FUS_MEASC
ID FUS_MEASC Reviewed; 550 AA.
AC Q786F3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 40.
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 Measles virus (strain Ichinose-B95a) (MeV) (Subacute sclerose
OS panencephalitis virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=645098;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10949953; DOI=10.1023/a:1008196729676;
RA Takeuchi K., Miyajima N., Kobune F., Tashiro M.;
RT "Comparative nucleotide sequence analyses of the entire genomes of B95a
RT cell-isolated and vero cell-isolated measles viruses from the same
RT patient.";
RL Virus Genes 20:253-257(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 20-494, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-29 AND ASN-61.
RX PubMed=29463726; DOI=10.1073/pnas.1718957115;
RA Hashiguchi T., Fukuda Y., Matsuoka R., Kuroda D., Kubota M., Shirogane Y.,
RA Watanabe S., Tsumoto K., Kohda D., Plemper R.K., Yanagi Y.;
RT "Structures of the prefusion form of measles virus fusion protein in
RT complex with inhibitors.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:2496-2501(2018).
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 H at the virion surface. Upon HN binding to its cellular receptor,
CC the hydrophobic fusion peptide is unmasked and interacts with the
CC 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; AB016162; BAA34981.1; -; Genomic_RNA.
DR RefSeq; NP_056922.1; NC_001498.1.
DR PDB; 5YXW; X-ray; 2.78 A; A=20-112, B=113-494.
DR PDB; 5YZC; X-ray; 2.33 A; A=20-112, B=113-494.
DR PDB; 5YZD; X-ray; 2.64 A; A=20-112, C=113-494.
DR PDBsum; 5YXW; -.
DR PDBsum; 5YZC; -.
DR PDBsum; 5YZD; -.
DR SMR; Q786F3; -.
DR iPTMnet; Q786F3; -.
DR GeneID; 1489800; -.
DR KEGG; vg:1489800; -.
DR Proteomes; UP000008699; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..550
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000394714"
FT CHAIN 24..112
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000394715"
FT CHAIN 113..550
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000394716"
FT TOPO_DOM 24..494
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..550
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 113..137
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT COILED 138..166
FT /evidence="ECO:0000255"
FT COILED 462..487
FT /evidence="ECO:0000255"
FT SITE 112..113
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:29463726,
FT ECO:0007744|PDB:5YXW, ECO:0007744|PDB:5YZC,
FT ECO:0007744|PDB:5YZD"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:29463726,
FT ECO:0007744|PDB:5YXW, ECO:0007744|PDB:5YZC,
FT ECO:0007744|PDB:5YZD"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 68..195
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000269|PubMed:29463726,
FT ECO:0007744|PDB:5YXW, ECO:0007744|PDB:5YZC,
FT ECO:0007744|PDB:5YZD"
FT DISULFID 334..343
FT /evidence="ECO:0000250"
FT DISULFID 358..366
FT /evidence="ECO:0000250"
FT DISULFID 390..395
FT /evidence="ECO:0000250"
FT DISULFID 397..420
FT /evidence="ECO:0000250"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:5YXW"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:5YZC"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 35..57
FT /evidence="ECO:0007829|PDB:5YZC"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:5YZC"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:5YZC"
FT HELIX 70..95
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:5YZC"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:5YZC"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:5YZC"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:5YZC"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:5YXW"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:5YZC"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:5YZC"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:5YZC"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:5YZC"
FT HELIX 195..217
FT /evidence="ECO:0007829|PDB:5YZC"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:5YZC"
FT TURN 231..239
FT /evidence="ECO:0007829|PDB:5YZC"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:5YZC"
FT HELIX 256..262
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:5YZC"
FT TURN 274..277
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 278..301
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:5YZC"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:5YZC"
FT HELIX 353..359
FT /evidence="ECO:0007829|PDB:5YZC"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:5YZC"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:5YZC"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:5YZC"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 421..425
FT /evidence="ECO:0007829|PDB:5YZC"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:5YZC"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:5YZC"
FT HELIX 456..480
FT /evidence="ECO:0007829|PDB:5YZC"
SQ SEQUENCE 550 AA; 59532 MW; 7AA4F1CA82169093 CRC64;
MGLKVNVSAI FMAVLLTLQT PTGQIHWGNL SKIGVVGIGS ASYKVMTRSS HQSLVIKLMP
NITLLNNCTR VEIAEYRRLL RTVLEPIRDA LNAMTQNIRP VQSVASSRRH KRFAGVVLAG
AALGVATAAQ ITAGIALHQS MLNSQAIDNL RASLETTNQA IEAIRQAGQE MILAVQGVQD
YINNELIPSM NQLSCDLIGQ KLGLKLLRYY TEILSLFGPS LRDPISAEIS IQALSYALGG
DINKVLEKLG YSGGDLLGIL ESRGIKARIT HVDTESYFIV LSIAYPTLSE IKGVIVHRLE
GVSYNIGSQE WYTTVPKYVA TQGYLISNFD ESSCTFMPEG TVCSQNALYP MSPLLQECLR
GSTKSCARTL VSGSFGNRFI LSQGNLIANC ASILCKCYTT GTIINQDPDK ILTYIAADHC
PVVEVNGVTI QVGSRRYPDA VYLHRIDLGP PISLERLDVG TNLGNAIAKL EDAKELLESS
DQILRSMKGL SSTSIVYILI AVCLGGLIGI PALICCCRGR CNKKGEQVGM SRPGLKPDLT
GTSKSYVRSL
