PK3CA_BOVIN
ID PK3CA_BOVIN Reviewed; 1068 AA.
AC P32871;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform;
DE Short=PI3-kinase subunit alpha;
DE Short=PI3K-alpha;
DE Short=PI3Kalpha;
DE Short=PtdIns-3-kinase subunit alpha;
DE EC=2.7.1.137 {ECO:0000269|PubMed:1322797, ECO:0000269|PubMed:14729945, ECO:0000305|PubMed:15178440};
DE EC=2.7.1.153 {ECO:0000250|UniProtKB:P42336};
DE AltName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha;
DE Short=PtdIns-3-kinase subunit p110-alpha;
DE Short=p110alpha;
DE AltName: Full=Phosphoinositide-3-kinase catalytic alpha polypeptide;
DE AltName: Full=Serine/threonine protein kinase PIK3CA;
DE EC=2.7.11.1 {ECO:0000269|PubMed:14729945, ECO:0000269|PubMed:15178440};
GN Name=PIK3CA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC TISSUE=Brain;
RX PubMed=1322797; DOI=10.1016/0092-8674(92)90166-a;
RA Hiles I.D., Otsu M., Volinia S., Fry M.J., Gout I., Dhand R., Panayotou G.,
RA Ruiz-Larrea F., Thompson A., Totty N.F., Hsuan J.J., Courtneidge S.A.,
RA Parker P.J., Waterfield M.D.;
RT "Phosphatidylinositol 3-kinase: structure and expression of the 110 kd
RT catalytic subunit.";
RL Cell 70:419-429(1992).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15178440; DOI=10.1016/j.bbrc.2004.04.191;
RA Foukas L.C., Shepherd P.R.;
RT "eIF4E binding protein 1 and H-Ras are novel substrates for the protein
RT kinase activity of class-I phosphoinositide 3-kinase.";
RL Biochem. Biophys. Res. Commun. 319:541-549(2004).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14729945; DOI=10.1128/mcb.24.3.966-975.2004;
RA Foukas L.C., Beeton C.A., Jensen J., Phillips W.A., Shepherd P.R.;
RT "Regulation of phosphoinositide 3-kinase by its intrinsic serine kinase
RT activity in vivo.";
RL Mol. Cell. Biol. 24:966-975(2004).
CC -!- FUNCTION: Phosphoinositide-3-kinase (PI3K) phosphorylates
CC phosphatidylinositol (PI) and its phosphorylated derivatives at
CC position 3 of the inositol ring to produce 3-phosphoinositides
CC (PubMed:1322797, PubMed:14729945). Uses ATP and PtdIns(4,5)P2
CC (phosphatidylinositol 4,5-bisphosphate) to generate
CC phosphatidylinositol 3,4,5-trisphosphate (PIP3) (By similarity). PIP3
CC plays a key role by recruiting PH domain-containing proteins to the
CC membrane, including AKT1 and PDPK1, activating signaling cascades
CC involved in cell growth, survival, proliferation, motility and
CC morphology. Participates in cellular signaling in response to various
CC growth factors. Involved in the activation of AKT1 upon stimulation by
CC receptor tyrosine kinases ligands such as EGF, insulin, IGF1, VEGFA and
CC PDGF. Involved in signaling via insulin-receptor substrate (IRS)
CC proteins. Essential in endothelial cell migration during vascular
CC development through VEGFA signaling, possibly by regulating RhoA
CC activity. Required for lymphatic vasculature development, possibly by
CC binding to RAS and by activation by EGF and FGF2, but not by PDGF.
CC Regulates invadopodia formation through the PDPK1-AKT1 pathway.
CC Participates in cardiomyogenesis in embryonic stem cells through a AKT1
CC pathway. Participates in vasculogenesis in embryonic stem cells through
CC PDK1 and protein kinase C pathway (By similarity). In addition to its
CC lipid kinase activity, it displays a serine-protein kinase activity
CC that results in the autophosphorylation of the p85alpha regulatory
CC subunit as well as phosphorylation of other proteins such as 4EBP1, H-
CC Ras, the IL-3 beta c receptor and possibly others (PubMed:15178440,
CC PubMed:14729945). Plays a role in the positive regulation of
CC phagocytosis and pinocytosis (By similarity).
CC {ECO:0000250|UniProtKB:P42336, ECO:0000250|UniProtKB:P42337,
CC ECO:0000269|PubMed:1322797, ECO:0000269|PubMed:14729945,
CC ECO:0000269|PubMed:15178440}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:14729945, ECO:0000269|PubMed:15178440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305|PubMed:14729945, ECO:0000305|PubMed:15178440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137; Evidence={ECO:0000269|PubMed:1322797,
CC ECO:0000269|PubMed:14729945, ECO:0000305|PubMed:15178440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000305|PubMed:1322797, ECO:0000305|PubMed:14729945,
CC ECO:0000305|PubMed:15178440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:21292,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57836,
CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.153;
CC Evidence={ECO:0000250|UniProtKB:P42336};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21293;
CC Evidence={ECO:0000250|UniProtKB:P42336};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + ATP = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:55632,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:83416,
CC ChEBI:CHEBI:83419, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P42336};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55633;
CC Evidence={ECO:0000250|UniProtKB:P42336};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-
CC 3-phospho-1D-myo-inositol 4,5-bisphosphate + ATP = 1-octadecanoyl-2-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-
CC inositol 3,4,5-triphosphate) + ADP + H(+); Xref=Rhea:RHEA:43396,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77137,
CC ChEBI:CHEBI:83243, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P42336};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43397;
CC Evidence={ECO:0000250|UniProtKB:P42336};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate
CC biosynthesis. {ECO:0000305|PubMed:1322797, ECO:0000305|PubMed:14729945,
CC ECO:0000305|PubMed:15178440}.
CC -!- SUBUNIT: Heterodimer of a catalytic subunit PIK3CA and a p85 regulatory
CC subunit (PIK3R1, PIK3R2 or PIK3R3). Interacts with IRS1 in nuclear
CC extracts. Interacts with RUFY3. Interacts with RASD2. Interacts with
CC APPL1. Interacts with HRAS and KRAS. Interaction with HRAS/KRAS is
CC required for PI3K pathway signaling and cell proliferation stimulated
CC by EGF and FGF2. Interacts with FAM83B; activates the PI3K/AKT
CC signaling cascade. {ECO:0000250|UniProtKB:P42336,
CC ECO:0000250|UniProtKB:P42337}.
CC -!- INTERACTION:
CC P32871; P23727: PIK3R1; NbExp=4; IntAct=EBI-1373130, EBI-520244;
CC P32871; P23726: PIK3R2; NbExp=3; IntAct=EBI-1373130, EBI-1555978;
CC -!- DOMAIN: The PI3K-ABD domain and the PI3K-RBD domain interact with the
CC PI3K/PI4K kinase domain. The C2 PI3K-type domain may facilitate the
CC recruitment to the plasma membrane. The inhibitory interactions with
CC PIK3R1 are mediated by the PI3K-ABD domain and the C2 PI3K-type domain
CC with the iSH2 (inter-SH2) region of PIK3R1, and the C2 PI3K-type
CC domain, the PI3K helical domain, and the PI3K/PI4K kinase domain with
CC the nSH2 (N-terminal SH2) region of PIK3R1.
CC {ECO:0000250|UniProtKB:P42336}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00877, ECO:0000255|PROSITE-ProRule:PRU00879,
CC ECO:0000255|PROSITE-ProRule:PRU00880}.
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DR EMBL; M93252; AAA30698.1; -; mRNA.
DR PIR; A43322; A43322.
DR RefSeq; NP_776999.1; NM_174574.1.
DR PDB; 2V1Y; X-ray; 2.40 A; A=1-108.
DR PDBsum; 2V1Y; -.
DR AlphaFoldDB; P32871; -.
DR SMR; P32871; -.
DR CORUM; P32871; -.
DR DIP; DIP-39319N; -.
DR IntAct; P32871; 4.
DR STRING; 9913.ENSBTAP00000012168; -.
DR BindingDB; P32871; -.
DR ChEMBL; CHEMBL2498; -.
DR iPTMnet; P32871; -.
DR PaxDb; P32871; -.
DR PRIDE; P32871; -.
DR Ensembl; ENSBTAT00000012168; ENSBTAP00000012168; ENSBTAG00000009232.
DR Ensembl; ENSBTAT00000072391; ENSBTAP00000068953; ENSBTAG00000009232.
DR GeneID; 282306; -.
DR KEGG; bta:282306; -.
DR CTD; 5290; -.
DR VEuPathDB; HostDB:ENSBTAG00000009232; -.
DR VGNC; VGNC:32889; PIK3CA.
DR eggNOG; KOG0904; Eukaryota.
DR GeneTree; ENSGT00940000155531; -.
DR HOGENOM; CLU_002191_1_1_1; -.
DR InParanoid; P32871; -.
DR OMA; EHANWTV; -.
DR OrthoDB; 204282at2759; -.
DR TreeFam; TF102031; -.
DR BRENDA; 2.7.1.137; 908.
DR Reactome; R-BTA-109704; PI3K Cascade.
DR Reactome; R-BTA-112399; IRS-mediated signalling.
DR Reactome; R-BTA-1250342; PI3K events in ERBB4 signaling.
DR Reactome; R-BTA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-BTA-1433557; Signaling by SCF-KIT.
DR Reactome; R-BTA-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-BTA-1963642; PI3K events in ERBB2 signaling.
DR Reactome; R-BTA-198203; PI3K/AKT activation.
DR Reactome; R-BTA-201556; Signaling by ALK.
DR Reactome; R-BTA-202424; Downstream TCR signaling.
DR Reactome; R-BTA-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-BTA-2424491; DAP12 signaling.
DR Reactome; R-BTA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-BTA-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-BTA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-BTA-5654689; PI-3K cascade:FGFR1.
DR Reactome; R-BTA-5654695; PI-3K cascade:FGFR2.
DR Reactome; R-BTA-5654710; PI-3K cascade:FGFR3.
DR Reactome; R-BTA-5654720; PI-3K cascade:FGFR4.
DR Reactome; R-BTA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-BTA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-BTA-9607240; FLT3 Signaling.
DR SABIO-RK; P32871; -.
DR UniPathway; UPA00220; -.
DR EvolutionaryTrace; P32871; -.
DR PRO; PR:P32871; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000009232; Expressed in neutrophil and 113 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:BHF-UCL.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IDA:BHF-UCL.
DR GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; IBA:GO_Central.
DR GO; GO:0005944; C:phosphatidylinositol 3-kinase complex, class IB; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IDA:BHF-UCL.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043560; F:insulin receptor substrate binding; IEA:Ensembl.
DR GO; GO:0035004; F:phosphatidylinositol 3-kinase activity; IDA:BHF-UCL.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0052812; F:phosphatidylinositol-3,4-bisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0030295; F:protein kinase activator activity; IEA:Ensembl.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0086003; P:cardiac muscle cell contraction; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0071464; P:cellular response to hydrostatic pressure; IEA:Ensembl.
DR GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR GO; GO:0044029; P:hypomethylation of CpG island; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; IEA:Ensembl.
DR GO; GO:2000811; P:negative regulation of anoikis; IEA:Ensembl.
DR GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:BHF-UCL.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0043457; P:regulation of cellular respiration; IEA:Ensembl.
DR GO; GO:2000653; P:regulation of genetic imprinting; IEA:Ensembl.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0055119; P:relaxation of cardiac muscle; IEA:Ensembl.
DR GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
DR GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; IEA:Ensembl.
DR CDD; cd05175; PI3Kc_IA_alpha; 1.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.70; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR003113; PI3K_ABD.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR037704; PI3Kalpha_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF02192; PI3K_p85B; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00143; PI3K_p85B; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51544; PI3K_ABD; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Angiogenesis; ATP-binding; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Phagocytosis; Proto-oncogene; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1068
FT /note="Phosphatidylinositol 4,5-bisphosphate 3-kinase
FT catalytic subunit alpha isoform"
FT /id="PRO_0000088784"
FT DOMAIN 16..105
FT /note="PI3K-ABD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00877"
FT DOMAIN 187..289
FT /note="PI3K-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00879"
FT DOMAIN 330..487
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT DOMAIN 517..694
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 765..1051
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 771..777
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 912..920
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 931..957
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:2V1Y"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:2V1Y"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:2V1Y"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:2V1Y"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:2V1Y"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:2V1Y"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2V1Y"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:2V1Y"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2V1Y"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:2V1Y"
SQ SEQUENCE 1068 AA; 124328 MW; C753DCC2F39FDDF0 CRC64;
MPPRPSSGEL WGIHLMPPRI LVECLLPNGM IVTLECLREA TLITIKHELF KEARKYPLHQ
LLQDESSYIF VSVTQEAERE EFFDETRRLC DLRLFQPFLK VIEPVGNREE KILNREIGFA
IGMPVCEFDM VKDPEVQDFR RNILNVCKEA VDLRDLNSPH SRAMYVYPPN VESSPELPKH
IYNKLDKGQI IVVIWVIVSP NNDKQKYTLK INHDCVPEQV IAEAIRKKTR SMLLSSEQLK
LCVLEYQGKY ILKVCGCDEY FLEKYPLSQY KYIRSCIMLG RMPNLMLMAK ESLYSQLPMD
CFTMPSYSRR ISTATPYMNG ETSTKSLWVI NSALRIKILC ATYVNVNIRD IDKIYVRTGI
YHGGEPLCDN VNTQRVPCSN PRWNEWLNYD IYIPDLPRAA RLCLSICSVK GRKGAKEEHC
PLAWGNINLF DYTDTLVSGK MALNLWPVPH GLEDLLNPIG VTGSNPNKET PCLELEFDWF
SSVVKFPDMS VIEEHANWSV SREAGFSYSH AGLSNRLARD NELRENDKEQ LRAICTRDPL
SEITEQEKDF LWSHRHYCVT IPEILPKLLL SVKWNSRDEV AQMYCLVKDW PPIKPEQAME
LLDCNYPDPM VRGFAVRCLE KYLTDDKLSQ YLIQLVQVLK YEQYLDNLLV RFLLKKALTN
QRIGHFFFWH LKSEMHNKTV SQRFGLLLES YCRACGMYLK HLNRQVEAME KLINLTDILK
QEKKDETQKV QMKFLVEQMR RPDFMDALQG FLSPLNPAHQ LGNLRLEECR IMSSAKRPLW
LNWENPDIMS ELLFQNNEII FKNGDDLRQD MLTLQIIRIM ENIWQNQGLD LRMLPYGCLS
IGDCVGLIEV VRNSHTIMQI QCKGGLKGAL QFNSHTLHQW LKDKNKGEIY DAAIDLFTRS
CAGYCVATFI LGIGDRHNSN IMVKDDGQLF HIDFGHFLDH KKKKFGYKRE RVPFVLTQDF
LIVISKGAQE CTKTREFERF QEMCYKAYLA IRQHANLFIN LFSMMLGSGM PELQSFDDIA
YIRKTLALDK TEQEALEYFM KQMNDAHHGG WTTKMDWIFH TIKQHALN
