PLCE1_RAT
ID PLCE1_RAT Reviewed; 2281 AA.
AC Q99P84;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000269|PubMed:11179219};
DE AltName: Full=Phosphoinositide phospholipase C-epsilon-1;
DE AltName: Full=Phospholipase C-epsilon-1;
DE Short=PLC-epsilon-1;
GN Name=Plce1 {ECO:0000312|RGD:69424}; Synonyms=Plce;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, COFACTOR, INTERACTION WITH HRAS AND RAP1A, AND
RP MUTAGENESIS OF LYS-2150 AND LYS-2152.
RC TISSUE=Heart;
RX PubMed=11179219; DOI=10.1093/emboj/20.4.743;
RA Kelley G.G., Reks S.E., Ondrako J.M., Smrcka A.V.;
RT "Phospholipase C(epsilon): a novel Ras effector.";
RL EMBO J. 20:743-754(2001).
RN [2]
RP ACTIVITY REGULATION.
RX PubMed=11641393; DOI=10.1074/jbc.c100574200;
RA Wing M.R., Houston D., Kelley G.G., Der C.J., Siderovski D.P., Harden T.K.;
RT "Activation of phospholipase C-epsilon by heterotrimeric G protein
RT betagamma-subunits.";
RL J. Biol. Chem. 276:48257-48261(2001).
RN [3]
RP ACTIVITY REGULATION.
RX PubMed=11788587; DOI=10.1074/jbc.m109059200;
RA Murphy G.A., Graham S.M., Morita S., Reks S.E., Rogers-Graham K.,
RA Vojtek A., Kelley G.G., Der C.J.;
RT "Involvement of phosphatidylinositol 3-kinase, but not RalGDS, in TC21/R-
RT Ras2-mediated transformation.";
RL J. Biol. Chem. 277:9966-9975(2002).
RN [4]
RP ACTIVITY REGULATION, AND INTERACTION WITH RHOA.
RX PubMed=12900402; DOI=10.1074/jbc.m306904200;
RA Wing M.R., Snyder J.T., Sondek J., Harden T.K.;
RT "Direct activation of phospholipase C-epsilon by Rho.";
RL J. Biol. Chem. 278:41253-41258(2003).
RN [5]
RP FUNCTION.
RX PubMed=12721365; DOI=10.1073/pnas.1031494100;
RA Czyzyk J., Brogdon J.L., Badou A., Henegariu O., Preston Hurlburt P.,
RA Flavell R., Bottomly K.;
RT "Activation of CD4 T cells by Raf-independent effectors of Ras.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:6003-6008(2003).
RN [6]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=15322077; DOI=10.1074/jbc.m407111200;
RA Seifert J.P., Wing M.R., Snyder J.T., Gershburg S., Sondek J., Harden T.K.;
RT "RhoA activates purified phospholipase C-epsilon by a guanine nucleotide-
RT dependent mechanism.";
RL J. Biol. Chem. 279:47992-47997(2004).
RN [7]
RP FUNCTION.
RX PubMed=16314422; DOI=10.1074/jbc.m507681200;
RA Kelley G.G., Kaproth-Joslin K.A., Reks S.E., Smrcka A.V.,
RA Wojcikiewicz R.J.H.;
RT "G-protein-coupled receptor agonists activate endogenous phospholipase
RT Cepsilon and phospholipase Cbeta3 in a temporally distinct manner.";
RL J. Biol. Chem. 281:2639-2648(2006).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH IQGAP1.
RX PubMed=17086182; DOI=10.1038/ng1918;
RA Hinkes B., Wiggins R.C., Gbadegesin R., Vlangos C.N., Seelow D.,
RA Nuernberg G., Garg P., Verma R., Chaib H., Hoskins B.E., Ashraf S.,
RA Becker C., Hennies H.C., Goyal M., Wharram B.L., Schachter A.D.,
RA Mudumana S., Drummond I., Kerjaschki D., Waldherr R., Dietrich A.,
RA Ozaltin F., Bakkaloglu A., Cleper R., Basel-Vanagaite L., Pohl M.,
RA Griebel M., Tsygin A.N., Soylu A., Mueller D., Sorli C.S., Bunney T.D.,
RA Katan M., Liu J., Attanasio M., O'toole J.F., Hasselbacher K., Mucha B.,
RA Otto E.A., Airik R., Kispert A., Kelley G.G., Smrcka A.V., Gudermann T.,
RA Holzman L.B., Nuernberg P., Hildebrandt F.;
RT "Positional cloning uncovers mutations in PLCE1 responsible for a nephrotic
RT syndrome variant that may be reversible.";
RL Nat. Genet. 38:1397-1405(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1093, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: The production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC by activated phosphatidylinositol-specific phospholipase C enzymes.
CC PLCE1 is a bifunctional enzyme which also regulates small GTPases of
CC the Ras superfamily through its Ras guanine-exchange factor (RasGEF)
CC activity. As an effector of heterotrimeric and small G-protein, it may
CC play a role in cell survival, cell growth, actin organization and T-
CC cell activation. In podocytes, is involved in the regulation of
CC lamellipodia formation. Acts downtream of AVIL to allow ARP2/3 complex
CC assembly (By similarity). {ECO:0000250|UniProtKB:Q9P212,
CC ECO:0000269|PubMed:12721365, ECO:0000269|PubMed:16314422,
CC ECO:0000269|PubMed:17086182}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC ChEBI:CHEBI:203600; EC=3.1.4.11;
CC Evidence={ECO:0000269|PubMed:11179219};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11179219};
CC -!- ACTIVITY REGULATION: Activated by the heterotrimeric G-protein subunits
CC GNA12, GNA13 and GNB1-GNG2. Activated by HRAS, RAP1A, RHOA, RHOB, RHOC,
CC RRAS and RRAS2. Activated by the G(s)-coupled GPCRs ADRB2, PTGER1 and
CC CHRM3 through cyclic-AMP formation and RAP2B activation. Inhibited by
CC G(i)-coupled GPCRs. {ECO:0000269|PubMed:11179219,
CC ECO:0000269|PubMed:11641393, ECO:0000269|PubMed:11788587,
CC ECO:0000269|PubMed:12900402, ECO:0000269|PubMed:15322077}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.0 uM for PtdIns(4,5)P2 {ECO:0000269|PubMed:15322077};
CC Vmax=10 umol/min/mg enzyme {ECO:0000269|PubMed:15322077};
CC -!- SUBUNIT: Interacts with RHOA (PubMed:12900402). Interacts with GTP-
CC bound HRAS, RAP1A, RAP2A, RAP2B and RRAS (By similarity). Interacts
CC with IQGAP1 (PubMed:17086182). Interacts with AVIL (By similarity).
CC {ECO:0000250|UniProtKB:Q9P212, ECO:0000269|PubMed:12900402,
CC ECO:0000269|PubMed:17086182}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9P212}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9P212}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9P212}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q9P212}. Note=Recruited to plasma membrane by
CC activated HRAS and RAP2. Recruited to perinuclear membrane by activated
CC RAP1A. Isoform 1 and isoform 2 associates with Golgi membranes.
CC {ECO:0000250|UniProtKB:Q9P212}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Detected in glomerular
CC podocytes (at protein level). {ECO:0000269|PubMed:11179219,
CC ECO:0000269|PubMed:17086182}.
CC -!- DOMAIN: The Ras-associating domain 1 is degenerated and may not bind
CC HRAS (By similarity). The Ras-associating domain 2 mediates interaction
CC with GTP-bound HRAS, RAP1A and probably RAP2A and RAP2B and recruitment
CC of HRAS to the cell membrane. {ECO:0000250}.
CC -!- DOMAIN: The Ras-GEF domain has a GEF activity towards HRAS and RAP1A.
CC Mediates activation of the mitogen-activated protein kinase pathway (By
CC similarity). {ECO:0000250}.
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DR EMBL; AF323615; AAK06775.1; -; mRNA.
DR RefSeq; NP_446210.1; NM_053758.2.
DR PDB; 6PMP; X-ray; 2.73 A; A/B/C/D=1284-2098.
DR PDBsum; 6PMP; -.
DR AlphaFoldDB; Q99P84; -.
DR SMR; Q99P84; -.
DR BioGRID; 250398; 1.
DR IntAct; Q99P84; 1.
DR STRING; 10116.ENSRNOP00000062667; -.
DR iPTMnet; Q99P84; -.
DR PhosphoSitePlus; Q99P84; -.
DR PaxDb; Q99P84; -.
DR PRIDE; Q99P84; -.
DR GeneID; 114633; -.
DR KEGG; rno:114633; -.
DR CTD; 51196; -.
DR RGD; 69424; Plce1.
DR eggNOG; KOG0169; Eukaryota.
DR InParanoid; Q99P84; -.
DR OrthoDB; 368239at2759; -.
DR BRENDA; 3.1.4.11; 5301.
DR Reactome; R-RNO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR SABIO-RK; Q99P84; -.
DR PRO; PR:Q99P84; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:RGD.
DR GO; GO:0004629; F:phospholipase C activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:RGD.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0032835; P:glomerulus development; ISO:RGD.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; IDA:RGD.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; ISS:UniProtKB.
DR Gene3D; 1.10.840.10; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR028398; PLC-epsilon1.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10336; PTHR10336; 2.
DR PANTHER; PTHR10336:SF6; PTHR10336:SF6; 2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00617; RasGEF; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00147; RasGEF; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Cell projection; Cytoplasm;
KW Golgi apparatus; Guanine-nucleotide releasing factor; Hydrolase;
KW Lipid degradation; Lipid metabolism; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transducer.
FT CHAIN 1..2281
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase epsilon-1"
FT /id="PRO_0000256240"
FT DOMAIN 528..781
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 1373..1521
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 1709..1825
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 1830..1955
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1991..2093
FT /note="Ras-associating 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 2114..2217
FT /note="Ras-associating 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1547..1572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1664..1703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1667..1743
FT /note="Required for activation by RHOA, RHOB, GNA12, GNA13
FT and G-beta gamma"
FT REGION 2239..2281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1683..1703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2239..2260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 1433
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT MOD_RES 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 2150
FT /note="K->A: Inhibits binding to HRAS by 59% and
FT phospholipase stimulation by HRAS by 51%. Inhibits binding
FT to HRAS by 97% and phospholipase stimulation by HRAS by
FT 86%; when associated with A-2152."
FT /evidence="ECO:0000269|PubMed:11179219"
FT MUTAGEN 2150
FT /note="K->E: Inhibits binding to HRAS by 99% and
FT phospholipase stimulation by HRAS by 94%. Inhibits binding
FT to HRAS by 97% and phospholipase stimulation by HRAS by
FT 94%; when associated with E-2152."
FT /evidence="ECO:0000269|PubMed:11179219"
FT MUTAGEN 2152
FT /note="K->A: Inhibits binding to HRAS by 19% and
FT phospholipase stimulation by HRAS by 30%. Inhibits binding
FT to HRAS by 97% and phospholipase stimulation by HRAS by
FT 86%; when associated with A-2150."
FT /evidence="ECO:0000269|PubMed:11179219"
FT MUTAGEN 2152
FT /note="K->E: Inhibits binding to HRAS by 67% and
FT phospholipase stimulation by HRAS by 47%. Inhibits binding
FT to HRAS by 97% and phospholipase stimulation by HRAS by
FT 94%; when associated with E-2150."
FT /evidence="ECO:0000269|PubMed:11179219"
FT HELIX 1307..1318
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1324..1334
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1338..1341
FT /evidence="ECO:0007829|PDB:6PMP"
FT TURN 1342..1344
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1348..1356
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1361..1364
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1365..1367
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1373..1375
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1379..1381
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1382..1384
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1386..1389
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1392..1394
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1396..1399
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1404..1412
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1416..1422
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1443..1453
FT /evidence="ECO:0007829|PDB:6PMP"
FT TURN 1454..1456
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1462..1468
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1472..1486
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1487..1489
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1497..1500
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1501..1503
FT /evidence="ECO:0007829|PDB:6PMP"
FT TURN 1509..1514
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1516..1521
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1529..1541
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1621..1623
FT /evidence="ECO:0007829|PDB:6PMP"
FT TURN 1624..1627
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1628..1630
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1644..1647
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1651..1655
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1732..1734
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1735..1740
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1741..1750
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1752..1761
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1762..1767
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1781..1785
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1789..1793
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1800..1808
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1809..1814
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1816..1819
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1822..1824
FT /evidence="ECO:0007829|PDB:6PMP"
FT TURN 1830..1834
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1844..1846
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1848..1859
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1869..1878
FT /evidence="ECO:0007829|PDB:6PMP"
FT TURN 1879..1881
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1883..1886
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1894..1896
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1898..1908
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1910..1912
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1914..1921
FT /evidence="ECO:0007829|PDB:6PMP"
FT TURN 1922..1925
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1926..1934
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1935..1937
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1940..1948
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1954..1967
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1978..1981
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 1985..1990
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 1991..1999
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 2001..2012
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 2017..2025
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 2038..2046
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 2059..2062
FT /evidence="ECO:0007829|PDB:6PMP"
FT HELIX 2069..2073
FT /evidence="ECO:0007829|PDB:6PMP"
FT STRAND 2078..2090
FT /evidence="ECO:0007829|PDB:6PMP"
SQ SEQUENCE 2281 AA; 255393 MW; 7409A739B61F69EF CRC64;
MTSEEMAASF LIPVPQRKVA SAQSVAEERG EKVSEAGIPK TRAGRQGGLT PRTISQRNEP
EEESPRTDFS QVFSIARGEL DSDENHNERC WEENVPGSTK NHAVNCNSLL QSHQHALPPS
QLCEVCDSVT EEHLCLQPGI PSPLERKVFP GIELEMEDSP MDVSPLGNQP GIMESSGPHS
DRNMAVFHFH YAGDRTMPGA FHTLSEKFIL DDCANCVTLP GGQQNKNYMA YTCKLVELTR
TCGSKNGQLK CDHCTSLRDE YLCFESSCRK AEALSSGGGF CEDGFTHGPS AKTFLNPLEE
FSDNCEDVDD IFKGKKERST LLVRRFCKND REVKKSVYTG TRAIVRTLPS GHIGLAAWSY
VDQKKAGLMW PCGNGMRPLS TVDVRQSGRQ RLSEAQWCLI YSAVRREETE DTVGSLLHCS
TQLPTPDTAH GRIGDGPCLK QCVRDSECEY RATLQRTSIA QYITGSLLEA TTSLGARSSL
LSSFGGSTGR IMLKERQPGT SMANSSPVPS SSAGISKELI DLQPLIQFPE EVASILTEQE
QNIYRRVLPM DYLCFLTRDL SSPECQRSLP RLKACISESI LMSQSGEHNA LEDLVMRFNE
VSSWVTWLIL TAGSMEEKRE VFSYLVHVAK CCWNMGNYNA VMEFLAGLRS RKVLKMWQFM
DQSDIETMRS LKDAMAQHES SVEYKKVVTR ALHIPGCKVV PFCGVFLKEL CEVLDGASGL
LKLCPRYSSQ EEALEFVADY SGQDNFLQRV GQNGLKNPEK ELTVNSIFQI IRSCSRSLET
EDEESASEGS GSRKNSLKDK TRWQFIIGDL LDSDNDIFEK SKECDPHGSE ESQKAFDHGT
ELIPWYVLSI QADVHQFLLQ GATVIHYDQD THLSARCFLQ LQPDNSTLTW MKPPTASPAG
ARLKLGVLSN VAEPGKFPSL GNAGVSGLVE GILDLFSVKA VYMGHPGIDI HTVCVQNKLS
SMLLSETGVT LLYGLQTTDN RLLHFVAPKH TAKMLFSGLL ELTTAVRKIR KFPDQRQQWL
RKQYVSFYQE DGRYEGPTLA HAVELFGGRR WSTRNPSPGM SAKNAEKPNM QRNNTLGIST
TKKKKKMLMR GESGEVTDDE MATRKAKMYR ECRSRSGSDP QEANEQEDSE ANVITNPPNP
LHSRRAYSLT TAGSPNLATG MSSPISAWSS SSWHGRIKGG MKGFQSFMVS DSNMSFIEFV
ELFKSFSIRS RKDLKDIFDI YSVPCNRSAS ESTPLYTNLT IEENTNDLQP DLDLLTRNVS
DLGLFMKSKQ QLSDNQRQIS DAIAAASIVT NGTGIESTSL GIFGVGILQL NDFLVNCQGE
HCTYDEILSI IQKFEPNISM CHQGLLSFEG FARFLMDKDN FASKNDESRE NKKDLQLPLS
YYYIESSHNT YLTGHQLKGE SSVELYSQVL LQGCRSIELD CWDGDDGMPI IYHGHTLTTK
IPFKEVVEAI DRSAFITSDL PIIISIENHC SLPQQRKMAE IFKSVFGEKL VAKFLFETDF
SDDPMLPSPD QLRRKVLLKN KKLKAHQTPV DILKQKAHQL ASMQTQAFTG GNANPPPASN
EEEEDEEDEY DYDYESLSDD NILEDRPENK SCADKLQFEY NEEVPKRIKK ADNSSGNKGK
VYDMELGEEF YLPQNKKESR QIAPELSDLV IYCQAVKFPG LSTLNSSGSG RGKERKSRKS
IFGNNPGRMS PGETASFNRT SGKSSCEGIR QIWEEPPLSP NTSLSAIIRT PKCYHISSLN
ENAAKRLCRR YSQKLIQHTA CQLLRTYPAA TRIDSSNPNP LMFWLHGIQL VALNYQTDDL
PLHLNAAMFE ANGGCGYVLK PPVLWDKSCP MYQKFSPLER DLDAMDPATY SLTIISGQNV
CPSNSTGSPC IEVDVLGMPL DSCHFRTKPI HRNTLNPMWN EQFLFRVHFE DLVFLRFAVV
ENNSSAITAQ RIIPLKALKR GYRHLQLRNL HNEILEISSL FINSRRMEDN PSGSTRPASL
MFNTEERKCS QTHKVTVHGV PGPEPFAVFT INEGTKAKQL LQQILAVDQD TKLTAADYFL
MEEKHFISKE KNECRKQPFQ RAVGPEEDIV QILNSWFPEE GYVGRIVLKP QQETLEEKNI
VHDDREVILS SEEESFFVQV HDVSPEQPRT VIKAPRVSTA QDVIQQTLCK AKYSYSILNN
PNPCDYVLLE EVMKDAPNKK SSTPKSSQRI LLDQECVFQA QSKWKGAGKF ILKLKEQVQA
SREDKRRGIS FASELKKLTK STKQTRGLTS PPQLVASESV QSKEEKPMGA LASGDTAGYQ
S
