ID A0A8K1RC01_9CRUS Unreviewed; 1043 AA. AC A0A8K1RC01; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 24-JAN-2024, entry version 6. DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084}; OS Parasacculina yatsui. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Cirripedia; Rhizocephala; Polyascidae; Parasacculina. OX NCBI_TaxID=2836420 {ECO:0000313|EMBL:UEK51584.1}; RN [1] {ECO:0000313|EMBL:UEK51584.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Endoparasitic structure interna {ECO:0000313|EMBL:UEK51584.1}; RA Wong Y.H., Okano K.; RT "Barnacle with a root-like body: structural and transcriptomic signatures RT of the interna, endoparasitic structure of the parasitic barnacle Sacculina RT yatsui."; RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases. 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; MW292188; UEK51584.1; -; mRNA. 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}; 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 115..137 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 149..168 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 310..335 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 341..365 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 873..894 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 934..952 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 972..993 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT TRANSMEM 1005..1021 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362084" FT DOMAIN 61..135 FT /note="Cation-transporting P-type ATPase N-terminal" FT /evidence="ECO:0000259|SMART:SM00831" FT REGION 19..50 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 233..252 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1043 AA; 115146 MW; 554468F832F5962C CRC64; MVQNDGSYRA ATNPILADDN ITAHGQLKTK RKAGGNRKNK NKKKKSEEMK MDDLKQELEM DEHVIPIEDL VQRLGTSIQN GLTTAQAVEN VERYGPNALT PPKKTPEWVK FCKNLFYGFS MLLWVGAILC FIAYTIQSTT DDEVPDDNLY LGVVLTAVVL VTGCFSYYQE SKSSKIMESF KNMVPQYALA VRDGQKINLK AEELTIGDVV EIKFGDRIPA DVRVVEAHNM KVDNSSLTGE SEPQSRGPEY TSDNPLETKN LAFFSTSAVE GTCKGVVINI GDNTVMGRIA GLASGIDSGS TPIAREIEHF IHIITGVAVF LGVTFFIVAL CLGYYWLDAV IFLIGIIVAN VPEGLLATVT VCLTLTAKRM AAKNCLVKNL EAVETLGSTS TICSDKTGTL TQNRMTVAHM WFDNKIIEAD TTENQSGSGY DRDAPGWGAL SRVAALCSRA EFRSNQQELP ILKREVNGDA SEAALLKCCE LAMGDVMKYR AKYPKLSEIP FNSSNKYQVS IHDVSSDTPD TPHLLAMKGA PERILDRCST IYVDGQDRVL DEQMKQSFND AYLSLGGLGE RVLGFCDLAL PGDQFPRGFA FDSDDVNYPL DGLRFVGLMS MIDPPRAAVP DAVCKCRSAG IKVIMVTGDH PITAKAIAKS VGIISEGSET VEDIAARLDL PVEEVDSRDA HAAVVHGSEL RDISPEQLDD ILTHHREIVF ARTSPQQKLI IVEGCQRQNA IVAVTGDGVN DSPALKKADI GVAMGISGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSNIPEISPF LLFILLDIPL PLGTVTILCI DLGTDMVPAI SLAYEKAESD IMKRQPRDPL NDKLVNERLI SMAYGQIGMM QAAAGFFSYT VIMAENGFLP QDLLGLRKAW DSRAVNDLVD SYGQEWTYED RKKLEYTCHT AFFVAIVIVQ WADLIICKTR RNSIIHQGMN NWILNFGLLF ETALACTLSY TPGMDKGLRM YPLRFVWWLP PLPFSLLIFV YDEIRRYLLR RNPGGWLEHE TYY //