ID A0A1Z5KLX1_FISSO Unreviewed; 1021 AA.
AC A0A1Z5KLX1;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN ORFNames=FisN_13Lh282 {ECO:0000313|EMBL:GAX27167.1};
OS Fistulifera solaris (Oleaginous diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Naviculaceae;
OC Fistulifera.
OX NCBI_TaxID=1519565 {ECO:0000313|EMBL:GAX27167.1, ECO:0000313|Proteomes:UP000198406};
RN [1] {ECO:0000313|EMBL:GAX27167.1, ECO:0000313|Proteomes:UP000198406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX27167.1,
RC ECO:0000313|Proteomes:UP000198406};
RX PubMed=25634988; DOI=10.1105/tpc.114.135194;
RA Tanaka T., Maeda Y., Veluchamy A., Tanaka M., Abida H., Marechal E.,
RA Bowler C., Muto M., Sunaga Y., Tanaka M., Yoshino T., Taniguchi T.,
RA Fukuda Y., Nemoto M., Matsumoto M., Wong P.S., Aburatani S., Fujibuchi W.;
RT "Oil accumulation by the oleaginous diatom Fistulifera solaris as revealed
RT by the genome and transcriptome.";
RL Plant Cell 27:162-176(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAX27167.1}.
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DR EMBL; BDSP01000253; GAX27167.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5KLX1; -.
DR InParanoid; A0A1Z5KLX1; -.
DR OrthoDB; 46741at2759; -.
DR Proteomes; UP000198406; 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:SF48; 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; SFLDG00002; C1.7:_P-type_atpase_like; 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 Hydrolase {ECO:0000313|EMBL:GAX27167.1};
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:UP000198406};
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 186..205
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 356..381
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 393..416
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 760..781
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 801..822
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 834..861
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 881..901
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 913..936
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 956..974
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT DOMAIN 143..211
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 123..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1021 AA; 112430 MW; EA6A4CB34C183F33 CRC64;
MASSEHPTEV DDLEAKDTFV AELPTTFPVS HPLRSRVKAQ SDLTGMDLEA KAFGLTRQKS
RINYRSVSDI SAMVHLAPEV VQTMEKRRRQ RSSSDVLAKF GQVPLSGGDD LRLAEQIQTY
GTRKERRQAG ISDEEIQSKI EQNEGVQPPD DFQFNHEGFS SDKAAELLKV HGPNELPEKI
TPKWLIFLRL FWAPMPIMIW LAIIIEAGIG NYLDMGILLI IQFANASISF YETNKAGNAI
AALKNSLKPT ATCKRDGAWK NIDARELVPG DLVLLGSGSA IPADCRVNEG EIDVDQAALT
GESLPVTFYK GDSCKMGSTV VRGEVEGTVE FTGANTFFGK TAALLKQTNE HSYLQVVLML
VMFTLVGLSI ALCLICFIYL MAKGQTLKES LSFTVVVLVA SIPLAIEIVT TTTLAIGSKS
LAKQGAIVAQ LSSIERMASM SILCSDKTGT LTLNQMVIQD ETPTYVPNET QESVLVSAAL
AAKWKEPPRD ALDRLVLGTV NMSLMDAYEQ LDYMPFDPQV KRTEGTIRHK ESNKEFKTSK
GAPHIILKLL GDEDDDVKDK VEADVARLGA IGVRSLAVAR TDEDGKWKML GLLTFLDPPR
ADTKQVIQDA NRYGVGVKMI TGDHLLIARN TAAQLDLGTH IFTSEYLPLL DAETKEKPEN
LAANYGDLCL AADGFAQVYP EHKYLIVECL RELGYAVGMT GDGVNDAPAL KRADVGIAVA
DSTDAARAAA DIVLTEPGLS AVSHGIVEAR KIFQRVNNFL TYRIAATLQL LVFFFISILA
FHPNEYSHPE TEEEWPKFFQ IPVILIMLIT LLNDGTLITI AYDHAEARAT PCIWNLPALF
VTSTTLGVVS CFSSLLLLHI LLDSWNEDGF FQKIGFQGVE YGQMILAMYL KISVSDFLTL
FSARTGTRFF YEVAPGPMLL AGGAFALFIS SLLSIVWKEG EIEEIPVNGL VNDMELFGFV
WIYSLLFFFL QDILKVGVFK WMYWQNFHNI ASTGVVVLPK SAEQLIKDME AALGESGNKH
H
//
