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Serine/threonine-protein kinase TBK1 (EC 2.7.11.1) (T2K) (TANK-binding kinase 1)

 TBK1_MOUSE              Reviewed;         729 AA.
Q9WUN2; Q9CT90; Q9DC03;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
23-MAY-2018, entry version 150.
RecName: Full=Serine/threonine-protein kinase TBK1;
EC=2.7.11.1;
AltName: Full=T2K;
AltName: Full=TANK-binding kinase 1;
Name=Tbk1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Spleen;
PubMed=10581243; DOI=10.1093/emboj/18.23.6694;
Pomerantz J.L., Baltimore D.;
"NF-kB activation by a signaling complex containing TRAF2, TANK, and
TBK1, a novel IKK-related kinase.";
EMBO J. 18:6694-6704(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Swiss Webster / NIH;
Wisniewski D., Marcy A.I.;
"Mus musculus homolog to human T2K cDNA.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
DISRUPTION PHENOTYPE.
PubMed=10990461; DOI=10.1093/emboj/19.18.4976;
Bonnard M., Mirtsos C., Suzuki S., Graham K., Huang J., Ng M.,
Itie A., Wakeham A., Shahinian A., Henzel W.J., Elia A.J.,
Shillinglaw W., Mak T.W., Cao Z., Yeh W.-C.;
"Deficiency of T2K leads to apoptotic liver degeneration and impaired
NF-kappaB-dependent gene transcription.";
EMBO J. 19:4976-4985(2000).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15210742; DOI=10.1084/jem.20040520;
Hemmi H., Takeuchi O., Sato S., Yamamoto M., Kaisho T., Sanjo H.,
Kawai T., Hoshino K., Takeda K., Akira S.;
"The roles of two IkappaB kinase-related kinases in lipopolysaccharide
and double stranded RNA signaling and viral infection.";
J. Exp. Med. 199:1641-1650(2004).
[6]
DISRUPTION PHENOTYPE.
PubMed=14679297; DOI=10.1073/pnas.2237236100;
McWhirter S.M., Fitzgerald K.A., Rosains J., Rowe D.C.,
Golenbock D.T., Maniatis T.;
"IFN-regulatory factor 3-dependent gene expression is defective in
Tbk1-deficient mouse embryonic fibroblasts.";
Proc. Natl. Acad. Sci. U.S.A. 101:233-238(2004).
[7]
FUNCTION.
PubMed=15661922; DOI=10.4049/jimmunol.174.3.1602;
O'Connell R.M., Vaidya S.A., Perry A.K., Saha S.K., Dempsey P.W.,
Cheng G.;
"Immune activation of type I IFNs by Listeria monocytogenes occurs
independently of TLR4, TLR2, and receptor interacting protein 2 but
involves TNFR-associated NF kappa B kinase-binding kinase 1.";
J. Immunol. 174:1602-1607(2005).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION IN ENERGY BALANCE, ENZYME REGULATION, AND PHOSPHORYLATION AT
SER-172.
PubMed=23396211; DOI=10.1038/nm.3082;
Reilly S.M., Chiang S.H., Decker S.J., Chang L., Uhm M., Larsen M.J.,
Rubin J.R., Mowers J., White N.M., Hochberg I., Downes M., Yu R.T.,
Liddle C., Evans R.M., Oh D., Li P., Olefsky J.M., Saltiel A.R.;
"An inhibitor of the protein kinases TBK1 and IKK-[?] improves
obesity-related metabolic dysfunctions in mice.";
Nat. Med. 19:313-321(2013).
[10]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-656 IN COMPLEX WITH
INHIBITORS, SUBUNIT, AND COILED-COIL.
PubMed=23746807; DOI=10.1016/j.str.2013.04.025;
Shu C., Sankaran B., Chaton C.T., Herr A.B., Mishra A., Peng J.,
Li P.;
"Structural insights into the functions of TBK1 in innate
antimicrobial immunity.";
Structure 21:1137-1148(2013).
-!- FUNCTION: Serine/threonine kinase that plays an essential role in
regulating inflammatory responses to foreign agents
(PubMed:10581243, PubMed:15210742, PubMed:15661922,
PubMed:23396211). Following activation of toll-like receptors by
viral or bacterial components, associates with TRAF3 and TANK and
phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7
as well as DDX3X (By similarity). This activity allows subsequent
homodimerization and nuclear translocation of the IRFs leading to
transcriptional activation of pro-inflammatory and antiviral genes
including IFNA and IFNB. In order to establish such an antiviral
state, TBK1 form several different complexes whose composition
depends on the type of cell and cellular stimuli. Thus, several
scaffolding molecules including FADD, TRADD, MAVS, AZI2, TANK or
TBKBP1/SINTBAD can be recruited to the TBK1-containing-complexes.
Under particular conditions, functions as a NF-kappa-B effector by
phosphorylating NF-kappa-B inhibitor alpha/NFKBIA, IKBKB or RELA
to translocate NF-Kappa-B to the nucleus. Restricts bacterial
proliferation by phosphorylating the autophagy receptor
OPTN/Optineurin on 'Ser-177', thus enhancing LC3 binding affinity
and antibacterial autophagy (By similarity). Phosphorylates SMCR8
component of the C9orf72-SMCR8 complex, promoting autophagosome
maturation (By similarity). Phosphorylates and activates AKT1.
Seems to play a role in energy balance regulation by sustaining a
state of chronic, low-grade inflammation in obesity, wich leads to
a negative impact on insulin sensitivity.
{ECO:0000250|UniProtKB:Q9UHD2, ECO:0000269|PubMed:10581243,
ECO:0000269|PubMed:15210742, ECO:0000269|PubMed:15661922,
ECO:0000269|PubMed:23396211}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Kinase activity is inhibited competitively by
amlexanox. {ECO:0000269|PubMed:23396211}.
-!- SUBUNIT: Homodimer. Interacts with DDX3X, TIRAP and TRAF2. Part of
a ternary complex consisting of TANK, TRAF2 and TBK1. Interacts
with AZI2, TANK and TBKBP1; these interactions are mutually
exclusive and mediate TBK1 activation. Interacts with GSK3B; this
interaction promotes TBK1 self-association and
autophosphorylation. Interacts with SIKE1; SIKE1 is associated
with TBK1 under physiological condition and dissociated from TBK1
upon viral infection or TLR3 stimulation. Interacts with IRF3 and
DDX58/RIG-I. Interacts with CYLD. Interacts with OPTN and TRAF3.
Interacts with SRC. Interacts with the exocyst complex subunit
SEC5/EXOC2; this interaction is sufficient to trigger TBK1
activity. Interacts with TMEM173/MITA. Interacts with IFIT3 (via
N-terminus). Interacts with MAVS only in the presence of IFIT3.
Interacts with TICAM1 and this interaction is enhanced in the
presence of WDFY1 (By similarity). Interacts with TRIM23 (By
similarity). {ECO:0000250|UniProtKB:Q9UHD2,
ECO:0000269|PubMed:23746807}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-764193, EBI-764193;
O41932:GAMMAHV.ORF11 (xeno); NbExp=3; IntAct=EBI-764193, EBI-9544132;
P70347:Tank; NbExp=7; IntAct=EBI-764193, EBI-646116;
A2A9T0:Tbkbp1; NbExp=2; IntAct=EBI-764193, EBI-7987134;
Q80UF7:Ticam1; NbExp=2; IntAct=EBI-764193, EBI-3649271;
Q3TBT3:Tmem173; NbExp=3; IntAct=EBI-764193, EBI-3862093;
-!- SUBCELLULAR LOCATION: Cytoplasm. Note=Upon mitogen stimulation or
triggering of the immune system, TBK1 is recruited to the exocyst
by EXOC2. {ECO:0000250}.
-!- DOMAIN: Comprises A N-terminal kinase domain, a ubiquitin-like
domain and a C-terminal coiled-coil region mediating
homodimerization. {ECO:0000269|PubMed:23746807}.
-!- PTM: Autophosphorylation at Ser-172 activates the kinase, and is
an essential step for virus-triggered signaling. Phosphorylated by
IKBKB/IKKB at Ser-172. Phosphorylation requires homodimerization
and ubiquitination at Lys-30 and Lys-401. Dephosphorylated at Ser-
172 by PPM1B and this negatively regulates its role in mediating
antiviral response. {ECO:0000250|UniProtKB:Q9UHD2}.
-!- PTM: 'Lys-63'-linked polyubiquitination by MIB1 after RNA virus
infection, or by NRDP1 after LPS stimulation at Lys-30 and Lys-
401, participates in kinase activation. 'Lys-48'-linked
polyubiquitination at Lys-670 by DTX4 leads to proteasomal
degradation. 'Lys-48'-linked polyubiquitination by TRAIP also
leads to proteasomal degradation. 'Lys-63'-linked
polyubiquitination by RNF128 at Lys-30 and Lys-401 leads to the
activation of antiviral responses. {ECO:0000250|UniProtKB:Q9UHD2}.
-!- DISRUPTION PHENOTYPE: Mice display embryonic lethality at E14.5
due to massive liver degeneration and apoptosis. Embryonic
fibroblasts from mice lacking Tbk1 exhibit dramatically reduced
transcription of NF-kappa-B, as well as marked defects in
interferon alpha and beta, and RANTES gene expression after
infection with Sendai or Newcastle disease virus.
{ECO:0000269|PubMed:10990461, ECO:0000269|PubMed:14679297,
ECO:0000269|PubMed:15210742}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. I-kappa-B kinase subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
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EMBL; AF191839; AAF05990.1; -; mRNA.
EMBL; AF145705; AAD34590.1; -; mRNA.
EMBL; AK004269; BAB23244.1; -; mRNA.
EMBL; AK004649; BAB23440.1; -; mRNA.
CCDS; CCDS24212.1; -.
RefSeq; NP_062760.3; NM_019786.4.
UniGene; Mm.34580; -.
PDB; 4JL9; X-ray; 3.10 A; A=2-656.
PDB; 4JLC; X-ray; 3.00 A; A=2-656.
PDBsum; 4JL9; -.
PDBsum; 4JLC; -.
ProteinModelPortal; Q9WUN2; -.
SMR; Q9WUN2; -.
BioGrid; 208009; 20.
DIP; DIP-29880N; -.
IntAct; Q9WUN2; 17.
MINT; Q9WUN2; -.
STRING; 10090.ENSMUSP00000020316; -.
BindingDB; Q9WUN2; -.
ChEMBL; CHEMBL2189160; -.
iPTMnet; Q9WUN2; -.
PhosphoSitePlus; Q9WUN2; -.
EPD; Q9WUN2; -.
MaxQB; Q9WUN2; -.
PaxDb; Q9WUN2; -.
PRIDE; Q9WUN2; -.
Ensembl; ENSMUST00000020316; ENSMUSP00000020316; ENSMUSG00000020115.
GeneID; 56480; -.
KEGG; mmu:56480; -.
UCSC; uc007hft.3; mouse.
CTD; 29110; -.
MGI; MGI:1929658; Tbk1.
eggNOG; KOG4250; Eukaryota.
eggNOG; ENOG410XRMU; LUCA.
GeneTree; ENSGT00910000144033; -.
HOGENOM; HOG000220867; -.
HOVERGEN; HBG008494; -.
InParanoid; Q9WUN2; -.
KO; K05410; -.
OMA; FRGRHKK; -.
OrthoDB; EOG091G0354; -.
PhylomeDB; Q9WUN2; -.
TreeFam; TF324269; -.
Reactome; R-MMU-3134975; Regulation of innate immune responses to cytosolic DNA.
Reactome; R-MMU-3249367; STAT6-mediated induction of chemokines.
Reactome; R-MMU-3270619; IRF3-mediated induction of type I IFN.
Reactome; R-MMU-9008059; Interleukin-37 signaling.
Reactome; R-MMU-936440; Negative regulators of DDX58/IFIH1 signaling.
Reactome; R-MMU-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
PRO; PR:Q9WUN2; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000020115; -.
CleanEx; MM_TBK1; -.
ExpressionAtlas; Q9WUN2; baseline and differential.
Genevisible; Q9WUN2; MM.
GO; GO:0016235; C:aggresome; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003676; F:nucleic acid binding; IDA:MGI.
GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0002218; P:activation of innate immune response; IMP:MGI.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0044565; P:dendritic cell proliferation; IGI:MGI.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0032727; P:positive regulation of interferon-alpha production; ISO:MGI.
GO; GO:0045359; P:positive regulation of interferon-beta biosynthetic process; IMP:MGI.
GO; GO:0032728; P:positive regulation of interferon-beta production; ISO:MGI.
GO; GO:0016239; P:positive regulation of macroautophagy; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:1904417; P:positive regulation of xenophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
3D-structure; Antiviral defense; ATP-binding; Coiled coil;
Complete proteome; Cytoplasm; Immunity; Innate immunity;
Isopeptide bond; Kinase; Nucleotide-binding; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Ubl conjugation.
CHAIN 1 729 Serine/threonine-protein kinase TBK1.
/FTId=PRO_0000086744.
DOMAIN 9 310 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 309 385 Ubiquitin-like.
NP_BIND 15 23 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 621 629 Interaction with AZI2, TANK and TBKBP1.
{ECO:0000250}.
COILED 407 657 {ECO:0000269|PubMed:23746807}.
COILED 658 713 {ECO:0000255}.
ACT_SITE 135 135 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 38 38 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 172 172 Phosphoserine; by autocatalysis and IKKB.
{ECO:0000269|PubMed:23396211}.
MOD_RES 716 716 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UHD2}.
CROSSLNK 30 30 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9UHD2}.
CROSSLNK 401 401 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9UHD2}.
CROSSLNK 670 670 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9UHD2}.
CONFLICT 468 468 L -> V (in Ref. 3; BAB23440).
{ECO:0000305}.
CONFLICT 594 594 A -> S (in Ref. 3; BAB23244).
{ECO:0000305}.
CONFLICT 631 631 L -> S (in Ref. 3; BAB23440).
{ECO:0000305}.
STRAND 5 14 {ECO:0000244|PDB:4JLC}.
STRAND 22 28 {ECO:0000244|PDB:4JLC}.
TURN 29 31 {ECO:0000244|PDB:4JLC}.
STRAND 34 39 {ECO:0000244|PDB:4JLC}.
HELIX 49 60 {ECO:0000244|PDB:4JLC}.
STRAND 70 75 {ECO:0000244|PDB:4JLC}.
TURN 77 79 {ECO:0000244|PDB:4JLC}.
STRAND 82 87 {ECO:0000244|PDB:4JLC}.
HELIX 94 98 {ECO:0000244|PDB:4JLC}.
HELIX 101 103 {ECO:0000244|PDB:4JLC}.
HELIX 109 127 {ECO:0000244|PDB:4JLC}.
STRAND 128 130 {ECO:0000244|PDB:4JLC}.
HELIX 138 140 {ECO:0000244|PDB:4JLC}.
STRAND 141 145 {ECO:0000244|PDB:4JLC}.
STRAND 149 155 {ECO:0000244|PDB:4JLC}.
HELIX 176 179 {ECO:0000244|PDB:4JLC}.
HELIX 182 192 {ECO:0000244|PDB:4JLC}.
STRAND 194 197 {ECO:0000244|PDB:4JLC}.
STRAND 200 202 {ECO:0000244|PDB:4JLC}.
HELIX 203 216 {ECO:0000244|PDB:4JLC}.
STRAND 220 222 {ECO:0000244|PDB:4JLC}.
HELIX 231 239 {ECO:0000244|PDB:4JLC}.
STRAND 247 249 {ECO:0000244|PDB:4JLC}.
STRAND 252 254 {ECO:0000244|PDB:4JLC}.
STRAND 258 262 {ECO:0000244|PDB:4JLC}.
HELIX 271 284 {ECO:0000244|PDB:4JLC}.
HELIX 289 292 {ECO:0000244|PDB:4JLC}.
HELIX 295 307 {ECO:0000244|PDB:4JLC}.
STRAND 309 315 {ECO:0000244|PDB:4JLC}.
TURN 316 319 {ECO:0000244|PDB:4JLC}.
STRAND 320 326 {ECO:0000244|PDB:4JLC}.
STRAND 328 330 {ECO:0000244|PDB:4JLC}.
HELIX 332 343 {ECO:0000244|PDB:4JLC}.
HELIX 347 349 {ECO:0000244|PDB:4JLC}.
STRAND 351 354 {ECO:0000244|PDB:4JLC}.
STRAND 357 359 {ECO:0000244|PDB:4JLC}.
HELIX 367 369 {ECO:0000244|PDB:4JLC}.
STRAND 375 377 {ECO:0000244|PDB:4JLC}.
STRAND 379 382 {ECO:0000244|PDB:4JLC}.
HELIX 408 483 {ECO:0000244|PDB:4JLC}.
STRAND 484 486 {ECO:0000244|PDB:4JLC}.
HELIX 495 524 {ECO:0000244|PDB:4JLC}.
STRAND 530 532 {ECO:0000244|PDB:4JLC}.
HELIX 536 539 {ECO:0000244|PDB:4JLC}.
HELIX 544 546 {ECO:0000244|PDB:4JLC}.
HELIX 548 571 {ECO:0000244|PDB:4JLC}.
HELIX 577 644 {ECO:0000244|PDB:4JLC}.
HELIX 645 647 {ECO:0000244|PDB:4JLC}.
SEQUENCE 729 AA; 83425 MW; 978ADDE3061DACD1 CRC64;
MQSTSNHLWL LSDILGQGAT ANVFRGRHKK TGDLYAVKVF NNISFLRPVD VQMREFEVLK
KLNHKNIVKL FAIEEETTTR HKVLIMEFCP CGSLYTVLEE PSNAYGLPES EFLIVLRDVV
GGMNHLRENG IVHRDIKPGN IMRVIGEDGQ SVYKLTDFGA ARELEDDEQF VSLYGTEEYL
HPDMYERAVL RKDHQKKYGA TVDLWSVGVT FYHAATGSLP FRPFEGPRRN KEVMYKIITG
KPSGAISGVQ KAENGPIDWS GDMPLSCSLS QGLQALLTPV LANILEADQE KCWGFDQFFA
ETSDVLHRMV IHVFSLQHMT AHKIYIHSYN TAAVFHELVY KQTKIVSSNQ ELIYEGRRLV
LELGRLAQHF PKTTEENPIF VTSREQLNTV GLRYEKISLP KIHPRYDLDG DASMAKAVTG
VVCYACRTAS TLLLYQELMR KGVRWLVELV KDDYNETVHK KTEVVITLDF CIRNIEKTVK
VYEKLMKVNL EAAELGEISD IHTKLLRLSS SQGTIESSLQ DISSRLSPGG LLADTWAHQE
GTHPRDRNVE KLQVLLNCIT EIYYQFKKDK AERRLAYNEE QIHKFDKQKL YYHATKAMSH
FSEECVRKYE AFKDKSEEWM RKMLHLRKQL LSLTNQCFDI EEEVSKYQDY TNELQETLPQ
KMLAASGGVK HAMAPIYPSS NTLVEMTLGM KKLKEEMEGV VKELAENNHI LERFGSLTMD
GGLRNVDCL


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