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Entry version 114 (08 May 2019)
Sequence version 3 (12 Apr 2005)
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Protein

Fusion glycoprotein F0

Gene

F

Organism
Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ))
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

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 plasma cell membrane fusion, the heptad repeat (HR) regions 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 plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) interacts with HN tetramer at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis.

Miscellaneous

Sendai virus or recombinant F protein are widely used in cellular biology to fuse cells.

<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 - 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, Viral penetration into host cytoplasm, Virus entry into host cell

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P04855

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.G.2.1.2 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
Short name:
Protein F
Cleaved into the following 2 chains:
<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>OrganismiSendai virus (strain Z) (SeV) (Sendai virus (strain HVJ))
<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 identifieri11198 [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 lineageiVirusesssRNA virusesssRNA negative-strand virusesNegarnaviricotaHaploviricotinaMonjiviricetesMononegaviralesParamyxoviridaeRespirovirus
<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 hostiCavia cutleri (Guinea pig) [TaxID: 10144]
Cricetidae sp. (Hamster) [TaxID: 36483]
Mus musculus (Mouse) [TaxID: 10090]
Rattus norvegicus (Rat) [TaxID: 10116]
<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
  • UP000181310 <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
  • UP000163956 Componenti: Genome
  • UP000169749 Componenti: Genome
  • UP000110830 Componenti: Genome
  • UP000006560 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 – 500ExtracellularAdd BLAST475
<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>Transmembranei501 – 521HelicalAdd BLAST21
Topological domaini522 – 565CytoplasmicAdd BLAST44

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, 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>Mutagenesisi70C → S: Inhibits transport of F and HN to the cell surface. 1 Publication1
Mutagenesisi104N → G: Loss of glycosylation, enhances cell fusion activity. 1 Publication1
Mutagenesisi199C → S: Inhibits transport of F and HN to the cell surface. 1 Publication1
Mutagenesisi245N → G: Loss of glycosylation, cell surface transport and F0 cleavage. 1 Publication1
Mutagenesisi338C → S: Inhibits transport of F and HN to the cell surface. 1 Publication1
Mutagenesisi347C → S: Inhibits transport of F and HN to the cell surface. 1 Publication1
Mutagenesisi362C → S: Inhibits transport of F and HN to the cell surface. 1 Publication1
Mutagenesisi370C → S: Inhibits transport of F and HN to the cell surface. 1 Publication1
Mutagenesisi394C → S: Inhibits transport of F and HN to the cell surface. 1 Publication1
Mutagenesisi399C → S: Inhibits transport of F and HN to the cell surface. 1 Publication1
Mutagenesisi401C → S: Inhibits transport of F and HN to the cell surface. 1 Publication1
Mutagenesisi424C → S: Inhibits transport of F and HN to the cell surface. 1 Publication1
Mutagenesisi449N → G: Loss of glycosylation. 1 Publication1

<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 – 25Add BLAST25
<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_000003937526 – 565Fusion glycoprotein F0Add BLAST540
ChainiPRO_000003937626 – 116Fusion glycoprotein F2Add BLAST91
ChainiPRO_0000039377117 – 565Fusion glycoprotein F1Add BLAST449

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi70 ↔ 199Interchain (between F2 and F1 chains)
<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>Glycosylationi104N-linked (GlcNAc...) asparagine; by host2 Publications1
Glycosylationi245N-linked (GlcNAc...) asparagine; by host2 Publications1
Disulfide bondi338 ↔ 347
Disulfide bondi362 ↔ 370
Disulfide bondi394 ↔ 399By similarity
Disulfide bondi401 ↔ 424By similarity
Glycosylationi449N-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 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

In natural infection, inactive F0 is matured into F1 and F2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is tryptase Clara. Unlike most paramyxoviruses, Sendai F0 processing occurs on the cell surface and induces a conformational change in the protein that unmasks the fusion peptide. F0 maturation is a primary determinant for organ tropism and pathogenicity. F1 and F2 display interchain and intrachain disulfide bonds, that are necessary for correct folding and intracellular transport.
N-glycosylated; glycans consist of a mixture of high mannose-type oligosaccharides and of complex-type oligosaccharides. Glycosylation at Asn-245 is essential for membrane localization and F0 cleavage.2 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>Sitei116 – 117Cleavage; by arginine-specific endoprotease2

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P04855

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
167

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P04855

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P04855

<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 of disulfide-linked F1-F2. Interacts with HN and M proteins.5 Publications

<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

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SMRi
P04855

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>Regioni117 – 141Fusion peptideAdd BLAST25
Regioni278 – 306Leucine-zipperSequence analysisAdd BLAST29

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 coili142 – 170Sequence analysisAdd BLAST29
Coiled coili466 – 491Sequence analysisAdd BLAST26

<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 cytoplasmic region mediates the interaction with HN and M proteins.1 Publication

<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>.<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.

P04855-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTAYIQRSQC ISTSLLVVLT TLVSCQIPRD RLSNIGVIVD EGKSLKIAGS
60 70 80 90 100
HESRYIVLSL VPGVDFENGC GTAQVIQYKS LLNRLLIPLR DALDLQEALI
110 120 130 140 150
TVTNDTTQNA GAPQSRFFGA VIGTIALGVA TSAQITAGIA LAEAREAKRD
160 170 180 190 200
IALIKESMTK THKSIELLQN AVGEQILALK TLQDFVNDEI KPAISELGCE
210 220 230 240 250
TAALRLGIKL TQHYSELLTA FGSNFGTIGE KSLTLQALSS LYSANITEIM
260 270 280 290 300
TTIKTGQSNI YDVIYTEQIK GTVIDVDLER YMVTLSVKIP ILSEVPGVLI
310 320 330 340 350
HKASSISYNI DGEEWYVTVP SHILSRASFL GGADITDCVE SRLTYICPRD
360 370 380 390 400
PAQLIPDSQQ KCILGDTTRC PVTKVVDSLI PKFAFVNGGV VANCIASTCT
410 420 430 440 450
CGTGRRPISQ DRSKGVVFLT HDNCGLIGVN GVELYANRRG HDATWGVQNL
460 470 480 490 500
TVGPAIAIRP IDISLNLADA TNFLQDSKAE LEKARKILSE VGRWYNSRET
510 520 530 540 550
VITIIVVMVV ILVVIIVIII VLYRLRRSML MGNPDDRIPR DTYTLEPKIR
560
HMYTNGGFDA MAEKR
Length:565
Mass (Da):61,644
Last modified:April 12, 2005 - v3
<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:i2EC5AA4DF96BC621
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti261Y → S (PubMed:3005975).Curated1

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 varianti38 – 39IV → TA in strain: Mutant KD-22 in Mutant KD-22M. 2
Natural varianti47I → V in Mutant KD-21 and Mutant KD-52. 1
Natural varianti56I → L in strain: Mutant KD-41. 1
Natural varianti63G → V in strain: Mutant F1-R, Mutant F1-R / T-5 revertant and Mutant ts-f1. 1
Natural varianti65 – 67DFE → HFD in strain: Mutant KD-32. 3
Natural varianti67E → Q in strain: Mutant KD-22M and Mutant KD-32M. 1
Natural varianti79K → N in strain: Mutant KD-62. 1
Natural varianti84R → M in strain: Mutant BF-41, Mutant BF-53, Mutant BF-82 and Mutant BF-132. 1
Natural varianti90R → S in strain: Mutant KD-51 and Mutant KD-51M. 1
Natural varianti91D → V in strain: Mutant KD-51M. 1
Natural varianti104N → S in strain: Mutant F1-R, Mutant F1-R / T-5 revertant and Mutant ts-f1. 1
Natural varianti105 – 106DT → AP in strain: Mutant KD-11 and Mutant KD-11M. 2
Natural varianti109N → L in strain: Mutant KD-31 and Mutant KD-61. 1
Natural varianti115 – 116SR → AT in strain: Mutant KD-52M. 2
Natural varianti115 – 116SR → PK in strain: Mutant F1-R and Mutant ts-f1. 2
Natural varianti116R → I in strain: Mutant KD-21 and Mutant KD-62. 1
Natural varianti116R → K in strain: Mutant F1-R / T-5 revertant. 1
Natural varianti129V → A in strain: Mutant KD-22M. 1
Natural varianti196E → D in strain: Mutant KD-32 and KD-32M. 1
Natural varianti200E → G in strain: Mutant KD-32 and KD-32M. 1
Natural varianti250M → I in strain: Mutant BY-4 and Mutant BY-13. 1
Natural varianti254K → R in strain: wild-type, Mutant F1-R, Mutant F1-R / T-5 revertant and Mutant ts-f1. 1
Natural varianti279E → K in strain: Mutant F1-R, Mutant F1-R / T-5 revertant and Mutant ts-f1. 1
Natural varianti318T → H in strain: Mutant BY-4, Mutant BY-5 and Mutant BY-13. 1
Natural varianti319V → A. 1
Natural varianti387N → Y in strain: Mutant KD-61. 1
Natural varianti395I → S in strain: Mutant KD-61. 1
Natural varianti399C → F in strain: Mutant KD-52M. 1
Natural varianti400T → P in strain: Mutant KD-61. 1
Natural varianti423N → H in strain: Mutant KD-52M. 1
Natural varianti456I → V in strain: Mutant KD-51 and Mutant KD-51M. 1
Natural varianti461I → V in strain: wild-type, Mutant F1-R, Mutant F1-R / T-5 revertant and Mutant ts-f1. 1
Natural varianti480E → G in strain: Mutant KD-22. 1
Natural varianti488L → I in strain: Mutant KD-51 and Mutant KD-51M. 1
Natural varianti555N → K in strain: Mutant F1-R, Mutant F1-R / T-5 revertant and Mutant ts-f1. 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
M12396 Genomic RNA Translation: AAA47809.1
X03614 Genomic RNA Translation: CAA27275.1
M30202 Genomic RNA Translation: AAB06281.1
M30203 Genomic RNA Translation: AAB06287.1
M30204 Genomic RNA Translation: AAB06199.1
M69046 Genomic RNA Translation: AAB06293.1
M55564 Genomic RNA Translation: AAA47804.1
U86411 Genomic DNA Translation: AAC82291.1
U86412 Genomic DNA Translation: AAC82292.1
U86413 Genomic DNA Translation: AAC82293.1
U86414 Genomic DNA Translation: AAC82294.1
U86415 Genomic DNA Translation: AAC82295.1
U86416 Genomic DNA Translation: AAC82296.1
U86417 Genomic DNA Translation: AAC82297.1
U86418 Genomic DNA Translation: AAC82298.1
U86419 Genomic DNA Translation: AAC82299.1
U86420 Genomic DNA Translation: AAC82300.1
U86421 Genomic DNA Translation: AAC82301.1
U86422 Genomic DNA Translation: AAC82302.1
U86423 Genomic DNA Translation: AAC82303.1
M76993 Genomic RNA Translation: AAB06520.1
M76994 Genomic RNA Translation: AAB06512.1
M76995 Genomic RNA Translation: AAB06513.1
M76996 Genomic RNA Translation: AAB06514.1
M76997 Genomic RNA Translation: AAB06515.1
M76998 Genomic RNA Translation: AAB06516.1
M76999 Genomic RNA Translation: AAB06517.1
M77000 Genomic RNA Translation: AAB06518.1
M77001 Genomic RNA Translation: AAB06519.1
M77002 Genomic RNA Translation: AAB06830.1
X00087 Genomic RNA Translation: CAA24948.1
AF001283 Genomic RNA Translation: AAC82320.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A04036 VGNZSV
A24516 VGNZSH

<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
M12396 Genomic RNA Translation: AAA47809.1
X03614 Genomic RNA Translation: CAA27275.1
M30202 Genomic RNA Translation: AAB06281.1
M30203 Genomic RNA Translation: AAB06287.1
M30204 Genomic RNA Translation: AAB06199.1
M69046 Genomic RNA Translation: AAB06293.1
M55564 Genomic RNA Translation: AAA47804.1
U86411 Genomic DNA Translation: AAC82291.1
U86412 Genomic DNA Translation: AAC82292.1
U86413 Genomic DNA Translation: AAC82293.1
U86414 Genomic DNA Translation: AAC82294.1
U86415 Genomic DNA Translation: AAC82295.1
U86416 Genomic DNA Translation: AAC82296.1
U86417 Genomic DNA Translation: AAC82297.1
U86418 Genomic DNA Translation: AAC82298.1
U86419 Genomic DNA Translation: AAC82299.1
U86420 Genomic DNA Translation: AAC82300.1
U86421 Genomic DNA Translation: AAC82301.1
U86422 Genomic DNA Translation: AAC82302.1
U86423 Genomic DNA Translation: AAC82303.1
M76993 Genomic RNA Translation: AAB06520.1
M76994 Genomic RNA Translation: AAB06512.1
M76995 Genomic RNA Translation: AAB06513.1
M76996 Genomic RNA Translation: AAB06514.1
M76997 Genomic RNA Translation: AAB06515.1
M76998 Genomic RNA Translation: AAB06516.1
M76999 Genomic RNA Translation: AAB06517.1
M77000 Genomic RNA Translation: AAB06518.1
M77001 Genomic RNA Translation: AAB06519.1
M77002 Genomic RNA Translation: AAB06830.1
X00087 Genomic RNA Translation: CAA24948.1
AF001283 Genomic RNA Translation: AAC82320.1
PIRiA04036 VGNZSV
A24516 VGNZSH

3D structure databases

SMRiP04855
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi1.G.2.1.2 the viral pore-forming membrane fusion protein-2 (vmfp2) family

PTM databases

GlyConnecti167
iPTMnetiP04855
UniCarbKBiP04855

Proteomic databases

PRIDEiP04855

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKiP04855

Family and domain databases

InterProiView protein in InterPro
IPR000776 Fusion_F0_Paramyxovir
PfamiView protein in Pfam
PF00523 Fusion_gly, 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 nameiFUS_SENDZ
<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: P04855
Secondary accession number(s): P04854
, P27564, Q6LC43, Q84202, Q84203, Q88251, Q88252, Q88253, Q88254, Q88255, Q88256, Q88257, Q88258, Q88259, Q88260, Q9YIY9, Q9YJP8, Q9YNH1, Q9YNH2, Q9YNH3, Q9YNH4, Q9YZ79
<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: August 13, 1987
Last sequence update: April 12, 2005
Last modified: May 8, 2019
This is version 114 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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