FUS_PHODV
ID FUS_PHODV Reviewed; 537 AA.
AC P28886;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 25-MAY-2022, entry version 98.
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 Phocine distemper virus (PDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=11240;
OH NCBI_TaxID=9709; Phocidae (true seals).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate DK88-4A;
RX PubMed=1765768; DOI=10.1099/0022-1317-72-12-2959;
RA Koevamees J., Blixenkrone-Moeller M., Sharma B., Oervell C., Norrby E.;
RT "The nucleotide sequence and deduced amino acid composition of the
RT haemagglutinin and fusion proteins of the morbillivirus phocid distemper
RT virus.";
RL J. Gen. Virol. 72:2959-2966(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Ulster/88;
RX PubMed=1524494; DOI=10.1007/bf01309692;
RA Curran M.D., Lu Y.J., Rima B.K.;
RT "The fusion protein gene of phocine distemper virus: nucleotide and deduced
RT amino acid sequences and a comparison of morbillivirus fusion proteins.";
RL Arch. Virol. 126:159-169(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Ulster/88;
RX PubMed=2264246;
RA Curran M.D., O'Loan D., Rima B.K., Kennedy S.;
RT "Nucleotide sequence analysis of phocine distemper virus reveals its
RT distinctness from canine distemper virus.";
RL Vet. Rec. 127:430-431(1990).
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=BAA01206.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D10371; BAA01206.1; ALT_INIT; Genomic_RNA.
DR PIR; A48346; A48346.
DR PIR; JQ1368; VGNZPD.
DR SMR; P28886; -.
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..10
FT /evidence="ECO:0000255"
FT CHAIN 11..537
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000039329"
FT CHAIN 11..99
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000039327"
FT CHAIN 100..537
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039328"
FT TOPO_DOM 11..483
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 100..124
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT COILED 125..153
FT /evidence="ECO:0000255"
FT COILED 449..474
FT /evidence="ECO:0000255"
FT SITE 99..100
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 55..182
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250"
FT DISULFID 321..330
FT /evidence="ECO:0000250"
FT DISULFID 345..353
FT /evidence="ECO:0000250"
FT DISULFID 377..382
FT /evidence="ECO:0000250"
FT DISULFID 384..407
FT /evidence="ECO:0000250"
SQ SEQUENCE 537 AA; 58295 MW; 31097C9C6085BF7C CRC64;
MVILVHCVMG QIHWTNLSTI GIIGTDSSHY KIMTRSSHQY LVLKLMPNVS IIDNCTKAEL
DEYEKLLNSV LEPINQALTL MTKNVKSLQS LGSGRRQRRF AGVVIAGAAL GVATAAQITA
GVALYQSNLN AQAIQSLRAS LEQSNKAIDE VRQASQNIII AVQGVQDYVN NEIVPALQHM
SCELIGQRLG LKLLRYYTEL LSVFGPSLRD PISAEISIQA LSYALGGEIH KILEKLGYSG
NDMVAILETK GIRAKITHVD LSGKFIVLSI SYPTLSEVKG VVVHRLEAVS YNIGSQEWYT
TVPRYVATNG YLISNFDESS CVFVSESAIC SQNSLYPMSP ILQQCLRGET ASCARTLVSG
TLGNKFILSK GNIIANCASI LCKCHSTSKI INQSPDKLLT FIASDTCSLV EIDGVTIQVG
SRQYPDVVYA SKVILGPAIS LERLDVGTNL GSALKKLDDA KVLIESSDQI LDTVKNSYLS
LGTLIALPVS IGLGLILLLL ICCCKKRYQH LFSQSTKVAP VFKPDLTGTS KSYVRSL
