AT1A_TETCF
ID AT1A_TETCF Reviewed; 1022 AA.
AC P05025;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha;
DE Short=Na(+)/K(+) ATPase alpha subunit;
DE EC=7.2.2.13;
DE AltName: Full=Sodium pump subunit alpha;
DE Flags: Precursor;
OS Tetronarce californica (Pacific electric ray) (Torpedo californica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
OX NCBI_TaxID=7787;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2993905; DOI=10.1038/316733a0;
RA Kawakami K., Noguchi S., Noda M., Takahashi H., Ohta T., Kawamura M.,
RA Nojima H., Nagano K., Hirose T., Inayama S., Hayashida H., Miyata T.,
RA Numa S.;
RT "Primary structure of the alpha-subunit of Torpedo californica (Na+ +
RT K+)ATPase deduced from cDNA sequence.";
RL Nature 316:733-736(1985).
RN [2]
RP PROTEIN SEQUENCE OF 386-402; 502-512; 671-689 AND 887-906.
RX PubMed=3008150; DOI=10.1073/pnas.83.7.2071;
RA Ohta T., Nagano K., Yoshida M.;
RT "The active site structure of Na+/K+-transporting ATPase: location of the
RT 5'-(p-fluorosulfonyl)benzoyladenosine binding site and soluble peptides
RT released by trypsin.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:2071-2075(1986).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) +
CC Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC EC=7.2.2.13;
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000305}.
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DR EMBL; X02810; CAA26578.1; -; mRNA.
DR PIR; S00503; S00503.
DR AlphaFoldDB; P05025; -.
DR SMR; P05025; -.
DR PRIDE; P05025; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0005391; F:P-type sodium:potassium-exchanging transporter activity; IEA:UniProtKB-EC.
DR CDD; cd02608; P-type_ATPase_Na-K_like; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Direct protein sequencing; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Potassium; Potassium transport; Sodium; Sodium transport;
KW Sodium/potassium transport; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT PROPEP 1..5
FT /id="PRO_0000002509"
FT CHAIN 6..1022
FT /note="Sodium/potassium-transporting ATPase subunit alpha"
FT /id="PRO_0000002510"
FT TOPO_DOM 6..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..131
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..320
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..771
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 772..791
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 792..801
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 802..822
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 823..842
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 843..865
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 866..917
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 918..937
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 938..950
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 951..969
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 970..984
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 985..1005
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1006..1022
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..84
FT /note="Interaction with phosphoinositide-3 kinase"
FT /evidence="ECO:0000250"
FT REGION 215..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 376
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 716
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 720
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 16
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 942
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1022 AA; 112430 MW; D92FE737847D73C2 CRC64;
MGKGAASEKY QPAATSENAK NSKKSKSKTT DLDELKKEVS LDDHKLNLDE LHQKYGTDLT
QGLTPARAKE ILARDGPNAL TPPPTTPEWI KFCRQLFGGF SILLWTGAIL CFLAYGIQVA
TVDNPANDNL YLGVVLSTVV IITGCFSYYQ EAKSSKIMDS FKNMVPQQAL VIRDGEKSSI
NAEQVVVGDL VEVKGGDRIP ADLRIISACS CKVDNSSLTG ESEPQSRSPE YSSENPLETK
NIAFFSTNCV EGTARGIVIN IGDHTVMGRI ATLASGLEVG QTPIAAEIEH FIHIITGVAV
FLGVSFFILS LILGYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGIS FDKTSLSWNA
LSRIAALCNR AVFQAGQDSV PILKRSVAGD ASESALLKCI ELCCGSVSQM RDRNPKIVEI
PFNSTNKYQL SIHENDKADS RYLLVMKGAP ERILDRCSTI LLNGEDKPLN EEMKEAFQNA
YLELGGLGER VLGFCHLKLS TSKFPEGYPF DVEEPNFPIT DLCFVGLMSM IDPPRAAVPD
AVGKCRSAGI KVIMVTGDHP ITAKAIAKGV GIISEGNETV EDIAARLNIP VNQVNPRDAK
ACVVHGTDLK DLSHENLDDI LHYHTEIVFA RTSPQQKLII VEGCQRQGAI VAVTGDGVND
SPALKKADIG VAMGIAGSDV SKQAADMILL DDNFASIVTG VEEGRLIFDN LKKSIAYTLT
SNIPEITPFL VFIIANVPLP LGTVTILCID LGTDMVPAIS LAYERAESDI MKRQPRNPKT
DKLVNERLIS MAYGQIGMIQ ALGGFFSYFV ILAENGFLPI DLIGIREKWD ELWTQDLEDS
YGQQWTYEQR KIVEYTCHTS FFVSIVIVQW ADLIICKTRR NSIFQQGMKN KILIFGLFEE
TALAAFLSYT PGTDIALRMY PLKPSWWFCA FPYSLIIFLY DEARRFILRR NPGGWVEQET
YY
