ID A0A0K3C9M6_RHOTO Unreviewed; 1001 AA.
AC A0A0K3C9M6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN Name=FGENESH: predicted gene_4.96 {ECO:0000313|EMBL:CTR06459.1};
GN ORFNames=AAT19DRAFT_13617 {ECO:0000313|EMBL:PRQ75560.1},
GN BN2166_0023200 {ECO:0000313|EMBL:CTR06459.1};
OS Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR06459.1, ECO:0000313|Proteomes:UP000199069};
RN [1] {ECO:0000313|EMBL:CTR06459.1, ECO:0000313|Proteomes:UP000199069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Single colony {ECO:0000313|EMBL:CTR06459.1};
RA Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PRQ75560.1, ECO:0000313|Proteomes:UP000239560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 0880 {ECO:0000313|EMBL:PRQ75560.1,
RC ECO:0000313|Proteomes:UP000239560};
RX PubMed=29521624;
RA Coradetti S.T., Pinel D., Geiselman G., Ito M., Mondo S., Reilly M.C.,
RA Cheng Y.F., Bauer S., Grigoriev I., Gladden J.M., Simmons B.A., Brem R.,
RA Arkin A.P., Skerker J.M.;
RT "Functional genomics of lipid metabolism in the oleaginous yeast
RT Rhodosporidium toruloides.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: The plasma membrane ATPase of plants and fungi is a hydrogen
CC ion pump. The proton gradient it generates drives the active transport
CC of nutrients by H(+)-symport. The resulting external acidification
CC and/or internal alkinization may mediate growth responses.
CC {ECO:0000256|ARBA:ARBA00003417}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1;
CC Evidence={ECO:0000256|RuleBase:RU362083};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362083};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU362083}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIA subfamily. {ECO:0000256|ARBA:ARBA00008804,
CC ECO:0000256|RuleBase:RU362083}.
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DR EMBL; CWKI01000004; CTR06459.1; -; Genomic_DNA.
DR EMBL; LCTV02000004; PRQ75560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K3C9M6; -.
DR STRING; 5286.A0A0K3C9M6; -.
DR OMA; VWTLLQC; -.
DR OrthoDB; 1058547at2759; -.
DR Proteomes; UP000199069; Unassembled WGS sequence.
DR Proteomes; UP000239560; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:UniProtKB-UniRule.
DR CDD; cd02076; P-type_ATPase_H; 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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR006534; P-type_ATPase_IIIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01647; ATPase-IIIA_H; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF21; PLASMA MEMBRANE ATPASE; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_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 PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362083};
KW Hydrogen ion transport {ECO:0000256|RuleBase:RU362083};
KW Ion transport {ECO:0000256|RuleBase:RU362083};
KW Magnesium {ECO:0000256|RuleBase:RU362083};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362083};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362083};
KW Reference proteome {ECO:0000313|Proteomes:UP000199069};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362083};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362083};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362083}; Transport {ECO:0000256|RuleBase:RU362083}.
FT TRANSMEM 132..159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 171..187
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 319..341
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 353..375
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 723..745
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 791..814
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 863..883
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 903..924
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT DOMAIN 88..160
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1001 AA; 109112 MW; 2B13197EAAA167E8 CRC64;
MSAPLHNNEH GAQPEVVEEK HAAPPAAAPA AAAPAPQQEG TAPAAPTEKK AGRFDKTFEE
EREVKHALVD MSTIELKAED LYDKDKVDLE QVEMEDVWTL LQCKEDGLTN AEAERRRGIF
GPNKLEHKET SVLLQFLSFM WNPLSWVMEG AALVAIALSN GEGRAPDWQD FVGIVLLLFI
NSTIGFYEER SAGNAVKALM ESLAPKAKCK RDGTWIEIES SDLVPGDVIS FKIGDIVPAD
CRLYDAINVS IDQAGLTGES LPQGKKVGDQ CFSSSICKQG EAEGVVIATG ANTFFGRAAS
LVGADDDSTG HLQQILAQIG LFCLVSIGIF ILLEILILYP RFHYSYRRGL DNILVLLIGG
IPIAMPTVLS VTLAVGAQQL AKYKAIVTRI TAIEELAGVT ILCSDKTGTL TTNKLTIDKS
TLKTYSSFNA DEVILYAAYA SRTENMDAID TCVTGALPSV ADARAGIKLL DFKPFNPVDK
RTEITYTVDA TGEMKRATKG MTGIIIELCS RNKTAEVEDQ LEKDVEEYAA RGLRALAVAV
EDVPSGNKDE PGNGFELIGL LAIFDPPRDD TKQTIDEAIA LGVRVKMVTG DQLAIAKETG
RRLGLGDHMY PAKVLQTGGF PEGGKHMNLD EMILDADGFA GVFPEHKYEI VKRLQGLGHL
CAMTGDGAND APALSRANVG IAVEGATDAA RGAADIVLTE PGLSTIVHAI RQSRVIFQRM
RNYSIYACAV TIRIVVGFAV MAFAFQFDFP PFMVLIIALL NDGTIMTLSL DRVLPSTTPD
SWDLGEIFTY AFAYGLYLAA GTIAFYCVII YTTFFTRKFG VNDITDHNDP DVHMIIYLQV
AQISQALIFV TRSHSFFFME RPSVALFLAF CLAQLISSII AAYGDWGFTN VRGVSGGWIG
ITWIWNIIWF FPLDFVKFGV RAGVRAWNRR RGKTPQAIKP VEGVPMTRTQ SRHESLYSNR
TSFLRRAQRS VGLGRKVHVS NADLQRFGSH QASASGAALR A
//
