ID K0GEY1_9HEMI Unreviewed; 1008 AA. AC K0GEY1; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 27-MAR-2024, entry version 52. DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084}; OS Lygaeus kalmii. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera; OC Pentatomomorpha; Lygaeoidea; Lygaeidae; Lygaeinae; Lygaeus. OX NCBI_TaxID=683892 {ECO:0000313|EMBL:AFU25682.1}; RN [1] {ECO:0000313|EMBL:AFU25682.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=23019645; DOI=10.1126/science.1226630; RA Zhen Y., Aardema M.L., Medina E.M., Schumer M., Andolfatto P.; RT "Parallel molecular evolution in an herbivore community."; RL Science 337:1634-1637(2012). CC -!- FUNCTION: This is the catalytic component of the active enzyme, which CC catalyzes the hydrolysis of ATP coupled with the exchange of sodium and CC potassium ions across the plasma membrane. This action creates the CC electrochemical gradient of sodium and potassium ions, providing the CC energy for active transport of various nutrients. CC {ECO:0000256|ARBA:ARBA00037422}. CC -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a CC catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an CC additional regulatory subunit. {ECO:0000256|ARBA:ARBA00038795}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362084}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}. 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 IIC subfamily. {ECO:0000256|ARBA:ARBA00006934, CC 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; JQ771513; AFU25682.1; -; mRNA. DR AlphaFoldDB; K0GEY1; -. 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 CDD; cd02608; P-type_ATPase_Na-K_like; 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; 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; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1. DR PANTHER; PTHR43294:SF13; 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; PF00702; Hydrolase; 1. DR PRINTS; PR00119; CATATPASE. DR PRINTS; PR00121; NAKATPASE. 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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1. DR PROSITE; PS00154; ATPASE_E1_E2; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362084}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, KW 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}; KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|RuleBase:RU362084}; KW Potassium transport {ECO:0000256|ARBA:ARBA00022538, KW ECO:0000256|RuleBase:RU362084}; 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 81..102 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 114..134 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 276..302 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 308..331 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 837..857 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 898..917 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 937..955 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 970..986 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT DOMAIN 27..101 FT /note="Cation-transporting P-type ATPase N-terminal" FT /evidence="ECO:0000259|SMART:SM00831" SQ SEQUENCE 1008 AA; 111756 MW; E132A9BB5719E10F CRC64; MSANNKPLVK KHKKGDLNEL KQELDIDFHK ISLEELYRRF ETNPETGLSH EKAKEILARD GPNALTPPKT TPEWIKFCKQ LFGGFALLLW VGAILCFVAY FITSTTVEEA SDNHMYLGLV LAGVVIITGV FSYYQENKSS RIMESFKNMV PQFACVIRQS EKITIRAEAI VLGDVVEVKF GDRIPADIRI IESRGFKVDN SSLTGESEPQ SRGIEMTNDN PLETKNLAFF STNAVEGTAK GIVISCGDHT VMGRIAGLAS GLDTGSTPIA KEIEHFIHII TGVAIFLGVS FFIIAFAMGY FWLDAVVFLI GIIVANVPEG LLATVTVCLT LTAKRMAAKN CLVKNLEAVE TLGSTSTICS DKTGTLTQNR MTVAHMWFDN QIIEADTTED QSGVQYDKTS PGFKALSRIA TLCNRAEFKP GQDGIPILRK EVNGDASEAA LVKCMELALG DIMSIRKRNK KVCEIPFNST NKYQVSIHET EDPNDSRYLM VMKGAPERIL ERCSTIFIGG EEKLLNEELK EAFNDAYLEL GGLGERVLGF CDFMLPPDKF PVGFNFNSEE PNFPLTGMRF VGLISMIDPP RAAVPDAVAK CRSAGIKVIM VTGDHPITAK AIAKSVGIIS EGNETVEDIA HRLNIPISEV NPRDAKAAVV HGTELRDITP EQLDEILRYH TEIVFARTSP QQKLIIVEGC QRMGAIVAVT GDGVNDSPAL KKADIGIAMG ISGSDVSKQA ADMILLDDNF ASIVTGVEEG RLIFDNLKKS IAYTLSSNIP EISPFLANVV LNIPLPLGAV TILCIDLGTD MVPAISLAYE EAESDIMKRQ PRNPFTDKLV NERLISLSYG QIGVIQAAAG FFVYFVIMAE NGFWPMSLFG LRKEWDSKAV NDLQDSYGQE WTYKERKALE YTCHTAFFIT IVIVQWADLI ISKTRRNSII HQGMRNWALN FGLVFETVLA AFLSYCPGMD KGLQMYPLKF VWWLPGLPFM IVIFIYDEVR KYYLRRNPGG WVERETYY //