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Fusion glycoprotein F0 (Protein F) [Cleaved into: Fusion glycoprotein F2'; Interchain peptide; Fusion glycoprotein F2; Fusion glycoprotein F1]

 FUS_HRSVA               Reviewed;         574 AA.
P03420; P88811;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 115.
RecName: Full=Fusion glycoprotein F0;
Short=Protein F;
Contains:
RecName: Full=Fusion glycoprotein F2' {ECO:0000305|PubMed:11493675};
Contains:
RecName: Full=Interchain peptide {ECO:0000305|PubMed:11493675};
Contains:
RecName: Full=Fusion glycoprotein F2;
Contains:
RecName: Full=Fusion glycoprotein F1;
Flags: Precursor;
Name=F;
Human respiratory syncytial virus A (strain A2).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Pneumoviridae; Orthopneumovirus.
NCBI_TaxID=11259;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6096849; DOI=10.1073/pnas.81.24.7683;
Collins P.L., Huang Y.T., Wertz G.W.;
"Nucleotide sequence of the gene encoding the fusion (F) glycoprotein
of human respiratory syncytial virus.";
Proc. Natl. Acad. Sci. U.S.A. 81:7683-7687(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Cold-passage attenuated;
PubMed=8918930; DOI=10.1006/viro.1996.0618;
Firestone C.Y., Whitehead S.S., Collins P.L., Murphy B.R.,
Crowe J.E. Jr.;
"Nucleotide sequence analysis of the respiratory syncytial virus
subgroup A cold-passaged (cp) temperature sensitive (ts) cpts-248/404
live attenuated virus vaccine candidate.";
Virology 225:419-422(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Cold-passage attenuated;
PubMed=9035372; DOI=10.1007/BF00366988;
Crowe J.E. Jr., Firestone C.Y., Whitehead S.S., Collins P.L.,
Murphy B.R.;
"Acquisition of the ts phenotype by a chemically mutagenized cold-
passaged human respiratory syncytial virus vaccine candidate results
from the acquisition of a single mutation in the polymerase (L)
gene.";
Virus Genes 13:269-273(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Cold-passage attenuated;
PubMed=7747420; DOI=10.1006/viro.1995.1178;
Connors M., Crowe J.E. Jr., Firestone C.Y., Murphy B.R., Collins P.L.;
"A cold-passaged, attenuated strain of human respiratory syncytial
virus contains mutations in the F and L genes.";
Virology 208:478-484(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Cold-passage attenuated;
PubMed=9557743;
Whitehead S.S., Juhasz K., Firestone C.Y., Collins P.L., Murphy B.R.;
"Recombinant respiratory syncytial virus (RSV) bearing a set of
mutations from cold-passaged RSV is attenuated in chimpanzees.";
J. Virol. 72:4467-4471(1998).
[6]
PALMITOYLATION AT CYS-550.
PubMed=2732224;
Arumugham R.G., Seid R.C. Jr., Doyle S., Hildreth S.W.,
Paradisio P.R.;
"Fatty acid acylation of the fusion glycoprotein of human respiratory
syncytial virus.";
J. Biol. Chem. 264:10339-10342(1989).
[7]
INTERACTION WITH HOST RHOA.
PubMed=10438814;
Pastey M.K., Crowe J.E. Jr., Graham B.S.;
"RhoA interacts with the fusion glycoprotein of respiratory syncytial
virus and facilitates virus-induced syncytium formation.";
J. Virol. 73:7262-7270(1999).
[8]
INTERACTION WITH HEPARAN SULFATE.
PubMed=10864656; DOI=10.1128/JVI.74.14.6442-6447.2000;
Feldman S.A., Audet S., Beeler J.A.;
"The fusion glycoprotein of human respiratory syncytial virus
facilitates virus attachment and infectivity via an interaction with
cellular heparan sulfate.";
J. Virol. 74:6442-6447(2000).
[9]
HOMOTRIMERIZATION.
PubMed=10846072; DOI=10.1128/JVI.74.13.5911-5920.2000;
Matthews J.M., Young T.F., Tucker S.P., Mackay J.P.;
"The core of the respiratory syncytial virus fusion protein is a
trimeric coiled coil.";
J. Virol. 74:5911-5920(2000).
[10]
CLEAVAGE BY HOST FURIN.
PubMed=11369882;
Sugrue R.J., Brown C., Brown G., Aitken J., McL Rixon H.W.;
"Furin cleavage of the respiratory syncytial virus fusion protein is
not a requirement for its transport to the surface of virus-infected
cells.";
J. Gen. Virol. 82:1375-1386(2001).
[11]
CLEAVAGE.
PubMed=11493675; DOI=10.1073/pnas.151098198;
Gonzalez-Reyes L., Ruiz-Argueello M.B., Garcia-Barreno B., Calder L.,
Lopez J.A., Albar J.P., Skehel J.J., Wiley D.C., Melero J.A.;
"Cleavage of the human respiratory syncytial virus fusion protein at
two distinct sites is required for activation of membrane fusion.";
Proc. Natl. Acad. Sci. U.S.A. 98:9859-9864(2001).
[12]
FUNCTION IN HOST CELL SPECIFICITY.
PubMed=12663767; DOI=10.1128/JVI.77.8.4609-4616.2003;
Schlender J., Zimmer G., Herrler G., Conzelmann K.K.;
"Respiratory syncytial virus (RSV) fusion protein subunit F2, not
attachment protein G, determines the specificity of RSV infection.";
J. Virol. 77:4609-4616(2003).
[13]
SUBCELLULAR LOCATION.
PubMed=16160180; DOI=10.1128/JVI.79.19.12528-12535.2005;
Brock S.C., Heck J.M., McGraw P.A., Crowe J.E. Jr.;
"The transmembrane domain of the respiratory syncytial virus F protein
is an orientation-independent apical plasma membrane sorting
sequence.";
J. Virol. 79:12528-12535(2005).
[14]
FUNCTION IN APOPTOSIS.
PubMed=18216092; DOI=10.1128/JVI.01887-07;
Eckardt-Michel J., Lorek M., Baxmann D., Grunwald T., Keil G.M.,
Zimmer G.;
"The fusion protein of respiratory syncytial virus triggers p53-
dependent apoptosis.";
J. Virol. 82:3236-3249(2008).
[15]
INTERACTION WITH GLYCOPROTEIN G.
PubMed=18036342; DOI=10.1016/j.bbrc.2007.11.042;
Low K.W., Tan T., Ng K., Tan B.H., Sugrue R.J.;
"The RSV F and G glycoproteins interact to form a complex on the
surface of infected cells.";
Biochem. Biophys. Res. Commun. 366:308-313(2008).
[16]
FUNCTION.
PubMed=23593008; DOI=10.1371/journal.ppat.1003309;
Krzyzaniak M.A., Zumstein M.T., Gerez J.A., Picotti P., Helenius A.;
"Host cell entry of respiratory syncytial virus involves
macropinocytosis followed by proteolytic activation of the F
protein.";
PLoS Pathog. 9:E1003309-E1003309(2013).
[17]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 254-277.
PubMed=20098425; DOI=10.1038/nsmb.1723;
McLellan J.S., Chen M., Kim A., Yang Y., Graham B.S., Kwong P.D.;
"Structural basis of respiratory syncytial virus neutralization by
motavizumab.";
Nat. Struct. Mol. Biol. 17:248-250(2010).
[18]
X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 159-209 OF 482-520.
PubMed=19966279; DOI=10.1073/pnas.0910108106;
Roymans D., De Bondt H.L., Arnoult E., Geluykens P., Gevers T.,
Van Ginderen M., Verheyen N., Kim H., Willebrords R., Bonfanti J.F.,
Bruinzeel W., Cummings M.D., van Vlijmen H., Andries K.;
"Binding of a potent small-molecule inhibitor of six-helix bundle
formation requires interactions with both heptad-repeats of the RSV
fusion protein.";
Proc. Natl. Acad. Sci. U.S.A. 107:308-313(2010).
[19]
X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF 26-109 OF 147-513.
PubMed=21613394; DOI=10.1128/JVI.00555-11;
McLellan J.S., Yang Y., Graham B.S., Kwong P.D.;
"Structure of respiratory syncytial virus fusion glycoprotein in the
postfusion conformation reveals preservation of neutralizing
epitopes.";
J. Virol. 85:7788-7796(2011).
[20]
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-524.
PubMed=21586636; DOI=10.1073/pnas.1106536108;
Swanson K.A., Settembre E.C., Shaw C.A., Dey A.K., Rappuoli R.,
Mandl C.W., Dormitzer P.R., Carfi A.;
"Structural basis for immunization with postfusion respiratory
syncytial virus fusion F glycoprotein (RSV F) to elicit high
neutralizing antibody titers.";
Proc. Natl. Acad. Sci. U.S.A. 108:9619-9624(2011).
[21]
X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 26-513.
PubMed=23618766; DOI=10.1126/science.1234914;
McLellan J.S., Chen M., Leung S., Graepel K.W., Du X., Yang Y.,
Zhou T., Baxa U., Yasuda E., Beaumont T., Kumar A., Modjarrad K.,
Zheng Z., Zhao M., Xia N., Kwong P.D., Graham B.S.;
"Structure of RSV fusion glycoprotein trimer bound to a prefusion-
specific neutralizing antibody.";
Science 340:1113-1117(2013).
[22]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 26-107 OF 137-513.
PubMed=24179220; DOI=10.1126/science.1243283;
McLellan J.S., Chen M., Joyce M.G., Sastry M., Stewart-Jones G.B.,
Yang Y., Zhang B., Chen L., Srivatsan S., Zheng A., Zhou T.,
Graepel K.W., Kumar A., Moin S., Boyington J.C., Chuang G.Y., Soto C.,
Baxa U., Bakker A.Q., Spits H., Beaumont T., Zheng Z., Xia N.,
Ko S.Y., Todd J.P., Rao S., Graham B.S., Kwong P.D.;
"Structure-based design of a fusion glycoprotein vaccine for
respiratory syncytial virus.";
Science 342:592-598(2013).
-!- FUNCTION: During virus entry, induces fusion of viral and cellular
membranes leading to delivery of the nucleocapsid into the
cytoplasm. The fusogenic activity is inactive untill entry into
host cell endosome, where a furin-like protease cleaves off a
small peptide between F1 and F2 (PubMed:18216092). Interacts
directly with heparan sulfate and may participate in virus
attachment (PubMed:10864656). Furthermore, the F2 subunit was
identifed as the major determinant of RSV host cell specificity
(PubMed:11493675). Later in infection, proteins F expressed at the
plasma membrane of infected cells can mediate fusion with adjacent
cells to form syncytia, a cytopathic effect that could lead to
tissue necrosis. The fusion protein is also able to trigger p53-
dependent apoptosis (PubMed:12663767).
{ECO:0000269|PubMed:10864656, ECO:0000269|PubMed:11493675,
ECO:0000269|PubMed:12663767, ECO:0000269|PubMed:18216092,
ECO:0000269|PubMed:23593008}.
-!- SUBUNIT: Homotrimer (PubMed:10846072). Interacts with glycoprotein
G (PubMed:18036342). Interacts with host RHOA; this interaction
facilitates virus-induced syncytium formation (PubMed:10438814).
{ECO:0000269|PubMed:10438814, ECO:0000269|PubMed:10846072,
ECO:0000269|PubMed:10864656, ECO:0000269|PubMed:18036342}.
-!- INTERACTION:
Self; NbExp=8; IntAct=EBI-10042897, EBI-10042897;
-!- SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane
protein. Host cell membrane; Single-pass membrane protein
{ECO:0000269|PubMed:16160180}.
-!- PTM: The F glycoprotein is synthesized as a F0 inactive precursor
that is heavily N-glycosylated and processed by host cell furin in
the Golgi to yield the mature F1 and F2 proteins
(PubMed:11369882). The cleavage site between F1 and F2 requires
the minimal sequence [KR]-X-[KR]-R. During entry a furin-like
protease cleaves F2 into F2' and a small peptide, leading to the
activation of fusogenic function (PubMed:23593008).
{ECO:0000269|PubMed:11369882, ECO:0000269|PubMed:23593008}.
-!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein
family. {ECO:0000305}.
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EMBL; M11486; AAB59858.1; -; Genomic_RNA.
EMBL; U50362; AAB86664.1; -; Genomic_RNA.
EMBL; U50363; AAB86676.1; -; Genomic_RNA.
EMBL; AF035006; AAC14902.1; -; Genomic_RNA.
EMBL; U63644; AAC55970.1; -; Genomic_RNA.
PIR; A04035; VGNZA2.
PIR; B28929; B28929.
PDB; 2MDP; NMR; -; A=1-85.
PDB; 3IXT; X-ray; 2.75 A; C/P=254-277.
PDB; 3KPE; X-ray; 1.47 A; A=159-209, B=482-520.
PDB; 3O41; X-ray; 1.95 A; C/P=423-436.
PDB; 3O45; X-ray; 2.87 A; C/P=423-438.
PDB; 3RKI; X-ray; 3.20 A; A/B/C=1-524.
PDB; 3RRR; X-ray; 2.82 A; A/C/E/G/I/M=26-109, B/D/F/H/L/N=147-513.
PDB; 3RRT; X-ray; 3.20 A; A/C/E=26-109, B/D/F=147-513.
PDB; 4CCF; X-ray; 2.65 A; A/B/C/D/E/F=1-574.
PDB; 4JHW; X-ray; 3.60 A; F=26-513.
PDB; 4MMQ; X-ray; 3.25 A; A=26-107, B=137-513.
PDB; 4MMR; X-ray; 3.10 A; A=26-107, B=137-513.
PDB; 4MMS; X-ray; 2.40 A; A/C/E=26-107, B/D/F=137-513.
PDB; 4MMT; X-ray; 3.05 A; A=26-107, B=137-513.
PDB; 4MMU; X-ray; 3.00 A; A=26-107, B=137-513.
PDB; 4MMV; X-ray; 2.81 A; A=26-107, B=137-513.
PDB; 4ZYP; X-ray; 5.50 A; A/B/C=26-513.
PDB; 5C69; X-ray; 2.30 A; A=26-513.
PDB; 5C6B; X-ray; 2.40 A; F=26-108, F=113-513.
PDB; 5EA3; X-ray; 2.75 A; F=1-513.
PDB; 5EA4; X-ray; 2.30 A; F=1-513.
PDB; 5EA5; X-ray; 3.05 A; F=1-513.
PDB; 5EA6; X-ray; 2.75 A; F=1-513.
PDB; 5EA7; X-ray; 2.85 A; F=1-513.
PDB; 5EA8; X-ray; 2.60 A; F=1-513.
PDB; 5J3D; X-ray; 4.08 A; E/G/J=26-98, F/I/K=147-513.
PDB; 5K6B; X-ray; 2.98 A; F=26-105, F=145-509.
PDB; 5K6C; X-ray; 3.58 A; F=26-103, F=145-509.
PDB; 5K6F; X-ray; 2.59 A; F=26-101, F=145-509.
PDB; 5K6G; X-ray; 2.90 A; F=26-96, F=145-509.
PDB; 5K6H; X-ray; 2.65 A; F=26-103, F=145-509.
PDB; 5K6I; X-ray; 2.92 A; F=26-101, F=145-509.
PDB; 5TOJ; X-ray; 3.30 A; A/B/C=1-513.
PDB; 5TOK; X-ray; 3.80 A; A/B/C=1-513.
PDB; 5TPN; X-ray; 3.14 A; A=27-108, A=113-513.
PDB; 5U68; X-ray; 3.08 A; A/B/C=1-513.
PDB; 5UDC; X-ray; 3.45 A; A/D/F=1-513.
PDBsum; 2MDP; -.
PDBsum; 3IXT; -.
PDBsum; 3KPE; -.
PDBsum; 3O41; -.
PDBsum; 3O45; -.
PDBsum; 3RKI; -.
PDBsum; 3RRR; -.
PDBsum; 3RRT; -.
PDBsum; 4CCF; -.
PDBsum; 4JHW; -.
PDBsum; 4MMQ; -.
PDBsum; 4MMR; -.
PDBsum; 4MMS; -.
PDBsum; 4MMT; -.
PDBsum; 4MMU; -.
PDBsum; 4MMV; -.
PDBsum; 4ZYP; -.
PDBsum; 5C69; -.
PDBsum; 5C6B; -.
PDBsum; 5EA3; -.
PDBsum; 5EA4; -.
PDBsum; 5EA5; -.
PDBsum; 5EA6; -.
PDBsum; 5EA7; -.
PDBsum; 5EA8; -.
PDBsum; 5J3D; -.
PDBsum; 5K6B; -.
PDBsum; 5K6C; -.
PDBsum; 5K6F; -.
PDBsum; 5K6G; -.
PDBsum; 5K6H; -.
PDBsum; 5K6I; -.
PDBsum; 5TOJ; -.
PDBsum; 5TOK; -.
PDBsum; 5TPN; -.
PDBsum; 5U68; -.
PDBsum; 5UDC; -.
ProteinModelPortal; P03420; -.
SMR; P03420; -.
DIP; DIP-48772N; -.
ELM; P03420; -.
IntAct; P03420; 2.
TCDB; 1.G.2.1.3; the viral pore-forming membrane fusion protein-2 (vmfp2) family.
OrthoDB; VOG0900006Q; -.
EvolutionaryTrace; P03420; -.
Proteomes; UP000007678; Genome.
Proteomes; UP000134464; Genome.
Proteomes; UP000181145; Genome.
Proteomes; UP000181262; Genome.
Proteomes; UP000181559; Genome.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
GO; GO:0060141; P:positive regulation of syncytium formation by virus; IEA:UniProtKB-KW.
InterPro; IPR000776; Fusion_F0_Paramyxovir.
Pfam; PF00523; Fusion_gly; 1.
1: Evidence at protein level;
3D-structure; Cleavage on pair of basic residues; Coiled coil;
Complete proteome; Disulfide bond;
Fusion of virus membrane with host cell membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host membrane; Lipoprotein; Membrane; Palmitate;
Reference proteome; Signal;
Syncytium formation induced by viral infection; Transmembrane;
Transmembrane helix; Viral envelope protein;
Viral penetration into host cytoplasm; Virion;
Virus entry into host cell.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 574 Fusion glycoprotein F0.
/FTId=PRO_0000039234.
CHAIN 26 136 Fusion glycoprotein F2.
{ECO:0000269|PubMed:21613394}.
/FTId=PRO_0000039235.
CHAIN 26 109 Fusion glycoprotein F2'.
{ECO:0000269|PubMed:11493675}.
/FTId=PRO_0000432663.
PEPTIDE 110 136 Interchain peptide.
{ECO:0000269|PubMed:11493675}.
/FTId=PRO_0000432664.
CHAIN 137 574 Fusion glycoprotein F1.
/FTId=PRO_0000039236.
TOPO_DOM 27 529 Extracellular.
{ECO:0000269|PubMed:16160180}.
TRANSMEM 530 550 Helical. {ECO:0000255}.
TOPO_DOM 551 574 Cytoplasmic.
{ECO:0000269|PubMed:16160180}.
REGION 137 157 Fusion peptide. {ECO:0000250}.
COILED 155 183 {ECO:0000255}.
COILED 491 516 {ECO:0000255}.
SITE 109 110 Cleavage; by host.
{ECO:0000269|PubMed:11493675}.
SITE 136 137 Cleavage; by host furin.
{ECO:0000269|PubMed:11369882}.
LIPID 550 550 S-palmitoyl cysteine; by host.
{ECO:0000269|PubMed:2732224}.
CARBOHYD 27 27 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 500 500 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 69 212 Interchain (between F2 and F1 chains).
{ECO:0000250}.
DISULFID 358 367 {ECO:0000250}.
DISULFID 382 393 {ECO:0000250}.
VARIANT 102 102 P -> A (in strain: Cold-passage
attenuated).
VARIANT 218 218 E -> A (in strain: Cold-passage
attenuated).
VARIANT 379 379 I -> V (in strain: Cold-passage
attenuated).
VARIANT 447 447 M -> V (in strain: Cold-passage
attenuated).
VARIANT 523 523 T -> I (in strain: Cold-passage
attenuated).
STRAND 29 33 {ECO:0000244|PDB:5C69}.
TURN 34 37 {ECO:0000244|PDB:5C69}.
STRAND 38 49 {ECO:0000244|PDB:5C69}.
STRAND 51 60 {ECO:0000244|PDB:5C69}.
HELIX 74 96 {ECO:0000244|PDB:5C69}.
STRAND 102 105 {ECO:0000244|PDB:5K6B}.
HELIX 138 141 {ECO:0000244|PDB:5C69}.
HELIX 145 147 {ECO:0000244|PDB:5K6H}.
HELIX 149 157 {ECO:0000244|PDB:5C69}.
HELIX 160 201 {ECO:0000244|PDB:3KPE}.
HELIX 204 206 {ECO:0000244|PDB:3KPE}.
STRAND 208 211 {ECO:0000244|PDB:5C69}.
HELIX 217 239 {ECO:0000244|PDB:5C69}.
TURN 240 242 {ECO:0000244|PDB:5C69}.
STRAND 243 246 {ECO:0000244|PDB:5C69}.
TURN 249 251 {ECO:0000244|PDB:5C69}.
HELIX 254 262 {ECO:0000244|PDB:5C69}.
STRAND 264 266 {ECO:0000244|PDB:5C69}.
HELIX 268 275 {ECO:0000244|PDB:5C69}.
HELIX 278 283 {ECO:0000244|PDB:5C69}.
STRAND 286 293 {ECO:0000244|PDB:5C69}.
STRAND 296 305 {ECO:0000244|PDB:5C69}.
STRAND 308 318 {ECO:0000244|PDB:5C69}.
HELIX 328 330 {ECO:0000244|PDB:5K6F}.
STRAND 333 336 {ECO:0000244|PDB:5C69}.
STRAND 340 345 {ECO:0000244|PDB:5C69}.
STRAND 348 353 {ECO:0000244|PDB:5C69}.
HELIX 355 357 {ECO:0000244|PDB:5C69}.
STRAND 358 361 {ECO:0000244|PDB:5C69}.
STRAND 364 368 {ECO:0000244|PDB:5C69}.
HELIX 369 371 {ECO:0000244|PDB:5C69}.
STRAND 373 375 {ECO:0000244|PDB:5C69}.
HELIX 377 380 {ECO:0000244|PDB:5C69}.
HELIX 381 384 {ECO:0000244|PDB:5C69}.
STRAND 386 388 {ECO:0000244|PDB:3RKI}.
STRAND 389 391 {ECO:0000244|PDB:5C69}.
STRAND 394 399 {ECO:0000244|PDB:5C69}.
STRAND 404 407 {ECO:0000244|PDB:5C69}.
STRAND 409 416 {ECO:0000244|PDB:5C69}.
STRAND 422 426 {ECO:0000244|PDB:5C69}.
TURN 427 429 {ECO:0000244|PDB:5C69}.
STRAND 430 434 {ECO:0000244|PDB:5C69}.
STRAND 437 444 {ECO:0000244|PDB:5C69}.
STRAND 449 452 {ECO:0000244|PDB:5C69}.
STRAND 455 458 {ECO:0000244|PDB:5C69}.
STRAND 465 469 {ECO:0000244|PDB:5C69}.
HELIX 474 477 {ECO:0000244|PDB:5C69}.
TURN 480 482 {ECO:0000244|PDB:5C69}.
HELIX 487 514 {ECO:0000244|PDB:3KPE}.
SEQUENCE 574 AA; 63453 MW; A4066D9DC98933AA CRC64;
MELLILKANA ITTILTAVTF CFASGQNITE EFYQSTCSAV SKGYLSALRT GWYTSVITIE
LSNIKENKCN GTDAKVKLIK QELDKYKNAV TELQLLMQST PPTNNRARRE LPRFMNYTLN
NAKKTNVTLS KKRKRRFLGF LLGVGSAIAS GVAVSKVLHL EGEVNKIKSA LLSTNKAVVS
LSNGVSVLTS KVLDLKNYID KQLLPIVNKQ SCSISNIETV IEFQQKNNRL LEITREFSVN
AGVTTPVSTY MLTNSELLSL INDMPITNDQ KKLMSNNVQI VRQQSYSIMS IIKEEVLAYV
VQLPLYGVID TPCWKLHTSP LCTTNTKEGS NICLTRTDRG WYCDNAGSVS FFPQAETCKV
QSNRVFCDTM NSLTLPSEIN LCNVDIFNPK YDCKIMTSKT DVSSSVITSL GAIVSCYGKT
KCTASNKNRG IIKTFSNGCD YVSNKGMDTV SVGNTLYYVN KQEGKSLYVK GEPIINFYDP
LVFPSDEFDA SISQVNEKIN QSLAFIRKSD ELLHNVNAGK STTNIMITTI IIVIIVILLS
LIAVGLLLYC KARSTPVTLS KDQLSGINNI AFSN


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