ID ATC8_YEAST Reviewed; 1656 AA.
AC Q12674; D6VZY4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 199.
DE RecName: Full=Probable phospholipid-transporting ATPase DNF3;
DE EC=7.6.2.1 {ECO:0000305|PubMed:16452632};
DE AltName: Full=Aminophospholipid translocase;
DE Short=APT;
DE AltName: Full=Phospholipid translocase {ECO:0000303|PubMed:17093059};
DE Short=PLT;
GN Name=DNF3; OrderedLocusNames=YMR162C; ORFNames=YM8520.11C;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 SUBCELLULAR LOCATION.
RX PubMed=12631737; DOI=10.1091/mbc.e02-08-0501;
RA Pomorski T., Lombardi R., Riezman H., Devaux P.F., van Meer G.,
RA Holthuis J.C.;
RT "Drs2p-related P-type ATPases Dnf1p and Dnf2p are required for phospholipid
RT translocation across the yeast plasma membrane and serve a role in
RT endocytosis.";
RL Mol. Biol. Cell 14:1240-1254(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16452632; DOI=10.1091/mbc.e05-10-0912;
RA Alder-Baerens N., Lisman Q., Luong L., Pomorski T., Holthuis J.C.;
RT "Loss of P4 ATPases Drs2p and Dnf3p disrupts aminophospholipid transport
RT and asymmetry in yeast post-Golgi secretory vesicles.";
RL Mol. Biol. Cell 17:1632-1642(2006).
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH YNR048W.
RX PubMed=17093059; DOI=10.1091/mbc.e06-05-0461;
RA Furuta N., Fujimura-Kamada K., Saito K., Yamamoto T., Tanaka K.;
RT "Endocytic recycling in yeast is regulated by putative phospholipid
RT translocases and the Ypt31p/32p-Rcy1p pathway.";
RL Mol. Biol. Cell 18:295-312(2007).
RN [7]
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 INTERACTION WITH YNR048W.
RX PubMed=19411703; DOI=10.1074/jbc.m109.013722;
RA Lenoir G., Williamson P., Puts C.F., Holthuis J.C.;
RT "Cdc50p plays a vital role in the ATPase reaction cycle of the putative
RT aminophospholipid transporter Drs2p.";
RL J. Biol. Chem. 284:17956-17967(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627, AND IDENTIFICATION BY
RP 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).
RN [10]
RP IDENTIFICATION IN A COMPLEX WITH YNR048W, AND INTERACTION WITH YNR048W.
RX PubMed=22791719; DOI=10.1074/jbc.m112.371088;
RA Puts C.F., Panatala R., Hennrich H., Tsareva A., Williamson P.,
RA Holthuis J.C.;
RT "Mapping functional interactions in a heterodimeric phospholipid pump.";
RL J. Biol. Chem. 287:30529-30540(2012).
CC -!- FUNCTION: Catalytic component of a P4-ATPase flippase complex which
CC catalyzes the hydrolysis of ATP coupled to the transport of
CC phosphatidylcholine and small amounts of phosphatidylethanolamine from
CC the lumen to the cytosolic leaflet of the trans-Golgi network and
CC ensures the maintenance of asymmetric distribution of phospholipids
CC (PubMed:16452632). May be involved in transport from early endosomes to
CC the trans-Golgi network (TGN) (Probable). {ECO:0000269|PubMed:16452632,
CC ECO:0000305|PubMed:17093059}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000305|PubMed:16452632};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a
CC 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:16452632};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584;
CC Evidence={ECO:0000305|PubMed:16452632};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:16452632};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000305|PubMed:16452632};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P39524};
CC -!- SUBUNIT: Component of a flippase complex consisting of DNF3 and
CC YNR048W/CRF1 (PubMed:22791719). Interacts with YNR048W/CRF1; the
CC interaction is direct and required for proper expression and
CC endoplasmic reticulum (ER) export of either partner (PubMed:17093059,
CC PubMed:19411703, PubMed:22791719). {ECO:0000269|PubMed:17093059,
CC ECO:0000269|PubMed:19411703, ECO:0000269|PubMed:22791719}.
CC -!- INTERACTION:
CC Q12674; P53740: YNR048W; NbExp=3; IntAct=EBI-3142, EBI-28524;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:12631737, ECO:0000269|PubMed:17093059}; Multi-pass
CC membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000269|PubMed:12631737, ECO:0000269|PubMed:16452632}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Decreases phosphatidylcholine and
CC phosphatidylethanolamine flippase activity in secretory vesicles;
CC simultaneous knockout of DRS2 exacerbates the effect.
CC {ECO:0000269|PubMed:16452632}.
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; Z49705; CAA89798.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10058.1; -; Genomic_DNA.
DR PIR; S54520; S54520.
DR RefSeq; NP_013885.1; NM_001182666.1.
DR AlphaFoldDB; Q12674; -.
DR SMR; Q12674; -.
DR BioGRID; 35339; 73.
DR ComplexPortal; CPX-1026; DNF3-CRF1 P4-ATPase complex.
DR IntAct; Q12674; 7.
DR MINT; Q12674; -.
DR STRING; 4932.YMR162C; -.
DR TCDB; 3.A.3.8.20; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; Q12674; -.
DR MaxQB; Q12674; -.
DR PaxDb; 4932-YMR162C; -.
DR PeptideAtlas; Q12674; -.
DR EnsemblFungi; YMR162C_mRNA; YMR162C; YMR162C.
DR GeneID; 855197; -.
DR KEGG; sce:YMR162C; -.
DR AGR; SGD:S000004772; -.
DR SGD; S000004772; DNF3.
DR VEuPathDB; FungiDB:YMR162C; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; Q12674; -.
DR OMA; GWFLWNI; -.
DR OrthoDB; 275833at2759; -.
DR BioCyc; YEAST:G3O-32852-MONOMER; -.
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 BioGRID-ORCS; 855197; 0 hits in 10 CRISPR screens.
DR PRO; PR:Q12674; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q12674; Protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; 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:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0140345; F:phosphatidylcholine flippase activity; IMP:SGD.
DR GO; GO:0090554; F:phosphatidylcholine floppase activity; IEA:RHEA.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IMP:SGD.
DR GO; GO:0140346; F:phosphatidylserine flippase activity; IGI:SGD.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0045332; P:phospholipid translocation; IMP:SGD.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 2.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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 NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF174; PHOSPHOLIPID-TRANSPORTING ATPASE DNF3-RELATED; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Endosome; Golgi apparatus; Lipid transport; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1656
FT /note="Probable phospholipid-transporting ATPase DNF3"
FT /id="PRO_0000046237"
FT TOPO_DOM 1..164
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..495
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..1157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1158..1178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1179..1318
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 1319..1339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1340..1365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1366..1386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1387..1395
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 1396..1416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1417..1432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1433..1453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1454..1473
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 1474..1494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1495..1656
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT REGION 36..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 566
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305"
FT BINDING 566
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 566
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 568
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39524"
FT BINDING 568
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 765
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 813
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 815
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P32660"
FT BINDING 818
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39524"
FT BINDING 838
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 1034
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 1035
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39524"
FT BINDING 1114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 1115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 1116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 1167..1174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 1208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 1229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 1232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 1233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1656 AA; 188319 MW; A20A823BEB401184 CRC64;
MGIADGQRRR SSSLRTQMFN KHLYDKYRGR TDDEIELEDI NESKTFSGSD NNDKDDRDET
SGNYAAEEDY EMEEYGSPDV SYSIITKILD TILDRRRTFH SKDGRHIPII LDHNAIEYKQ
AATKRDGHLI DERFNKPYCD NRITSSRYTF YSFLPRQLYA QFSKLANTYF FIVAVLQMIP
GWSTTGTYTT IIPLCVFMGI SMTREAWDDF RRHRLDKEEN NKPVGVLVKD GNNDAQEVYT
LPSSVVSSTA YLTKSAAAEN NPPLNDDRNS SQGHFLDTHF NNFELLKNKY NVHIHQKKWE
KLRVGDFVLL TQDDWVPADL LLLTCDGENS ECFVETMALD GETNLKSKQP HPELNKLTKA
ASGLANINAQ VTVEDPNIDL YNFEGNLELK NHRNDTIMKY PLGPDNVIYR GSILRNTQNV
VGMVIFSGEE TKIRMNALKN PRTKAPKLQR KINMIIVFMV FVVATISLFS YLGHVLHKKK
YIDQNKAWYL FQADAGVAPT IMSFIIMYNT VIPLSLYVTM EIIKVVQSKM MEWDIDMYHA
ETNTPCESRT ATILEELGQV SYIFSDKTGT LTDNKMIFRK FSLCGSSWLH NVDLGNSEDN
FEDNRDNTNS LRLPPKAHNG SSIDVVSIGD QNVLDRLGFS DAPIEKGHRP SLDNFPKSRN
SIEYKGNSSA IYTGRPSMRS LFGKDNSHLS KQASVISPSE TFSENIKSSF DLIQFIQRYP
TALFSQKAKF FFLSLALCHS CLPKKTHNES IGEDSIEYQS SSPDELALVT AARDLGYIVL
NRNAQILTIK TFPDGFDGEA KLENYEILNY IDFNSQRKRM SVLVRMPNQP NQVLLICKGA
DNVIMERLHD RELAAKKMAD ICTSTKERKD AEAELVLQQR KSLERMVDEE AMARTSLRNS
LSSVPRASLS LQAVRKSLSM KNSRTRDPEK QIDSIDQFLE TVKKSDQEIG SVVNKSRKSL
HKQQIEKYGP RISIDGTHFP NNNVPIDTRK EGLQHDYDTE ILEHIGSDEL ILNEEYVIER
TLQAIDEFST EGLRTLVYAY KWIDIGQYEN WNKRYHQAKT SLTDRKIKVD EAGAEIEDGL
NLLGVTAIED KLQDGVSEAI EKIRRAGIKM WMLTGDKRET AINIGYSCML IKDYSTVVIL
TTTDENIISK MNAVSQEVDS GNIAHCVVVI DGATMAMFEG NPTYMSVFVE LCTKTDSVIC
CRASPSQKAL MVSNIRNTDP NLVTLAIGDG ANDIAMIQSA DIGVGIAGKE GLQASRVSDY
SIGQFRFLLK LLFVHGRYNY IRTSKFMLCT FYKEITFYFT QLIYQRYTMF SGSSLYEPWS
LSMFNTLFTS LPVLCIGMFE KDLKPMTLLT VPELYSYGRL SQGFNWLIFM EWVILATTNS
LIITFLNVVM WGMSSLSDNT MYPLGLINFT AIVALINVKS QFVEMHNRNW LAFTSVVLSC
GGWLVWCCAL PILNNTDQIY DVAYGFYNHF GKDITFWCTS LVLALLPITL DIVYKTFKVM
IWPSDSDIFA ELEQKSDIRK KLELGAYSEM RQGWTWDKDP STFTRYTDKV LSRPRTNSRA
SAKTHNSSIY SMSNGNVDHS SKKNFFGNSS KKSSERYEVL PSGKLIKRPS LKTQSSKDSI
GGNITTKLTK KLKLPSRNVE DEDVNQIIQA RLKDLE
//