FUS_CDVO
ID FUS_CDVO Reviewed; 662 AA.
AC P12569; Q65991;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
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 Canine distemper virus (strain Onderstepoort) (CDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=11233;
OH NCBI_TaxID=9646; Ailuropoda melanoleuca (Giant panda).
OH NCBI_TaxID=9649; Ailurus fulgens (Lesser panda) (Red panda).
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH NCBI_TaxID=9665; Mustela.
OH NCBI_TaxID=9689; Panthera leo (Lion).
OH NCBI_TaxID=9654; Procyon lotor (Raccoon).
OH NCBI_TaxID=9704; Zalophus californianus (California sealion).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3433924; DOI=10.1016/0168-1702(87)90009-8;
RA Barrett T., Clarke D.K., Evans S.A., Rima B.K.;
RT "The nucleotide sequence of the gene encoding the F protein of canine
RT distemper virus: a comparison of the deduced amino acid sequence with other
RT paramyxoviruses.";
RL Virus Res. 8:373-386(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8470428; DOI=10.1016/0264-410x(93)90285-6;
RA Wild T.F., Bernard A., Spehner D., Villeval D., Drillien R.;
RT "Vaccination of mice against canine distemper virus-induced encephalitis
RT with vaccinia virus recombinants encoding measles or canine distemper virus
RT antigens.";
RL Vaccine 11:438-444(1993).
RN [3]
RP CLEAVAGE OF N-TERMINUS.
RX PubMed=11932382; DOI=10.1128/jvi.76.9.4172-4180.2002;
RA von Messling V., Cattaneo R.;
RT "Amino-terminal precursor sequence modulates canine distemper virus fusion
RT protein function.";
RL J. Virol. 76:4172-4180(2002).
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 -!- CAUTION: The N-terminal extension is not a classical signal sequence.
CC Its cleavage is post-translational and occurs before the mature protein
CC is transported to the cell surface. This unusual signal sequence has a
CC negative regulatory effect on F protein activity. {ECO:0000305}.
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DR EMBL; M21849; AAA42878.1; -; Genomic_RNA.
DR EMBL; X65509; CAA46481.1; -; Genomic_RNA.
DR PIR; JS0321; VGNZCD.
DR PIR; S21382; S21382.
DR SMR; P12569; -.
DR PRIDE; P12569; -.
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 1: Evidence at protein level;
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..135
FT /evidence="ECO:0000255"
FT CHAIN 136..662
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000039251"
FT CHAIN 136..224
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000039249"
FT CHAIN 225..662
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039250"
FT TOPO_DOM 136..608
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 630..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..249
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT COILED 250..278
FT /evidence="ECO:0000255"
FT COILED 574..599
FT /evidence="ECO:0000255"
FT COMPBIAS 8..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 224..225
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 180..307
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250"
FT DISULFID 446..455
FT /evidence="ECO:0000250"
FT DISULFID 470..478
FT /evidence="ECO:0000250"
FT DISULFID 502..507
FT /evidence="ECO:0000250"
FT DISULFID 509..532
FT /evidence="ECO:0000250"
FT CONFLICT 3
FT /note="R -> K (in Ref. 2; CAA46481)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="D -> N (in Ref. 2; CAA46481)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="N -> S (in Ref. 2; CAA46481)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="I -> M (in Ref. 2; CAA46481)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="A -> V (in Ref. 2; CAA46481)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="L -> H (in Ref. 2; CAA46481)"
FT /evidence="ECO:0000305"
SQ 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
