ID   FUS_RINDK               Reviewed;         546 AA.
AC   P12574;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 97.
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 Kabete O) (RDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=11242;
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=3413983; DOI=10.1016/0042-6822(88)90156-0;
RA   Hsu D., Yamanaka M., Miller J., Dale B., Grubman M., Yilma T.;
RT   "Cloning of the fusion gene of rinderpest virus: comparative sequence
RT   analysis with other morbilliviruses.";
RL   Virology 166:149-153(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; M21514; AAA47400.1; -; Genomic_RNA.
DR   PIR; A31051; VGNZRK.
DR   SMR; P12574; -.
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_0000039354"
FT   CHAIN           20..108
FT                   /note="Fusion glycoprotein F2"
FT                   /id="PRO_0000039355"
FT   CHAIN           109..546
FT                   /note="Fusion glycoprotein F1"
FT                   /id="PRO_0000039356"
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;  58662 MW;  476D74DCC18BCFCF CRC64;
     MKILFATLLV VTTPHLVTGQ IHWGNLSKIG VVGTGSASYK VMTQSSHQTL VIKLMPNITA
     IDNCTKTEIE EYKRLLGTVL QPIKVALNAI TKNIKPIRSS TTSRRHRRFA GVALAGAALG
     VATAAQITAG IALHQSMMNT QAIESLKASL ETTNQAIEEI RQAGQEMILA VQGVQDYINN
     ELVPAMGQLS CDIVGQKLGL KLLRYYTEIL SLFGPSLRDP ISAEISIQAL SYALGGDINK
     ILEKLGYSGS DLLAILESKG IKAKITYVDI ESYFIVLSIA YPSLSEIKGV IIHALEGVSY
     NIGSQEWYTT VPRYVATQGY LISNFDDTPC AFTPEGTICS QNALYPMSPL LQECFRGSTR
     SCARTLVSGS IGNRFILSKG NLIANCASIL CKCYTTGSII SQDPDKILTY IAADQCPIVE
     VDGVTIQVGS REYPDAVYLH KIDLGPPISL EKLDVGTNLG NAVTKLEKAK DLLDSSDLIL
     ETIKGASVTN TGHILVGAGL IAVVGILIVT CCCRKRSNDS KVSTVILNPG LKPDLTGTSK
     SYVRSL