ATC8_YEAST
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 03-AUG-2022, entry version 191.
DE RecName: Full=Probable phospholipid-transporting ATPase DNF3;
DE EC=7.6.2.1;
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 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 [4]
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 [5]
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 [6]
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 [7]
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).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of phospholipids (Probable). Forms a
CC heteromeric phospholipid translocase (PLT) DNF3-CRF1, implicated in the
CC translocation of phospholipids from the outer to the inner leaflet of
CC membrane bilayers. Shares an essential function for cell growth with
CC PLTs DRS2-CDC50 and DNF1/2-LEM3. May be involved in transport from
CC early endosomes to the trans-Golgi network (TGN) (Probable).
CC {ECO:0000305, ECO:0000305|PubMed:17093059}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC -!- SUBUNIT: Interacts with YNR048W/CRF1; interaction is required for
CC proper expression and endoplasmic reticulum (ER) export of either
CC partner. {ECO:0000269|PubMed:17093059, ECO:0000269|PubMed:19411703}.
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:17093059}; Multi-pass membrane protein
CC {ECO:0000255}.
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; 69.
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; Q12674; -.
DR PRIDE; Q12674; -.
DR EnsemblFungi; YMR162C_mRNA; YMR162C; YMR162C.
DR GeneID; 855197; -.
DR KEGG; sce:YMR162C; -.
DR SGD; S000004772; DNF3.
DR VEuPathDB; FungiDB:YMR162C; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; Q12674; -.
DR OMA; FIIMFNT; -.
DR BioCyc; YEAST:G3O-32852-MON; -.
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 PRO; PR:Q12674; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q12674; protein.
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; 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:0090555; F:phosphatidylethanolamine flippase activity; IMP:SGD.
DR GO; GO:0140346; F:phosphatidylserine flippase activity; IGI:SGD.
DR GO; GO:0045332; P:phospholipid translocation; IMP:SGD.
DR GO; GO:0000749; P:response to pheromone triggering conjugation with cellular fusion; IGI:SGD.
DR Gene3D; 3.40.1110.10; -; 2.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 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; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Golgi apparatus; Magnesium; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix.
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 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
