ID R4ZHW8_DANPL Unreviewed; 788 AA. AC R4ZHW8; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 14-DEC-2022, entry version 46. DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084}; DE Flags: Fragment; GN Name=K+ ATPase alpha subunit {ECO:0000313|EMBL:CCW28388.1}; GN Synonyms=Na+ {ECO:0000313|EMBL:CCW28388.1}; OS Danaus plexippus (Monarch butterfly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea; OC Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus. OX NCBI_TaxID=13037 {ECO:0000313|EMBL:CCW28388.1}; RN [1] {ECO:0000313|EMBL:CCW28388.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Central nervous system {ECO:0000313|EMBL:CCW28388.1}; RX PubMed=24033181; DOI=10.1111/evo.12152; RA Petschenka G., Fandrich S., Sander N., Wagschal V., Boppre M., Dobler S.; RT "Stepwise evolution of resistance to toxic cardenolides via genetic RT substitutions in the na(+) /k(+) -ATPase of milkweed butterflies RT (lepidoptera: danaini)."; RL Evolution 67:2753-2761(2013). 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|RuleBase:RU362084}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|RuleBase:RU362084}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HF945454; CCW28388.1; -; mRNA. DR AlphaFoldDB; R4ZHW8; -. DR EnsemblMetazoa; XM_032665106.1; XP_032520997.1; LOC116772833. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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:0008556; F:P-type potassium transmembrane transporter activity; IEA:InterPro. DR Gene3D; 3.40.1110.10; -; 1. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C. 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 Pfam; PF00689; Cation_ATPase_C; 1. DR SFLD; SFLDF00027; p-type_atpase; 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 TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1. DR TIGRFAMs; TIGR01494; ATPase_P-type; 2. DR PROSITE; PS00154; ATPASE_E1_E2; 1. PE 2: Evidence at transcript level; KW ATP-binding {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|RuleBase:RU362084}; KW Potassium {ECO:0000256|RuleBase:RU362084}; KW Potassium transport {ECO:0000256|RuleBase:RU362084}; KW Signal {ECO:0000256|SAM:SignalP}; 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 SIGNAL 1..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..788 FT /note="Sodium/potassium-transporting ATPase subunit alpha" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004384461" FT TRANSMEM 28..48 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 190..214 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 220..243 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 752..771 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT DOMAIN 698..775 FT /note="Cation_ATPase_C" FT /evidence="ECO:0000259|Pfam:PF00689" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:CCW28388.1" FT NON_TER 788 FT /evidence="ECO:0000313|EMBL:CCW28388.1" SQ SEQUENCE 788 AA; 85492 MW; 0A13E6B829FA4511 CRC64; LLLWIGAILC FIAYGIVAST VEEPSDDHLY LGIVLAAVVI VTGIFSYYQE SKSSKIMESF KNMVPQFATV IREGEKLTLR AEDLVLGDVV EVKFGDRIPA DIRIIEARGF KVDNSSLTGE SEPQSRGPEF TNENPLETKN LAFFSTNAVE GTAKGIVICC GDNTVMGRIA GLASGLDTGE TPIAKEIHHF IHLITGVAVF LGVTFFIIAF ILGYHWLDAV IFLIGIIVAN VPEGLLATVT VCLTLTAKRM ASKNCLVKNL EAVETLGSTS TICSDKTGTL TQNRMTVAHM WFDNQIIEAD TTEDQSGVQY DRTSPGFKAL AKIASLCNRA EFKGGQDGVP ILKKEVAGDA SEAALLKCME LALGDVLSIR KRNKKVCEIP FNSTNKYQVS IHESDDPSDP RHLLVMKGAP ERILERCSTI FIGGKEKVLD EEMKEAFNNA YLELGGLGER VLGFCDLQLP SDKYPIGYKF NTDDPNFPLD NLRFVGLMSM IDPPRAAVPD AVAKCRSAGI KVIMVTGDHP ITAKAIAKSV GIISEGNETV EDIAARLNIP VSEVNPREAK AAVVHGTELR DLNSDQLDEI LKFHTEIVFA RTSPQQKLII VEGCQRLGAI VAVTGDGVND SPALKKADIG VAMGIAGSDV SKQAADMILL DDNFASIVTG VEEGRLIFDN LKKSIAYTLT SNIPEISPFL AFILCDIPLP LGTVTILCID LGTDMVPAIA LAYEEAEADI MKRPPRNPFN DKLVNERLIS MAYGQIGMIQ AAAGFFVYFV IMAENGFLPT KLFGIRKQ //