ID   FUS_SV41                Reviewed;         561 AA.
AC   P25181;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 108.
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   Simian virus 41 (SV41).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC   Orthorubulavirus.
OX   NCBI_TaxID=2560766;
OH   NCBI_TaxID=314293; Simiiformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Toshiba/Chanock;
RX   PubMed=2173260; DOI=10.1016/0042-6822(90)90141-d;
RA   Tsurudome M., Bando H., Nishio M., Iwamoto Y., Kawano M., Kondo K.,
RA   Komada H., Ito Y.;
RT   "Antigenic and structural properties of a paramyxovirus simian virus 41
RT   (SV41) reveal a close relationship with human parainfluenza type 2 virus.";
RL   Virology 179:738-748(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Toshiba/Chanock;
RX   PubMed=1651608; DOI=10.1016/0042-6822(91)90825-v;
RA   Tsurudome M., Bando H., Kawano M., Matsumura H., Komada H., Nishio M.,
RA   Ito Y.;
RT   "Transcripts of simian virus 41 (SV41) matrix gene are exclusively
RT   dicistronic with the fusion gene which is also transcribed as a
RT   monocistron.";
RL   Virology 184:93-100(1991).
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; S48627; AAB19494.1; -; mRNA.
DR   EMBL; X64275; CAA45567.1; -; Genomic_RNA.
DR   EMBL; M62733; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   PIR; B40563; VGNZ41.
DR   SMR; P25181; -.
DR   Proteomes; UP000108270; Genome.
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   2: Evidence at transcript 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; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..561
FT                   /note="Fusion glycoprotein F0"
FT                   /id="PRO_0000039381"
FT   CHAIN           27..109
FT                   /note="Fusion glycoprotein F2"
FT                   /id="PRO_0000039382"
FT   CHAIN           110..561
FT                   /note="Fusion glycoprotein F1"
FT                   /id="PRO_0000039383"
FT   TOPO_DOM        27..495
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        496..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        517..561
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          110..134
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000250"
FT   COILED          135..163
FT                   /evidence="ECO:0000255"
FT   COILED          459..484
FT                   /evidence="ECO:0000255"
FT   SITE            109..110
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        359
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        434
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        440
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        464
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        71..192
FT                   /note="Interchain (between F2 and F1 chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        331..340
FT                   /evidence="ECO:0000250"
FT   DISULFID        355..363
FT                   /evidence="ECO:0000250"
FT   DISULFID        387..392
FT                   /evidence="ECO:0000250"
FT   DISULFID        394..417
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   561 AA;  59819 MW;  EEBA618D72418D9B CRC64;
     MRLTPYPIAL TTLMIALTTL PETGLGIARD ALSQVGVIQS KARSLMYYSD GSSSFIVVKL
     LPTLPTPSGN CNLTSITAYN TTLFKLLTPL MENLDTIVSA NQAGSRRKRF AGVVVGLAAL
     GVATAAQVTA AVAVVKANAN AAAINKLAAS IQSTNAAISD VISSTRTLAT AIQAVQDHVN
     GVLASGLTEA NCRSQDALIG SILNLYLTEL TTIFHNQIVN PALTPLSIQA LRIILGSTLP
     LIVESRWNTN LNTAELLSSG LLTGQIISIS PSYMQMVIQI TVPTFVMQPG AKIIDLVTIT
     ANRMEEEVLI QVPPRILEYA NEIQAYTADD CVVTPHAVFC KYNDGSPISD SLYQCLKGNL
     TSCVFTPVVG NYLKRFAFAN GVMYVNCKAL LCRCADPPMV ITQDDLAGIT VIDITVCREV
     MLDTLAFKIT SLNNVTYGAN FSMLAAAIKD LSPLDLSAQL AQVNKSLASA EEKIAQSSSL
     AAQAVSQEAT ITVGSVAMLI AVLALIAGCT GIMIAVQMSR RLEVLRHLTD QSIISNHHYA
     ELNPPPYNHS YESLHPIPQS H