FUS_PI2HG
ID FUS_PI2HG Reviewed; 551 AA.
AC P27286;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 92.
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 Greer) (HPIV-2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Orthorubulavirus; Human parainfluenza 2 virus.
OX NCBI_TaxID=11213;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1846648; DOI=10.1099/0022-1317-72-1-89;
RA Varsanyi T.M., Koevamees J., Norrby E.;
RT "Molecular cloning and sequence analysis of human parainfluenza type 2
RT virus mRNA encoding the fusion glycoprotein.";
RL J. Gen. Virol. 72:89-95(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 PIR; A38509; VGNZPG.
DR SMR; P27286; -.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..551
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000039336"
FT CHAIN 24..106
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000039337"
FT CHAIN 107..551
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039338"
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; 59624 MW; F204D743083F809B CRC64;
MHHLHPMIVC IFVMYTGIVG SDAIAGDQLL NIGVIQSKIR SLMYYTDGGA SFIVVKLLPN
LPPSNGTCNI TSLDAYNVTL FKLLTPLIEN LSKISTVTDT KTRQKRFAGV VVGLAALGVA
TAAQITAAVA IVKANANAAA INNLASSIQS TNKAVSDVID ASRTIATAVQ AIQDHINGAI
VNGITSASCR AHDALIGSIL NLYLTELTTI FHNQITNPAL TPLSIQALRI LLGSTLPIVI
ESKLNTNLNT AELLSSGLLT GQIISISPMY MQMLIQINVP TFIMQPGAKV IDLIAISANH
KLQEVVVQVP NRILEYANEL QNYPANDCVV TPNSVCCRYN EGSPIPESQY QCLRGNLNSC
TFTPIIGNFL KRFAFANGVL YANCKSLLCR CADPPHVVSQ DDTQGISIID IKRCSEMMLD
TFSFRITSTF NATYVTDFSM INANIVHLSP LDLSNQINSI NKSLKSAEDW IADSNFFANQ
ARTAKTLYSL SAIALILSVI TLVVVGLLIA YIIKLVSQIH QFRSLAATTM FHRENPAFFS
KNNHGNIYGI S
