ID K0GEX4_DANGI Unreviewed; 1009 AA. AC K0GEX4; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 27-MAR-2024, entry version 51. DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084}; OS Danaus gilippus (Queen butterfly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea; OC Nymphalidae; Danainae; Danaini; Danaina; Danaus; Anosia. OX NCBI_TaxID=166024 {ECO:0000313|EMBL:AFU25675.1}; RN [1] {ECO:0000313|EMBL:AFU25675.1} 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; JQ771506; AFU25675.1; -; mRNA. DR AlphaFoldDB; K0GEX4; -. 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; 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 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 82..104 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 116..135 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 277..301 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 307..330 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 839..858 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 899..918 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 938..959 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 971..987 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT DOMAIN 28..102 FT /note="Cation-transporting P-type ATPase N-terminal" FT /evidence="ECO:0000259|SMART:SM00831" SQ SEQUENCE 1009 AA; 111478 MW; D3139775160849A5 CRC64; MGETRRKPPA KKRKAGDLDD LKQELDIDYH KVTPEELYQR FQTHPENGLS HAKAKENLER DGPNALTPPK QTPEWVKFCK NLFGGFALLL WIGAILCFIA YGIVASTVEE PSDDNLYLGI VLAAVVIVTG IFSYYQESKS SKIMESFKNM VPQFATVIRE GEKLTLRAED LVLGDVVEVK FGDRIPADIR IIEARGFKVD NSSLTGESEP QSRGPEFTNE NPLETKNLAF FSTNAVEGTA KGIVICCGDN TVMGRIAGLA SGLDTGETPI AKEIHHFIHL ITGVAVFLGV TFFIIAFILG YHWLDAVIFL IGIIVANVPE GLLATVTVCL TLTAKRMASK NCLVKNLEAV ETLGSTSTIC SDKTGTLTQN RMTVAHMWFD NQIIEADTTE DQSGVQYDRT SPGFKALAKI ASLCNRAEFK GGQDGVPILK KEVAGDASEA ALLKCMELAL GDVLSIRKRN KKVCEIPFNS TNKYQVSVHE SDDPSDPRHL LVMKGAPERI LERCSTIFIG GKEKVLDEEM KEAFNNAYLE LGGLGERVLG FCDLQLPSDK YPIGYKFNTD DPNFPLDNLR FVGLMSMIDP PRAAVPDAVA KCRSAGIKVI MVTGDHPITA KAIAKSVGII SEGNETVEDI AARLNIPVSE VNPREAKAAV VHGTELRDLN SDQLDEILKF HTEIVFARTS PQQKLIIVEG CQRLGAIVAV TGDGVNDSPA LKKADIGVAM GIAGSDVSKQ AADMILLDDN FASIVTGVEE GRLIFDNLKK SIAYTLTSNI PEISPFLAFI LCDIPLPLGT VTILCIDLGT DMVPAISLAY EEAESDIMKR QPRNPFTDKL VNERLISMAY GQIGMIQAAA GFFVYFVIMA ENGFLPTKLF GIRKQWDSKA INDLPDSYGQ EWTYRDRKAL EFTCHTAFFV SIVVVQWADL IICKTRRNSI VHQGMRNWAL NFGLVFETAL AAFLSYTPGM DKGLRMYPLK FVWWLPAIPF MLSIFIYDEI RRFYLRRNPG GWLEQETYY //