SPIKE_MERS1
ID SPIKE_MERS1 Reviewed; 1353 AA.
AC K9N5Q8;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
DE Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04099};
DE AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04099};
DE AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04099};
DE Contains:
DE RecName: Full=Spike protein S1 {ECO:0000255|HAMAP-Rule:MF_04099};
DE Contains:
DE RecName: Full=Spike protein S2 {ECO:0000255|HAMAP-Rule:MF_04099};
DE Contains:
DE RecName: Full=Spike protein S2' {ECO:0000255|HAMAP-Rule:MF_04099};
DE Flags: Precursor;
GN Name=S {ECO:0000255|HAMAP-Rule:MF_04099}; ORFNames=3;
OS Middle East respiratory syndrome-related coronavirus (isolate United
OS Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Merbecovirus.
OX NCBI_TaxID=1263720;
OH NCBI_TaxID=9838; Camelus dromedarius (Dromedary) (Arabian camel).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=23078800;
RA Bermingham A., Chand M.A., Brown C.S., Aarons E., Tong C., Langrish C.,
RA Hoschler K., Brown K., Galiano M., Myers R., Pebody R.G., Green H.K.,
RA Boddington N.L., Gopal R., Price N., Newsholme W., Drosten C.,
RA Fouchier R.A., Zambon M.;
RT "Severe respiratory illness caused by a novel coronavirus, in a patient
RT transferred to the United Kingdom from the Middle East, September 2012.";
RL Eurosurveillance 17:20290-20290(2012).
RN [2]
RP FUNCTION, AND INTERACTION WITH HOST DPP4.
RX PubMed=23486063; DOI=10.1038/nature12005;
RA Raj V.S., Mou H., Smits S.L., Dekkers D.H., Muller M.A., Dijkman R.,
RA Muth D., Demmers J.A., Zaki A., Fouchier R.A., Thiel V., Drosten C.,
RA Rottier P.J., Osterhaus A.D., Bosch B.J., Haagmans B.L.;
RT "Dipeptidyl peptidase 4 is a functional receptor for the emerging human
RT coronavirus-EMC.";
RL Nature 495:251-254(2013).
CC -!- FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane
CC by interacting with host receptor, initiating the infection (By
CC similarity). Interacts with host DPP4 to mediate virla entry.
CC {ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:23486063}.
CC -!- FUNCTION: [Spike protein S2]: Mediates fusion of the virion and
CC cellular membranes by acting as a class I viral fusion protein. Under
CC the current model, the protein has at least three conformational
CC states: pre-fusion native state, pre-hairpin intermediate state, and
CC post-fusion hairpin state. During viral and target cell membrane
CC fusion, the coiled coil regions (heptad repeats) assume a trimer-of-
CC hairpins structure, positioning the fusion peptide in close proximity
CC to the C-terminal region of the ectodomain. The formation of this
CC structure appears to drive apposition and subsequent fusion of viral
CC and target cell membranes. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- FUNCTION: [Spike protein S2']: Acts as a viral fusion peptide which is
CC unmasked following S2 cleavage occurring upon virus endocytosis.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- SUBUNIT: Homotrimer; each monomer consists of a S1 and a S2 subunit.
CC The resulting peplomers protrude from the virus surface as spikes. S1
CC interacts with murine DPP4. {ECO:0000255|HAMAP-Rule:MF_04099,
CC ECO:0000269|PubMed:23486063}.
CC -!- INTERACTION:
CC K9N5Q8; PRO_0000000092 [P05067]: APP; Xeno; NbExp=2; IntAct=EBI-25474996, EBI-821758;
CC K9N5Q8; M1PFC6: DPP4; Xeno; NbExp=2; IntAct=EBI-25474996, EBI-25570499;
CC K9N5Q8; P27487: DPP4; Xeno; NbExp=7; IntAct=EBI-25474996, EBI-2871277;
CC K9N5Q8; P09958: FURIN; Xeno; NbExp=3; IntAct=EBI-25474996, EBI-1056807;
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass
CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host cell
CC membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_04099}. Note=Accumulates in the
CC endoplasmic reticulum-Golgi intermediate compartment, where it
CC participates in virus particle assembly. Some S oligomers are
CC transported to the host plasma membrane, where they may mediate cell-
CC cell fusion. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- DOMAIN: Fusion peptide 1 (FP1) and fusion peptide 2 (FP2) function
CC cooperatively and have a membrane-ordering effect on lipid headgroups
CC and shallow hydrophobic regions of target bilayers. They are considered
CC as two domains of an extended, bipartite FP. The membrane-ordering
CC activity is calcium-dependent and also dependent on correct folding,
CC which is maintained by an internal disulfide bond in FP2.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC precursor is processed into S1 and S2 by host cell furin or another
CC cellular protease to yield the mature S1 and S2 proteins. Additionally,
CC a second cleavage leads to the release of a fusion peptide after viral
CC attachment to host cell receptor. {ECO:0000255|HAMAP-Rule:MF_04099}.
CC -!- PTM: The cytoplasmic Cys-rich domain is palmitoylated. Spike
CC glycoprotein is digested within host endosomes. {ECO:0000255|HAMAP-
CC Rule:MF_04099}.
CC -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04099}.
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DR EMBL; KC164505; AFY13307.1; -; Genomic_RNA.
DR PDB; 4L72; X-ray; 3.00 A; B=382-585.
DR PDB; 4MOD; X-ray; 1.90 A; A/B=992-1055, A/B=1250-1286.
DR PDB; 4XAK; X-ray; 2.45 A; A/B=367-601.
DR PDB; 4ZPT; X-ray; 2.59 A; R/S=381-588.
DR PDB; 4ZPV; X-ray; 3.20 A; R/S=381-588.
DR PDB; 4ZPW; X-ray; 3.02 A; R/S=381-588.
DR PDB; 5GMQ; X-ray; 2.70 A; A=366-588.
DR PDB; 5GR7; X-ray; 2.40 A; C=292-300.
DR PDB; 5GSB; X-ray; 1.80 A; C=291-300.
DR PDB; 5GSR; X-ray; 2.20 A; P/Q=292-300.
DR PDB; 5GSV; X-ray; 2.00 A; C=1191-1200.
DR PDB; 5GSX; X-ray; 2.50 A; C/F=1191-1200.
DR PDB; 5VYH; X-ray; 2.00 A; A=18-353.
DR PDB; 5W9H; EM; 4.00 A; A/D/G/p/q/r=1-1291.
DR PDB; 5W9I; EM; 3.60 A; A/B/E/F/I/J=1-1291.
DR PDB; 5W9J; EM; 4.80 A; A/D/G/J/K/L=1-1291.
DR PDB; 5W9K; EM; 4.60 A; A/D/G/J/K/L=1-1291.
DR PDB; 5W9L; EM; 4.80 A; A/B/C/D/G/J=1-1291.
DR PDB; 5W9M; EM; 4.70 A; A/D/E/F/G/J=1-1291.
DR PDB; 5W9N; EM; 5.00 A; A/D/G/H/I/J=1-1291.
DR PDB; 5W9O; EM; 4.50 A; A/D/G/J/K/L=1-1291.
DR PDB; 5W9P; EM; 4.00 A; A/B/C/H/I/J=1-1291.
DR PDB; 5X4R; X-ray; 1.50 A; A=18-353.
DR PDB; 5X59; EM; 3.70 A; A/B/C=18-1294.
DR PDB; 5X5C; EM; 4.10 A; A/B/C=18-1294.
DR PDB; 5X5F; EM; 4.20 A; A/B/C=18-1294.
DR PDB; 5YY5; X-ray; 2.80 A; A/B=380-588.
DR PDB; 5ZVK; X-ray; 3.31 A; A/B/C=984-1062.
DR PDB; 5ZXV; X-ray; 4.48 A; A/B=381-588.
DR PDB; 6C6Y; X-ray; 3.32 A; R/S=381-588.
DR PDB; 6C6Z; X-ray; 2.10 A; A/B=367-589.
DR PDB; 6J11; X-ray; 3.00 A; A/B/C=18-353.
DR PDB; 6J2J; X-ray; 2.50 A; C/F=422-430.
DR PDB; 6L8Q; X-ray; 3.10 A; B/D/F/H=367-606.
DR PDB; 6PXH; X-ray; 2.30 A; A/B=18-351.
DR PDB; 6WAR; X-ray; 3.40 A; A/C/E/G/I/K/M/O=367-589.
DR PDB; 7C02; X-ray; 2.91 A; A/B=367-606.
DR PDB; 7COE; X-ray; 2.05 A; A/D=367-589.
DR PDB; 7M55; X-ray; 1.40 A; A=1230-1244.
DR PDB; 7M5E; EM; 2.50 A; A/C/E=19-1294.
DR PDBsum; 4L72; -.
DR PDBsum; 4MOD; -.
DR PDBsum; 4XAK; -.
DR PDBsum; 4ZPT; -.
DR PDBsum; 4ZPV; -.
DR PDBsum; 4ZPW; -.
DR PDBsum; 5GMQ; -.
DR PDBsum; 5GR7; -.
DR PDBsum; 5GSB; -.
DR PDBsum; 5GSR; -.
DR PDBsum; 5GSV; -.
DR PDBsum; 5GSX; -.
DR PDBsum; 5VYH; -.
DR PDBsum; 5W9H; -.
DR PDBsum; 5W9I; -.
DR PDBsum; 5W9J; -.
DR PDBsum; 5W9K; -.
DR PDBsum; 5W9L; -.
DR PDBsum; 5W9M; -.
DR PDBsum; 5W9N; -.
DR PDBsum; 5W9O; -.
DR PDBsum; 5W9P; -.
DR PDBsum; 5X4R; -.
DR PDBsum; 5X59; -.
DR PDBsum; 5X5C; -.
DR PDBsum; 5X5F; -.
DR PDBsum; 5YY5; -.
DR PDBsum; 5ZVK; -.
DR PDBsum; 5ZXV; -.
DR PDBsum; 6C6Y; -.
DR PDBsum; 6C6Z; -.
DR PDBsum; 6J11; -.
DR PDBsum; 6J2J; -.
DR PDBsum; 6L8Q; -.
DR PDBsum; 6PXH; -.
DR PDBsum; 6WAR; -.
DR PDBsum; 7C02; -.
DR PDBsum; 7COE; -.
DR PDBsum; 7M55; -.
DR PDBsum; 7M5E; -.
DR SMR; K9N5Q8; -.
DR BioGRID; 4383879; 8.
DR ComplexPortal; CPX-5766; MERS-CoV cleaved Spike protein complex.
DR ComplexPortal; CPX-7089; MERS-CoV uncleaved Spike protein complex.
DR IntAct; K9N5Q8; 7.
DR BindingDB; K9N5Q8; -.
DR ABCD; K9N5Q8; 131 sequenced antibodies.
DR SABIO-RK; K9N5Q8; -.
DR Proteomes; UP000139997; Genome.
DR GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0019031; C:viral envelope; IC:ComplexPortal.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0061025; P:membrane fusion; IC:ComplexPortal.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IC:ComplexPortal.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IC:ComplexPortal.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IC:ComplexPortal.
DR GO; GO:0046718; P:viral entry into host cell; IC:ComplexPortal.
DR CDD; cd21486; human_MERS-CoV_Spike_S1_RBD; 1.
DR CDD; cd21626; MERS-CoV-like_Spike_S1_NTD; 1.
DR DisProt; DP02880; -.
DR Gene3D; 2.60.120.960; -; 1.
DR HAMAP; MF_04099; BETA_CORONA_SPIKE; 1.
DR InterPro; IPR032500; bCoV_S1_N.
DR InterPro; IPR042578; BETA_CORONA_SPIKE.
DR InterPro; IPR043607; CoV_S1_C.
DR InterPro; IPR043473; S2_sf_CoV.
DR InterPro; IPR043002; Spike_N_sf.
DR InterPro; IPR044337; Spike_S1_N_MERS-CoV-like.
DR InterPro; IPR018548; Spike_S1_RBD_bCoV.
DR InterPro; IPR044376; Spike_S1_RBD_MERS-CoV.
DR InterPro; IPR036326; Spike_S1_RBD_sf_bCoV.
DR InterPro; IPR002552; Spike_S2_CoV.
DR InterPro; IPR043614; Spike_S2_CoV_C.
DR InterPro; IPR044873; Spike_S2_CoV_HR1.
DR InterPro; IPR044874; Spike_S2_CoV_HR2.
DR Pfam; PF16451; bCoV_S1_N; 1.
DR Pfam; PF09408; bCoV_S1_RBD; 1.
DR Pfam; PF19209; CoV_S1_C; 1.
DR Pfam; PF01601; CoV_S2; 1.
DR Pfam; PF19214; CoV_S2_C; 1.
DR SUPFAM; SSF111474; SSF111474; 2.
DR SUPFAM; SSF143587; SSF143587; 1.
DR PROSITE; PS51921; BCOV_S1_CTD; 1.
DR PROSITE; PS51922; BCOV_S1_NTD; 1.
DR PROSITE; PS51923; COV_S2_HR1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW Membrane; Palmitate; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virulence;
KW Virus entry into host cell.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CHAIN 18..1353
FT /note="Spike glycoprotein"
FT /id="PRO_0000422465"
FT CHAIN 18..751
FT /note="Spike protein S1"
FT /id="PRO_0000422466"
FT CHAIN 752..1353
FT /note="Spike protein S2"
FT /id="PRO_0000422467"
FT CHAIN 888..1353
FT /note="Spike protein S2'"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT /id="PRO_0000444090"
FT TOPO_DOM 18..1296
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TRANSMEM 1297..1317
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT TOPO_DOM 1318..1353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DOMAIN 18..351
FT /note="BetaCoV S1-NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DOMAIN 381..587
FT /note="BetaCoV S1-CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT REGION 888..909
FT /note="Fusion peptide 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 907..929
FT /note="Fusion peptide 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 994..1044
FT /note="Heptad repeat 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT REGION 1246..1285
FT /note="Heptad repeat 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 1023..1067
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT COILED 1258..1286
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT MOTIF 1351..1353
FT /note="KxHxx"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT SITE 751..752
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 887..888
FT /note="Cleavage"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 774
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 785
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 870
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1176
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1213
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1225
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1241
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1256
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1277
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT CARBOHYD 1288
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT DISULFID 185..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 339..349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01270"
FT DISULFID 383..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 425..478
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 437..585
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01269"
FT DISULFID 912..925
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04099"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:6PXH"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:5X4R"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:5X4R"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:5X4R"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:6J11"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:5X4R"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:5X4R"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:5X4R"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 179..189
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6PXH"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:5X4R"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 232..244
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 252..259
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:5X4R"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:5X4R"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:5X4R"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 319..327
FT /evidence="ECO:0007829|PDB:5X4R"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:5X4R"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:5X4R"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:5X4R"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:5VYH"
FT STRAND 358..366
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:6C6Z"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:6C6Z"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:6C6Z"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:6C6Z"
FT HELIX 411..415
FT /evidence="ECO:0007829|PDB:6C6Z"
FT STRAND 418..426
FT /evidence="ECO:0007829|PDB:6C6Z"
FT TURN 430..434
FT /evidence="ECO:0007829|PDB:4XAK"
FT STRAND 440..447
FT /evidence="ECO:0007829|PDB:6C6Z"
FT HELIX 450..455
FT /evidence="ECO:0007829|PDB:6C6Z"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:6C6Z"
FT HELIX 463..467
FT /evidence="ECO:0007829|PDB:6C6Z"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:6C6Z"
FT STRAND 477..483
FT /evidence="ECO:0007829|PDB:6C6Z"
FT STRAND 495..506
FT /evidence="ECO:0007829|PDB:6C6Z"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:4ZPV"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:6C6Z"
FT HELIX 525..528
FT /evidence="ECO:0007829|PDB:6C6Z"
FT STRAND 540..544
FT /evidence="ECO:0007829|PDB:6C6Z"
FT TURN 547..550
FT /evidence="ECO:0007829|PDB:6C6Z"
FT STRAND 551..562
FT /evidence="ECO:0007829|PDB:6C6Z"
FT STRAND 568..576
FT /evidence="ECO:0007829|PDB:6C6Z"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:4XAK"
FT HELIX 597..599
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 602..608
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 611..619
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 638..642
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 648..652
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 657..664
FT /evidence="ECO:0007829|PDB:7M5E"
FT TURN 665..668
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 669..675
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 679..681
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 707..709
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 712..726
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 728..732
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 735..738
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 757..762
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 774..776
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 778..796
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 801..804
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 806..811
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 815..821
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 822..824
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 827..853
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:7M5E"
FT TURN 863..868
FT /evidence="ECO:0007829|PDB:7M5E"
FT TURN 872..874
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 889..896
FT /evidence="ECO:0007829|PDB:7M5E"
FT TURN 905..907
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 908..914
FT /evidence="ECO:0007829|PDB:7M5E"
FT TURN 923..926
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 927..930
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 932..935
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 941..952
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 955..958
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 959..962
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 967..969
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 972..981
FT /evidence="ECO:0007829|PDB:7M5E"
FT TURN 982..984
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 987..992
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 995..1038
FT /evidence="ECO:0007829|PDB:4MOD"
FT HELIX 1051..1057
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 1060..1106
FT /evidence="ECO:0007829|PDB:7M5E"
FT TURN 1114..1116
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 1117..1130
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 1133..1153
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 1155..1157
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 1160..1174
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 1184..1188
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 1191..1195
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 1201..1205
FT /evidence="ECO:0007829|PDB:7M5E"
FT STRAND 1211..1214
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 1220..1222
FT /evidence="ECO:0007829|PDB:7M5E"
FT HELIX 1231..1239
FT /evidence="ECO:0007829|PDB:7M55"
SQ SEQUENCE 1353 AA; 149411 MW; D73276432FA5D515 CRC64;
MIHSVFLLMF LLTPTESYVD VGPDSVKSAC IEVDIQQTFF DKTWPRPIDV SKADGIIYPQ
GRTYSNITIT YQGLFPYQGD HGDMYVYSAG HATGTTPQKL FVANYSQDVK QFANGFVVRI
GAAANSTGTV IISPSTSATI RKIYPAFMLG SSVGNFSDGK MGRFFNHTLV LLPDGCGTLL
RAFYCILEPR SGNHCPAGNS YTSFATYHTP ATDCSDGNYN RNASLNSFKE YFNLRNCTFM
YTYNITEDEI LEWFGITQTA QGVHLFSSRY VDLYGGNMFQ FATLPVYDTI KYYSIIPHSI
RSIQSDRKAW AAFYVYKLQP LTFLLDFSVD GYIRRAIDCG FNDLSQLHCS YESFDVESGV
YSVSSFEAKP SGSVVEQAEG VECDFSPLLS GTPPQVYNFK RLVFTNCNYN LTKLLSLFSV
NDFTCSQISP AAIASNCYSS LILDYFSYPL SMKSDLSVSS AGPISQFNYK QSFSNPTCLI
LATVPHNLTT ITKPLKYSYI NKCSRFLSDD RTEVPQLVNA NQYSPCVSIV PSTVWEDGDY
YRKQLSPLEG GGWLVASGST VAMTEQLQMG FGITVQYGTD TNSVCPKLEF ANDTKIASQL
GNCVEYSLYG VSGRGVFQNC TAVGVRQQRF VYDAYQNLVG YYSDDGNYYC LRACVSVPVS
VIYDKETKTH ATLFGSVACE HISSTMSQYS RSTRSMLKRR DSTYGPLQTP VGCVLGLVNS
SLFVEDCKLP LGQSLCALPD TPSTLTPRSV RSVPGEMRLA SIAFNHPIQV DQLNSSYFKL
SIPTNFSFGV TQEYIQTTIQ KVTVDCKQYV CNGFQKCEQL LREYGQFCSK INQALHGANL
RQDDSVRNLF ASVKSSQSSP IIPGFGGDFN LTLLEPVSIS TGSRSARSAI EDLLFDKVTI
ADPGYMQGYD DCMQQGPASA RDLICAQYVA GYKVLPPLMD VNMEAAYTSS LLGSIAGVGW
TAGLSSFAAI PFAQSIFYRL NGVGITQQVL SENQKLIANK FNQALGAMQT GFTTTNEAFH
KVQDAVNNNA QALSKLASEL SNTFGAISAS IGDIIQRLDV LEQDAQIDRL INGRLTTLNA
FVAQQLVRSE SAALSAQLAK DKVNECVKAQ SKRSGFCGQG THIVSFVVNA PNGLYFMHVG
YYPSNHIEVV SAYGLCDAAN PTNCIAPVNG YFIKTNNTRI VDEWSYTGSS FYAPEPITSL
NTKYVAPQVT YQNISTNLPP PLLGNSTGID FQDELDEFFK NVSTSIPNFG SLTQINTTLL
DLTYEMLSLQ QVVKALNESY IDLKELGNYT YYNKWPWYIW LGFIAGLVAL ALCVFFILCC
TGCGTNCMGK LKCNRCCDRY EEYDLEPHKV HVH
