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Fusion glycoprotein F0 [Cleaved into: Fusion glycoprotein F2; Fusion glycoprotein F1]

 FUS_CDVO                Reviewed;         662 AA.
P12569; Q65991;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
10-MAY-2017, entry version 90.
RecName: Full=Fusion glycoprotein F0;
Contains:
RecName: Full=Fusion glycoprotein F2;
Contains:
RecName: Full=Fusion glycoprotein F1;
Flags: Precursor;
Name=F;
Canine distemper virus (strain Onderstepoort) (CDV).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Paramyxoviridae; Morbillivirus.
NCBI_TaxID=11233;
NCBI_TaxID=9646; Ailuropoda melanoleuca (Giant panda).
NCBI_TaxID=9649; Ailurus fulgens (Lesser panda) (Red panda).
NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
NCBI_TaxID=9665; Mustela.
NCBI_TaxID=9689; Panthera leo (Lion).
NCBI_TaxID=9654; Procyon lotor (Raccoon).
NCBI_TaxID=9704; Zalophus californianus (California sealion).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3433924; DOI=10.1016/0168-1702(87)90009-8;
Barrett T., Clarke D.K., Evans S.A., Rima B.K.;
"The nucleotide sequence of the gene encoding the F protein of canine
distemper virus: a comparison of the deduced amino acid sequence with
other paramyxoviruses.";
Virus Res. 8:373-386(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=8470428; DOI=10.1016/0264-410X(93)90285-6;
Wild T.F., Bernard A., Spehner D., Villeval D., Drillien R.;
"Vaccination of mice against canine distemper virus-induced
encephalitis with vaccinia virus recombinants encoding measles or
canine distemper virus antigens.";
Vaccine 11:438-444(1993).
[3]
CLEAVAGE OF N-TERMINUS.
PubMed=11932382; DOI=10.1128/JVI.76.9.4172-4180.2002;
von Messling V., Cattaneo R.;
"Amino-terminal precursor sequence modulates canine distemper virus
fusion protein function.";
J. Virol. 76:4172-4180(2002).
-!- FUNCTION: 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 H 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). {ECO:0000250}.
-!- SUBUNIT: Homotrimer of disulfide-linked F1-F2. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Host cell membrane
{ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
-!- PTM: The inactive precursor F0 is glycosylated and proteolytically
cleaved into F1 and F2 to be functionally active. The cleavage is
mediated by cellular proteases during the transport and maturation
of the polypeptide (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein
family. {ECO:0000305}.
-!- CAUTION: The N-terminal extension is not a classical signal
sequence. Its cleavage is post-translational and occurs before the
mature protein is transported to the cell surface. This unusual
signal sequence has a negative regulatory effect on F protein
activity. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M21849; AAA42878.1; -; Genomic_RNA.
EMBL; X65509; CAA46481.1; -; Genomic_RNA.
PIR; JS0321; VGNZCD.
PIR; S21382; S21382.
ProteinModelPortal; P12569; -.
SMR; P12569; -.
PRIDE; P12569; -.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
InterPro; IPR000776; Fusion_F0_Paramyxovir.
Pfam; PF00523; Fusion_gly; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
Fusion of virus membrane with host cell membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host membrane; Membrane; Signal; Transmembrane;
Transmembrane helix; Viral envelope protein;
Viral penetration into host cytoplasm; Virion;
Virus entry into host cell.
SIGNAL 1 135 {ECO:0000255}.
CHAIN 136 662 Fusion glycoprotein F0.
/FTId=PRO_0000039251.
CHAIN 136 224 Fusion glycoprotein F2.
/FTId=PRO_0000039249.
CHAIN 225 662 Fusion glycoprotein F1.
/FTId=PRO_0000039250.
TOPO_DOM 136 608 Extracellular. {ECO:0000250}.
TRANSMEM 609 629 Helical. {ECO:0000255}.
TOPO_DOM 630 662 Cytoplasmic. {ECO:0000250}.
REGION 225 249 Fusion peptide. {ECO:0000250}.
COILED 250 278 {ECO:0000255}.
COILED 574 599 {ECO:0000255}.
COMPBIAS 620 625 Poly-Leu.
SITE 224 225 Cleavage; by host. {ECO:0000250}.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 180 307 Interchain (between F2 and F1 chains).
{ECO:0000250}.
DISULFID 446 455 {ECO:0000250}.
DISULFID 470 478 {ECO:0000250}.
DISULFID 502 507 {ECO:0000250}.
DISULFID 509 532 {ECO:0000250}.
CONFLICT 3 3 R -> K (in Ref. 2; CAA46481).
{ECO:0000305}.
CONFLICT 140 140 D -> N (in Ref. 2; CAA46481).
{ECO:0000305}.
CONFLICT 152 152 N -> S (in Ref. 2; CAA46481).
{ECO:0000305}.
CONFLICT 171 171 I -> M (in Ref. 2; CAA46481).
{ECO:0000305}.
CONFLICT 174 174 A -> V (in Ref. 2; CAA46481).
{ECO:0000305}.
CONFLICT 662 662 L -> H (in Ref. 2; CAA46481).
{ECO:0000305}.
SEQUENCE 662 AA; 72971 MW; FB2C81C9797805F0 CRC64;
MHRGIPKSSK TQTHTQQDRP PQPSTELEET RTSRARHSTT SAQRSTHYDP RTSDRPVSYT
MNRTRSRKQT SHRLKNIPVH GNHEATIQHI PESVSKGARS QIERRQPNAI NSGSHCTWLV
LWCLGMASLF LCSKAQIHWD NLSTIGIIGT DNVHYKIMTR PSHQYLVIKL IPNASLIENC
TKAELGEYEK LLNSVLEPIN QALTLMTKNV KPLQSLGSGR RQRRFAGVVL AGVALGVATA
AQITAGIALH QSNLNAQAIQ SLRTSLEQSN KAIEEIREAT QETVIAVQGV QDYVNNELVP
AMQHMSCELV GQRLGLRLLR YYTELLSIFG PSLRDPISAE ISIQALIYAL GGEIHKILEK
LGYSGSDMIA ILESRGIKTK ITHVDLPGKF IILSISYPTL SEVKGVIVHR LEAVSYNIGS
QEWYTTVPRY IATNGYLISN FDESSCVFVS ESAICSQNSL YPMSPLLQQC IRGDTSSCAR
TLVSGTMGNK FILSKGNIVA NCASILCKCY STSTIINQSP DKLLTFIASD TCPLVEIDGA
TIQVGGRQYP DMVYEGKVAL GPAISLDRLD VGTNLGNALK KLDDAKVLID SSNQILETVR
RSSFNFGSLL SVPILSCTAL ALLLLIYCCK RRYQQTLKQH TKVDPAFKPD LTGTSKSYVR
SL


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