ATC5_YEAST
ID ATC5_YEAST Reviewed; 1571 AA.
AC P32660; D3DM74;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Phospholipid-transporting ATPase DNF1;
DE EC=7.6.2.1;
DE AltName: Full=Flippase DNF1;
GN Name=DNF1; OrderedLocusNames=YER166W; ORFNames=SYGP-ORF7;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; THR-85 AND SER-1506, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [6]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY FPK1 AND KIN82.
RX PubMed=18199685; DOI=10.1091/mbc.e07-07-0646;
RA Nakano K., Yamamoto T., Kishimoto T., Noji T., Tanaka K.;
RT "Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid
RT asymmetry.";
RL Mol. Biol. Cell 19:1783-1797(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-351 AND SER-1506, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; THR-70; SER-81; THR-85;
RP SER-92; THR-94; SER-104; THR-109; SER-365; SER-1506; THR-1551; SER-1552 AND
RP SER-1563, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of phospholipids. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC -!- INTERACTION:
CC P32660; P32660: DNF1; NbExp=3; IntAct=EBI-3121, EBI-3121;
CC P32660; Q12675: DNF2; NbExp=3; IntAct=EBI-3121, EBI-3114;
CC P32660; P53739: FPK1; NbExp=2; IntAct=EBI-3121, EBI-9813;
CC P32660; P42838: LEM3; NbExp=8; IntAct=EBI-3121, EBI-28396;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18199685};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18199685}. Endosome
CC membrane {ECO:0000269|PubMed:18199685}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18199685}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:18199685}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18199685}.
CC -!- PTM: Phosphorylated by FPK1 and KIN82. {ECO:0000269|PubMed:18199685}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
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DR EMBL; U18922; AAB64693.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07828.1; -; Genomic_DNA.
DR PIR; S50669; S50669.
DR RefSeq; NP_011093.3; NM_001179056.3.
DR PDB; 7DRX; EM; 2.90 A; A=1-1571.
DR PDB; 7DSH; EM; 3.67 A; A=1-1571.
DR PDB; 7DSI; EM; 3.21 A; A=1-1571.
DR PDB; 7F7F; EM; 3.81 A; A=1-1571.
DR PDB; 7KY6; EM; 3.10 A; A=1-1571.
DR PDB; 7KYB; EM; 3.20 A; A=1-1571.
DR PDB; 7KYC; EM; 2.80 A; A=1-1571.
DR PDB; 7WHV; EM; 2.80 A; A=1-1571.
DR PDB; 7WHW; EM; 3.10 A; A=1-1571.
DR PDBsum; 7DRX; -.
DR PDBsum; 7DSH; -.
DR PDBsum; 7DSI; -.
DR PDBsum; 7F7F; -.
DR PDBsum; 7KY6; -.
DR PDBsum; 7KYB; -.
DR PDBsum; 7KYC; -.
DR PDBsum; 7WHV; -.
DR PDBsum; 7WHW; -.
DR AlphaFoldDB; P32660; -.
DR SMR; P32660; -.
DR BioGRID; 36919; 139.
DR ComplexPortal; CPX-1021; DNF1-LEM3 P4-ATPase complex.
DR DIP; DIP-7949N; -.
DR IntAct; P32660; 20.
DR MINT; P32660; -.
DR STRING; 4932.YER166W; -.
DR TCDB; 3.A.3.8.4; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; P32660; -.
DR MaxQB; P32660; -.
DR PaxDb; P32660; -.
DR PRIDE; P32660; -.
DR EnsemblFungi; YER166W_mRNA; YER166W; YER166W.
DR GeneID; 856913; -.
DR KEGG; sce:YER166W; -.
DR SGD; S000000968; DNF1.
DR VEuPathDB; FungiDB:YER166W; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000167741; -.
DR HOGENOM; CLU_000846_0_1_1; -.
DR InParanoid; P32660; -.
DR OMA; QALRCGR; -.
DR BioCyc; YEAST:G3O-30327-MON; -.
DR BRENDA; 7.6.2.1; 984.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-936837; Ion transport by P-type ATPases.
DR PRO; PR:P32660; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32660; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070867; C:mating projection tip membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IPI:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0140345; F:phosphatidylcholine flippase activity; IMP:SGD.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IGI:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IGI:SGD.
DR GO; GO:0045332; P:phospholipid translocation; IMP:SGD.
DR GO; GO:0000749; P:response to pheromone triggering conjugation with cellular fusion; IGI:SGD.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR InterPro; IPR026871; PLip_transp_ATPase.
DR PANTHER; PTHR24092:SF91; PTHR24092:SF91; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Endosome; Golgi apparatus;
KW Isopeptide bond; Lipid transport; Magnesium; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..1571
FT /note="Phospholipid-transporting ATPase DNF1"
FT /id="PRO_0000046235"
FT TOPO_DOM 1..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..553
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 575..594
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 616..1188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1189..1209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1210..1219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1220..1240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1241..1270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1271..1291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1292..1307
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1308..1328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1329..1334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1335..1355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1356..1375
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1376..1396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1397..1571
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 667
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 94
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12675"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12675"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 368
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q12675"
FT MOD_RES 1506
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1551
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 895
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q12675"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:7KYC"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 218..233
FT /evidence="ECO:0007829|PDB:7KYC"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 245..273
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 417..426
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:7KYC"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:7KYC"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 459..464
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 467..472
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 483..488
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 495..500
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 511..514
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 516..524
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 530..535
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 544..576
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:7KY6"
FT HELIX 581..585
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 594..608
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 616..633
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 636..638
FT /evidence="ECO:0007829|PDB:7KY6"
FT TURN 641..644
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 655..659
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 660..667
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 668..672
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 673..684
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 687..689
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 695..704
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 708..733
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 741..743
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 749..756
FT /evidence="ECO:0007829|PDB:7KYC"
FT TURN 757..759
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 761..776
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 799..811
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 813..816
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 820..822
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 824..827
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 830..833
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 836..840
FT /evidence="ECO:0007829|PDB:7KYC"
FT TURN 844..846
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 848..855
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 865..872
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 874..879
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 892..905
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 909..918
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 920..935
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 940..952
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 956..967
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 971..980
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 984..988
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 993..1002
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 1011..1014
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1019..1025
FT /evidence="ECO:0007829|PDB:7KYC"
FT TURN 1029..1031
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1032..1043
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1051..1059
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 1068..1072
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1074..1082
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1084..1095
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 1096..1102
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1107..1119
FT /evidence="ECO:0007829|PDB:7KYC"
FT TURN 1120..1122
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 1124..1132
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1133..1139
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 1141..1147
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1154..1157
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 1159..1165
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1168..1206
FT /evidence="ECO:0007829|PDB:7KYC"
FT TURN 1207..1211
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1219..1227
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1231..1240
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1246..1251
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1253..1256
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1257..1261
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1267..1292
FT /evidence="ECO:0007829|PDB:7KYC"
FT TURN 1293..1295
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1308..1329
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 1332..1335
FT /evidence="ECO:0007829|PDB:7KY6"
FT HELIX 1336..1357
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 1362..1365
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1368..1373
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1376..1403
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 1407..1416
FT /evidence="ECO:0007829|PDB:7KYC"
FT TURN 1417..1422
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 1432..1434
FT /evidence="ECO:0007829|PDB:7KY6"
SQ SEQUENCE 1571 AA; 177798 MW; 3CC3FBA8ADDE8960 CRC64;
MSGTFHGDGH APMSPFEDTF QFEDNSSNED THIAPTHFDD GATSNKYSRP QVSFNDETPK
NKREDAEEFT FNDDTEYDNH SFQPTPKLNN GSGTFDDVEL DNDSGEPHTN YDGMKRFRMG
TKRNKKGNPI MGRSKTLKWA RKNIPNPFED FTKDDIDPGA INRAQELRTV YYNMPLPKDM
IDEEGNPIMQ YPRNKIRTTK YTPLTFLPKN ILFQFHNFAN VYFLVLIILG AFQIFGVTNP
GLSAVPLVVI VIITAIKDAI EDSRRTVLDL EVNNTKTHIL EGVENENVST DNISLWRRFK
KANSRLLFKF IQYCKEHLTE EGKKKRMQRK RHELRVQKTV GTSGPRSSLD SIDSYRVSAD
YGRPSLDYDN LEQGAGEANI VDRSLPPRTD CKFAKNYWKG VKVGDIVRIH NNDEIPADII
LLSTSDTDGA CYVETKNLDG ETNLKVRQSL KCTNTIRTSK DIARTKFWIE SEGPHSNLYT
YQGNMKWRNL ADGEIRNEPI TINNVLLRGC TLRNTKWAMG VVMFTGGDTK IMLNSGITPT
KKSRISRELN FSVVINFVLL FILCFVSGIA NGVYYDKKGR SRFSYEFGTI AGSAATNGFV
SFWVAVILYQ SLVPISLYIS VEIIKTAQAA FIYGDVLLYN AKLDYPCTPK SWNISDDLGQ
VEYIFSDKTG TLTQNVMEFK KCTINGVSYG RAYTEALAGL RKRQGIDVET EGRREKAEIA
KDRDTMIDEL RALSGNSQFY PEEVTFVSKE FVRDLKGASG EVQQRCCEHF MLALALCHSV
LVEANPDNPK KLDLKAQSPD EAALVATARD VGFSFVGKTK KGLIIEMQGI QKEFEILNIL
EFNSSRKRMS CIVKIPGLNP GDEPRALLIC KGADSIIYSR LSRQSGSNSE AILEKTALHL
EQYATEGLRT LCIAQRELSW SEYEKWNEKY DIAAASLANR EDELEVVADS IERELILLGG
TAIEDRLQDG VPDCIELLAE AGIKLWVLTG DKVETAINIG FSCNLLNNEM ELLVIKTTGD
DVKEFGSEPS EIVDALLSKY LKEYFNLTGS EEEIFEAKKD HEFPKGNYAI VIDGDALKLA
LYGEDIRRKF LLLCKNCRAV LCCRVSPSQK AAVVKLVKDS LDVMTLAIGD GSNDVAMIQS
ADVGIGIAGE EGRQAVMCSD YAIGQFRYLA RLVLVHGRWS YKRLAEMIPE FFYKNMIFAL
ALFWYGIYND FDGSYLYEYT YMMFYNLAFT SLPVIFLGIL DQDVNDTISL VVPQLYRVGI
LRKEWNQRKF LWYMLDGLYQ SIICFFFPYL VYHKNMIVTS NGLGLDHRYF VGVYVTTIAV
ISCNTYVLLH QYRWDWFSGL FIALSCLVVF AWTGIWSSAI ASREFFKAAA RIYGAPSFWA
VFFVAVLFCL LPRFTYDSFQ KFFYPTDVEI VREMWQHGHF DHYPPGYDPT DPNRPKVTKA
GQHGEKIIEG IALSDNLGGS NYSRDSVVTE EIPMTFMHGE DGSPSGYQKQ ETWMTSPKET
QDLLQSPQFQ QAQTFGRGPS TNVRSSLDRT REQMIATNQL DNRYSVERAR TSLDLPGVTN
AASLIGTQQN N
