FUS_MEASF
ID FUS_MEASF Reviewed; 550 AA.
AC P69354; P08300;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Fusion glycoprotein F0;
DE Contains:
DE RecName: Full=Fusion glycoprotein F2;
DE Contains:
DE RecName: Full=Fusion glycoprotein F1;
DE Flags: Precursor;
GN Name=F;
OS Measles virus (strain Edmonston B) (MeV) (Subacute sclerose panencephalitis
OS virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=70146;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Billeter M.A.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Class I viral fusion protein. Under the current model, the
CC protein has at least 3 conformational states: pre-fusion native state,
CC pre-hairpin intermediate state, and post-fusion hairpin state. During
CC viral and plasma cell membrane fusion, the heptad repeat (HR) regions
CC assume a trimer-of-hairpins structure, positioning the fusion peptide
CC in close proximity to the C-terminal region of the ectodomain. The
CC formation of this structure appears to drive apposition and subsequent
CC fusion of viral and plasma cell membranes. Directs fusion of viral and
CC cellular membranes leading to delivery of the nucleocapsid into the
CC cytoplasm. This fusion is pH independent and occurs directly at the
CC outer cell membrane. The trimer of F1-F2 (F protein) probably interacts
CC with H at the virion surface. Upon HN binding to its cellular receptor,
CC the hydrophobic fusion peptide is unmasked and interacts with the
CC cellular membrane, inducing the fusion between cell and virion
CC membranes. Later in infection, F proteins expressed at the plasma
CC membrane of infected cells could mediate fusion with adjacent cells to
CC form syncytia, a cytopathic effect that could lead to tissue necrosis
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer of disulfide-linked F1-F2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- PTM: The inactive precursor F0 is glycosylated and proteolytically
CC cleaved into F1 and F2 to be functionally active. The cleavage is
CC mediated by cellular proteases during the transport and maturation of
CC the polypeptide (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA91367.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z66517; CAA91367.1; ALT_INIT; Genomic_RNA.
DR EMBL; Z66517; CAA91368.1; -; Genomic_RNA.
DR RefSeq; NP_056922.1; NC_001498.1.
DR SMR; P69354; -.
DR GeneID; 1489800; -.
DR KEGG; vg:1489800; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR InterPro; IPR000776; Fusion_F0_Paramyxovir.
DR Pfam; PF00523; Fusion_gly; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
KW Fusion of virus membrane with host cell membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Membrane; Signal; Transmembrane;
KW Transmembrane helix; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..550
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000039258"
FT CHAIN 24..112
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000039259"
FT CHAIN 113..550
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039260"
FT TOPO_DOM 24..494
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..550
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 113..137
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT COILED 138..166
FT /evidence="ECO:0000255"
FT COILED 462..487
FT /evidence="ECO:0000255"
FT SITE 112..113
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 68..195
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000255"
FT DISULFID 334..343
FT /evidence="ECO:0000250"
FT DISULFID 358..366
FT /evidence="ECO:0000250"
FT DISULFID 390..395
FT /evidence="ECO:0000250"
FT DISULFID 397..420
FT /evidence="ECO:0000250"
SQ SEQUENCE 550 AA; 59532 MW; 7AA4F1CA82169093 CRC64;
MGLKVNVSAI FMAVLLTLQT PTGQIHWGNL SKIGVVGIGS ASYKVMTRSS HQSLVIKLMP
NITLLNNCTR VEIAEYRRLL RTVLEPIRDA LNAMTQNIRP VQSVASSRRH KRFAGVVLAG
AALGVATAAQ ITAGIALHQS MLNSQAIDNL RASLETTNQA IEAIRQAGQE MILAVQGVQD
YINNELIPSM NQLSCDLIGQ KLGLKLLRYY TEILSLFGPS LRDPISAEIS IQALSYALGG
DINKVLEKLG YSGGDLLGIL ESRGIKARIT HVDTESYFIV LSIAYPTLSE IKGVIVHRLE
GVSYNIGSQE WYTTVPKYVA TQGYLISNFD ESSCTFMPEG TVCSQNALYP MSPLLQECLR
GSTKSCARTL VSGSFGNRFI LSQGNLIANC ASILCKCYTT GTIINQDPDK ILTYIAADHC
PVVEVNGVTI QVGSRRYPDA VYLHRIDLGP PISLERLDVG TNLGNAIAKL EDAKELLESS
DQILRSMKGL SSTSIVYILI AVCLGGLIGI PALICCCRGR CNKKGEQVGM SRPGLKPDLT
GTSKSYVRSL
