ID Q9SXK5_HETAK Unreviewed; 1330 AA. AC Q9SXK5; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2001, sequence version 2. DT 27-MAR-2024, entry version 121. DE SubName: Full=Na-ATPase {ECO:0000313|EMBL:BAA82752.2}; GN Name=HANA {ECO:0000313|EMBL:BAA82752.2}; OS Heterosigma akashiwo (Chromophytic alga) (Heterosigma carterae). OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Raphidophyceae; Chattonellales; OC Chattonellaceae; Heterosigma. OX NCBI_TaxID=2829 {ECO:0000313|EMBL:BAA82752.2}; RN [1] {ECO:0000313|EMBL:BAA82752.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=OHE-1 {ECO:0000313|EMBL:BAA82752.2}; RX PubMed=11248217; DOI=10.1016/S0005-2736(01)00266-8; RA Shono M., Wada M., Hara Y., Fujii T.; RT "Molecular cloning of Na(+)-ATPase cDNA from a marine alga, Heterosigma RT akashiwo."; RL Biochim. Biophys. Acta 1511:193-199(2001). CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) CC family. Type IIC subfamily. {ECO:0000256|ARBA:ARBA00006934}. 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; AB017481; BAA82752.2; -; mRNA. DR TCDB; 3.A.3.1.3; the p-type atpase (p-atpase) superfamily. DR GO; GO:0016020; C: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:0008556; F:P-type potassium transmembrane transporter activity; IEA:InterPro. 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; 2. 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:SF22; P-TYPE ATPASE; 1. DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1. DR Pfam; PF13246; Cation_ATPase; 1. DR Pfam; PF00689; Cation_ATPase_C; 2. 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; 2. 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}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 82..101 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 107..127 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 270..294 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 300..325 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 893..914 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1251..1272 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 27..100 FT /note="Cation-transporting P-type ATPase N-terminal" FT /evidence="ECO:0000259|SMART:SM00831" SQ SEQUENCE 1330 AA; 146517 MW; EDFB870FC0949751 CRC64; MGLMKKKAGG DSNSRRVDDL KKNVVMTEHK EEWEELFAKL GSSVEGLSQE EAQKRNREFG DDRLTPPPTT PKWVKFLKEM TGFFSLLLWG GGILCFIRYG LRKEVDNMYL GIVLFAVVFV TGCFSFFQNS KSENLMKSFE KLLPPSINAK RNGEFIKVPS EKLVKGDVIR LEGGELVPCD VRIITCTDNC VVDNASLTGE AEPQKRKNEA THDEPLETAN LAFFGTNVPE GSLEGVVVNI GDDTVMGRIA SLTLQVGAQQ TPINKEIHHF ILIISSIAIF LGVTFFIIGL ALGTELIENL VFLISIIVAN VPEGLLATVT VCLTLTARRM HSKMVLVKNL EGVETLGSTS CICSDKTGTL TQNIMTVAQI VYGNQDAVHI QDTGSSLSHG LKTYNPENAA FQSLLRCAML NNTSTFGKYR LDENGDPTDE LLPFKAEVVQ GDGSVIEQVM WRVNGNASEA AMIKFAQNHE DVDDFRKRNP MVFQIPFNSR NKYQVHVHCQ EKFNQEDGTN SGPRVVLMKG APERVLARCS QAKLGGNIVP MTPELMAEIE RLQVQMSANG LRVLGFAERE LPKTKFPADY KYHDGSEEDK STPNFPLGEF AMEAEREKNP PKLPVHDASM QGLIFIGLMA LIDPPRPAVP GAVEKCKTAG VKVIMVTGDH PVTAQAIAQK VGILWSKTRA EAMAHNEAYQ LNPGDAGFED PEECKAIVVP GWELNNDMTE EAWDAILDNP QVVFARTSPQ QKLVIVSENQ KRGHIVAVTG DGVNDSPALK QADIGVAMGI SGSEVSKQAA DMILLDDNFA SIVAGVEEGR LIFDNLKKSI CYTLTSNIPE ISPFLCFIVI GTPLPLSTVL ILGIDLGTDM VPAISMAYEQ AEADIMKRPP RDSQLDRLVT KKLIVFAYLQ IGMIQAAAGF YTWMVVLNDY GFPPHILPGL GRGGFWQQHP LYCKFDGGQY VSLDGEASSD LDPSSDAPTR AYPFWDVGDH GNIVNCEFPI KNLRGGSGVP SGFDISEADT YDDSSTSGFN QMTYESLLAL EAQNYFHYVP WRARQSPFWK NSWFFWDVED EETPGGAFGG AADITYFLHQ KAGLWSLCAK DEDLSEGTGN SDFLGTQAAW DLYENDFDFT GVGACSVNSA TMKNQMYKDA YFCNNYPHSS GYASGAKPGC EAGANTHPLN NVWCADSCSQ ACYEAGGDGG DAYNCANVAS RMAQKEALHH AQGSYFVSIV IVQWADLLIC KTRWLSLRQQ GMKNSTMNFA LFFETLLAGW LCYCLPINVG LGTRNLRFTH WFPAIPFSVA IFVYDEVRKY LMRTTSPETT DKATGQVTRI AGWLETNTYY //