrugCentral

More...
DrugCentrali
P03420

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 25Sequence analysisAdd BLAST25
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003923426 – 574Fusion glycoprotein F0Add BLAST549
ChainiPRO_000003923526 – 109Fusion glycoprotein F21 PublicationAdd BLAST84
<p>This subsection of the 'PTM / Processing' section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_0000432664110 – 136p271 PublicationAdd BLAST27
ChainiPRO_0000039236137 – 574Fusion glycoprotein F1Add BLAST438

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>Glycosylationi27N-linked (GlcNAc...) asparagine; by host1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi37 ↔ 439Interchain (between F2 and F1 chains)1 Publication1 Publication
Disulfide bondi69 ↔ 212Interchain (between F2 and F1 chains)1 Publication
Glycosylationi70N-linked (GlcNAc...) asparagine; by host2 Publications1
Glycosylationi116N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi120N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi126N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi313 ↔ 3431 Publication
Disulfide bondi322 ↔ 3331 Publication
Disulfide bondi358 ↔ 3671 Publication
Disulfide bondi382 ↔ 3931 Publication
Disulfide bondi416 ↔ 4222 Publications
Glycosylationi500N-linked (GlcNAc...) asparagine; by host2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi550S-palmitoyl cysteine; by host1 Publication1

<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

The F glycoprotein is synthesized as a F0 inactive precursor that is heavily N-glycosylated and processed at two sites by a host furin-like protease probably in the Golgi (PubMed:11493675, PubMed:11369882, PubMed:23593008, PubMed:11418598). The cleavage site between p27 and F1 may occur after endocytosis to yield the mature F1 and F2 proteins (Probable). Both cleavages are required for membrane fusion and p27 is released from the processed protein (PubMed:11493675, PubMed:23593008, PubMed:12127793).1 Publication5 Publications

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>Sitei109 – 110Cleavage; by host furin-like protease2 Publications2
Sitei136 – 137Cleavage; by host furin-like protease2 Publications2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

<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

Homotrimer (PubMed:23618766, PubMed:26333350). Heterodimer with fusion protein F2; disulfide-linked (PubMed:16723026, PubMed:21613394).

Interacts with host NCL; this interaction plays a role in viral entry into the host cell (PubMed:21841784). As a heterodimer with F2, interacts with host heparan sulfate (PubMed:10864656). As a heterodimer with F2, interacts with host IGFR1; this interaction activates PRKCZ/PKCzeta that recruits NCL/nucleolin from the host nucleus to the plasma membrane (PubMed:32494007).

Part of a complex composed of F1, F2 and G glycoproteins (PubMed:18036342). As a heterodimer with F2, interacts with host RHOA; this interaction facilitates virus-induced syncytium formation (PubMed:10438814).

9 Publications

Homotrimer (PubMed:26333350, PubMed:23618766). Heterodimer with fusion protein F1; disulfide-linked (PubMed:26333350, PubMed:16723026, PubMed:21613394). As a heterodimer with F1, interacts with host heparan sulfate (PubMed:10864656). As a heterodimer with F1, interacts with host IGFR1; this interaction activates PRKCZ/PKCzeta that recruits NCL/nucleolin from the host nucleus to the plasma membrane (PubMed:32494007).

Part of a complex composed of F1, F2 and G glycoproteins (PubMed:18036342). As a heterodimer with F1, interacts with host RHOA; this interaction facilitates virus-induced syncytium formation (PubMed:10438814).

8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

P03420
With#Exp.IntAct
itself8EBI-10042897,EBI-10042897

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-48772N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P03420

Protein interaction database and analysis system

More...
IntActi
P03420, 2 interactors

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P03420

<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

Secondary structure

1574
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P03420

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P03420

<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>Regioni137 – 157Fusion peptideBy similarityAdd BLAST21

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili76 – 962 PublicationsAdd BLAST21
Coiled coili158 – 2091 Publication2 PublicationsAdd BLAST52
Coiled coili481 – 5161 Publication1 PublicationAdd BLAST36

<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 N-terminus is a hydrophobic fusion peptide that inserts into the target host membrane (By similarity). It is buried in the center of the trimer cavity before cleavage by host furin (PubMed:23618766). The coiled coil (heptad repeat) regions are probably involved in homotrimerization, heterodimerization and in the formation of a fusion-active hairpin structure (PubMed:10846072, PubMed:29212939).By similarity3 Publications
The N-terminus is a hydrophobic fusion peptide that inserts into the target host membrane (By similarity). It is buried in the center of the trimer cavity before cleavage by host furin (PubMed:23618766). The coiled coil (heptad repeat) regions are probably involved in homotrimerization, heterodimerization and in the formation of a fusion-active hairpin structure (PubMed:10846072).By similarity2 Publications

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000776, Fusion_F0_Paramyxovir

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00523, Fusion_gly, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

P03420-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MELLILKANA ITTILTAVTF CFASGQNITE EFYQSTCSAV SKGYLSALRT
60 70 80 90 100
GWYTSVITIE LSNIKENKCN GTDAKVKLIK QELDKYKNAV TELQLLMQST
110 120 130 140 150
PPTNNRARRE LPRFMNYTLN NAKKTNVTLS KKRKRRFLGF LLGVGSAIAS
160 170 180 190 200
GVAVSKVLHL EGEVNKIKSA LLSTNKAVVS LSNGVSVLTS KVLDLKNYID
210 220 230 240 250
KQLLPIVNKQ SCSISNIETV IEFQQKNNRL LEITREFSVN AGVTTPVSTY
260 270 280 290 300
MLTNSELLSL INDMPITNDQ KKLMSNNVQI VRQQSYSIMS IIKEEVLAYV
310 320 330 340 350
VQLPLYGVID TPCWKLHTSP LCTTNTKEGS NICLTRTDRG WYCDNAGSVS
360 370 380 390 400
FFPQAETCKV QSNRVFCDTM NSLTLPSEIN LCNVDIFNPK YDCKIMTSKT
410 420 430 440 450
DVSSSVITSL GAIVSCYGKT KCTASNKNRG IIKTFSNGCD YVSNKGMDTV
460 470 480 490 500
SVGNTLYYVN KQEGKSLYVK GEPIINFYDP LVFPSDEFDA SISQVNEKIN
510 520 530 540 550
QSLAFIRKSD ELLHNVNAGK STTNIMITTI IIVIIVILLS LIAVGLLLYC
560 570
KARSTPVTLS KDQLSGINNI AFSN
Length:574
Mass (Da):63,453
Last modified:July 21, 1986 - 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:iA4066D9DC98933AA
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti102P → A in strain: Cold-passage attenuated. 1
Natural varianti218E → A in strain: Cold-passage attenuated. 1
Natural varianti379I → V in strain: Cold-passage attenuated. 1
Natural varianti447M → V in strain: Cold-passage attenuated. 1
Natural varianti523T → I in strain: Cold-passage attenuated. 1

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
M11486 Genomic RNA Translation: AAB59858.1
U50362 Genomic RNA Translation: AAB86664.1
U50363 Genomic RNA Translation: AAB86676.1
AF035006 Genomic RNA Translation: AAC14902.1
U63644 Genomic RNA Translation: AAC55970.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A04035, VGNZA2
B28929

<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
M11486 Genomic RNA Translation: AAB59858.1
U50362 Genomic RNA Translation: AAB86664.1
U50363 Genomic RNA Translation: AAB86676.1
AF035006 Genomic RNA Translation: AAC14902.1
U63644 Genomic RNA Translation: AAC55970.1
PIRiA04035, VGNZA2
B28929

3D structure databases

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Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MDPNMR-A1-85[»]
3IXTX-ray2.75C/P254-277[»]
3KPEX-ray1.47A159-209[»]
B482-520[»]
3O41X-ray1.95C/P423-436[»]
3O45X-ray2.87C/P423-438[»]
3RKIX-ray3.20A/B/C1-524[»]
3RRRX-ray2.82A/C/E/G/I/M26-109[»]
B/D/F/H/L/N147-513[»]
3RRTX-ray3.20A/C/E26-109[»]
B/D/F147-513[»]
4CCFX-ray2.65A/B/C/D/E/F1-574[»]
4JHWX-ray3.60F26-513[»]
4MMQX-ray3.25A26-107[»]
B137-513[»]
4MMRX-ray3.10A26-107[»]
B137-513[»]
4MMSX-ray2.40A/C/E26-107[»]
B/D/F137-513[»]
4MMTX-ray3.05A26-107[»]
B137-513[»]
4MMUX-ray3.00A26-107[»]
B137-513[»]
4MMVX-ray2.81A26-107[»]
B137-513[»]
4ZYPX-ray5.50A/B/C26-513[»]
5C69X-ray2.30A26-513[»]
5C6BX-ray2.40F26-108[»]
F113-513[»]
5EA3X-ray2.75F1-513[»]
5EA4X-ray2.30F1-513[»]
5EA5X-ray3.05F1-513[»]
5EA6X-ray2.75F1-513[»]
5EA7X-ray2.85F1-513[»]
5EA8X-ray2.60F1-513[»]
5J3DX-ray4.08E/G/J26-98[»]
F/I/K147-513[»]
5K6BX-ray2.98F26-105[»]
F145-509[»]
5K6CX-ray3.58F26-103[»]
F145-509[»]
5K6FX-ray2.59F26-101[»]
F145-509[»]
5K6GX-ray2.90F26-96[»]
F145-509[»]
5K6HX-ray2.65F26-103[»]
F145-509[»]
5K6IX-ray2.92F26-101[»]
F145-509[»]
5KWWX-ray2.50F1-513[»]
5TOJX-ray3.30A/B/C1-513[»]
5TOKX-ray3.80A/B/C1-513[»]
5TPNX-ray3.14A27-108[»]
A113-513[»]
5U68X-ray3.08A/B/C1-513[»]
5UDCX-ray3.45A/D/F1-513[»]
5W23X-ray3.40A/B/C1-513[»]
6APBX-ray3.00A/B/C1-513[»]
6APDX-ray4.10A/B/C1-513[»]
6CXCelectron microscopy3.90A/B/C/D/E/F26-526[»]
6DC3X-ray3.50F1-513[»]
6DC5X-ray3.50A/D/G1-513[»]
6EADX-ray2.80F1-513[»]
6EAEX-ray2.90F1-513[»]
6EAFX-ray3.00A/B/C1-513[»]
6EAGX-ray3.30F1-513[»]
6EAHX-ray3.00A/B/C1-513[»]
6EAIX-ray2.80A/B/C1-513[»]
6EAJX-ray2.85F1-513[»]
6EAKX-ray2.60F1-513[»]
6EALX-ray2.75F1-513[»]
6EAMX-ray2.74F1-513[»]
6EANX-ray2.90F1-513[»]
6NTXX-ray2.20A/B159-209[»]
6OE4X-ray3.30A/D1-513[»]
6OE5X-ray4.10A1-513[»]
6OJ7X-ray1.45A159-209[»]
6OUSX-ray3.40A/C/E/G/I/K26-109[»]
B/D/F/H/J/L137-513[»]
6VKCX-ray2.60F1-513[»]
6VKDX-ray2.50F1-513[»]
6VKEX-ray2.10F1-513[»]
6W52X-ray3.74A26-107[»]
SMRiP03420
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-48772N
ELMiP03420
IntActiP03420, 2 interactors

Chemistry databases

BindingDBiP03420
ChEMBLiCHEMBL3856166
DrugCentraliP03420

Protein family/group databases

TCDBi1.G.2.1.3, the viral pore-forming membrane fusion protein-2 (vmfp2) family

Protocols and materials databases

ABCD curated depository of sequenced antibodies

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ABCDi
P03420, 28 sequenced antibodies

Miscellaneous databases

EvolutionaryTraceiP03420

Family and domain databases

InterProiView protein in InterPro
IPR000776, Fusion_F0_Paramyxovir
PfamiView protein in Pfam
PF00523, Fusion_gly, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiFUS_HRSVA
<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: P03420
Secondary accession number(s): P88811
<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 21, 1986
Last sequence update: July 21, 1986
Last modified: September 29, 2021
This is version 140 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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