PK3CG_PIG
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 03-AUG-2022, entry version 158.
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}.
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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 PDBsum; 1E7U; -.
DR PDBsum; 1E7V; -.
DR PDBsum; 1E8W; -.
DR PDBsum; 1E8X; -.
DR PDBsum; 1E90; -.
DR AlphaFoldDB; O02697; -.
DR SMR; O02697; -.
DR IntAct; O02697; 2.
DR STRING; 9823.ENSSSCP00000024176; -.
DR PaxDb; O02697; -.
DR PRIDE; O02697; -.
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 BRENDA; 2.7.1.137; 6170.
DR UniPathway; UPA00220; -.
DR EvolutionaryTrace; O02697; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; O02697; SS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016303; F:1-phosphatidylinositol-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:0052812; F:phosphatidylinositol-3,4-bisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; ISS:UniProtKB.
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:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR015433; PI_Kinase.
DR InterPro; IPR045580; PIK3CG_ABD.
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; 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; 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; 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
