ID T1ELT9_HELRO Unreviewed; 1011 AA.
AC T1ELT9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
GN Name=20197539 {ECO:0000313|EnsemblMetazoa:HelroP156333};
GN ORFNames=HELRODRAFT_156333 {ECO:0000313|EMBL:ESO10963.1};
OS Helobdella robusta (Californian leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP156333, ECO:0000313|Proteomes:UP000015101};
RN [1] {ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESO10963.1, ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:HelroP156333}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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}.
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DR EMBL; AMQM01002786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB095858; ESO10963.1; -; Genomic_DNA.
DR RefSeq; XP_009011232.1; XM_009012984.1.
DR AlphaFoldDB; T1ELT9; -.
DR STRING; 6412.T1ELT9; -.
DR EnsemblMetazoa; HelroT156333; HelroP156333; HelroG156333.
DR GeneID; 20197539; -.
DR KEGG; hro:HELRODRAFT_156333; -.
DR CTD; 20197539; -.
DR eggNOG; KOG0203; Eukaryota.
DR HOGENOM; CLU_002360_4_1_1; -.
DR InParanoid; T1ELT9; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000015101; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0005391; F:P-type sodium:potassium-exchanging transporter activity; IBA:GO_Central.
DR GO; GO:0030007; P:intracellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006883; P:intracellular sodium ion homeostasis; IBA:GO_Central.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000015101};
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 103..125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 137..156
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 298..322
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 328..351
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 837..860
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 901..920
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 940..958
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 973..989
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT DOMAIN 49..123
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1011 AA; 113304 MW; 4B752C4E4835C45A CRC64;
MREREREREE ERREVDEKER EGKKKGKRKR KKNKDESDLE QLKREVEMSD HKLSLAELAS
KYQTDLQRGL RIEQYKEILS RDGPNQLTPP KTVPEWIKFC KQLFGGFSML LWIGAVLCFV
AYGIVVSSVE SPPGDHLYLG IVLTGVVIVT GIFSYYQEAK SSKIMESFKN MVPQFALVIR
EGEKLNVRAE DLVIGDLVEI KSGDRVPADV RIISCSGFKV DNSSLTGESE PQSRVVECTH
DAPLEAKNLA FFSTNAVEGT ARGIVVNTGD RTVIGRIANL ASGIEMSETP IAKEIAHFIH
LITGVAVFLG VVFFIIAFIL GYNWLDAVIF LIGIIVANVP EGLLATVTVC LTLTAKRMAK
KNCLVKHLEA VETLGSTSTI CSDKTGTLTQ NRMTVSHMWL DDTFFQIDLT KSNDALRSPK
LSRSWNEYSR VGMLCSRAEF KRGQENIEVM KRECIGDASE SAILKIMELG GTNVEEYRQR
LRKVCEVPFN SVNKYQLSIH ELENENDFSS HILVMKGAPE KIFEKCNRIL MHGTGLELNK
YWKRRFDMHC LRLGNIGDRV LGFCDLELPK DSYPRGFEFN ADDINFPVTG LRFLGLISMV
DPPRANVPDA VRKCRSAGIK VIMVTGDHPT TAMAIAKNVG IITEGEATKA CVVHGSQLKE
MDQDEVDDIL SEHDEIVFAR TSPQQKLVIV EGCQRLGAIV AVTGDGVNDS PALKKADIGV
AMGISGSDVS KQAADMILLD DNFASIVTGV EEGRLIFDNL KKSIAYTLTS NIPEISPFLF
YITANIPLPL GTITILCIDL GTDMVPAISL AYEKAESDIM DRKPRDPLKD KLVNNRLISM
AYGQIGMIQA CAGFYVYFVI MAENGFTPLR LLGLRVEWDS PSVNDLLDSY GQEWTYGQRK
VLEYTCHTAF FASIVIVQWA DLIICKTRMN SVIHQGMTNY RLVFGLFFET TLAIFLAYCP
GLDKGLRMYP LKWTWWFAPL PFSVVILLYD EIRKAIMRGQ SEGWLKDETY Y
//
