ID K0GEY1_9HEMI Unreviewed; 1008 AA. AC K0GEY1; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 12-AUG-2020, entry version 42. 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 -!- SUBCELLULAR LOCATION: Membrane {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 --------------------------------------------------------------------------- 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 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008556; F:potassium transmembrane transporter activity, phosphorylative mechanism; IEA:InterPro. DR CDD; cd02608; P-type_ATPase_Na-K_like; 1. 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; 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 Pfam; PF00689; Cation_ATPase_C; 1. DR Pfam; PF00690; Cation_ATPase_N; 1. DR SMART; SM00831; Cation_ATPase_N; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR SUPFAM; SSF81653; SSF81653; 1. DR SUPFAM; SSF81660; SSF81660; 1. DR SUPFAM; SSF81665; SSF81665; 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|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 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_ATPase_N" 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 //