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Database: UniProt
Entry: Q23D88_TETTS
LinkDB: Q23D88_TETTS
Original site: Q23D88_TETTS 
ID   Q23D88_TETTS            Unreviewed;      1202 AA.
AC   Q23D88;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 2.
DT   24-JAN-2024, entry version 104.
DE   RecName: Full=Na(+)/K(+)-exchanging ATPase {ECO:0000256|ARBA:ARBA00039096};
DE            EC=7.2.2.13 {ECO:0000256|ARBA:ARBA00039096};
GN   ORFNames=TTHERM_00049030 {ECO:0000313|EMBL:EAR94535.2};
OS   Tetrahymena thermophila (strain SB210).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR94535.2, ECO:0000313|Proteomes:UP000009168};
RN   [1] {ECO:0000313|Proteomes:UP000009168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX   PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA   Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA   Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA   Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA   Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA   Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA   Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA   Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA   Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA   Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA   Hamilton E.P., Orias E.;
RT   "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT   model eukaryote.";
RL   PLoS Biol. 4:1620-1642(2006).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {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}.
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DR   EMBL; GG662712; EAR94535.2; -; Genomic_DNA.
DR   RefSeq; XP_001014798.2; XM_001014798.2.
DR   AlphaFoldDB; Q23D88; -.
DR   STRING; 312017.Q23D88; -.
DR   EnsemblProtists; EAR94535; EAR94535; TTHERM_00049030.
DR   GeneID; 7839775; -.
DR   KEGG; tet:TTHERM_00049030; -.
DR   eggNOG; KOG0203; Eukaryota.
DR   HOGENOM; CLU_002360_4_1_1; -.
DR   InParanoid; Q23D88; -.
DR   OrthoDB; 276509at2759; -.
DR   Proteomes; UP000009168; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009168};
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        174..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        198..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        361..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        392..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        869..892
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        898..917
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        937..962
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1097..1118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1130..1150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1165..1182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          116..190
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          44..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1202 AA;  135686 MW;  72212D6A979C151E CRC64;
     MLGANYKKTH HQEYTEPIPE SARGSVIRTF EELRQSLQLN NAVTEHRQSQ MSNRQSSMNR
     DRNMNAGDNG IRQSINQSRK YQEPNSQYKA TVPEPTNENN EKEHKNQTKE ALGMMDDHKI
     PLEELRERYQ TDYQKGLSST KATQLNEQFG DNKLSEKERE PLWKKFLKEV SNGFAIMLWV
     GAALCILVYI LQTDDPSNLY LGIVLILVIF LTGYITFQQT AKSEALMESF KNFLPQQCTV
     IRDGENKSID ALKLVVGDVV LVKAGEKIPA DIRILMSNEM KVDNSPLTGE SEPLLRTTEC
     THPENPLETS NLAFFGTLCK EGQGRGVVVR IGDNTTLGQI ADLSSTDKKV KSPLRQELDR
     FVIMITIIAL FLGVLFFLLA WLLMHYNILQ CLIFGIGILV ANVPEGLLGC ITISLAITAK
     TLSEKNVLVK NLEAVETLGS TSCICSDKTG TLTQNVMTVE HMWYNDQVIR AKNKSLASPQ
     EIEYDETEKG FQNLHYAAMC SSEARFDLTD IVDRDNIDYM KCPVMGDATE TGLVRFYQYI
     EDIDATRNRF KTAEHKGQPA RMPFNSTVKF ALTIVEQKTS DSDYCIYMKG APEKVWLYCS
     HILIGERKHE INQEWKTKFD NVNKRFGKKG ERVLGFAKLH LLREEYPQGS TVFNVTSPAN
     FNFKLAGFSF CGLVSLIDPP KTRVPNAILE CRSAGIKVIM VTGDQPPTAA SIARQVNIIP
     QSVKTVDEII ETENISWEEA AEKCDAIVVH GDRIVESLVR EQEEGKEEFS YLRTWVKKPY
     CVFARTTPAQ KLQIVQACQA EGYVCAVTGD GVNDSPAIKQ GDIGISMNLT GSDVTKDAAD
     MVLLDDDFAS IVVGVEEGRK IFDNLKKTVV YLLTSNIPEI IPFLAFIIIQ IPLPLSNIFM
     LCICVGTDIL PALSLAYEEA EIDIMTRKPR KKTDHLVSMV LITCAYLQMG MISTCAGFAA
     YYTVFNYYGF TPDGLFNLAN VYGYQPDDNA FNWTTYPPNV DPVLAETLFK DPMYFNTQLY
     NAVKSAGQTT CTNVKLPDDY NINWALIDQG KYDLRKALLK CEDGYFQPTT TWNHECNLSE
     TSPVTDYPVC YSIDANFYAQ TAFFVAIVLV QWSNVFACKS RKMSFTTSPV NKVMFMGVLV
     ETILCIFLFY TPGVQKVFGA RPLEFWQFGI PGLPFSILLL LWEEFRKFLL RSSKWFNKHC
     LW
//
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