NCAP_EBOZM
ID NCAP_EBOZM Reviewed; 739 AA.
AC P18272; Q773N6; Q8JS64; Q9DQD3; Q9YMG4;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Nucleoprotein;
DE AltName: Full=Ebola NP {ECO:0000303|PubMed:29474922};
DE Short=eNP {ECO:0000303|PubMed:29474922};
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=NP;
OS Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=128952;
OH NCBI_TaxID=77231; Epomops franqueti (Franquet's epauleted fruit bat).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2718390; DOI=10.1016/0042-6822(89)90354-1;
RA Sanchez A., Kiley M.P., Holloway B.P., McCormick J.B., Auperin D.D.;
RT "The nucleoprotein gene of Ebola virus: cloning, sequencing, and in vitro
RT expression.";
RL Virology 170:81-91(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8237108; DOI=10.1016/0168-1702(93)90063-s;
RA Sanchez A., Kiley M.P., Holloway B.P., Auperin D.D.;
RT "Sequence analysis of the Ebola virus genome: organization, genetic
RT elements, and comparison with the genome of Marburg virus.";
RL Virus Res. 29:215-240(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate guinea pig-adapted;
RX PubMed=11062045; DOI=10.1006/viro.2000.0572;
RA Volchkov V.E., Chepurnov A.A., Volchkova V.A., Ternovoj V.A., Klenk H.D.;
RT "Molecular characterization of guinea pig-adapted variants of Ebola
RT virus.";
RL Virology 277:147-155(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate mouse-adapted;
RA Wilson J.A., Kondig J.P., Kuehne A.I., Hart M.K.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH VP35; VP30 AND VP24.
RX PubMed=12191476; DOI=10.1016/s1097-2765(02)00588-9;
RA Huang Y., Xu L., Sun Y., Nabel G.J.;
RT "The assembly of Ebola virus nucleocapsid requires virion-associated
RT proteins 35 and 24 and posttranslational modification of nucleoprotein.";
RL Mol. Cell 10:307-316(2002).
RN [6]
RP GLYCOSYLATION.
RX PubMed=16571791; DOI=10.1128/jvi.80.8.3743-3751.2006;
RA Watanabe S., Noda T., Kawaoka Y.;
RT "Functional mapping of the nucleoprotein of Ebola virus.";
RL J. Virol. 80:3743-3751(2006).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16719918; DOI=10.1186/1743-422x-3-31;
RA Johnson R.F., Bell P., Harty R.N.;
RT "Effect of Ebola virus proteins GP, NP and VP35 on VP40 VLP morphology.";
RL Virol. J. 3:31-31(2006).
RN [8]
RP INTERACTION WITH VP40.
RX PubMed=17229682; DOI=10.1128/jvi.02183-06;
RA Noda T., Watanabe S., Sagara H., Kawaoka Y.;
RT "Mapping of the VP40-binding regions of the nucleoprotein of Ebola virus.";
RL J. Virol. 81:3554-3562(2007).
RN [9]
RP FUNCTION.
RX PubMed=22247782; DOI=10.1371/journal.pone.0029608;
RA Beniac D.R., Melito P.L., Devarennes S.L., Hiebert S.L., Rabb M.J.,
RA Lamboo L.L., Jones S.M., Booth T.F.;
RT "The organisation of Ebola virus reveals a capacity for extensive, modular
RT polyploidy.";
RL PLoS ONE 7:E29608-E29608(2012).
RN [10]
RP FUNCTION, AND INTERACTION WITH VP35.
RX PubMed=26119732; DOI=10.1016/j.celrep.2015.06.003;
RA Kirchdoerfer R.N., Abelson D.M., Li S., Wood M.R., Saphire E.O.;
RT "Assembly of the Ebola Virus Nucleoprotein from a Chaperoned VP35
RT Complex.";
RL Cell Rep. 12:140-149(2015).
RN [11]
RP FUNCTION, INTERACTION WITH VP24, AND SUBCELLULAR LOCATION.
RX PubMed=28794491; DOI=10.1038/s41598-017-08167-8;
RA Banadyga L., Hoenen T., Ambroggio X., Dunham E., Groseth A., Ebihara H.;
RT "Ebola virus VP24 interacts with NP to facilitate nucleocapsid assembly and
RT genome packaging.";
RL Sci. Rep. 7:7698-7698(2017).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VP30 AND HOST PPP2R5C.
RX PubMed=29290611; DOI=10.1016/j.molcel.2017.11.034;
RA Kruse T., Biedenkopf N., Hertz E.P.T., Dietzel E., Stalmann G.,
RA Lopez-Mendez B., Davey N.E., Nilsson J., Becker S.;
RT "The Ebola virus nucleoprotein recruits the host PP2A-B56 Phosphatase to
RT activate transcriptional support activity of VP30.";
RL Mol. Cell 69:136-145(2018).
RN [13]
RP FUNCTION, AND INTERACTION WITH HOST STAU1.
RX PubMed=30301857; DOI=10.1128/mbio.01771-18;
RA Fang J., Pietzsch C., Ramanathan P., Santos R.I., Ilinykh P.A.,
RA Garcia-Blanco M.A., Bukreyev A., Bradrick S.S.;
RT "Staufen1 Interacts with Multiple Components of the Ebola Virus
RT Ribonucleoprotein and Enhances Viral RNA Synthesis.";
RL MBio 9:0-0(2018).
RN [14]
RP FUNCTION.
RX PubMed=29339477; DOI=10.1073/pnas.1712263115;
RA Takamatsu Y., Kolesnikova L., Becker S.;
RT "Ebola virus proteins NP, VP35, and VP24 are essential and sufficient to
RT mediate nucleocapsid transport.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:1075-1080(2018).
RN [15]
RP ACETYLATION.
RX PubMed=30205953; DOI=10.1016/j.bbrc.2018.09.007;
RA Hatakeyama D., Ohmi N., Saitoh A., Makiyama K., Morioka M., Okazaki H.,
RA Kuzuhara T.;
RT "Acetylation of lysine residues in the recombinant nucleoprotein and VP40
RT matrix protein of Zaire Ebolavirus by eukaryotic histone
RT acetyltransferases.";
RL Biochem. Biophys. Res. Commun. 504:635-640(2018).
RN [16]
RP INTERACTION WITH HOST NXF1.
RX PubMed=31940815; DOI=10.3390/cells9010187;
RA Wendt L., Brandt J., Bodmer B.S., Reiche S., Schmidt M.L., Traeger S.,
RA Hoenen T.;
RT "The Ebola Virus Nucleoprotein Recruits the Nuclear RNA Export Factor NXF1
RT into Inclusion Bodies to Facilitate Viral Protein Expression.";
RL Cells 9:0-0(2020).
RN [17]
RP INTERACTION WITH HOST CCDC92, AND SUBCELLULAR LOCATION.
RX PubMed=32528005; DOI=10.1038/s41467-020-16768-7;
RA Kuroda M., Halfmann P.J., Hill-Batorski L., Ozawa M., Lopes T.J.S.,
RA Neumann G., Schoggins J.W., Rice C.M., Kawaoka Y.;
RT "Identification of interferon-stimulated genes that attenuate Ebola virus
RT infection.";
RL Nat. Commun. 11:2953-2953(2020).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 641-739.
RX PubMed=25195755; DOI=10.1107/s1399004714014710;
RA Dziubanska P.J., Derewenda U., Ellena J.F., Engel D.A., Derewenda Z.S.;
RT "The structure of the C-terminal domain of the Zaire ebolavirus
RT nucleoprotein.";
RL Acta Crystallogr. D 70:2420-2429(2014).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (3.71 ANGSTROMS) OF 38-385, FUNCTION, REGION,
RP INTERACTION WITH VP35, AND MUTAGENESIS OF TYR-21 AND HIS-22.
RX PubMed=25865894; DOI=10.1016/j.celrep.2015.03.034;
RA Leung D.W., Borek D., Luthra P., Binning J.M., Anantpadma M., Liu G.,
RA Harvey I.B., Su Z., Endlich-Frazier A., Pan J., Shabman R.S., Chiu W.,
RA Davey R.A., Otwinowski Z., Basler C.F., Amarasinghe G.K.;
RT "An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral
RT RNA Synthesis by Modulating Nucleoprotein-RNA Interactions.";
RL Cell Rep. 11:376-389(2015).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 36-351, AND INTERACTION WITH
RP VP35.
RX PubMed=25910597; DOI=10.1007/s13238-015-0163-3;
RA Dong S., Yang P., Li G., Liu B., Wang W., Liu X., Xia B., Yang C., Lou Z.,
RA Guo Y., Rao Z.;
RT "Insight into the Ebola virus nucleocapsid assembly mechanism: crystal
RT structure of Ebola virus nucleoprotein core domain at 1.8 Aa resolution.";
RL Protein Cell 6:351-362(2015).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 600-627, INTERACTION WITH VP30,
RP AND FUNCTION.
RX PubMed=27755595; DOI=10.1371/journal.ppat.1005937;
RA Kirchdoerfer R.N., Moyer C.L., Abelson D.M., Saphire E.O.;
RT "The Ebola virus VP30-NP interaction is a regulator of viral RNA
RT synthesis.";
RL PLoS Pathog. 12:E1005937-E1005937(2016).
RN [22]
RP STRUCTURE BY ELECTRON MICROSCOPY (6.60 ANGSTROMS), INTERACTION WITH VP24,
RP AND FUNCTION.
RX PubMed=29144446; DOI=10.1038/nature24490;
RA Wan W., Kolesnikova L., Clarke M., Koehler A., Noda T., Becker S.,
RA Briggs J.A.G.;
RT "Structure and assembly of the Ebola virus nucleocapsid.";
RL Nature 551:394-397(2017).
RN [23]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.80 ANGSTROMS) OF 25-457, AND
RP NOMENCLATURE.
RX PubMed=29474922; DOI=10.1016/j.cell.2018.02.009;
RA Su Z., Wu C., Shi L., Luthra P., Pintilie G.D., Johnson B., Porter J.R.,
RA Ge P., Chen M., Liu G., Frederick T.E., Binning J.M., Bowman G.R.,
RA Zhou Z.H., Basler C.F., Gross M.L., Leung D.W., Chiu W., Amarasinghe G.K.;
RT "Electron Cryo-microscopy Structure of Ebola Virus Nucleoprotein Reveals a
RT Mechanism for Nucleocapsid-like Assembly.";
RL Cell 172:966-978(2018).
RN [24]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 19-406, AND FUNCTION.
RX PubMed=30333622; DOI=10.1038/s41586-018-0630-0;
RA Sugita Y., Matsunami H., Kawaoka Y., Noda T., Wolf M.;
RT "Cryo-EM structure of the Ebola virus nucleoprotein-RNA complex at 3.6 Aa
RT resolution.";
RL Nature 563:137-140(2018).
CC -!- FUNCTION: Oligomerizes into helical capsid to encapsidate the viral
CC genome, protecting it from nucleases and the cellular innate immune
CC response (PubMed:26119732, PubMed:25865894, PubMed:30333622,
CC PubMed:16719918). VP35 binds to and stabilizes monomeric NP, keeping it
CC soluble (PubMed:26119732, PubMed:25865894). Upon virus replication, NP
CC is recruited to bind cooperatively viral genomic RNA and VP35 is
CC released (PubMed:29144446). The encapsidated genomic RNA is termed the
CC nucleocapsid and serves as template for transcription and replication.
CC The nucleocapsid is helical with a pitch of 10.81 NP per turn and a
CC diameter of about 22nm (PubMed:22247782). Each NP binds to six
CC nucleotides of viral genomic RNA, three being exposed to the solvant
CC and three hidden into the nucleocapsid (PubMed:30333622). Recruits also
CC host PPP2R5C phosphatase to dephosphorylate VP30 and thereby promote
CC viral transcription (PubMed:29290611, PubMed:27755595). Upon virion
CC assembly and budding, NP binds to VP24 and possibly host STAU1
CC (PubMed:28794491, PubMed:30301857). {ECO:0000269|PubMed:16719918,
CC ECO:0000269|PubMed:22247782, ECO:0000269|PubMed:25865894,
CC ECO:0000269|PubMed:26119732, ECO:0000269|PubMed:27755595,
CC ECO:0000269|PubMed:28794491, ECO:0000269|PubMed:29144446,
CC ECO:0000269|PubMed:29290611, ECO:0000269|PubMed:30301857,
CC ECO:0000269|PubMed:30333622}.
CC -!- SUBUNIT: Homooligomer. Homomultimerizes to form the nucleocapsid. Binds
CC to viral genomic RNA. Interacts with VP35 and VP30 to form the
CC nucleocapsid (PubMed:12191476, PubMed:26119732, PubMed:25865894,
CC PubMed:25910597, PubMed:27755595). Interacts with host PPP2R5C; this
CC interaction leads to VP30 dephosphorylation and viral transcription
CC (PubMed:29290611). Interacts with VP24; this interaction facilitates
CC nucleocapsid assembly and genome packaging (PubMed:12191476,
CC PubMed:28794491, PubMed:29144446, PubMed:29339477). Interacts with
CC matrix protein VP40; this interaction allows recruitment of the
CC nucleocapsid into progeny virions (PubMed:17229682). Interacts with
CC host STAU1 (PubMed:30301857). Interacts with host NXF1 (via RNA-binding
CC domain); this interaction recruits NXF1 to the inclusion bodies were
CC viral replication takes place, probably to export viral mRNA-NXF1
CC complexes from these sites (PubMed:31940815). Interacts with host
CC CCDC92; this interaction sequesters NP in the host cytoplasm
CC (PubMed:32528005). {ECO:0000269|PubMed:12191476,
CC ECO:0000269|PubMed:17229682, ECO:0000269|PubMed:25865894,
CC ECO:0000269|PubMed:25910597, ECO:0000269|PubMed:26119732,
CC ECO:0000269|PubMed:27755595, ECO:0000269|PubMed:28794491,
CC ECO:0000269|PubMed:29144446, ECO:0000269|PubMed:29290611,
CC ECO:0000269|PubMed:29339477, ECO:0000269|PubMed:30301857,
CC ECO:0000269|PubMed:31940815, ECO:0000269|PubMed:32528005}.
CC -!- INTERACTION:
CC P18272; Q05127: VP35; NbExp=2; IntAct=EBI-9820219, EBI-6148294;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16719918}. Host
CC cytoplasm {ECO:0000269|PubMed:28794491, ECO:0000269|PubMed:29290611,
CC ECO:0000269|PubMed:32528005}.
CC -!- DOMAIN: Comprizes a N-terminal arm involved in oligomerization, a NP
CC core region involved in RNA binding, a disordered region follwoed by a
CC C-terminal tail involved in protein-protein interactions
CC (PubMed:25865894, PubMed:30333622). During oligomerization, NP N-
CC terminal arm binds to a neighbor NP thereby displacing VP35 bound to
CC monomeric NP (PubMed:30333622). {ECO:0000269|PubMed:25865894,
CC ECO:0000269|PubMed:30333622}.
CC -!- PTM: Phosphorylated by host. {ECO:0000269|PubMed:16571791}.
CC -!- PTM: O-glycosylated by host. {ECO:0000269|PubMed:16571791}.
CC -!- PTM: Acetylated by host EP300 in vitro. {ECO:0000269|PubMed:30205953}.
CC -!- SIMILARITY: Belongs to the filoviruses nucleoprotein family.
CC {ECO:0000305}.
CC -!- CAUTION: Acetylation has been show in vitro using purified recombinant
CC proteins. Additional evidence are however required to confirm this
CC result in vivo. {ECO:0000269|PubMed:30205953}.
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DR EMBL; J04337; AAA42977.1; -; Genomic_RNA.
DR EMBL; L11365; AAB81001.1; -; Genomic_RNA.
DR EMBL; AF086833; AAD14590.1; -; Genomic_RNA.
DR EMBL; AF272001; AAG40164.1; -; Genomic_RNA.
DR EMBL; AY142960; AAN37504.1; -; Genomic_RNA.
DR EMBL; AF499101; AAM76031.1; -; Genomic_RNA.
DR PIR; A31471; VHIWEB.
DR RefSeq; NP_066243.1; NC_002549.1.
DR PDB; 4QAZ; X-ray; 1.98 A; A=641-739.
DR PDB; 4QB0; X-ray; 1.75 A; A=641-739.
DR PDB; 4YPI; X-ray; 3.71 A; A/B/C/D=38-385.
DR PDB; 4Z9P; X-ray; 1.79 A; A=36-351.
DR PDB; 4ZTA; X-ray; 2.40 A; A=33-367.
DR PDB; 4ZTG; X-ray; 2.80 A; A=33-367.
DR PDB; 4ZTI; X-ray; 2.40 A; A/B=33-367.
DR PDB; 5T3T; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=600-627.
DR PDB; 5Z9W; EM; 3.90 A; A=19-406.
DR PDB; 6C54; EM; 5.80 A; A/B=25-457.
DR PDB; 6EHL; EM; 6.60 A; A=1-739.
DR PDB; 6EHM; EM; 7.30 A; A/B=1-739.
DR PDB; 6NUT; EM; 3.10 A; A=1-450.
DR PDBsum; 4QAZ; -.
DR PDBsum; 4QB0; -.
DR PDBsum; 4YPI; -.
DR PDBsum; 4Z9P; -.
DR PDBsum; 4ZTA; -.
DR PDBsum; 4ZTG; -.
DR PDBsum; 4ZTI; -.
DR PDBsum; 5T3T; -.
DR PDBsum; 5Z9W; -.
DR PDBsum; 6C54; -.
DR PDBsum; 6EHL; -.
DR PDBsum; 6EHM; -.
DR PDBsum; 6NUT; -.
DR SMR; P18272; -.
DR ELM; P18272; -.
DR IntAct; P18272; 2.
DR ABCD; P18272; 2 sequenced antibodies.
DR GeneID; 911830; -.
DR KEGG; vg:911830; -.
DR Proteomes; UP000007209; Genome.
DR Proteomes; UP000109874; Genome.
DR Proteomes; UP000149419; Genome.
DR Proteomes; UP000150973; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IDA:CACAO.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0019074; P:viral RNA genome packaging; IEA:InterPro.
DR InterPro; IPR008609; Ebola_NP.
DR Pfam; PF05505; Ebola_NP; 1.
DR PIRSF; PIRSF003900; N_FiloV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Capsid protein; Helical capsid protein;
KW Host cytoplasm; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW RNA-binding; Virion.
FT CHAIN 1..739
FT /note="Nucleoprotein"
FT /id="PRO_0000222171"
FT REGION 1..25
FT /note="Oligomerization, N-terminal arm"
FT /evidence="ECO:0000269|PubMed:25865894,
FT ECO:0000303|PubMed:30333622"
FT REGION 26..405
FT /note="NP core"
FT /evidence="ECO:0000303|PubMed:30333622"
FT REGION 415..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 562..567
FT /note="Host PPP2R5C-binding motif"
FT /evidence="ECO:0000269|PubMed:29290611"
FT MOTIF 606..611
FT /note="VP30-binding motif"
FT /evidence="ECO:0000269|PubMed:29290611"
FT COMPBIAS 500..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..592
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 72
FT /note="S -> G (in strain: Isolate mouse-adapted)"
FT VARIANT 524
FT /note="S -> F (in strain: Isolate guinea pig-adapted)"
FT VARIANT 648
FT /note="F -> L (in strain: Isolate guinea pig-adapted)"
FT MUTAGEN 21
FT /note="Y->A: More than 90% loss of oligomerization; when
FT associated with A-21."
FT /evidence="ECO:0000269|PubMed:25865894"
FT MUTAGEN 22
FT /note="H->A: More than 90% loss of oligomerization; when
FT associated with A-22."
FT /evidence="ECO:0000269|PubMed:25865894"
FT CONFLICT 170
FT /note="E -> R (in Ref. 1; AAA42977)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="F -> L (in Ref. 1; AAA42977)"
FT /evidence="ECO:0000305"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:6NUT"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:6NUT"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:4Z9P"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:4Z9P"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:4Z9P"
FT TURN 156..160
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 165..181
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 227..239
FT /evidence="ECO:0007829|PDB:4Z9P"
FT TURN 240..243
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:4Z9P"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:4ZTA"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:4ZTA"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 274..288
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 289..296
FT /evidence="ECO:0007829|PDB:4Z9P"
FT TURN 297..301
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 314..324
FT /evidence="ECO:0007829|PDB:4Z9P"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:4ZTI"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:6NUT"
FT HELIX 336..349
FT /evidence="ECO:0007829|PDB:4Z9P"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:6NUT"
FT HELIX 371..405
FT /evidence="ECO:0007829|PDB:6NUT"
FT HELIX 646..659
FT /evidence="ECO:0007829|PDB:4QB0"
FT HELIX 661..672
FT /evidence="ECO:0007829|PDB:4QB0"
FT STRAND 676..679
FT /evidence="ECO:0007829|PDB:4QB0"
FT STRAND 685..688
FT /evidence="ECO:0007829|PDB:4QB0"
FT HELIX 690..692
FT /evidence="ECO:0007829|PDB:4QB0"
FT STRAND 693..696
FT /evidence="ECO:0007829|PDB:4QB0"
FT HELIX 702..706
FT /evidence="ECO:0007829|PDB:4QB0"
FT HELIX 708..711
FT /evidence="ECO:0007829|PDB:4QB0"
FT STRAND 712..715
FT /evidence="ECO:0007829|PDB:4QB0"
FT STRAND 718..721
FT /evidence="ECO:0007829|PDB:4QB0"
FT HELIX 722..724
FT /evidence="ECO:0007829|PDB:4QB0"
FT HELIX 727..737
FT /evidence="ECO:0007829|PDB:4QB0"
SQ SEQUENCE 739 AA; 83287 MW; 159C254EA0478886 CRC64;
MDSRPQKIWM APSLTESDMD YHKILTAGLS VQQGIVRQRV IPVYQVNNLE EICQLIIQAF
EAGVDFQESA DSFLLMLCLH HAYQGDYKLF LESGAVKYLE GHGFRFEVKK RDGVKRLEEL
LPAVSSGKNI KRTLAAMPEE ETTEANAGQF LSFASLFLPK LVVGEKACLE KVQRQIQVHA
EQGLIQYPTA WQSVGHMMVI FRLMRTNFLI KFLLIHQGMH MVAGHDANDA VISNSVAQAR
FSGLLIVKTV LDHILQKTER GVRLHPLART AKVKNEVNSF KAALSSLAKH GEYAPFARLL
NLSGVNNLEH GLFPQLSAIA LGVATAHGST LAGVNVGEQY QQLREAATEA EKQLQQYAES
RELDHLGLDD QEKKILMNFH QKKNEISFQQ TNAMVTLRKE RLAKLTEAIT AASLPKTSGH
YDDDDDIPFP GPINDDDNPG HQDDDPTDSQ DTTIPDVVVD PDDGSYGEYQ SYSENGMNAP
DDLVLFDLDE DDEDTKPVPN RSTKGGQQKN SQKGQHIEGR QTQSRPIQNV PGPHRTIHHA
SAPLTDNDRR NEPSGSTSPR MLTPINEEAD PLDDADDETS SLPPLESDDE EQDRDGTSNR
TPTVAPPAPV YRDHSEKKEL PQDEQQDQDH TQEARNQDSD NTQSEHSFEE MYRHILRSQG
PFDAVLYYHM MKDEPVVFST SDGKEYTYPD SLEEEYPPWL TEKEAMNEEN RFVTLDGQQF
YWPVMNHKNK FMAILQHHQ
