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Probable phospholipid-transporting ATPase NEO1 (EC 3.6.3.1)

 ATC7_YEAST              Reviewed;        1151 AA.
P40527; D6VVN3;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
23-MAY-2018, entry version 175.
RecName: Full=Probable phospholipid-transporting ATPase NEO1;
EC=3.6.3.1;
Name=NEO1; OrderedLocusNames=YIL048W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169870;
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N.,
Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G.,
Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N.,
Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
Nature 387:84-87(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
INTERACTION WITH MON2, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=15314152; DOI=10.1128/MCB.24.17.7402-7418.2004;
Wicky S., Schwarz H., Singer-Krueger B.;
"Molecular interactions of yeast Neo1p, an essential member of the
Drs2 family of aminophospholipid translocases, and its role in
membrane trafficking within the endomembrane system.";
Mol. Cell. Biol. 24:7402-7418(2004).
[4]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-551, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis
of ATP coupled with the transport of phospholipids (Potential).
Leads to neomycin-resistance when overexpressed. Required for
traffic between late Golgi and early endosomes.
{ECO:0000269|PubMed:15314152, ECO:0000305}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(Side 1) = ADP +
phosphate + phospholipid(Side 2).
-!- SUBUNIT: Interacts with MON2. {ECO:0000269|PubMed:15314152}.
-!- INTERACTION:
Q03921:DOP1; NbExp=3; IntAct=EBI-3137, EBI-34442;
-!- SUBCELLULAR LOCATION: Endosome membrane
{ECO:0000269|PubMed:15314152}; Multi-pass membrane protein
{ECO:0000269|PubMed:15314152}. Golgi apparatus membrane
{ECO:0000269|PubMed:15314152}; Multi-pass membrane protein
{ECO:0000269|PubMed:15314152}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IV subfamily. {ECO:0000305}.
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EMBL; Z38060; CAA86174.1; -; Genomic_DNA.
EMBL; BK006942; DAA08499.1; -; Genomic_DNA.
PIR; S48431; S48431.
RefSeq; NP_012216.1; NM_001179398.1.
ProteinModelPortal; P40527; -.
BioGrid; 34942; 434.
DIP; DIP-2548N; -.
IntAct; P40527; 7.
MINT; P40527; -.
STRING; 4932.YIL048W; -.
TCDB; 3.A.3.8.18; the p-type atpase (p-atpase) superfamily.
iPTMnet; P40527; -.
MaxQB; P40527; -.
PaxDb; P40527; -.
PRIDE; P40527; -.
EnsemblFungi; YIL048W; YIL048W; YIL048W.
GeneID; 854763; -.
KEGG; sce:YIL048W; -.
EuPathDB; FungiDB:YIL048W; -.
SGD; S000001310; NEO1.
GeneTree; ENSGT00550000074723; -.
HOGENOM; HOG000201571; -.
InParanoid; P40527; -.
KO; K01530; -.
OMA; TQNEMEM; -.
OrthoDB; EOG092C0BQ4; -.
BioCyc; YEAST:G3O-31319-MONOMER; -.
Reactome; R-SCE-936837; Ion transport by P-type ATPases.
PRO; PR:P40527; -.
Proteomes; UP000002311; Chromosome IX.
GO; GO:0005768; C:endosome; IDA:SGD.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
GO; GO:0000139; C:Golgi membrane; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0015662; F:ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism; ISS:SGD.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004012; F:phospholipid-translocating ATPase activity; ISS:SGD.
GO; GO:0006897; P:endocytosis; IMP:SGD.
GO; GO:0045332; P:phospholipid translocation; IMP:SGD.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IMP:SGD.
GO; GO:0007033; P:vacuole organization; IMP:SGD.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006539; P-type_ATPase_IV.
InterPro; IPR032631; P-type_ATPase_N.
InterPro; IPR001757; P_typ_ATPase.
InterPro; IPR032630; P_typ_ATPase_c.
PANTHER; PTHR24092; PTHR24092; 1.
Pfam; PF16212; PhoLip_ATPase_C; 1.
Pfam; PF16209; PhoLip_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 1.
SUPFAM; SSF81653; SSF81653; 2.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 3.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Endosome; Golgi apparatus; Hydrolase;
Magnesium; Membrane; Nucleotide-binding; Phosphoprotein;
Protein transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 1151 Probable phospholipid-transporting ATPase
NEO1.
/FTId=PRO_0000046236.
TOPO_DOM 1 184 Extracellular. {ECO:0000255}.
TRANSMEM 185 205 Helical. {ECO:0000255}.
TOPO_DOM 206 209 Cytoplasmic. {ECO:0000255}.
TRANSMEM 210 230 Helical. {ECO:0000255}.
TOPO_DOM 231 367 Extracellular. {ECO:0000255}.
TRANSMEM 368 388 Helical. {ECO:0000255}.
TOPO_DOM 389 416 Cytoplasmic. {ECO:0000255}.
TRANSMEM 417 437 Helical. {ECO:0000255}.
TOPO_DOM 438 438 Extracellular. {ECO:0000255}.
TRANSMEM 439 459 Helical. {ECO:0000255}.
TOPO_DOM 460 947 Cytoplasmic. {ECO:0000255}.
TRANSMEM 948 968 Helical. {ECO:0000255}.
TOPO_DOM 969 970 Extracellular. {ECO:0000255}.
TRANSMEM 971 991 Helical. {ECO:0000255}.
TOPO_DOM 992 1020 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1021 1041 Helical. {ECO:0000255}.
TOPO_DOM 1042 1052 Extracellular. {ECO:0000255}.
TRANSMEM 1053 1073 Helical. {ECO:0000255}.
TOPO_DOM 1074 1078 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1079 1099 Helical. {ECO:0000255}.
TOPO_DOM 1100 1109 Extracellular. {ECO:0000255}.
TRANSMEM 1110 1130 Helical. {ECO:0000255}.
TOPO_DOM 1131 1151 Cytoplasmic. {ECO:0000255}.
REGION 1131 1151 Required for endosomal targeting.
ACT_SITE 503 503 4-aspartylphosphate intermediate.
{ECO:0000305}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 551 551 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
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


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