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Ribosomal protein S6 kinase alpha-3 (S6K-alpha-3) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 3) (p90-RSK 3) (p90RSK3) (MAP kinase-activated protein kinase 1b) (MAPK-activated protein kinase 1b) (MAPKAP kinase 1b) (MAPKAPK-1b) (Ribosomal S6 kinase 2) (RSK-2) (pp90RSK2)

 KS6A3_MOUSE             Reviewed;         740 AA.
P18654; B1AXN4; Q03140; Q8K3J8;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
25-MAR-2003, sequence version 2.
18-JUL-2018, entry version 188.
RecName: Full=Ribosomal protein S6 kinase alpha-3;
Short=S6K-alpha-3;
EC=2.7.11.1;
AltName: Full=90 kDa ribosomal protein S6 kinase 3;
Short=p90-RSK 3;
Short=p90RSK3;
AltName: Full=MAP kinase-activated protein kinase 1b;
Short=MAPK-activated protein kinase 1b;
Short=MAPKAP kinase 1b;
Short=MAPKAPK-1b;
AltName: Full=Ribosomal S6 kinase 2;
Short=RSK-2;
AltName: Full=pp90RSK2;
Name=Rps6ka3; Synonyms=Mapkapk1b, Rps6ka-rs1, Rsk2;
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].
PubMed=12016217; DOI=10.1074/jbc.M202663200;
Chrestensen C.A., Sturgill T.W.;
"Characterization of the p90 ribosomal S6 kinase 2 carboxyl-terminal
domain as a protein kinase.";
J. Biol. Chem. 277:27733-27741(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 108-740.
PubMed=2779569; DOI=10.1128/MCB.9.9.3850;
Alcorta D.A., Crews C.M., Sweet L.J., Bankston L., Jones S.W.,
Erikson R.L.;
"Sequence and expression of chicken and mouse rsk: homologs of Xenopus
laevis ribosomal S6 kinase.";
Mol. Cell. Biol. 9:3850-3859(1989).
[4]
ENZYME REGULATION, PHOSPHORYLATION AT SER-227 AND SER-386, AND
MUTAGENESIS OF SER-227 AND SER-386.
PubMed=10480933; DOI=10.1074/jbc.274.38.27168;
Jensen C.J., Buch M.-B., Krag T.O., Hemmings B.A., Gammeltoft S.,
Froedin M.;
"90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-
phosphoinositide-dependent protein kinase-1.";
J. Biol. Chem. 274:27168-27176(1999).
[5]
FUNCTION, ENZYME REGULATION, AND MUTAGENESIS OF SER-386.
PubMed=10856237; DOI=10.1093/emboj/19.12.2924;
Froedin M., Jensen C.J., Merienne K., Gammeltoft S.;
"A phosphoserine-regulated docking site in the protein kinase RSK2
that recruits and activates PDK1.";
EMBO J. 19:2924-2934(2000).
[6]
FUNCTION IN PHOSPHORYLATION OF CDKN1B.
PubMed=14504289; DOI=10.1074/jbc.M306614200;
Fujita N., Sato S., Tsuruo T.;
"Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein
S6 kinases promotes its binding to 14-3-3 and cytoplasmic
localization.";
J. Biol. Chem. 278:49254-49260(2003).
[7]
FUNCTION IN HEMATOPOIETIC TRANSFORMATION, PHOSPHORYLATION AT TYR-529,
AND MUTAGENESIS OF TYR-529.
PubMed=17785202; DOI=10.1016/j.ccr.2007.08.003;
Kang S., Dong S., Gu T.L., Guo A., Cohen M.S., Lonial S., Khoury H.J.,
Fabbro D., Gilliland D.G., Bergsagel P.L., Taunton J.,
Polakiewicz R.D., Chen J.;
"FGFR3 activates RSK2 to mediate hematopoietic transformation through
tyrosine phosphorylation of RSK2 and activation of the MEK/ERK
pathway.";
Cancer Cell 12:201-214(2007).
[8]
FUNCTION IN TOLL-LIKE RECEPTOR SIGNALING, AND PHOSPHORYLATION AT
SER-386.
PubMed=17906627; DOI=10.1038/ni1517;
Zaru R., Ronkina N., Gaestel M., Arthur J.S., Watts C.;
"The MAPK-activated kinase Rsk controls an acute Toll-like receptor
signaling response in dendritic cells and is activated through two
distinct pathways.";
Nat. Immunol. 8:1227-1235(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365; SER-369; SER-415
AND SER-715, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
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).
[10]
FUNCTION.
PubMed=22827337; DOI=10.1042/BJ20120938;
Saha M., Carriere A., Cheerathodi M., Zhang X., Lavoie G., Rush J.,
Roux P.P., Ballif B.A.;
"RSK phosphorylates SOS1 creating 14-3-3-docking sites and negatively
regulating MAPK activation.";
Biochem. J. 447:159-166(2012).
[11]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 399-740.
PubMed=18084304; DOI=10.1038/nsmb1347;
Malakhova M., Tereshko V., Lee S.Y., Yao K., Cho Y.Y., Bode A.,
Dong Z.;
"Structural basis for activation of the autoinhibitory C-terminal
kinase domain of p90 RSK2.";
Nat. Struct. Mol. Biol. 15:112-113(2008).
[12]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 44-367.
PubMed=19956600; DOI=10.1371/journal.pone.0008044;
Malakhova M., Kurinov I., Liu K., Zheng D., D'Angelo I., Shim J.H.,
Steinman V., Bode A.M., Dong Z.;
"Structural diversity of the active N-terminal kinase domain of p90
ribosomal S6 kinase 2.";
PLoS ONE 4:E8044-E8044(2009).
-!- FUNCTION: Serine/threonine-protein kinase that acts downstream of
ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic
and stress-induced activation of the transcription factors CREB1,
ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and
EIF4B phosphorylation, and mediates cellular proliferation,
survival, and differentiation by modulating mTOR signaling and
repressing pro-apoptotic function of BAD and DAPK1. In fibroblast,
is required for EGF-stimulated phosphorylation of CREB1 and
histone H3 at 'Ser-10', which results in the subsequent
transcriptional activation of several immediate-early genes. In
response to mitogenic stimulation (EGF and PMA), phosphorylates
and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and
the cofactor CREBBP. Upon insulin-derived signal, acts indirectly
on the transcription regulation of several genes by
phosphorylating GSK3B at 'Ser-9' and inhibiting its activity.
Phosphorylates RPS6 in response to serum or EGF via an mTOR-
independent mechanism and promotes translation initiation by
facilitating assembly of the preinitiation complex. In response to
insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the
EIF3 complex and stimulating cap-dependent translation. Is
involved in the mTOR nutrient-sensing pathway by directly
phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2
ability to suppress mTOR signaling, and mediates phosphorylation
of RPTOR, which regulates mTORC1 activity and may promote
rapamycin-sensitive signaling independently of the PI3K/AKT
pathway. Mediates cell survival by phosphorylating the pro-
apoptotic proteins BAD and DAPK1 and suppressing their pro-
apoptotic function. Promotes the survival of hepatic stellate
cells by phosphorylating CEBPB in response to the hepatotoxin
carbon tetrachloride (CCl4). Is involved in cell cycle regulation
by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B
association with 14-3-3 proteins and prevents its translocation to
the nucleus and inhibition of G1 progression. In LPS-stimulated
dendritic cells, is involved in TLR4-induced macropinocytosis, and
in myeloma cells, acts as effector of FGFR3-mediated
transformation signaling, after direct phosphorylation at Tyr-529
by FGFR3. Phosphorylates DAPK1 (By similarity). Negatively
regulates EGF-induced MAPK1/3 phosphorylation via phosphorylation
of SOS1. Phosphorylates SOS1 at 'Ser-1134' and 'Ser-1161' that
create YWHAB and YWHAE binding sites and which contribute to the
negative regulation of MAPK1/3 phosphorylation (PubMed:22827337).
Phosphorylates EPHA2 at 'Ser-897',the RPS6KA-EPHA2 signaling
pathway controls cell migration (By similarity).
{ECO:0000250|UniProtKB:P51812, ECO:0000269|PubMed:10856237,
ECO:0000269|PubMed:14504289, ECO:0000269|PubMed:17785202,
ECO:0000269|PubMed:17906627, ECO:0000269|PubMed:22827337}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Upon extracellular signal or mitogen
stimulation, phosphorylated at Thr-577 in the C-terminal kinase
domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD
then autophosphorylates Ser-386, allowing binding of PDPK1, which
in turn phosphorylates Ser-227 in the N-terminal kinase domain
(NTDK) leading to the full activation of the protein and
subsequent phosphorylation of the substrates by the NTKD (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in
quiescent cells. Transiently dissociates following mitogenic
stimulation (By similarity). Interacts with NFATC4, ETV1/ER81 and
FGFR1 (By similarity). {ECO:0000250}.
-!- INTERACTION:
P30309:cdc25-1-b (xeno); NbExp=3; IntAct=EBI-397744, EBI-15888737;
P97879:Grip1 (xeno); NbExp=3; IntAct=EBI-397744, EBI-936113;
P28223-1:HTR2A (xeno); NbExp=2; IntAct=EBI-397744, EBI-15573967;
Q4L1J4:Magi1 (xeno); NbExp=2; IntAct=EBI-397744, EBI-5259666;
Q9WV48:Shank1 (xeno); NbExp=2; IntAct=EBI-397744, EBI-80909;
Q9JLU4:Shank3 (xeno); NbExp=2; IntAct=EBI-397744, EBI-6271152;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Intestine, thymus, lung, heart and brain.
-!- PTM: Activated by phosphorylation at Ser-227 by PDPK1.
Autophosphorylated on Ser-386, as part of the activation process.
May be phosphorylated at Thr-365 and Ser-369 by MAPK1/ERK2 and
MAPK3/ERK1. Can also be activated via phosphorylation at Ser-386
by MAPKAPK2. {ECO:0000269|PubMed:10480933,
ECO:0000269|PubMed:17785202, ECO:0000269|PubMed:17906627}.
-!- PTM: N-terminal myristoylation results in an activated kinase in
the absence of added growth factors. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. S6 kinase subfamily. {ECO:0000305}.
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EMBL; AY083469; AAM00022.1; -; mRNA.
EMBL; AL808146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS30502.1; -.
PIR; C32571; C32571.
PIR; S30504; S30504.
RefSeq; NP_683747.1; NM_148945.2.
UniGene; Mm.328476; -.
UniGene; Mm.392829; -.
PDB; 2QR7; X-ray; 2.00 A; A=399-740.
PDB; 2QR8; X-ray; 2.00 A; A=399-740.
PDB; 3G51; X-ray; 1.80 A; A=44-367.
PDB; 3UBD; X-ray; 1.53 A; A=45-346.
PDB; 4EL9; X-ray; 1.55 A; A=45-346.
PDB; 4GUE; X-ray; 1.80 A; A=45-346.
PDB; 4M8T; X-ray; 3.00 A; A=399-740.
PDB; 4MAO; X-ray; 2.60 A; A=399-740.
PDB; 5O1S; X-ray; 1.90 A; A=400-740.
PDBsum; 2QR7; -.
PDBsum; 2QR8; -.
PDBsum; 3G51; -.
PDBsum; 3UBD; -.
PDBsum; 4EL9; -.
PDBsum; 4GUE; -.
PDBsum; 4M8T; -.
PDBsum; 4MAO; -.
PDBsum; 5O1S; -.
ProteinModelPortal; P18654; -.
SMR; P18654; -.
BioGrid; 225783; 10.
CORUM; P18654; -.
DIP; DIP-31554N; -.
ELM; P18654; -.
IntAct; P18654; 10.
MINT; P18654; -.
STRING; 10090.ENSMUSP00000033671; -.
BindingDB; P18654; -.
ChEMBL; CHEMBL3297641; -.
iPTMnet; P18654; -.
PhosphoSitePlus; P18654; -.
SwissPalm; P18654; -.
EPD; P18654; -.
MaxQB; P18654; -.
PaxDb; P18654; -.
PeptideAtlas; P18654; -.
PRIDE; P18654; -.
DNASU; 110651; -.
Ensembl; ENSMUST00000033671; ENSMUSP00000033671; ENSMUSG00000031309.
GeneID; 110651; -.
KEGG; mmu:110651; -.
UCSC; uc009usj.2; mouse.
CTD; 6197; -.
MGI; MGI:104557; Rps6ka3.
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00920000148962; -.
HOVERGEN; HBG108317; -.
InParanoid; P18654; -.
KO; K04373; -.
OMA; YTLNRQD; -.
OrthoDB; EOG091G05Z7; -.
PhylomeDB; P18654; -.
TreeFam; TF313438; -.
Reactome; R-MMU-198753; ERK/MAPK targets.
Reactome; R-MMU-199920; CREB phosphorylation.
Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-MMU-442742; CREB phosphorylation through the activation of Ras.
Reactome; R-MMU-444257; RSK activation.
Reactome; R-MMU-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
ChiTaRS; Rps6ka3; mouse.
EvolutionaryTrace; P18654; -.
PRO; PR:P18654; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000031309; -.
CleanEx; MM_RPS6KA3; -.
ExpressionAtlas; P18654; baseline and differential.
Genevisible; P18654; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISO:MGI.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0002224; P:toll-like receptor signaling pathway; IMP:UniProtKB.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR016239; Ribosomal_S6_kinase_II.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 2.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000606; Ribsml_S6_kin_2; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 2.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell cycle; Complete proteome; Cytoplasm;
Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Stress response; Transferase.
CHAIN 1 740 Ribosomal protein S6 kinase alpha-3.
/FTId=PRO_0000086204.
DOMAIN 68 327 Protein kinase 1. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 328 397 AGC-kinase C-terminal.
DOMAIN 422 679 Protein kinase 2. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 74 82 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 428 436 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 193 193 Proton acceptor. {ECO:0000250}.
ACT_SITE 539 539 Proton acceptor. {ECO:0000250}.
BINDING 100 100 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 451 451 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 227 227 Phosphoserine; by PDPK1.
{ECO:0000269|PubMed:10480933}.
MOD_RES 365 365 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000250|UniProtKB:P51812}.
MOD_RES 386 386 Phosphoserine; by autocatalysis and
MAPKAPK2. {ECO:0000269|PubMed:10480933,
ECO:0000269|PubMed:17906627}.
MOD_RES 415 415 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 529 529 Phosphotyrosine; by FGFR3.
{ECO:0000269|PubMed:17785202}.
MOD_RES 556 556 Phosphoserine.
{ECO:0000250|UniProtKB:P51812}.
MOD_RES 715 715 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MUTAGEN 227 227 S->E: Loss of phosphorylation and
activation by PDPK1.
{ECO:0000269|PubMed:10480933}.
MUTAGEN 386 386 S->A: Loss of phosphorylation by PDPK1;
loss of activation by PDPK1 and EGF.
{ECO:0000269|PubMed:10480933,
ECO:0000269|PubMed:10856237}.
MUTAGEN 386 386 S->E: Loss of interaction with PDPK1 and
phosphorylation at S-227.
{ECO:0000269|PubMed:10480933,
ECO:0000269|PubMed:10856237}.
MUTAGEN 529 529 Y->F: Attenuates activation by MAPK1/ERK1
and MAPK3/ERK2.
{ECO:0000269|PubMed:17785202}.
STRAND 50 56 {ECO:0000244|PDB:3UBD}.
HELIX 65 67 {ECO:0000244|PDB:3UBD}.
STRAND 68 75 {ECO:0000244|PDB:3UBD}.
HELIX 77 79 {ECO:0000244|PDB:3UBD}.
STRAND 81 87 {ECO:0000244|PDB:3UBD}.
TURN 91 94 {ECO:0000244|PDB:3UBD}.
STRAND 96 111 {ECO:0000244|PDB:3UBD}.
HELIX 121 124 {ECO:0000244|PDB:3G51}.
STRAND 133 139 {ECO:0000244|PDB:3UBD}.
STRAND 142 147 {ECO:0000244|PDB:3UBD}.
HELIX 156 162 {ECO:0000244|PDB:3UBD}.
HELIX 167 186 {ECO:0000244|PDB:3UBD}.
HELIX 196 198 {ECO:0000244|PDB:3UBD}.
STRAND 199 201 {ECO:0000244|PDB:3UBD}.
STRAND 207 216 {ECO:0000244|PDB:3UBD}.
HELIX 232 234 {ECO:0000244|PDB:3UBD}.
HELIX 237 241 {ECO:0000244|PDB:3UBD}.
HELIX 248 263 {ECO:0000244|PDB:3UBD}.
HELIX 273 282 {ECO:0000244|PDB:3UBD}.
HELIX 293 302 {ECO:0000244|PDB:3UBD}.
HELIX 307 309 {ECO:0000244|PDB:3UBD}.
TURN 315 317 {ECO:0000244|PDB:3UBD}.
HELIX 318 322 {ECO:0000244|PDB:3UBD}.
HELIX 325 327 {ECO:0000244|PDB:3UBD}.
HELIX 332 336 {ECO:0000244|PDB:3UBD}.
HELIX 418 421 {ECO:0000244|PDB:2QR7}.
STRAND 422 430 {ECO:0000244|PDB:2QR7}.
STRAND 432 441 {ECO:0000244|PDB:2QR7}.
TURN 442 444 {ECO:0000244|PDB:2QR7}.
STRAND 447 454 {ECO:0000244|PDB:2QR7}.
TURN 455 457 {ECO:0000244|PDB:2QR7}.
HELIX 461 470 {ECO:0000244|PDB:2QR7}.
STRAND 479 484 {ECO:0000244|PDB:2QR7}.
STRAND 486 493 {ECO:0000244|PDB:2QR7}.
STRAND 498 500 {ECO:0000244|PDB:4M8T}.
HELIX 501 506 {ECO:0000244|PDB:2QR7}.
HELIX 513 532 {ECO:0000244|PDB:2QR7}.
HELIX 542 544 {ECO:0000244|PDB:2QR7}.
STRAND 545 551 {ECO:0000244|PDB:2QR7}.
HELIX 554 556 {ECO:0000244|PDB:2QR7}.
STRAND 557 559 {ECO:0000244|PDB:2QR7}.
HELIX 562 564 {ECO:0000244|PDB:4M8T}.
HELIX 587 613 {ECO:0000244|PDB:2QR7}.
STRAND 614 616 {ECO:0000244|PDB:4M8T}.
STRAND 619 621 {ECO:0000244|PDB:4M8T}.
HELIX 626 635 {ECO:0000244|PDB:2QR7}.
TURN 643 647 {ECO:0000244|PDB:2QR7}.
HELIX 650 659 {ECO:0000244|PDB:2QR7}.
TURN 664 666 {ECO:0000244|PDB:2QR7}.
HELIX 670 673 {ECO:0000244|PDB:2QR7}.
HELIX 677 680 {ECO:0000244|PDB:2QR7}.
HELIX 682 684 {ECO:0000244|PDB:2QR7}.
HELIX 696 710 {ECO:0000244|PDB:2QR7}.
TURN 711 713 {ECO:0000244|PDB:2QR7}.
SEQUENCE 740 AA; 83694 MW; 0CD54E5918567007 CRC64;
MPLAQLADPW QKMAVESPSD SAENGQQIMD EPMGEEEINP QTEEGSIKEI AITHHVKEGH
EKADPSQFEL LKVLGQGSFG KVFLVKKISG SDARQLYAMK VLKKATLKVR DRVRTKMERD
ILVEVNHPFI VKLHYAFQTE GKLYLILDFL RGGDLFTRLS KEVMFTEEDV KFYLAELALA
LDHLHSLGII YRDLKPENIL LDEEGHIKLT DFGLSKESID HEKKAYSFCG TVEYMAPEVV
NRRGHTQSAD WWSFGVLMFE MLTGTLPFQG KDRKETMTMI LKAKLGMPQF LSPEAQSLLR
MLFKRNPANR LGAGPDGVEE IKRHSFFSTI DWNKLYRREI HPPFKPATGR PEDTFYFDPE
FTAKTPKDSP GIPPSANAHQ LFRGFSFVAI TSDDESQAMQ TVGVHSIVQQ LHRNSIQFTD
GYEVKEDIGV GSYSVCKRCI HKATNMEFAV KIIDKSKRDP TEEIEILLRY GQHPNIITLK
DVYDDGKYVY VVTELMKGGE LLDKILRQKF FSEREASAVL FTITKTVEYL HAQGVVHRDL
KPSNILYVDE SGNPESIRIC DFGFAKQLRA ENGLLMTPCY TANFVAPEVL KRQGYDAACD
IWSLGVLLYT MLTGYTPFAN GPDDTPEEIL ARIGSGKFSL SGGYWNSVSD TAKDLVSKML
HVDPHQRLTA ALVLRHPWIV HWDQLPQYQL NRQDAPHLVK GAMAATYSAL NRNQSPVLEP
VGRSTLAQRR GIKKITSTAL


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