FUS_RINDL
ID FUS_RINDL Reviewed; 546 AA.
AC P10864;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 91.
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 Rinderpest virus (strain L) (RDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=11243;
OH NCBI_TaxID=9915; Bos indicus (Zebu).
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=89462; Bubalus bubalis (Domestic water buffalo).
OH NCBI_TaxID=9925; Capra hircus (Goat).
OH NCBI_TaxID=9933; Gazella (gazelles).
OH NCBI_TaxID=9894; Giraffa camelopardalis (Giraffe).
OH NCBI_TaxID=9832; Hippopotamus.
OH NCBI_TaxID=9940; Ovis aries (Sheep).
OH NCBI_TaxID=9821; Suidae (pigs).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3285575; DOI=10.1016/0042-6822(88)90567-3;
RA Tsukiyama K., Yoshikawa Y., Yamanouchi K.;
RT "Fusion glycoprotein (F) of rinderpest virus: entire nucleotide sequence of
RT the F mRNA, and several features of the F protein.";
RL Virology 164:523-530(1988).
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 HN at the virion surface. Upon HN binding to its cellular
CC receptor, the hydrophobic fusion peptide is unmasked and interacts with
CC the 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}.
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DR EMBL; M20870; AAA47399.1; -; Genomic_RNA.
DR PIR; A28921; VGNZRL.
DR SMR; P10864; -.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..546
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000039357"
FT CHAIN 20..108
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000039358"
FT CHAIN 109..546
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039359"
FT TOPO_DOM 20..491
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 513..546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 109..133
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT COILED 134..162
FT /evidence="ECO:0000255"
FT COILED 458..483
FT /evidence="ECO:0000255"
FT SITE 108..109
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 64..191
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250"
FT DISULFID 330..339
FT /evidence="ECO:0000250"
FT DISULFID 354..362
FT /evidence="ECO:0000250"
FT DISULFID 386..391
FT /evidence="ECO:0000250"
FT DISULFID 393..416
FT /evidence="ECO:0000250"
SQ SEQUENCE 546 AA; 58911 MW; 985029418F28FFB5 CRC64;
MGILFAALLA MTNPHLATGQ IHWGNLSKIG VVGTGSASYK VMTQSSHQSL VIKLMPNITA
IDNCTKTEIM EYKRLLGTVL KPIREALNAI TKNIKPIQSS TTSRRHKRFA GVVLAGAALG
VATAAQITAG IALHQSMMNS QAIESLKASL ETTNQAIEEI RQAGQEMVLA VQGVQDYINN
ELVPAMGQLS CEIVGQKLGL KLLRYYTEIL SLFGPSLRDP VSAELSIQAL SYALGGDINK
ILEKLGYSGS DLLAILESKG IKAKITYVDI ESYFIVLSIA YPSLSEIKGV IVHRLESVSY
NIGSQEWYTT VPRYVATQGY LISNFDDTPC AFTPEGTICS QNAIYPMSPL LQECFRGSTR
SCARTLVLGS IGNRFILSKG NLIGNCASIL CKCYTTGSII SQDPDKILTY IAADQCPVVE
VGGVTIQVGS REYSDAVYLH EIDLGPPISL EKLDVGTNLW NAVTKLEKAK DLLDSSDLIL
ENIKGVSVTN TGYILVGVGL IAVVGILIIT CCCKKRRTDN KVSTMVLNPG LRPDLTGTSK
SYVRSL
