ID PK3CG_PIG Reviewed; 1102 AA. AC O02697; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 27-MAR-2024, entry version 167. DE RecName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform; DE Short=PI3-kinase subunit gamma; DE Short=PI3K-gamma; DE Short=PI3Kgamma; DE Short=PtdIns-3-kinase subunit gamma; DE EC=2.7.1.137 {ECO:0000250|UniProtKB:P48736}; DE EC=2.7.1.153 {ECO:0000250|UniProtKB:P48736}; DE EC=2.7.1.154 {ECO:0000250|UniProtKB:P48736}; DE AltName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma; DE Short=PtdIns-3-kinase subunit p110-gamma; DE Short=p110gamma; DE AltName: Full=Phosphoinositide-3-kinase catalytic gamma polypeptide; DE AltName: Full=Serine/threonine protein kinase PIK3CG {ECO:0000250|UniProtKB:P48736}; DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P48736}; DE AltName: Full=p120-PI3K; GN Name=PIK3CG; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND INTERACTION WITH RP PIK3R5. RC TISSUE=Neutrophil; RX PubMed=9094719; DOI=10.1016/s0092-8674(00)80187-7; RA Stephens L.R., Eguinoa A., Erdjument-Bromage H., Lui M., Cooke F., RA Coadwell J., Smrcka A.S., Thelen M., Cadwallader K., Tempst P., RA Hawkins P.T.; RT "The G beta gamma sensitivity of a PI3K is dependent upon a tightly RT associated adaptor, p101."; RL Cell 89:105-114(1997). RN [2] RP SEQUENCE REVISION. RA Stephens L.R.; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 144-1102 IN COMPLEX WITH ATP AND RP INHIBITORS. RX PubMed=11090628; DOI=10.1016/s1097-2765(05)00089-4; RA Walker E.H., Pacold M.E., Perisic O., Stephens L., Hawkins P.T., RA Wymann M.P., Williams R.L.; RT "Structural determinants of phosphoinositide 3-kinase inhibition by RT wortmannin, LY294002, quercetin, myricetin, and staurosporine."; RL Mol. Cell 6:909-919(2000). CC -!- FUNCTION: Phosphoinositide-3-kinase (PI3K) that phosphorylates CC PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate CC phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role CC by recruiting PH domain-containing proteins to the membrane, including CC AKT1 and PDPK1, activating signaling cascades involved in cell growth, CC survival, proliferation, motility and morphology. Links G-protein CC coupled receptor activation to PIP3 production. Involved in immune, CC inflammatory and allergic responses. Modulates leukocyte chemotaxis to CC inflammatory sites and in response to chemoattractant agents. May CC control leukocyte polarization and migration by regulating the spatial CC accumulation of PIP3 and by regulating the organization of F-actin CC formation and integrin-based adhesion at the leading edge. Controls CC motility of dendritic cells. Participates in T-lymphocyte migration. CC Regulates T-lymphocyte proliferation and cytokine production. Required CC for B-lymphocyte development and signaling. Together with other PI3Ks CC are involved in the oxidative burst produced by neutrophils in response CC to chemotactic agents. Together with PIK3CD regulate neutrophil CC extravasation. Together with PIK3CB promotes platelet aggregation and CC thrombosis. Regulates alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) CC adhesive function in platelets downstream of P2Y12 through a lipid CC kinase activity-independent mechanism. May have also a lipid kinase CC activity-dependent function in platelet aggregation. Involved in CC endothelial progenitor cell migration. Negative regulator of cardiac CC contractility. Modulates cardiac contractility by anchoring protein CC kinase A (PKA) and PDE3B activation, reducing cAMP levels. Regulates CC cardiac contractility also by promoting beta-adrenergic receptor CC internalization by binding to GRK2 and by non-muscle tropomyosin CC phosphorylation. Also has serine/threonine protein kinase activity: CC both lipid and protein kinase activities are required for beta- CC adrenergic receptor endocytosis. May also have a scaffolding role in CC modulating cardiac contractility. Contribute to cardiac hypertrophy CC under pathological stress. Through simultaneous binding of PDE3B to CC RAPGEF3 and PIK3R6 is assembled in a signaling complex in which the CC PI3K gamma complex is activated by RAPGEF3 and which is involved in CC angiogenesis (By similarity). {ECO:0000250|UniProtKB:P48736}. 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:P48736}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21293; CC Evidence={ECO:0000250|UniProtKB:P48736}; 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:0000250|UniProtKB:P48736}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710; CC Evidence={ECO:0000250|UniProtKB:P48736}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4- CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- CC inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658, CC ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154; CC Evidence={ECO:0000250|UniProtKB:P48736}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374; CC Evidence={ECO:0000250|UniProtKB:P48736}; 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:0000250|UniProtKB:P48736}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; CC Evidence={ECO:0000250|UniProtKB:P48736}; CC -!- ACTIVITY REGULATION: Activated by both the alpha and the beta-gamma G CC proteins following stimulation of G protein-coupled receptors (GPCRs). CC Activation by GPCRs is assisted by the regulatory subunits (PIK3R5 or CC PIK3R6) leading to the translocation from the cytosol to the plasma CC membrane and to kinase activation. When bound to PIK3R5 the PI3K CC activity of PIK3CG could be activated greater than 100-fold by the CC beta-gamma G proteins. CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate CC biosynthesis. CC -!- SUBUNIT: Heterodimer of a catalytic subunit PIK3CG and a PIK3R5 or CC PIK3R6 regulatory subunit. Interacts with GRK2 through the PIK helical CC domain. Interaction with GRK2 is required for targeting to agonist- CC occupied receptor. Interacts with PDE3B; regulates PDE3B activity and CC thereby cAMP levels in cells. Interacts with TPM2. Interacts with CC EPHA8; regulates integrin-mediated cell adhesion to substrate. CC Interacts with HRAS; the interaction is required for membrane CC recruitment and beta-gamma G protein dimer-dependent activation of the CC PI3K gamma complex PIK3CG:PIK3R6 (By similarity). CC {ECO:0000250|UniProtKB:P48736, ECO:0000250|UniProtKB:Q9JHG7}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48736}. Cell CC membrane {ECO:0000250|UniProtKB:P48736}. CC -!- PTM: Autophosphorylation at Ser-1101 has no effect on the CC phosphatidylinositol-4,5-bisphosphate 3-kinase activity. CC {ECO:0000250|UniProtKB:P48736}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y10743; CAA71731.1; -; mRNA. DR RefSeq; NP_999104.1; NM_213939.1. DR PDB; 1E7U; X-ray; 2.00 A; A=144-1102. DR PDB; 1E7V; X-ray; 2.40 A; A=144-1102. DR PDB; 1E8W; X-ray; 2.50 A; A=144-1102. DR PDB; 1E8X; X-ray; 2.20 A; A=144-1102. DR PDB; 1E90; X-ray; 2.70 A; A=144-1102. DR PDB; 8AJ8; X-ray; 8.50 A; A/C/E/G=1-1102. DR PDBsum; 1E7U; -. DR PDBsum; 1E7V; -. DR PDBsum; 1E8W; -. DR PDBsum; 1E8X; -. DR PDBsum; 1E90; -. DR PDBsum; 8AJ8; -. DR AlphaFoldDB; O02697; -. DR SMR; O02697; -. DR IntAct; O02697; 2. DR STRING; 9823.ENSSSCP00000046980; -. DR PaxDb; 9823-ENSSSCP00000024176; -. DR GeneID; 396979; -. DR KEGG; ssc:396979; -. DR CTD; 5294; -. DR eggNOG; KOG0904; Eukaryota. DR HOGENOM; CLU_145774_0_0_1; -. DR InParanoid; O02697; -. DR OrthoDB; 10350at2759; -. DR BRENDA; 2.7.1.137; 6170. DR UniPathway; UPA00220; -. DR EvolutionaryTrace; O02697; -. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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; ISS:UniProtKB. DR GO; GO:0046934; F:1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity; ISS:UniProtKB. DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0106310; F:protein serine kinase activity; ISS:UniProtKB. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW. DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IBA:GO_Central. DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISS:UniProtKB. DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd08399; C2_PI3K_class_I_gamma; 1. DR CDD; cd00872; PI3Ka_I; 1. DR CDD; cd00894; PI3Kc_IB_gamma; 1. DR Gene3D; 3.10.20.770; -; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1. DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 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; IPR015433; PI_Kinase. DR InterPro; IPR045580; PIK3CG_ABD. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR10048:SF34; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT GAMMA ISOFORM; 1. DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1. DR Pfam; PF00454; PI3_PI4_kinase; 1. DR Pfam; PF00792; PI3K_C2; 1. DR Pfam; PF00794; PI3K_rbd; 1. DR Pfam; PF00613; PI3Ka; 1. DR Pfam; PF19710; PIK3CG_ABD; 1. DR SMART; SM00142; PI3K_C2; 1. DR SMART; SM00144; PI3K_rbd; 1. DR SMART; SM00145; PI3Ka; 1. DR SMART; SM00146; PI3Kc; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF54236; Ubiquitin-like; 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. DR Genevisible; O02697; SS. PE 1: Evidence at protein level; KW 3D-structure; Angiogenesis; ATP-binding; Cell membrane; Chemotaxis; KW Cytoplasm; Direct protein sequencing; Endocytosis; Immunity; KW Inflammatory response; Kinase; Lipid metabolism; Membrane; KW Nucleotide-binding; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..1102 FT /note="Phosphatidylinositol 4,5-bisphosphate 3-kinase FT catalytic subunit gamma isoform" FT /id="PRO_0000088794" FT DOMAIN 34..141 FT /note="PI3K-ABD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00877" FT DOMAIN 217..309 FT /note="PI3K-RBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00879" FT DOMAIN 357..521 FT /note="C2 PI3K-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00880" FT DOMAIN 541..723 FT /note="PIK helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878" FT DOMAIN 797..1080 FT /note="PI3K/PI4K catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT REGION 803..809 FT /note="G-loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT REGION 943..951 FT /note="Catalytic loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT REGION 962..988 FT /note="Activation loop" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269" FT BINDING 829..838 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:11090628" FT BINDING 864..872 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:11090628" FT BINDING 961..969 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:11090628" FT MOD_RES 1024 FT /note="Phosphothreonine; by PKA" FT /evidence="ECO:0000250|UniProtKB:Q9JHG7" FT MOD_RES 1101 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P48736" FT HELIX 145..158 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 172..190 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 193..198 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 209..212 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:1E8X" FT STRAND 216..228 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 230..236 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 241..251 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 271..274 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 283..285 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 291..299 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 303..308 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 313..316 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 359..369 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 379..389 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 392..398 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 406..419 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 420..422 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 428..437 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 460..469 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 473..475 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 478..483 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 499..502 FT /evidence="ECO:0007829|PDB:1E7U" FT TURN 510..512 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 515..520 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 549..559 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 563..565 FT /evidence="ECO:0007829|PDB:1E7V" FT HELIX 569..577 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 579..582 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 586..588 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 589..593 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 601..612 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 615..619 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 624..629 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 638..648 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 653..666 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 667..669 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 671..674 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 676..687 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 689..705 FT /evidence="ECO:0007829|PDB:1E7U" FT TURN 707..709 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 710..721 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 726..748 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 750..753 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 754..756 FT /evidence="ECO:0007829|PDB:1E8X" FT HELIX 761..776 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 783..785 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 788..796 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 798..800 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 805..808 FT /evidence="ECO:0007829|PDB:1E7V" FT STRAND 811..818 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 828..836 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 839..857 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 869..873 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 876..880 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 883..887 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 888..895 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 898..900 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 906..914 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 918..941 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 949..951 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 952..955 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 960..962 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 989..994 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 998..1001 FT /evidence="ECO:0007829|PDB:1E7V" FT HELIX 1004..1021 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 1024..1037 FT /evidence="ECO:0007829|PDB:1E7U" FT STRAND 1039..1041 FT /evidence="ECO:0007829|PDB:1E8X" FT HELIX 1045..1054 FT /evidence="ECO:0007829|PDB:1E7U" FT TURN 1055..1058 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 1061..1078 FT /evidence="ECO:0007829|PDB:1E7U" FT HELIX 1081..1090 FT /evidence="ECO:0007829|PDB:1E7U" SQ SEQUENCE 1102 AA; 126658 MW; 9E7D4211FD626DFC CRC64; MELENYEQPV VLREDNRRRR RRMKPRSTAA SLSSMELIPI EFVLPTSQRN TKTPETALLH VAGHGNVEQM KAQVWLRALE TSVSADFYHR LGPDHFLLLY QKKGQWYEIY DKYQVVQTLD CLRYWKVLHR SPGQIHVVQR HAPSEETLAF QRQLNALIGY DVTDVSNVHD DELEFTRRRL VTPRMAEVAG RDPKLYAMHP WVTSKPLPEY LLKKITNNCV FIVIHRSTTS QTIKVSADDT PGTILQSFFT KMAKKKSLMD IPESQNERDF VLRVCGRDEY LVGETPIKNF QWVRQCLKNG EEIHLVLDTP PDPALDEVRK EEWPLVDDCT GVTGYHEQLT IHGKDHESVF TVSLWDCDRK FRVKIRGIDI PVLPRTADLT VFVEANIQYG QQVLCQRRTS PKPFTEEVLW NVWLEFSIKI KDLPKGALLN LQIYCGKAPA LSGKTSAEMP SPESKGKAQL LYYVNLLLID HRFLLRHGEY VLHMWQLSGK GEDQGSFNAD KLTSRTNPDK ENSMSISILL DNYCHPIALP KHRPTPDPEG DRVRAEMPNQ LRKQLEAIIA TDPLNPLTAE DKELLWHFRY ESLKDPKAYP KLFSSVKWGQ QEIVAKTYQL LAKREVWDQS ALDVGLTMQL LDCNFSDENV RAIAVQKLES LEDDDVLHYL LQLVQAVKFE PYHDSALARF LLKRGLRNKR IGHFLFWFLR SEIAQSRHYQ QRFAVILEAY LRGCGTAMLH DFTQQVQVID MLQKVTIDIK SLSAEKYDVS SQVISQLKQK LENLQNLNLP QSFRVPYDPG LKAGALVIEK CKVMASKKKP LWLEFKCADP TALSNETIGI IFKHGDDLRQ DMLILQILRI MESIWETESL DLCLLPYGCI STGDKIGMIE IVKDATTIAK IQQSTVGNTG AFKDEVLSHW LKEKCPIEEK FQAAVERFVY SCAGYCVATF VLGIGDRHND NIMISETGNL FHIDFGHILG NYKSFLGINK ERVPFVLTPD FLFVMGTSGK KTSLHFQKFQ DVCVKAYLAL RHHTNLLIIL FSMMLMTGMP QLTSKEDIEY IRDALTVGKS EEDAKKYFLD QIEVCRDKGW TVQFNWFLHL VLGIKQGEKH SA //