ID   FUS_PI2HT               Reviewed;         551 AA.
AC   P26629;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 110.
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   Human parainfluenza 2 virus (strain Toshiba) (HPIV-2).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC   Orthorubulavirus; Human parainfluenza 2 virus.
OX   NCBI_TaxID=11214;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2167555; DOI=10.1016/0042-6822(90)90406-h;
RA   Kawano M., Bando H., Ohgimoto S., Kondo K., Tsurudome M., Nishio M.,
RA   Ito Y.;
RT   "Sequence of the fusion protein gene of human parainfluenza type 2 virus
RT   and its 3' intergenic region: lack of small hydrophobic (SH) gene.";
RL   Virology 178:289-292(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 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; M55698; AAA46842.1; -; Genomic_RNA.
DR   EMBL; X57559; CAA40786.1; -; Genomic_DNA.
DR   PIR; A37078; VGNZP2.
DR   SMR; P26629; -.
DR   Proteomes; UP000000472; 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   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; 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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..551
FT                   /note="Fusion glycoprotein F0"
FT                   /id="PRO_0000039339"
FT   CHAIN           24..106
FT                   /note="Fusion glycoprotein F2"
FT                   /id="PRO_0000039340"
FT   CHAIN           107..551
FT                   /note="Fusion glycoprotein F1"
FT                   /id="PRO_0000039341"
FT   TOPO_DOM        24..492
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        514..551
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          107..131
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000250"
FT   COILED          132..160
FT                   /evidence="ECO:0000255"
FT   COILED          456..481
FT                   /evidence="ECO:0000255"
FT   SITE            106..107
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        431
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        68..189
FT                   /note="Interchain (between F2 and F1 chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        328..337
FT                   /evidence="ECO:0000250"
FT   DISULFID        352..360
FT                   /evidence="ECO:0000250"
FT   DISULFID        384..389
FT                   /evidence="ECO:0000250"
FT   DISULFID        391..414
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   551 AA;  59721 MW;  3646780A0DA518B2 CRC64;
     MHHLHPMIVC IFVMYTGIVG SDAIAGDQLL NIGVIQSKIR SLMYYTDGGA SFIVVKLLPN
     LPPSNGTCNI TSLDAYNVTL FKLLTPLIEN LSKISTVTDT KTRQKRFAGV VVGLAALGVA
     TAAQITAAVA IVKANANAAA INNLASSIQS TNKAVSDVID ASRTIATAVQ AIQDRINGAI
     VNGITSASCR AHDALIGSIL NLYLTELTTI FHNQITNPAL TPLSIQALRI LLGSTLPIVI
     ESKLNTNFNT AELLSSGLLT GQIISISPMY MQMLIQINVP TFIMQPGAKV IDLIAISANH
     KLQEVVVQVP NRILEYANEL QNYPANDCVV TPNSVFCRYN EGSPIPESQY QCLRGNLNSC
     TFTPIIGNFL KRFAFANGVL YANCKSLLCR CADPPHVVSQ DDTQGISIID IKRCSEMMLD
     TFSFRITSTF NATYVTDFSM INANIVHLSP LDLSNQINSI NKSLKSAEDW IADSNFFANQ
     ARTAKTLYSL SAIALILSVI TLVVVGLLIA YIIKLVSQIH QFRSLAATTM FHRENPAFFS
     KNNHGNIYGI S