ID F1A2S2_DICPU Unreviewed; 984 AA.
AC F1A2S2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
GN ORFNames=DICPUDRAFT_42780 {ECO:0000313|EMBL:EGC29505.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC29505.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362084};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000256|ARBA:ARBA00006934,
CC ECO:0000256|RuleBase:RU362084}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362084}.
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DR EMBL; GL871423; EGC29505.1; -; Genomic_DNA.
DR RefSeq; XP_003293965.1; XM_003293917.1.
DR AlphaFoldDB; F1A2S2; -.
DR STRING; 5786.F1A2S2; -.
DR EnsemblProtists; EGC29505; EGC29505; DICPUDRAFT_42780.
DR GeneID; 10505281; -.
DR KEGG; dpp:DICPUDRAFT_42780; -.
DR eggNOG; KOG0203; Eukaryota.
DR InParanoid; F1A2S2; -.
DR OMA; NGQEYSM; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IBA:GO_Central.
DR GO; GO:0030007; P:intracellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006883; P:intracellular sodium ion homeostasis; IBA:GO_Central.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
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; IPR006068; ATPase_P-typ_cation-transptr_C.
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; IPR005775; P-type_ATPase_IIC.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01106; ATPase-IIC_X-K; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43294:SF4; CATION TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF08282; Hydrolase_3; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362084};
KW Ion transport {ECO:0000256|RuleBase:RU362084};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362084};
KW Metal-binding {ECO:0000256|RuleBase:RU362084};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362084}; Potassium {ECO:0000256|RuleBase:RU362084};
KW Potassium transport {ECO:0000256|RuleBase:RU362084};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362084};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362084}; Transport {ECO:0000256|RuleBase:RU362084}.
FT TRANSMEM 71..89
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 915..937
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 949..966
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT DOMAIN 7..88
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGC29505.1"
SQ SEQUENCE 984 AA; 108438 MW; 4F33A5F6AB2D6019 CRC64;
AAEYDVNEHE LTLEQLSDKF TTDINFSDPS QSGGLTSSLA SELLSRYGKN VLKPPKEIPW
YVQLAKCFTN FFMILLEVAG ALCFLAYGLD RSIRVNLYLA CVLYAIVIFT CLLTFSQERQ
TGNIMKSFKN LLPQSCRVIR DGSETKIKVE DIVIGDIVVV SAGDKVPGDI RIITCNGMKV
DNSSLTGESE AQSCTVTCTD DNPLESHNLA FYGTLVMDGS ARGVVIRTGT NTLIGKIADM
ASNTEQTETT LQIETKRFVH FITVLGITMG LLFFIIGFCV GIKPIPNLIN VLGLIVANVP
EGLPSTITAC LTVTARRLSK RNVYSKKLES IETLGSITLI ASDKTGTLTQ NRMTVSHMWY
DNTIFRAIEN GGTIDRTLFD LGTPTCSNLI RVGACCNRAD FDRLLEGNME RPIENRLILG
DASESALVRL CHKIEDIEIT RAKNSKVFEI PFNSTNKWQL SIHKLENDNS SSRILYMKGA
PEIIFEKCSK IMQNGKEIPI DEKINADFIT AYEALGSMGE RCLGFAQLLL TDENTVPNDL
YDAQILNFPM TGLTFVGLCS LLDPPRENVP FAVHQCKTAG IKVIMVTGDH PITAKAIAKK
VGIISSPTVE DIAQERGVPV SEVDDSEAGA IVLHGAQLRE FTEADWDRVL SKGEIVFART
SPQQKSQIVE NAQRRKEVVA VTGDGVNDSP ALKKADIGVA MGVVGSDVAK ETADIILLDD
NFASIVAGIE EGRIIFDNLK KSIAYTLSHA IPEIAPFLLN IVSGIPLAIT SFLILCIDLG
TEMAPAISLA YEKGEKDIMT RKPRVLGKDH LVTTNLLSYS YLQAGPIEAI VSFLNFFLVM
AAEGFPPHIL PGTTQDYFIE TALPLNGKNA HQQITALRKA QTAYFMTLVM CQFFNLITNK
TRVVPLWRHG MMNMYVNIGL IIEAGICCFV IYTPFIHTII ESEVFPGKFW AYPLPMVFCL
FAWNEIRKRI AFDHSFKISS SLAF
//