FUS_MEASI
ID FUS_MEASI Reviewed; 529 AA.
AC P26031; Q83298;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 92.
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 IP-3-Ca) (MeV) (Subacute sclerose panencephalitis
OS virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=11237;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1585658; DOI=10.1016/0042-6822(92)90552-z;
RA Schmid A., Spielhofer P., Cattaneo R., Baczko K., Ter Meulen V.,
RA Billeter M.A.;
RT "Subacute sclerosing panencephalitis is typically characterized by
RT alterations in the fusion protein cytoplasmic domain of the persisting
RT measles virus.";
RL Virology 188:910-915(1992).
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=CAA34568.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X16566; CAA34567.1; -; Genomic_RNA.
DR EMBL; X16566; CAA34568.1; ALT_INIT; Genomic_RNA.
DR SMR; P26031; -.
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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..529
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000039264"
FT CHAIN 27..115
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000039265"
FT CHAIN 116..529
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039266"
FT TOPO_DOM 27..499
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 521..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 116..140
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT COILED 141..169
FT /evidence="ECO:0000255"
FT COILED 465..490
FT /evidence="ECO:0000255"
FT SITE 115..116
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 71..198
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250"
FT DISULFID 337..346
FT /evidence="ECO:0000250"
FT DISULFID 361..369
FT /evidence="ECO:0000250"
FT DISULFID 393..398
FT /evidence="ECO:0000250"
FT DISULFID 400..423
FT /evidence="ECO:0000250"
SQ SEQUENCE 529 AA; 57332 MW; AE987BC9F07E9AA9 CRC64;
MSIMGLKVNV SAIFMAVLLT LQTPTGQIHW GNLSKIGVVG IGSASYKVMT RSSHQSLVIK
LMPNITLLNN CTRVEIAEYR RLLRTVLEPI RDALNAMTQN IRLVQSVASS RRHKRFAGVV
LAGAALGVAT AAQITAGIAL HQSMLSSQAI DNLRASLETT NQAIEAIRQA GQEMILAVQG
VQDYINNELI PSMNQLSCDL IGQKLGLKLL RYYTEILSLF GPSLRDPISA EISIQALSYA
LGGDINKVLE KLGYSGGDLL GILESRGIKA RITHVDTESY FIVLSIAYPT LSEIKEVIVH
RLEGVSYNIG SQEWYTTVPK YVATQGYLIS NFDESSCTFM PEGTVCSQNA LYPMSPLLQE
CLRGSTKSCA RTLVSGSFGN RFILSQGNLI ANCASILCKC YTTGTIIRQD PDKILTYIAA
DHCPVVEVNG VTIQVGSRRY PDAVDLHRID LGPPISLERL DVGTNLGSAI AKLEDAKELL
ESSDQILRSM KGLSSTSIVY ILIAVCLGGL IGIPALICCC RGRCNKKGE
