ATC4_YEAST
ID ATC4_YEAST Reviewed; 1612 AA.
AC Q12675; D6VS80;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Phospholipid-transporting ATPase DNF2;
DE EC=7.6.2.1;
DE AltName: Full=Flippase DNF2;
GN Name=DNF2; OrderedLocusNames=YDR093W; ORFNames=YD8557.01;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12221123; DOI=10.1091/mbc.e02-03-0172;
RA Hua Z., Fatheddin P., Graham T.R.;
RT "An essential subfamily of Drs2p-related P-type ATPases is required for
RT protein trafficking between Golgi complex and endosomal/vacuolar system.";
RL Mol. Biol. Cell 13:3162-3177(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1542, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70; SER-389; SER-392 AND
RP SER-1542, AND 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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1542 AND SER-1592, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-396; SER-403;
RP TYR-406; THR-782; SER-1542 AND SER-1592, AND IDENTIFICATION BY MASS
RP 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).
RN [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-938, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of phospholipids. Required for protein
CC transport from Golgi to vacuoles. {ECO:0000269|PubMed:12221123}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC -!- INTERACTION:
CC Q12675; P32660: DNF1; NbExp=3; IntAct=EBI-3114, EBI-3121;
CC Q12675; P42838: LEM3; NbExp=2; IntAct=EBI-3114, EBI-28396;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12221123,
CC ECO:0000269|PubMed:18199685}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12221123, 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; Z47746; CAA87668.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11940.1; -; Genomic_DNA.
DR PIR; S51243; S51243.
DR RefSeq; NP_010378.1; NM_001180401.1.
DR PDB; 7KY5; EM; 3.98 A; A=1-1612.
DR PDB; 7KY7; EM; 3.08 A; A=1-1612.
DR PDB; 7KY8; EM; 3.85 A; A=1-1612.
DR PDB; 7KY9; EM; 4.05 A; A=1-1612.
DR PDB; 7KYA; EM; 3.50 A; A=1-1612.
DR PDBsum; 7KY5; -.
DR PDBsum; 7KY7; -.
DR PDBsum; 7KY8; -.
DR PDBsum; 7KY9; -.
DR PDBsum; 7KYA; -.
DR AlphaFoldDB; Q12675; -.
DR SMR; Q12675; -.
DR BioGRID; 32150; 118.
DR ComplexPortal; CPX-1022; DNF2-LEM3 P4-ATPase complex.
DR DIP; DIP-8055N; -.
DR IntAct; Q12675; 4.
DR MINT; Q12675; -.
DR STRING; 4932.YDR093W; -.
DR TCDB; 3.A.3.8.5; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; Q12675; -.
DR MaxQB; Q12675; -.
DR PaxDb; Q12675; -.
DR PRIDE; Q12675; -.
DR EnsemblFungi; YDR093W_mRNA; YDR093W; YDR093W.
DR GeneID; 851667; -.
DR KEGG; sce:YDR093W; -.
DR SGD; S000002500; DNF2.
DR VEuPathDB; FungiDB:YDR093W; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000167741; -.
DR HOGENOM; CLU_000846_0_1_1; -.
DR InParanoid; Q12675; -.
DR OMA; CETALDQ; -.
DR BioCyc; YEAST:G3O-29698-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-936837; Ion transport by P-type ATPases.
DR PRO; PR:Q12675; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12675; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070867; C:mating projection tip membrane; IDA:SGD.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0015247; F:aminophospholipid flippase activity; IMP: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:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0140346; F:phosphatidylserine 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:0045332; P:phospholipid translocation; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; Isopeptide bond; Lipid transport;
KW Magnesium; Membrane; Nucleotide-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubl conjugation.
FT CHAIN 1..1612
FT /note="Phospholipid-transporting ATPase DNF2"
FT /id="PRO_0000046234"
FT TOPO_DOM 1..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..598
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..639
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 661..1231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1232..1252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1253..1262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1263..1283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1284..1313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1314..1334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1335..1350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1351..1371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1372..1377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1378..1398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1399..1418
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1419..1439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1440..1612
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1544..1563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 712
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 406
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 782
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 938
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:7KYA"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:7KYA"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:7KYA"
FT HELIX 244..252
FT /evidence="ECO:0007829|PDB:7KYA"
FT HELIX 256..269
FT /evidence="ECO:0007829|PDB:7KYA"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:7KYA"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:7KYA"
FT HELIX 283..298
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:7KYA"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:7KYA"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:7KYA"
FT STRAND 464..471
FT /evidence="ECO:0007829|PDB:7KYA"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:7KYA"
FT TURN 481..483
FT /evidence="ECO:0007829|PDB:7KYA"
FT STRAND 490..493
FT /evidence="ECO:0007829|PDB:7KYA"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:7KYA"
FT HELIX 504..507
FT /evidence="ECO:0007829|PDB:7KYA"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:7KYA"
FT STRAND 528..533
FT /evidence="ECO:0007829|PDB:7KYA"
FT STRAND 535..538
FT /evidence="ECO:0007829|PDB:7KYA"
FT STRAND 540..545
FT /evidence="ECO:0007829|PDB:7KYA"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:7KYA"
FT STRAND 563..567
FT /evidence="ECO:0007829|PDB:7KYA"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:7KYA"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:7KYA"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:7KYA"
FT HELIX 589..620
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 627..630
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 641..653
FT /evidence="ECO:0007829|PDB:7KY7"
FT TURN 654..656
FT /evidence="ECO:0007829|PDB:7KYA"
FT HELIX 660..678
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 681..683
FT /evidence="ECO:0007829|PDB:7KY7"
FT TURN 686..689
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 693..695
FT /evidence="ECO:0007829|PDB:7KYA"
FT HELIX 703..705
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 708..712
FT /evidence="ECO:0007829|PDB:7KY7"
FT TURN 713..716
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 717..729
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 732..735
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 740..749
FT /evidence="ECO:0007829|PDB:7KY7"
FT TURN 753..756
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 757..778
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 786..788
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 795..802
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 807..821
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 826..829
FT /evidence="ECO:0007829|PDB:7KYA"
FT STRAND 834..836
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 837..840
FT /evidence="ECO:0007829|PDB:7KYA"
FT HELIX 844..855
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 858..861
FT /evidence="ECO:0007829|PDB:7KYA"
FT STRAND 865..867
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 870..872
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 875..877
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 881..885
FT /evidence="ECO:0007829|PDB:7KYA"
FT TURN 889..891
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 893..900
FT /evidence="ECO:0007829|PDB:7KYA"
FT STRAND 910..917
FT /evidence="ECO:0007829|PDB:7KYA"
FT TURN 919..921
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 922..924
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 928..931
FT /evidence="ECO:0007829|PDB:7KYA"
FT HELIX 934..949
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 952..957
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 966..976
FT /evidence="ECO:0007829|PDB:7KY7"
FT TURN 981..983
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 985..993
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 995..997
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 1000..1010
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1014..1023
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 1027..1031
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1037..1045
FT /evidence="ECO:0007829|PDB:7KY7"
FT TURN 1046..1048
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 1055..1057
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 1060..1063
FT /evidence="ECO:0007829|PDB:7KYA"
FT HELIX 1072..1086
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1095..1101
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 1112..1115
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1117..1121
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 1124..1126
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1127..1136
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 1140..1145
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1150..1161
FT /evidence="ECO:0007829|PDB:7KY7"
FT TURN 1162..1165
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 1167..1169
FT /evidence="ECO:0007829|PDB:7KYA"
FT HELIX 1175..1181
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 1184..1186
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 1188..1190
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 1192..1194
FT /evidence="ECO:0007829|PDB:7KYA"
FT HELIX 1197..1200
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 1202..1209
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1211..1216
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1219..1247
FT /evidence="ECO:0007829|PDB:7KY7"
FT TURN 1248..1250
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1251..1254
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1264..1270
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1275..1283
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1289..1294
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1296..1299
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1300..1303
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1310..1336
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 1342..1346
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1351..1372
FT /evidence="ECO:0007829|PDB:7KY7"
FT STRAND 1375..1378
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1381..1400
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1403..1405
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1411..1415
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1419..1446
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1450..1460
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 1462..1464
FT /evidence="ECO:0007829|PDB:7KY7"
SQ SEQUENCE 1612 AA; 182619 MW; 09719DF264256BEC CRC64;
MSSPSKPTSP FVDDIEHESG SASNGLSSMS PFDDSFQFEK PSSAHGNIEV AKTGGSVLKR
QSKPMKDIST PDLSKVTFDG IDDYSNDNDI NDDDELNGKK TEIHEHENEV DDDLHSFQAT
PMPNTGGFED VELDNNEGSN NDSQADHKLK RVRFGTRRNK SGRIDINRSK TLKWAKKNFH
NAIDEFSTKE DSLENSALQN RSDELRTVYY NLPLPEDMLD EDGLPLAVYP RNKIRTTKYT
PLTFFPKNIL FQFHNFANIY FLILLILGAF QIFGVTNPGF ASVPLIVIVI ITAIKDGIED
SRRTVLDLEV NNTRTHILSG VKNENVAVDN VSLWRRFKKA NTRALIKIFE YFSENLTAAG
REKKLQKKRE ELRRKRNSRS FGPRGSLDSI GSYRMSADFG RPSLDYENLN QTMSQANRYN
DGENLVDRTL QPNPECRFAK DYWKNVKVGD IVRVHNNDEI PADMILLSTS DVDGACYVET
KNLDGETNLK VRQSLKCSKI IKSSRDITRT KFWVESEGPH ANLYSYQGNF KWQDTQNGNI
RNEPVNINNL LLRGCTLRNT KWAMGMVIFT GDDTKIMINA GVTPTKKSRI SRELNFSVIL
NFVLLFILCF TAGIVNGVYY KQKPRSRDYF EFGTIGGSAS TNGFVSFWVA VILYQSLVPI
SLYISVEIIK TAQAIFIYTD VLLYNAKLDY PCTPKSWNIS DDLGQIEYIF SDKTGTLTQN
VMEFKKCTIN GVSYGRAYTE ALAGLRKRQG VDVESEGRRE KEEIAKDRET MIDELRSMSD
NTQFCPEDLT FVSKEIVEDL KGSSGDHQQK CCEHFLLALA LCHSVLVEPN KDDPKKLDIK
AQSPDESALV STARQLGYSF VGSSKSGLIV EIQGVQKEFQ VLNVLEFNSS RKRMSCIIKI
PGSTPKDEPK ALLICKGADS VIYSRLDRTQ NDATLLEKTA LHLEEYATEG LRTLCLAQRE
LTWSEYERWV KTYDVAAASV TNREEELDKV TDVIERELIL LGGTAIEDRL QDGVPDSIAL
LAEAGIKLWV LTGDKVETAI NIGFSCNVLN NDMELLVVKA SGEDVEEFGS DPIQVVNNLV
TKYLREKFGM SGSEEELKEA KREHGLPQGN FAVIIDGDAL KVALNGEEMR RKFLLLCKNC
KAVLCCRVSP AQKAAVVKLV KKTLDVMTLA IGDGSNDVAM IQSADVGVGI AGEEGRQAVM
CSDYAIGQFR YVTRLVLVHG KWCYKRLAEM IPQFFYKNVI FTLSLFWYGI YNNFDGSYLF
EYTYLTFYNL AFTSVPVILL AVLDQDVSDT VSMLVPQLYR VGILRKEWNQ TKFLWYMLDG
VYQSVICFFF PYLAYHKNMV VTENGLGLDH RYFVGVFVTA IAVTSCNFYV FMEQYRWDWF
CGLFICLSLA VFYGWTGIWT SSSSSNEFYK GAARVFAQPA YWAVLFVGVL FCLLPRFTID
CIRKIFYPKD IEIVREMWLR GDFDLYPQGY DPTDPSRPRI NEIRPLTDFK EPISLDTHFD
GVSHSQETIV TEEIPMSILN GEQGSRKGYR VSTTLERRDQ LSPVTTTNNL PRRSMASARG
NKLRTSLDRT REEMLANHQL DTRYSVERAR ASLDLPGINH AETLLSQRSR DR
