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Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (PI3-kinase subunit alpha) (PI3K-alpha) (PI3Kalpha) (PtdIns-3-kinase subunit alpha) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha) (PtdIns-3-kinase subunit p110-alpha) (p110alpha) (Phosphoinositide-3-kinase catalytic alpha polypeptide) (Serine/threonine protein kinase PIK3CA) (EC 2.7.11.1)

 PK3CA_MOUSE             Reviewed;        1068 AA.
P42337; Q0VGQ5;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
22-NOV-2017, entry version 162.
RecName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform;
Short=PI3-kinase subunit alpha;
Short=PI3K-alpha;
Short=PI3Kalpha;
Short=PtdIns-3-kinase subunit alpha;
EC=2.7.1.153 {ECO:0000250|UniProtKB:P32871};
AltName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha;
Short=PtdIns-3-kinase subunit p110-alpha;
Short=p110alpha;
AltName: Full=Phosphoinositide-3-kinase catalytic alpha polypeptide;
AltName: Full=Serine/threonine protein kinase PIK3CA;
EC=2.7.11.1 {ECO:0000250|UniProtKB:P32871};
Name=Pik3ca;
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 SUBUNIT.
STRAIN=BALB/cJ;
PubMed=8139567; DOI=10.1128/MCB.14.4.2675;
Klippel A., Escobedo J.A., Hirano M., Williams L.T.;
"The interaction of small domains between the subunits of
phosphatidylinositol 3-kinase determines enzyme activity.";
Mol. Cell. Biol. 14:2675-2685(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH IRS1.
PubMed=15197263; DOI=10.1073/pnas.0403328101;
Drakas R., Tu X., Baserga R.;
"Control of cell size through phosphorylation of upstream binding
factor 1 by nuclear phosphatidylinositol 3-kinase.";
Proc. Natl. Acad. Sci. U.S.A. 101:9272-9276(2004).
[5]
FUNCTION.
PubMed=16647110; DOI=10.1016/j.cell.2006.03.035;
Knight Z.A., Gonzalez B., Feldman M.E., Zunder E.R., Goldenberg D.D.,
Williams O., Loewith R., Stokoe D., Balla A., Toth B., Balla T.,
Weiss W.A., Williams R.L., Shokat K.M.;
"A pharmacological map of the PI3-K family defines a role for
p110alpha in insulin signaling.";
Cell 125:733-747(2006).
[6]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-933.
PubMed=16625210; DOI=10.1038/nature04694;
Foukas L.C., Claret M., Pearce W., Okkenhaug K., Meek S., Peskett E.,
Sancho S., Smith A.J.H., Withers D.J., Vanhaesebroeck B.;
"Critical role for the p110alpha phosphoinositide-3-OH kinase in
growth and metabolic regulation.";
Nature 441:366-370(2006).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17060635; DOI=10.1073/pnas.0607899103;
Zhao J.J., Cheng H., Jia S., Wang L., Gjoerup O.V., Mikami A.,
Roberts T.M.;
"The p110alpha isoform of PI3K is essential for proper growth factor
signaling and oncogenic transformation.";
Proc. Natl. Acad. Sci. U.S.A. 103:16296-16300(2006).
[8]
FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH HRAS AND KRAS, AND
MUTAGENESIS OF THR-208 AND LYS-227.
PubMed=17540175; DOI=10.1016/j.cell.2007.03.051;
Gupta S., Ramjaun A.R., Haiko P., Wang Y., Warne P.H., Nicke B.,
Nye E., Stamp G., Alitalo K., Downward J.;
"Binding of ras to phosphoinositide 3-kinase p110alpha is required for
ras-driven tumorigenesis in mice.";
Cell 129:957-968(2007).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18449193; DOI=10.1038/nature06892;
Graupera M., Guillermet-Guibert J., Foukas L.C., Phng L.-K.,
Cain R.J., Salpekar A., Pearce W., Meek S., Millan J., Cutillas P.R.,
Smith A.J.H., Ridley A.J., Ruhrberg C., Gerhardt H.,
Vanhaesebroeck B.;
"Angiogenesis selectively requires the p110alpha isoform of PI3K to
control endothelial cell migration.";
Nature 453:662-666(2008).
[10]
FUNCTION.
PubMed=19604150; DOI=10.1042/BJ20090687;
Tamura N., Hazeki K., Okazaki N., Kametani Y., Murakami H., Takaba Y.,
Ishikawa Y., Nigorikawa K., Hazeki O.;
"Specific role of phosphoinositide 3-kinase p110alpha in the
regulation of phagocytosis and pinocytosis in macrophages.";
Biochem. J. 423:99-108(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, and Spleen;
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).
[12]
FUNCTION IN CARDIOMYOGENESIS, AND FUNCTION IN VASCULOGENESIS.
PubMed=21540297; DOI=10.1242/jcs.077594;
Bekhite M.M., Finkensieper A., Binas S., Mueller J., Wetzker R.,
Figulla H.-R., Sauer H., Wartenberg M.;
"VEGF-mediated PI3K class IA and PKC signaling in cardiomyogenesis and
vasculogenesis of mouse embryonic stem cells.";
J. Cell Sci. 124:1819-1830(2011).
-!- FUNCTION: Phosphoinositide-3-kinase (PI3K) that phosphorylates
PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-
phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-
bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate
(PIP3). PIP3 plays a key role by recruiting PH domain-containing
proteins to the membrane, including AKT1 and PDPK1, activating
signaling cascades involved in cell growth, survival,
proliferation, motility and morphology. Participates in cellular
signaling in response to various growth factors. Involved in the
activation of AKT1 upon stimulation by receptor tyrosine kinases
ligands such as EGF, insulin, IGF1, VEGFA and PDGF. Involved in
signaling via insulin-receptor substrate (IRS) proteins. Essential
in endothelial cell migration during vascular development through
VEGFA signaling, possibly by regulating RhoA activity. Required
for lymphatic vasculature development, possibly by binding to RAS
and by activation by EGF and FGF2, but not by PDGF. Regulates
invadopodia formation through the PDPK1-AKT1 pathway. Participates
in cardiomyogenesis in embryonic stem cells through a AKT1
pathway. Participates in vasculogenesis in embryonic stem cells
through PDK1 and protein kinase C pathway. Also has serine-protein
kinase activity: phosphorylates PIK3R1 (p85alpha regulatory
subunit), EIF4EBP1 and HRAS. Plays a role in the positive
regulation of phagocytosis and pinocytosis (PubMed:19604150).
{ECO:0000269|PubMed:16625210, ECO:0000269|PubMed:16647110,
ECO:0000269|PubMed:17060635, ECO:0000269|PubMed:17540175,
ECO:0000269|PubMed:18449193, ECO:0000269|PubMed:19604150,
ECO:0000269|PubMed:21540297}.
-!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4,5-
bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-
trisphosphate. {ECO:0000250|UniProtKB:P32871}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:P32871}.
-!- SUBUNIT: Heterodimer of a catalytic subunit PIK3CA and a p85
regulatory subunit (PIK3R1, PIK3R2 or PIK3R3) (PubMed:8139567).
Interacts with IRS1 in nuclear extracts (PubMed:15197263).
Interacts with RUFY3. Interacts with RASD2. Interacts with APPL1
(By similarity). Interacts with HRAS and KRAS (PubMed:17540175).
Interaction with HRAS/KRAS is required for PI3K pathway signaling
and cell proliferation stimulated by EGF and FGF2
(PubMed:17540175). Interacts with FAM83B; activates the PI3K/AKT
signaling cascade (By similarity). {ECO:0000250|UniProtKB:P42336,
ECO:0000269|PubMed:15197263, ECO:0000269|PubMed:17540175,
ECO:0000269|PubMed:8139567}.
-!- INTERACTION:
P41241:Csk; NbExp=2; IntAct=EBI-641748, EBI-2553183;
P01112:HRAS (xeno); NbExp=2; IntAct=EBI-641748, EBI-350145;
P26450:Pik3r1; NbExp=7; IntAct=EBI-641748, EBI-641764;
-!- DOMAIN: The PI3K-ABD domain and the PI3K-RBD domain interact with
the PI3K/PI4K kinase domain. The C2 PI3K-type domain may
facilitate the recruitment to the plasma membrane. The inhibitory
interactions with PIK3R1 are mediated by the PI3K-ABD domain and
the C2 PI3K-type domain with the iSH2 (inter-SH2) region of
PIK3R1, and the C2 PI3K-type domain, the PI3K helical domain, and
the PI3K/PI4K kinase domain with the nSH2 (N-terminal SH2) region
of PIK3R1. {ECO:0000250|UniProtKB:P42336}.
-!- DISRUPTION PHENOTYPE: Lethal. Embryonic fibroblasts cells are
resistant to oncogenic transformation induced by oncogenic
receptor tyrosine kinases (RTKs), are unable to differentiate into
adipocytes and deficient in cellular signaling in response to
various growth factors. Defective responsiveness to insulin led to
reduced somatic growth, hyperinsulinemia, glucose intolerance,
hyperphagia and increased adiposity. {ECO:0000269|PubMed:16625210,
ECO:0000269|PubMed:17060635, ECO:0000269|PubMed:17540175,
ECO:0000269|PubMed:18449193}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
{ECO:0000255|PROSITE-ProRule:PRU00877, ECO:0000255|PROSITE-
ProRule:PRU00879, ECO:0000255|PROSITE-ProRule:PRU00880}.
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EMBL; U03279; AAA18334.1; -; mRNA.
EMBL; CH466530; EDL34990.1; -; Genomic_DNA.
EMBL; BC089038; AAH89038.1; -; mRNA.
EMBL; BC130228; AAI30229.1; -; mRNA.
CCDS; CCDS38409.1; -.
RefSeq; NP_032865.2; NM_008839.2.
RefSeq; XP_006535472.1; XM_006535409.3.
RefSeq; XP_006535473.1; XM_006535410.3.
UniGene; Mm.260521; -.
PDB; 4A55; X-ray; 3.50 A; A=1-1068.
PDBsum; 4A55; -.
ProteinModelPortal; P42337; -.
SMR; P42337; -.
BioGrid; 202160; 6.
CORUM; P42337; -.
DIP; DIP-32095N; -.
IntAct; P42337; 13.
MINT; MINT-219865; -.
STRING; 10090.ENSMUSP00000029201; -.
BindingDB; P42337; -.
ChEMBL; CHEMBL2499; -.
iPTMnet; P42337; -.
PhosphoSitePlus; P42337; -.
EPD; P42337; -.
MaxQB; P42337; -.
PaxDb; P42337; -.
PRIDE; P42337; -.
Ensembl; ENSMUST00000029201; ENSMUSP00000029201; ENSMUSG00000027665.
Ensembl; ENSMUST00000108243; ENSMUSP00000103878; ENSMUSG00000027665.
GeneID; 18706; -.
KEGG; mmu:18706; -.
UCSC; uc008owd.2; mouse.
CTD; 5290; -.
MGI; MGI:1206581; Pik3ca.
eggNOG; KOG0904; Eukaryota.
eggNOG; COG5032; LUCA.
GeneTree; ENSGT00760000119110; -.
HOGENOM; HOG000252911; -.
HOVERGEN; HBG052721; -.
InParanoid; P42337; -.
KO; K00922; -.
OMA; PMVRAFA; -.
OrthoDB; EOG091G027R; -.
TreeFam; TF102031; -.
BRENDA; 2.7.1.137; 3474.
BRENDA; 2.7.1.153; 3474.
Reactome; R-MMU-109704; PI3K Cascade.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-1250342; PI3K events in ERBB4 signaling.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-1266695; Interleukin-7 signaling.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-MMU-180292; GAB1 signalosome.
Reactome; R-MMU-186763; Downstream signal transduction.
Reactome; R-MMU-1963642; PI3K events in ERBB2 signaling.
Reactome; R-MMU-198203; PI3K/AKT activation.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
Reactome; R-MMU-210993; Tie2 Signaling.
Reactome; R-MMU-2424491; DAP12 signaling.
Reactome; R-MMU-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-MMU-388841; Costimulation by the CD28 family.
Reactome; R-MMU-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-MMU-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-MMU-416476; G alpha (q) signalling events.
Reactome; R-MMU-416482; G alpha (12/13) signalling events.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-MMU-5654689; PI-3K cascade:FGFR1.
Reactome; R-MMU-5654695; PI-3K cascade:FGFR2.
Reactome; R-MMU-5654710; PI-3K cascade:FGFR3.
Reactome; R-MMU-5654720; PI-3K cascade:FGFR4.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-8851907; MET activates PI3K/AKT signaling.
Reactome; R-MMU-8853659; RET signaling.
Reactome; R-MMU-912526; Interleukin receptor SHC signaling.
Reactome; R-MMU-912631; Regulation of signaling by CBL.
ChiTaRS; Pik3ca; mouse.
PRO; PR:P42337; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000027665; -.
ExpressionAtlas; P42337; baseline and differential.
Genevisible; P42337; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0030027; C:lamellipodium; IDA:MGI.
GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IPI:MGI.
GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IDA:MGI.
GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043560; F:insulin receptor substrate binding; IPI:MGI.
GO; GO:0016301; F:kinase activity; ISO:MGI.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IBA:GO_Central.
GO; GO:0030295; F:protein kinase activator activity; IDA:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0002250; P:adaptive immune response; IBA:GO_Central.
GO; GO:0060612; P:adipose tissue development; IMP:MGI.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
GO; GO:0071333; P:cellular response to glucose stimulus; IMP:MGI.
GO; GO:0097009; P:energy homeostasis; IMP:MGI.
GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
GO; GO:0044029; P:hypomethylation of CpG island; IDA:BHF-UCL.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0001889; P:liver development; IMP:MGI.
GO; GO:2000811; P:negative regulation of anoikis; ISO:MGI.
GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IDA:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
GO; GO:0016310; P:phosphorylation; ISO:MGI.
GO; GO:0030168; P:platelet activation; IBA:GO_Central.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0043491; P:protein kinase B signaling; IMP:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0043457; P:regulation of cellular respiration; IMP:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:2000653; P:regulation of genetic imprinting; IDA:BHF-UCL.
GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
Gene3D; 1.10.1070.11; -; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
InterPro; IPR036940; PI3/4_kinase_cat_sf.
InterPro; IPR018936; PI3/4_kinase_CS.
InterPro; IPR003113; PI3K_adapt-bd_dom.
InterPro; IPR002420; PI3K_C2_dom.
InterPro; IPR000341; PI3K_Ras-bd_dom.
InterPro; IPR008290; PI3K_Vps34.
InterPro; IPR015433; PI_Kinase.
InterPro; IPR001263; PInositide-3_kin_accessory_dom.
InterPro; IPR029071; Ubiquitin-like_domsf.
PANTHER; PTHR10048; PTHR10048; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
Pfam; PF00792; PI3K_C2; 1.
Pfam; PF02192; PI3K_p85B; 1.
Pfam; PF00794; PI3K_rbd; 1.
Pfam; PF00613; PI3Ka; 1.
PIRSF; PIRSF000587; PI3K_Vps34; 1.
SMART; SM00142; PI3K_C2; 1.
SMART; SM00143; PI3K_p85B; 1.
SMART; SM00144; PI3K_rbd; 1.
SMART; SM00145; PI3Ka; 1.
SMART; SM00146; PI3Kc; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00915; PI3_4_KINASE_1; 1.
PROSITE; PS00916; PI3_4_KINASE_2; 1.
PROSITE; PS50290; PI3_4_KINASE_3; 1.
PROSITE; PS51544; PI3K_ABD; 1.
PROSITE; PS51547; PI3K_C2; 1.
PROSITE; PS51546; PI3K_RBD; 1.
PROSITE; PS51545; PIK_HELICAL; 1.
1: Evidence at protein level;
3D-structure; Angiogenesis; ATP-binding; Complete proteome; Kinase;
Nucleotide-binding; Phagocytosis; Proto-oncogene; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 1068 Phosphatidylinositol 4,5-bisphosphate 3-
kinase catalytic subunit alpha isoform.
/FTId=PRO_0000088786.
DOMAIN 16 105 PI3K-ABD. {ECO:0000255|PROSITE-
ProRule:PRU00877}.
DOMAIN 187 289 PI3K-RBD. {ECO:0000255|PROSITE-
ProRule:PRU00879}.
DOMAIN 330 487 C2 PI3K-type. {ECO:0000255|PROSITE-
ProRule:PRU00880}.
DOMAIN 517 694 PIK helical. {ECO:0000255|PROSITE-
ProRule:PRU00878}.
DOMAIN 797 1068 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
MUTAGEN 208 208 T->D: Abolishes binding to HRAS and KRAS;
does not affect kinase activity; displays
defective development of the lymphatic
vasculature, resulting in perinatal
appearance of chylous ascites and is
highly resistant to endogenous Ras
oncogene-induced tumorigenesis; when
associated with A-227.
{ECO:0000269|PubMed:17540175}.
MUTAGEN 227 227 K->A: Abolishes binding to HRAS and KRAS;
does not affect kinase activity; displays
defective development of the lymphatic
vasculature, resulting in perinatal
appearance of chylous ascites and is
highly resistant to endogenous Ras
oncogene-induced tumorigenesis; when
associated with D-208.
{ECO:0000269|PubMed:17540175}.
MUTAGEN 933 933 D->A: Loss of kinase activity; displays
early embryonic lethality at E10-11 and
severe defects in angiogenic sprouting
and vascular remodeling. Heterozygous
mice yield adult mice with markedly
impaired insulin signaling and reduced
activation of effector pathways such as
Akt/PKB. {ECO:0000269|PubMed:16625210}.
CONFLICT 399 399 A -> L (in Ref. 1; AAA18334).
{ECO:0000305}.
STRAND 8 12 {ECO:0000244|PDB:4A55}.
STRAND 18 25 {ECO:0000244|PDB:4A55}.
STRAND 31 37 {ECO:0000244|PDB:4A55}.
HELIX 42 52 {ECO:0000244|PDB:4A55}.
HELIX 53 55 {ECO:0000244|PDB:4A55}.
TURN 57 60 {ECO:0000244|PDB:4A55}.
HELIX 65 67 {ECO:0000244|PDB:4A55}.
STRAND 69 74 {ECO:0000244|PDB:4A55}.
STRAND 77 81 {ECO:0000244|PDB:4A55}.
HELIX 90 92 {ECO:0000244|PDB:4A55}.
STRAND 94 102 {ECO:0000244|PDB:4A55}.
HELIX 109 112 {ECO:0000244|PDB:4A55}.
HELIX 117 121 {ECO:0000244|PDB:4A55}.
HELIX 125 129 {ECO:0000244|PDB:4A55}.
HELIX 134 142 {ECO:0000244|PDB:4A55}.
HELIX 144 153 {ECO:0000244|PDB:4A55}.
TURN 154 157 {ECO:0000244|PDB:4A55}.
HELIX 158 165 {ECO:0000244|PDB:4A55}.
HELIX 179 182 {ECO:0000244|PDB:4A55}.
STRAND 189 196 {ECO:0000244|PDB:4A55}.
TURN 199 202 {ECO:0000244|PDB:4A55}.
STRAND 205 212 {ECO:0000244|PDB:4A55}.
HELIX 217 230 {ECO:0000244|PDB:4A55}.
HELIX 236 246 {ECO:0000244|PDB:4A55}.
HELIX 247 249 {ECO:0000244|PDB:4A55}.
STRAND 250 254 {ECO:0000244|PDB:4A55}.
HELIX 267 269 {ECO:0000244|PDB:4A55}.
HELIX 271 279 {ECO:0000244|PDB:4A55}.
STRAND 284 289 {ECO:0000244|PDB:4A55}.
HELIX 290 295 {ECO:0000244|PDB:4A55}.
STRAND 324 327 {ECO:0000244|PDB:4A55}.
STRAND 332 340 {ECO:0000244|PDB:4A55}.
STRAND 348 350 {ECO:0000244|PDB:4A55}.
STRAND 354 364 {ECO:0000244|PDB:4A55}.
STRAND 378 380 {ECO:0000244|PDB:4A55}.
STRAND 382 392 {ECO:0000244|PDB:4A55}.
TURN 393 395 {ECO:0000244|PDB:4A55}.
STRAND 401 408 {ECO:0000244|PDB:4A55}.
STRAND 423 430 {ECO:0000244|PDB:4A55}.
STRAND 434 436 {ECO:0000244|PDB:4A55}.
STRAND 439 444 {ECO:0000244|PDB:4A55}.
STRAND 454 456 {ECO:0000244|PDB:4A55}.
STRAND 458 460 {ECO:0000244|PDB:4A55}.
STRAND 468 470 {ECO:0000244|PDB:4A55}.
STRAND 472 477 {ECO:0000244|PDB:4A55}.
STRAND 481 485 {ECO:0000244|PDB:4A55}.
HELIX 489 499 {ECO:0000244|PDB:4A55}.
TURN 529 535 {ECO:0000244|PDB:4A55}.
HELIX 545 553 {ECO:0000244|PDB:4A55}.
HELIX 555 558 {ECO:0000244|PDB:4A55}.
HELIX 562 564 {ECO:0000244|PDB:4A55}.
HELIX 565 569 {ECO:0000244|PDB:4A55}.
HELIX 578 588 {ECO:0000244|PDB:4A55}.
HELIX 595 598 {ECO:0000244|PDB:4A55}.
TURN 599 602 {ECO:0000244|PDB:4A55}.
HELIX 609 621 {ECO:0000244|PDB:4A55}.
HELIX 625 630 {ECO:0000244|PDB:4A55}.
HELIX 632 636 {ECO:0000244|PDB:4A55}.
HELIX 639 641 {ECO:0000244|PDB:4A55}.
STRAND 643 646 {ECO:0000244|PDB:4A55}.
HELIX 648 659 {ECO:0000244|PDB:4A55}.
HELIX 661 673 {ECO:0000244|PDB:4A55}.
HELIX 678 694 {ECO:0000244|PDB:4A55}.
TURN 695 697 {ECO:0000244|PDB:4A55}.
HELIX 698 720 {ECO:0000244|PDB:4A55}.
HELIX 728 738 {ECO:0000244|PDB:4A55}.
HELIX 742 747 {ECO:0000244|PDB:4A55}.
STRAND 749 752 {ECO:0000244|PDB:4A55}.
STRAND 759 761 {ECO:0000244|PDB:4A55}.
STRAND 779 784 {ECO:0000244|PDB:4A55}.
HELIX 790 792 {ECO:0000244|PDB:4A55}.
STRAND 795 805 {ECO:0000244|PDB:4A55}.
HELIX 808 827 {ECO:0000244|PDB:4A55}.
STRAND 838 842 {ECO:0000244|PDB:4A55}.
STRAND 845 849 {ECO:0000244|PDB:4A55}.
STRAND 854 856 {ECO:0000244|PDB:4A55}.
HELIX 857 860 {ECO:0000244|PDB:4A55}.
HELIX 876 884 {ECO:0000244|PDB:4A55}.
HELIX 887 889 {ECO:0000244|PDB:4A55}.
HELIX 890 911 {ECO:0000244|PDB:4A55}.
TURN 918 920 {ECO:0000244|PDB:4A55}.
STRAND 921 924 {ECO:0000244|PDB:4A55}.
STRAND 929 931 {ECO:0000244|PDB:4A55}.
HELIX 941 945 {ECO:0000244|PDB:4A55}.
HELIX 957 964 {ECO:0000244|PDB:4A55}.
STRAND 965 967 {ECO:0000244|PDB:4A55}.
HELIX 975 993 {ECO:0000244|PDB:4A55}.
HELIX 995 1004 {ECO:0000244|PDB:4A55}.
STRAND 1013 1015 {ECO:0000244|PDB:4A55}.
HELIX 1016 1025 {ECO:0000244|PDB:4A55}.
HELIX 1032 1043 {ECO:0000244|PDB:4A55}.
TURN 1046 1049 {ECO:0000244|PDB:4A55}.
TURN 1057 1059 {ECO:0000244|PDB:4A55}.
SEQUENCE 1068 AA; 124412 MW; D593283B416ABFD0 CRC64;
MPPRPSSGEL WGIHLMPPRI LVECLLPNGM IVTLECLREA TLVTIKHELF REARKYPLHQ
LLQDETSYIF VSVTQEAERE EFFDETRRLC DLRLFQPFLK VIEPVGNREE KILNREIGFV
IGMPVCEFDM VKDPEVQDFR RNILNVCKEA VDLRDLNSPH SRAMYVYPPN VESSPELPKH
IYNKLDKGQI IVVIWVIVSP NNDKQKYTLK INHDCVPEQV IAEAIRKKTR SMLLSSEQLK
LCVLEYQGKY ILKVCGCDEY FLEKYPLSQY KYIRSCIMLG RMPNLMLMAK ESLYSQLPID
SFTMPSYSRR ISTATPYMNG ETSTKSLWVI NSALRIKILC ATYVNVNIRD IDKIYVRTGI
YHGGEPLCDN VNTQRVPCSN PRWNEWLNYD IYIPDLPRAA RLCLSICSVK GRKGAKEEHC
PLAWGNINLF DYTDTLVSGK MALNLWPVPH GLEDLLNPIG VTGSNPNKET PCLELEFDWF
SSVVKFPDMS VIEEHANWSV SREAGFSYSH TGLSNRLARD NELRENDKEQ LRALCTRDPL
SEITEQEKDF LWSHRHYCVT IPEILPKLLL SVKWNSRDEV AQMYCLVKDW PPIKPEQAME
LLDCNYPDPM VRSFAVRCLE KYLTDDKLSQ YLIQLVQVLK YEQYLDNLLV RFLLKKALTN
QRIGHFFFWH LKSEMHNKTV SQRFGLLLES YCRACGMYLK HLNRQVEAME KLINLTDILK
QEKKDETQKV QMKFLVEQMR QPDFMDALQG FLSPLNPAHQ LGNLRLEECR IMSSAKRPLW
LNWENPDIMS ELLFQNNEII FKNGDDLRQD MLTLQIIRIM ENIWQNQGLD LRMLPYGCLS
IGDCVGLIEV VRNSHTIMQI QCKGGLKGAL QFNSHTLHQW LKDKNKGEIY DAAIDLFTRS
CAGYCVATFI LGIGDRHNSN IMVKDDGQLF HIDFGHFLDH KKKKFGYKRE RVPFVLTQDF
LIVISKGAQE YTKTREFERF QEMCYKAYLA IRQHANLFIN LFSMMLGSGM PELQSFDDIA
YIRKTLALDK TEQEALEYFT KQMNDAHHGG WTTKMDWIFH TIKQHALN


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