Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-11251-00412
Entry Name
UniProt Accession
Theoretical PI
9.09
Molecular Weight
63688.45
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Fusion glycoprotein F1
Protein Synonyms/Alias
Gene Name
F
Gene Synonyms/Alias
Created Date
01-JAN-1990
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
550
Canonical
AIGLLLYCKAKNTPV
[1]
S-Palmitoylation
Organism
Human respiratory syncytial virus B (strain 18537)
NCBI Taxa ID
11251
Reference
[1] Branigan PJ, Day ND, Liu C, Gutshall LL, Melero JA, Sarisky RT, Del VecchioAM. The cytoplasmic domain of the F protein of Human respiratory syncytial virus is not required for cell fusion. J Gen Virol. 2006 Feb;87(Pt 2):395-8. PubMedPMID: 16432027.[PMID:16432027]
Functional Description
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) probably interacts with HN 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 (By similarity).
Sequence Annotation
Topological domain: 27 529 Extracellular.
Transmembrane: 530 550 Helical.
Topological domain: 551 574 Cytoplasmic.
Region: 137 157 Fusion peptide.
Functional site: 136 137 Cleavage; by host.
Protein Length
574 AA.
Protein Sequence
(Canonical)
MELLIHRSSA IFLTLAVNAL YLTSSQNITE EFYQSTCSAV SRGYFSALRT GWYTSVITIE  60
LSNIKETKCN GTDTKVKLIK QELDKYKNAV TELQLLMQNT PAANNRARRE APQYMNYTIN  120
TTKNLNVSIS KKRKRRFLGF LLGVGSAIAS GIAVSKVLHL EGEVNKIKNA LLSTNKAVVS  180
LSNGVSVLTS KVLDLKNYIN NRLLPIVNQQ SCRISNIETV IEFQQMNSRL LEITREFSVN  240
AGVTTPLSTY MLTNSELLSL INDMPITNDQ KKLMSSNVQI VRQQSYSIMS IIKEEVLAYV  300
VQLPIYGVID TPCWKLHTSP LCTTNIKEGS NICLTRTDRG WYCDNAGSVS FFPQADTCKV  360
QSNRVFCDTM NSLTLPSEVS LCNTDIFNSK YDCKIMTSKT DISSSVITSL GAIVSCYGKT  420
KCTASNKNRG IIKTFSNGCD YVSNKGVDTV SVGNTLYYVN KLEGKNLYVK GEPIINYYDP  480
LVFPSDEFDA SISQVNEKIN QSLAFIRRSD ELLHNVNTGK STTNIMITTI IIVIIVVLLS  540
LIAIGLLLYC KAKNTPVTLS KDQLSGINNI AFSK                              574
FASTA
(Canonical)
>LipidDB-11251-00412|P13843
MELLIHRSSAIFLTLAVNALYLTSSQNITEEFYQSTCSAVSRGYFSALRTGWYTSVITIE
LSNIKETKCNGTDTKVKLIKQELDKYKNAVTELQLLMQNTPAANNRARREAPQYMNYTIN
TTKNLNVSISKKRKRRFLGFLLGVGSAIASGIAVSKVLHLEGEVNKIKNALLSTNKAVVS
LSNGVSVLTSKVLDLKNYINNRLLPIVNQQSCRISNIETVIEFQQMNSRLLEITREFSVN
AGVTTPLSTYMLTNSELLSLINDMPITNDQKKLMSSNVQIVRQQSYSIMSIIKEEVLAYV
VQLPIYGVIDTPCWKLHTSPLCTTNIKEGSNICLTRTDRGWYCDNAGSVSFFPQADTCKV
QSNRVFCDTMNSLTLPSEVSLCNTDIFNSKYDCKIMTSKTDISSSVITSLGAIVSCYGKT
KCTASNKNRGIIKTFSNGCDYVSNKGVDTVSVGNTLYYVNKLEGKNLYVKGEPIINYYDP
LVFPSDEFDASISQVNEKINQSLAFIRRSDELLHNVNTGKSTTNIMITTIIIVIIVVLLS
LIAIGLLLYCKAKNTPVTLSKDQLSGINNIAFSK
Gene Ontology
GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0019031; C:viral envelope; IEA:UniProtKB-KW
GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW
GO:0060141; P:positive regulation of syncytium formation by virus; IEA:UniProtKB-KW
Interpro
InterPro; IPR000776; Fusion_F0_Paramyxovir
Pfam
Pfam; PF00523; Fusion_gly;
SMART
PROSITE
PRINTS