FUS_MUMPM
ID FUS_MUMPM Reviewed; 538 AA.
AC P11236; Q783V9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, 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 Mumps virus (strain Miyahara vaccine) (MuV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Orthorubulavirus; Mumps orthorubulavirus.
OX NCBI_TaxID=11171;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2762156; DOI=10.1093/nar/17.14.5839;
RA Takeuchi K., Tanahayashi K., Hishiyama M., Yamada A., Sugiura A.;
RT "Cloning and sequencing of the fusion protein gene of mumps virus (Miyahara
RT strain).";
RL Nucleic Acids Res. 17:5839-5839(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1585659; DOI=10.1016/0042-6822(92)90555-4;
RA Okazaki K., Tanabayashi K., Takeuchi K., Hishiyama M., Okazaki K.,
RA Yamada A.;
RT "Molecular cloning and sequence analysis of the mumps virus gene encoding
RT the L protein and the trailer sequence.";
RL Virology 188:926-930(1992).
RN [3]
RP PROCESSING, AND INTERACTION WITH HOST LAMP1; LAMP2 AND LAMP3.
RX PubMed=32295904; DOI=10.1128/jvi.00050-20;
RA Ueo A., Kubota M., Shirogane Y., Ohno S., Hashiguchi T., Yanagi Y.;
RT "Lysosome-Associated Membrane Proteins Support the Furin-Mediated
RT Processing of the Mumps Virus Fusion Protein.";
RL J. Virol. 94:0-0(2020).
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. Interacts with host
CC LAMP1; LAMP2 and LAMP3; these interactions promote the cleavage of the
CC viral fusion protein F. {ECO:0000269|PubMed:32295904}.
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 including host FURIN during the
CC transport and maturation of the polypeptide.
CC {ECO:0000269|PubMed:32295904}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; X15285; CAA33359.1; -; mRNA.
DR EMBL; AB040874; BAA94388.1; -; Genomic_RNA.
DR PIR; A34062; VGNZMM.
DR PDB; 2FYZ; X-ray; 2.20 A; A/C/E=124-181, B/D/F=447-485.
DR PDBsum; 2FYZ; -.
DR SMR; P11236; -.
DR EvolutionaryTrace; P11236; -.
DR Proteomes; UP000002331; 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 3D-structure; Cleavage on pair of basic residues; Coiled coil;
KW Disulfide bond; 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..19
FT /evidence="ECO:0000250"
FT CHAIN 20..538
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000039279"
FT CHAIN 20..102
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000039280"
FT CHAIN 103..538
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039281"
FT TOPO_DOM 20..486
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 103..127
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT COILED 128..156
FT /evidence="ECO:0000255"
FT COILED 452..477
FT /evidence="ECO:0000255"
FT SITE 102..103
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 64..185
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250"
FT DISULFID 324..333
FT /evidence="ECO:0000250"
FT DISULFID 348..356
FT /evidence="ECO:0000250"
FT DISULFID 380..385
FT /evidence="ECO:0000250"
FT DISULFID 387..410
FT /evidence="ECO:0000250"
FT HELIX 126..173
FT /evidence="ECO:0007829|PDB:2FYZ"
FT TURN 174..178
FT /evidence="ECO:0007829|PDB:2FYZ"
FT HELIX 449..474
FT /evidence="ECO:0007829|PDB:2FYZ"
FT TURN 475..478
FT /evidence="ECO:0007829|PDB:2FYZ"
SQ SEQUENCE 538 AA; 58712 MW; C2589DE460C40F67 CRC64;
MKVFLVTCLG FAVFSSSVCV NINILQQIGY IKQQVRQLSY YSQSSSSYIV VKLLPNIQPT
DNSCEFKSVT QYNKTLSNLL LPIAENINNI ASPSSGSRRH KRFAGIAIGI AALGVATAAQ
VTAAVSLVQA QTNARAIAAM KNSIQATNRA VFEVKEGTQR LAIAVQAIQD HINTIMNTQL
NNMSCQILDN QLATSLGLYL TELTTVFQPQ LINPALSPIS IQALRSLLGS MTPAVVQATL
STSISAAEIL SAGLMEGQIV SVLLDEMQMI VKINIPTIVT QSNALVIDFY SISSFINNQE
SIIQLPDRIL EIGNEQWSYP AKNCKLTRHH IFCQYNEAER LSLESKLCLA GNISACVFSP
IAGSYMRRFV ALDGTIVANC RSLTCLCKSP SYPIYQPDHH AVTTIDLTAC QTLSLDGLDF
SIVSLSNITY AENLTISLSQ TINTQPIDIS TELSKVNASL QNAVKYIKES NHQLQSVNVN
SKIGAIIVAA LVLSILSIII SLLFCCWAYV ATKEIRRINF KTNHINTISS SVDDLIRY
