FUS_HMPVC
ID FUS_HMPVC Reviewed; 539 AA.
AC Q6WB98;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Fusion glycoprotein F0;
DE Short=Protein F;
DE Contains:
DE RecName: Full=Fusion glycoprotein F2;
DE Contains:
DE RecName: Full=Fusion glycoprotein F1;
DE Flags: Precursor;
GN Name=F;
OS Human metapneumovirus (strain CAN97-83) (HMPV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Metapneumovirus.
OX NCBI_TaxID=694067;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=14592754; DOI=10.1016/s0042-6822(03)00528-2;
RA Biacchesi S., Skiadopoulos M.H., Boivin G., Hanson C.T., Murphy B.R.,
RA Collins P.L., Buchholz U.J.;
RT "Genetic diversity between human metapneumovirus subgroups.";
RL Virology 315:1-9(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16306583; DOI=10.1128/jvi.79.24.15114-15122.2005;
RA Pham Q.N., Biacchesi S., Skiadopoulos M.H., Murphy B.R., Collins P.L.,
RA Buchholz U.J.;
RT "Chimeric recombinant human metapneumoviruses with the nucleoprotein or
RT phosphoprotein open reading frame replaced by that of avian metapneumovirus
RT exhibit improved growth in vitro and attenuation in vivo.";
RL J. Virol. 79:15114-15122(2005).
RN [3]
RP INTERACTION WITH HOST ITGAV/ITGB1 INTEGRIN.
RX PubMed=19164533; DOI=10.1073/pnas.0801433106;
RA Cseke G., Maginnis M.S., Cox R.G., Tollefson S.J., Podsiad A.B.,
RA Wright D.W., Dermody T.S., Williams J.V.;
RT "Integrin alphavbeta1 promotes infection by human metapneumovirus.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1566-1571(2009).
RN [4]
RP FUNCTION.
RX PubMed=22238303; DOI=10.1128/jvi.06706-11;
RA Chang A., Masante C., Buchholz U.J., Dutch R.E.;
RT "Human metapneumovirus (HMPV) binding and infection are mediated by
RT interactions between the HMPV fusion protein and heparan sulfate.";
RL J. Virol. 86:3230-3243(2012).
CC -!- FUNCTION: [Fusion glycoprotein F0]: Inactive precursor that is cleaved
CC to give rise to the mature F1 and F2 fusion glycoproteins.
CC {ECO:0000250|UniProtKB:P03420}.
CC -!- FUNCTION: [Fusion glycoprotein F1]: Class I viral fusion protein. Under
CC the current model, the protein has at least 3 conformational states:
CC pre-fusion native state, pre-hairpin intermediate state, and post-
CC fusion hairpin state. During viral and plasma cell membrane fusion, the
CC coiled coil regions assume a trimer-of-hairpins structure, positioning
CC the fusion peptide in close proximity to the C-terminal region of the
CC ectodomain. The formation of this structure appears to drive apposition
CC and subsequent fusion of viral and cellular membranes leading to
CC delivery of the nucleocapsid into the cytoplasm. This fusion is pH
CC independent and occurs at the plasma or endosomal membrane. The trimer
CC of F1-F2 (F protein) also facilitates the attachment to host cell by
CC binding to host heparan sulfate. {ECO:0000250|UniProtKB:P03420}.
CC -!- FUNCTION: [Fusion glycoprotein F2]: Major determinant of the species
CC specificity of RSV infection (By similarity). The trimer of F1-F2 (F
CC protein) also facilitates the attachment to host cell by binding to
CC host heparan sulfate (PubMed:22238303). {ECO:0000250|UniProtKB:P03420,
CC ECO:0000269|PubMed:22238303}.
CC -!- SUBUNIT: [Fusion glycoprotein F1]: Homotrimer. Heterodimer with fusion
CC protein F2; disulfide-linked. As a heterodimer with F2, interacts with
CC host heparan sulfate (PubMed:22238303). As a heterodimer with F2,
CC interacts with host integrin ITGAV/ITGB1 (PubMed:19164533). Part of a
CC complex composed of F1, F2 and G glycoproteins (By similarity).
CC {ECO:0000250|UniProtKB:P03420, ECO:0000269|PubMed:19164533,
CC ECO:0000269|PubMed:22238303}.
CC -!- SUBUNIT: [Fusion glycoprotein F2]: Homotrimer. Heterodimer with fusion
CC protein F1; disulfide-linked. As a heterodimer with F1, interacts with
CC host heparan sulfate (PubMed:22238303). As a heterodimer with F2,
CC interacts with host integrin ITGAV/ITGB1 (PubMed:19164533). Part of a
CC complex composed of F1, F2 and G glycoproteins (By similarity).
CC {ECO:0000250|UniProtKB:P03420, ECO:0000269|PubMed:19164533,
CC ECO:0000269|PubMed:22238303}.
CC -!- SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane
CC protein. Host cell membrane {ECO:0000250}; Single-pass membrane protein
CC {ECO:0000250}.
CC -!- DOMAIN: [Fusion glycoprotein F0]: The N-terminus is a hydrophobic
CC fusion peptide that inserts into the target host membrane (By
CC similarity). It is buried in the center of the trimer cavity before
CC cleavage. The coiled coil (heptad repeat) regions are probably involved
CC in homotrimerization, heterodimerization and in the formation of a
CC fusion-active hairpin structure (By similarity).
CC {ECO:0000250|UniProtKB:P03420, ECO:0000250|UniProtKB:P11209}.
CC -!- DOMAIN: [Fusion glycoprotein F1]: The N-terminus is a hydrophobic
CC fusion peptide that inserts into the target host membrane (By
CC similarity). It is buried in the center of the trimer cavity before
CC cleavage. The coiled coil (heptad repeat) regions are probably involved
CC in homotrimerization, heterodimerization and in the formation of a
CC fusion-active hairpin structure (By similarity).
CC {ECO:0000250|UniProtKB:P03420, ECO:0000250|UniProtKB:P11209}.
CC -!- PTM: [Fusion glycoprotein F0]: The F glycoprotein is synthesized as a
CC F0 inactive precursor that is heavily N-glycosylated and processed.
CC {ECO:0000250|UniProtKB:P03420}.
CC -!- MISCELLANEOUS: The cleavage peptide sequence for the hMPV F protein
CC (RQSR) varies from the one described for other pneumoviruses, and
CC differs from the furin protease motif (R/K-X-R/K-R). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY297749; AAQ67695.1; -; Genomic_RNA.
DR RefSeq; YP_012608.1; NC_004148.2.
DR SMR; Q6WB98; -.
DR PRIDE; Q6WB98; -.
DR ABCD; Q6WB98; 1 sequenced antibody.
DR Proteomes; UP000001398; 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 1: Evidence at protein level;
KW Cleavage on pair of basic residues; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..539
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000394806"
FT CHAIN 20..102
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000394807"
FT CHAIN 103..539
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000394808"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 103..127
FT /note="Fusion peptide"
FT /evidence="ECO:0000250|UniProtKB:P11209"
FT REGION 520..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 329..331
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 28..407
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 60..182
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 283..311
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 292..301
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 326..335
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 350..361
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 384..390
FT /evidence="ECO:0000250|UniProtKB:P03420"
SQ SEQUENCE 539 AA; 58477 MW; 2987E611786A64BA CRC64;
MSWKVVIIFS LLITPQHGLK ESYLEESCST ITEGYLSVLR TGWYTNVFTL EVGDVENLTC
SDGPSLIKTE LDLTKSALRE LKTVSADQLA REEQIENPRQ SRFVLGAIAL GVATAAAVTA
GVAIAKTIRL ESEVTAIKNA LKTTNEAVST LGNGVRVLAT AVRELKDFVS KNLTRAINKN
KCDIDDLKMA VSFSQFNRRF LNVVRQFSDN AGITPAISLD LMTDAELARA VSNMPTSAGQ
IKLMLENRAM VRRKGFGILI GVYGSSVIYM VQLPIFGVID TPCWIVKAAP SCSGKKGNYA
CLLREDQGWY CQNAGSTVYY PNEKDCETRG DHVFCDTAAG INVAEQSKEC NINISTTNYP
CKVSTGRHPI SMVALSPLGA LVACYKGVSC SIGSNRVGII KQLNKGCSYI TNQDADTVTI
DNTVYQLSKV EGEQHVIKGR PVSSSFDPIK FPEDQFNVAL DQVFENIENS QALVDQSNRI
LSSAEKGNTG FIIVIILIAV LGSSMILVSI FIIIKKTKKP TGAPPELSGV TNNGFIPHS
