ID   ATC7_YEAST              Reviewed;        1151 AA.
AC   P40527; D6VVN3;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 209.
DE   RecName: Full=Phospholipid-transporting ATPase NEO1;
DE            EC=7.6.2.1 {ECO:0000305|PubMed:34645814};
GN   Name=NEO1 {ECO:0000303|PubMed:15314152};
GN   OrderedLocusNames=YIL048W {ECO:0000312|SGD:S000001310};
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=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(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, AND SUBCELLULAR LOCATION.
RX   PubMed=12960419; DOI=10.1091/mbc.e03-07-0463;
RA   Hua Z., Graham T.R.;
RT   "Requirement for neo1p in retrograde transport from the Golgi complex to
RT   the endoplasmic reticulum.";
RL   Mol. Biol. Cell 14:4971-4983(2003).
RN   [5]
RP   FUNCTION, INTERACTION WITH MON2, AND SUBCELLULAR LOCATION.
RX   PubMed=15314152; DOI=10.1128/mcb.24.17.7402-7418.2004;
RA   Wicky S., Schwarz H., Singer-Krueger B.;
RT   "Molecular interactions of yeast Neo1p, an essential member of the Drs2
RT   family of aminophospholipid translocases, and its role in membrane
RT   trafficking within the endomembrane system.";
RL   Mol. Cell. Biol. 24:7402-7418(2004).
RN   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP   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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-551, 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-102, 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   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-503.
RX   PubMed=27235400; DOI=10.1074/jbc.m115.686253;
RA   Takar M., Wu Y., Graham T.R.;
RT   "The Essential Neo1 Protein from Budding Yeast Plays a Role in Establishing
RT   Aminophospholipid Asymmetry of the Plasma Membrane.";
RL   J. Biol. Chem. 291:15727-15739(2016).
RN   [11]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 65-PHE--MET-67.
RX   PubMed=28404745; DOI=10.1091/mbc.e16-11-0772;
RA   Dalton L.E., Bean B.D.M., Davey M., Conibear E.;
RT   "Quantitative high-content imaging identifies novel regulators of Neo1
RT   trafficking at endosomes.";
RL   Mol. Biol. Cell 28:1539-1550(2017).
RN   [12]
RP   FUNCTION, AND INTERACTION WITH ANY1.
RX   PubMed=30824614; DOI=10.1194/jlr.m093526;
RA   Takar M., Huang Y., Graham T.R.;
RT   "The PQ-loop protein Any1 segregates Drs2 and Neo1 functions required for
RT   viability and plasma membrane phospholipid asymmetry.";
RL   J. Lipid Res. 60:1032-1042(2019).
RN   [13]
RP   INTERACTION WITH ANY1, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP   MUTAGENESIS OF GLN-209; TYR-222; PHE-228; GLU-237; SER-452; VAL-457 AND
RP   ASP-503.
RX   PubMed=31786280; DOI=10.1016/j.bbalip.2019.158581;
RA   Huang Y., Takar M., Best J.T., Graham T.R.;
RT   "Conserved mechanism of phospholipid substrate recognition by the P4-ATPase
RT   Neo1 from Saccharomyces cerevisiae.";
RL   Biochim. Biophys. Acta 1865:158581-158581(2020).
RN   [14] {ECO:0007744|PDB:7RD6, ECO:0007744|PDB:7RD7, ECO:0007744|PDB:7RD8}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.08 ANGSTROMS) IN COMPLEX WITH
RP   MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP   MUTAGENESIS OF GLN-193; GLN-209; SER-221; GLU-237; ARG-247; SER-452;
RP   THR-453; PRO-456 AND SER-488.
RX   PubMed=34645814; DOI=10.1038/s41467-021-26273-0;
RA   Bai L., Jain B.K., You Q., Duan H.D., Takar M., Graham T.R., Li H.;
RT   "Structural basis of the P4B ATPase lipid flippase activity.";
RL   Nat. Commun. 12:5963-5963(2021).
CC   -!- FUNCTION: Flippase that catalyzes the hydrolysis of ATP coupled to the
CC       transport of lysophosphatidylserine, phosphatidylethanolamine, and
CC       phosphatidylserine from the lumenal to the cytosolic leaflet of the
CC       Golgi apparatus membrane and ensures the maintenance of asymmetric
CC       distribution of phospholipids (PubMed:34645814, PubMed:27235400,
CC       PubMed:30824614). Does not appear to transport phosphatidylcholine or
CC       sphingomyelin (PubMed:34645814). May be involved in recycling from
CC       endosomes by driving the formation of SNX3-dependent recycling tubules
CC       (PubMed:28404745). Required for COPI retrograde transport from the
CC       Golgi to the endoplasmic reticulum, Golgi-endosome trafficking, and
CC       Golgi-dependent protein glycosylation (PubMed:15314152,
CC       PubMed:12960419). {ECO:0000269|PubMed:12960419,
CC       ECO:0000269|PubMed:15314152, ECO:0000269|PubMed:27235400,
CC       ECO:0000269|PubMed:28404745, ECO:0000269|PubMed:30824614,
CC       ECO:0000269|PubMed:34645814}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC         phospholipidSide 2.; EC=7.6.2.1;
CC         Evidence={ECO:0000305|PubMed:34645814};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O =
CC         a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) +
CC         phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57262, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000305|PubMed:34645814};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568;
CC         Evidence={ECO:0000305|PubMed:34645814};
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:34645814};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC         Evidence={ECO:0000305|PubMed:34645814};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:34645814};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=97.1 uM for phosphatidylethanolamine and for ATPase activity (at
CC         37 degrees Celsius and at pH 7.4) {ECO:0000269|PubMed:34645814};
CC         KM=62.9 uM for phosphatidylserine and for ATPase activity (at 37
CC         degrees Celsius and at pH 7.4) {ECO:0000269|PubMed:34645814};
CC         KM=50.3 uM for lysophosphatidylserine and for ATPase activity (at 37
CC         degrees Celsius and at pH 7.4) {ECO:0000269|PubMed:34645814};
CC         Vmax=0.56 nmol/min/ug enzyme for phosphatidylethanolamine and for
CC         ATPase activity (at 37 degrees Celsius and at pH 7.4)
CC         {ECO:0000269|PubMed:34645814};
CC         Vmax=0.559 nmol/min/ug enzyme for phosphatidylserine and for ATPase
CC         activity (at 37 degrees Celsius and at pH 7.4)
CC         {ECO:0000269|PubMed:34645814};
CC         Vmax=0.585 nmol/min/ug enzyme for lysophosphatidylserine and for
CC         ATPase activity (at 37 degrees Celsius and at pH 7.4)
CC         {ECO:0000269|PubMed:34645814};
CC   -!- SUBUNIT: Interacts with MON2 (PubMed:15314152). Interacts with ANY1
CC       (PubMed:30824614, PubMed:31786280). Functions without a CDC50/LEM3
CC       family accessory subunit (PubMed:34645814).
CC       {ECO:0000269|PubMed:15314152, ECO:0000269|PubMed:30824614,
CC       ECO:0000269|PubMed:31786280, ECO:0000269|PubMed:34645814}.
CC   -!- INTERACTION:
CC       P40527; Q03921: DOP1; NbExp=3; IntAct=EBI-3137, EBI-34442;
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:12631737,
CC       ECO:0000269|PubMed:15314152, ECO:0000269|PubMed:31786280}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:15314152}. Golgi apparatus
CC       membrane {ECO:0000269|PubMed:12960419, ECO:0000269|PubMed:15314152,
CC       ECO:0000269|PubMed:31786280, ECO:0000269|PubMed:34645814}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:15314152}.
CC   -!- DISRUPTION PHENOTYPE: Inviable; simultaneous knockout of ANY1 rescues
CC       inviability. {ECO:0000269|PubMed:27235400, ECO:0000269|PubMed:28404745,
CC       ECO:0000269|PubMed:31786280, ECO:0000269|PubMed:34645814}.
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; Z38060; CAA86174.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08499.1; -; Genomic_DNA.
DR   PIR; S48431; S48431.
DR   RefSeq; NP_012216.1; NM_001179398.1.
DR   PDB; 7RD6; EM; 3.25 A; A=1-1151.
DR   PDB; 7RD7; EM; 3.08 A; A=1-1151.
DR   PDB; 7RD8; EM; 5.64 A; A=1-1151.
DR   PDBsum; 7RD6; -.
DR   PDBsum; 7RD7; -.
DR   PDBsum; 7RD8; -.
DR   AlphaFoldDB; P40527; -.
DR   EMDB; EMD-24413; -.
DR   EMDB; EMD-24414; -.
DR   EMDB; EMD-24415; -.
DR   SMR; P40527; -.
DR   BioGRID; 34942; 504.
DR   ComplexPortal; CPX-1028; NEO1-MON2-ARL1-DOP1 membrane remodeling complex.
DR   DIP; DIP-2548N; -.
DR   IntAct; P40527; 7.
DR   MINT; P40527; -.
DR   STRING; 4932.YIL048W; -.
DR   TCDB; 3.A.3.8.18; the p-type atpase (p-atpase) superfamily.
DR   iPTMnet; P40527; -.
DR   MaxQB; P40527; -.
DR   PaxDb; 4932-YIL048W; -.
DR   PeptideAtlas; P40527; -.
DR   EnsemblFungi; YIL048W_mRNA; YIL048W; YIL048W.
DR   GeneID; 854763; -.
DR   KEGG; sce:YIL048W; -.
DR   AGR; SGD:S000001310; -.
DR   SGD; S000001310; NEO1.
DR   VEuPathDB; FungiDB:YIL048W; -.
DR   eggNOG; KOG0210; Eukaryota.
DR   GeneTree; ENSGT00940000168130; -.
DR   HOGENOM; CLU_000846_6_0_1; -.
DR   InParanoid; P40527; -.
DR   OMA; IAITTWH; -.
DR   OrthoDB; 275833at2759; -.
DR   BioCyc; YEAST:G3O-31319-MONOMER; -.
DR   Reactome; R-SCE-936837; Ion transport by P-type ATPases.
DR   BioGRID-ORCS; 854763; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P40527; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P40527; Protein.
DR   GO; GO:0005768; C:endosome; IDA:SGD.
DR   GO; GO:0010008; C:endosome membrane; NAS:ComplexPortal.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR   GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR   GO; GO:0005770; C:late endosome; IDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005802; C:trans-Golgi network; 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; ISS:SGD.
DR   GO; GO:0180013; F:lysophosphatidylserine flippase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IDA:UniProtKB.
DR   GO; GO:0140346; F:phosphatidylserine flippase activity; IDA:UniProtKB.
DR   GO; GO:0090556; F:phosphatidylserine floppase activity; IEA:RHEA.
DR   GO; GO:0006897; P:endocytosis; IMP:SGD.
DR   GO; GO:0045332; P:phospholipid translocation; IDA:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:SGD.
DR   GO; GO:0098629; P:trans-Golgi network membrane organization; NAS:ComplexPortal.
DR   GO; GO:0007033; P:vacuole organization; IMP:SGD.
DR   CDD; cd07541; P-type_ATPase_APLT_Neo1-like; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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   NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR24092:SF5; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 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   3D-structure; ATP-binding; Endosome; Golgi apparatus; Lipid transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Protein transport; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1151
FT                   /note="Phospholipid-transporting ATPase NEO1"
FT                   /id="PRO_0000046236"
FT   TOPO_DOM        1..184
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        206..209
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        231..367
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        389..416
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        438
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        460..947
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        948..968
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        969..970
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        971..991
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        992..1020
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1021..1041
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1042..1052
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1053..1073
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1074..1078
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1079..1099
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1100..1109
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1110..1130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1131..1151
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          51..104
FT                   /note="Required for endosome-to-Golgi sorting"
FT                   /evidence="ECO:0000269|PubMed:28404745"
FT   REGION          73..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1131..1151
FT                   /note="Required for endosomal targeting"
FT   COMPBIAS        73..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        503
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000305"
FT   BINDING         503
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         503
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         504
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         505
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:34645814,
FT                   ECO:0007744|PDB:7RD8"
FT   BINDING         505
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         597
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         640
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         642
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P32660"
FT   BINDING         645
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:34645814,
FT                   ECO:0007744|PDB:7RD8"
FT   BINDING         664
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         693
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         694
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P39524"
FT   BINDING         774
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         775
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         776
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         856
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         862
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         882
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         885
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         886
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         886
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT   MOD_RES         102
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         551
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         65..67
FT                   /note="FEM->AAA: Sensitive to neomycin and trifluoperazine;
FT                   sensitivity is suppressed by knockout of ANY1."
FT                   /evidence="ECO:0000269|PubMed:28404745"
FT   MUTAGEN         193
FT                   /note="Q->A: Sensitive to duramycin
FT                   (phosphatidylethanolamine-binding cytoxin). Localization to
FT                   the Golgi apparatus appears normal."
FT                   /evidence="ECO:0000269|PubMed:34645814"
FT   MUTAGEN         209
FT                   /note="Q->G: Sensitive to duramycin
FT                   (phosphatidylethanolamine-binding cytoxin) and papuamide A
FT                   (phosphatidylserine-binding cytotoxin). Localization to the
FT                   Golgi apparatus appears normal."
FT                   /evidence="ECO:0000269|PubMed:31786280,
FT                   ECO:0000269|PubMed:34645814"
FT   MUTAGEN         221
FT                   /note="S->L: Sensitive to duramycin
FT                   (phosphatidylethanolamine-binding cytoxin)."
FT                   /evidence="ECO:0000269|PubMed:34645814"
FT   MUTAGEN         222
FT                   /note="Y->S,A: May enhance substrate loading. Decreases
FT                   cell population growth; when associated with V-228 and
FT                   D-237."
FT                   /evidence="ECO:0000269|PubMed:31786280"
FT   MUTAGEN         222
FT                   /note="Y->S: Does not appear to affect its physical
FT                   interaction with ANY1. Increases localization to late Golgi
FT                   compartments. Decreases cell population growth; when
FT                   associated with V-228 and D-237."
FT                   /evidence="ECO:0000269|PubMed:31786280"
FT   MUTAGEN         228
FT                   /note="F->V: Decreases cell population growth; when
FT                   associated with S-222 and D-237."
FT                   /evidence="ECO:0000269|PubMed:31786280"
FT   MUTAGEN         237
FT                   /note="E->D: Sensitive to duramycin
FT                   (phosphatidylethanolamine-binding cytoxin) and papuamide A
FT                   (phosphatidylserine-binding cytotoxin). Localization to the
FT                   Golgi apparatus appears normal. Decreases cell population
FT                   growth; when associated with S-222 and V-228."
FT                   /evidence="ECO:0000269|PubMed:31786280,
FT                   ECO:0000269|PubMed:34645814"
FT   MUTAGEN         247
FT                   /note="R->A,L: Sensitive to duramycin
FT                   (phosphatidylethanolamine-binding cytoxin)."
FT                   /evidence="ECO:0000269|PubMed:34645814"
FT   MUTAGEN         452
FT                   /note="S->A,Q: Sensitive to duramycin
FT                   (phosphatidylethanolamine-binding cytoxin)."
FT                   /evidence="ECO:0000269|PubMed:31786280,
FT                   ECO:0000269|PubMed:34645814"
FT   MUTAGEN         452
FT                   /note="S->Q: Sensitive to papuamide A
FT                   (phosphatidylserine-binding cytotoxin). Localization to the
FT                   Golgi apparatus appears normal."
FT                   /evidence="ECO:0000269|PubMed:31786280,
FT                   ECO:0000269|PubMed:34645814"
FT   MUTAGEN         453
FT                   /note="T->S: Sensitive to papuamide A."
FT                   /evidence="ECO:0000269|PubMed:34645814"
FT   MUTAGEN         456
FT                   /note="P->A: No apparent effect on viability. Sensitive to
FT                   duramycin (phosphatidylethanolamine-binding cytoxin) and
FT                   papuamide A (phosphatidylserine-binding cytotoxin).
FT                   Localization to the Golgi apparatus appears normal."
FT                   /evidence="ECO:0000269|PubMed:34645814"
FT   MUTAGEN         456
FT                   /note="P->G: Inviable."
FT                   /evidence="ECO:0000269|PubMed:34645814"
FT   MUTAGEN         457
FT                   /note="V->A,E,F: Sensitive to duramycin
FT                   (phosphatidylethanolamine-binding cytoxin)."
FT                   /evidence="ECO:0000269|PubMed:31786280"
FT   MUTAGEN         488
FT                   /note="S->A,W: Sensitive to duramycin
FT                   (phosphatidylethanolamine-binding cytoxin) and papuamide A
FT                   (phosphatidylserine-binding cytotoxin)."
FT                   /evidence="ECO:0000269|PubMed:34645814"
FT   MUTAGEN         488
FT                   /note="S->A: Localization to the Golgi apparatus appears
FT                   normal."
FT                   /evidence="ECO:0000269|PubMed:34645814"
FT   MUTAGEN         503
FT                   /note="D->N: Inviable."
FT                   /evidence="ECO:0000269|PubMed:27235400,
FT                   ECO:0000269|PubMed:31786280"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           162..166
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          167..170
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           186..193
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          194..196
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           197..208
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           212..214
FT                   /evidence="ECO:0007829|PDB:7RD6"
FT   TURN            219..222
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           224..249
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          255..258
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   TURN            259..261
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          263..266
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   TURN            267..269
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          275..279
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          286..297
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          299..303
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   TURN            305..307
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          312..317
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   TURN            320..322
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          335..338
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          350..354
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   TURN            355..357
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          358..362
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           364..366
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          376..386
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           392..395
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           406..433
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           440..451
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           455..474
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          478..480
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          484..486
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           493..495
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          499..502
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   TURN            505..508
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          509..520
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          523..529
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           531..537
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           538..540
FT                   /evidence="ECO:0007829|PDB:7RD6"
FT   HELIX           561..575
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          580..582
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          585..587
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          589..591
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           595..607
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          610..614
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          616..619
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          621..624
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          630..638
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   TURN            642..644
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          646..656
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          659..665
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           667..670
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   TURN            671..673
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           680..688
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   TURN            689..691
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          693..702
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           704..711
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   TURN            734..736
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          741..752
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           757..765
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          769..773
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           778..787
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          823..826
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           828..837
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           839..846
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          848..850
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          852..854
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           859..872
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          877..881
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           884..886
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           887..891
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          893..899
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          901..903
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           906..910
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          911..918
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           920..926
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           928..960
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          961..963
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   TURN            966..968
FT                   /evidence="ECO:0007829|PDB:7RD6"
FT   HELIX           972..978
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   TURN            979..982
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           983..989
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           997..999
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   TURN            1000..1002
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           1005..1010
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          1015..1017
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           1018..1043
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   STRAND          1046..1049
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           1050..1071
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   TURN            1078..1080
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           1081..1092
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   TURN            1096..1099
FT                   /evidence="ECO:0007829|PDB:7RD7"
FT   HELIX           1110..1137
FT                   /evidence="ECO:0007829|PDB:7RD7"
SQ   SEQUENCE   1151 AA;  130218 MW;  DC7225CC9577DBE6 CRC64;
     MPNPPSFKSH KQNLFNSNNN QHANSVDSFD LHLDDSFDAA LDSLQINNNP EPLSKHNTVG
     DRESFEMRTV DDLDNFSNHS SDSHRKSSNT DTHPLMYDNR LSQDDNFKFT NIASSPPSSS
     NNIFSKALSY LKVSNTKNWS KFGSPIELSD QHIEREIHPD TTPVYDRNRY VSNELSNAKY
     NAVTFVPTLL YEQFKFFYNL YFLVVALSQA VPALRIGYLS SYIVPLAFVL TVTMAKEAID
     DIQRRRRDRE SNNELYHVIT RNRSIPSKDL KVGDLIKVHK GDRIPADLVL LQSSEPSGES
     FIKTDQLDGE TDWKLRVACP LTQNLSENDL INRISITASA PEKSIHKFLG KVTYKDSTSN
     PLSVDNTLWA NTVLASSGFC IACVVYTGRD TRQAMNTTTA KVKTGLLELE INSISKILCA
     CVFALSILLV AFAGFHNDDW YIDILRYLIL FSTIIPVSLR VNLDLAKSVY AHQIEHDKTI
     PETIVRTSTI PEDLGRIEYL LSDKTGTLTQ NDMQLKKIHL GTVSYTSETL DIVSDYVQSL
     VSSKNDSLNN SKVALSTTRK DMSFRVRDMI LTLAICHNVT PTFEDDELTY QAASPDEIAI
     VKFTESVGLS LFKRDRHSIS LLHEHSGKTL NYEILQVFPF NSDSKRMGII VRDEQLDEYW
     FMQKGADTVM SKIVESNDWL EEETGNMARE GLRTLVIGRK KLNKKIYEQF QKEYNDASLS
     MLNRDQQMSQ VITKYLEHDL ELLGLTGVED KLQKDVKSSI ELLRNAGIKI WMLTGDKVET
     ARCVSISAKL ISRGQYVHTI TKVTRPEGAF NQLEYLKINR NACLLIDGES LGMFLKHYEQ
     EFFDVVVHLP TVIACRCTPQ QKADVALVIR KMTGKRVCCI GDGGNDVSMI QCADVGVGIV
     GKEGKQASLA ADFSITQFCH LTELLLWHGR NSYKRSAKLA QFVMHRGLII AICQAVYSIC
     SLFEPIALYQ GWLMVGYATC YTMAPVFSLT LDHDIEESLT KIYPELYKEL TEGKSLSYKT
     FFVWVLLSLF QGSVIQLFSQ AFTSLLDTDF TRMVAISFTA LVVNELIMVA LEIYTWNKTM
     LVTEIATLLF YIVSVPFLGD YFDLGYMTTV NYYAGLLVIL LISIFPVWTA KAIYRRLHPP
     SYAKVQEFAT P
//