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Database: UniProt
Entry: ATC8_YEAST
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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
//
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