AT1A_TAESO
ID AT1A_TAESO Reviewed; 1014 AA.
AC Q6RWA9;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 AltName: Full=TNaK1-alpha;
OS Taenia solium (Pork tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX NCBI_TaxID=6204;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15500918; DOI=10.1016/j.molbiopara.2004.07.009;
RA Willms K., Shoemaker C.B., Skelly P.J., Landa A.;
RT "Cloning and expression of a Na(+), K(+)-ATPase alpha-subunit from Taenia
RT solium (TNaK1alpha).";
RL Mol. Biochem. Parasitol. 138:79-82(2004).
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 (By similarity).
CC {ECO:0000250}.
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:0000269|PubMed:15500918};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15500918}.
CC -!- TISSUE SPECIFICITY: Preferentially localized in muscle cells and
CC protonephridial ducts, and in small quantities in the tegument of
CC cysticerci. {ECO:0000269|PubMed:15500918}.
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; AY487828; AAS59168.1; -; mRNA.
DR AlphaFoldDB; Q6RWA9; -.
DR SMR; Q6RWA9; -.
DR PRIDE; Q6RWA9; -.
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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium;
KW Potassium transport; Sodium; Sodium transport; Sodium/potassium transport;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1014
FT /note="Sodium/potassium-transporting ATPase subunit alpha"
FT /id="PRO_0000291569"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 764..783
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 794..814
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 834..856
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 909..928
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 942..960
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 976..996
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 368
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 708
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 712
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1014 AA; 111990 MW; 595741648A93D5D1 CRC64;
MGKSRGDKYR DATDGKKDAK KDLNELKQEL AMDEHQISLD ELYARLGTNP DTGLTSEQAK
TRLDRDGPNA LTPPKTTPEW VKFCKNMFGG FSLLLWIGAV LCFIAHGIPC WCAGEPYLYD
NLYLGIVLAA VVVITGCFSY YQESKSSKIM ESFAKLVPQY AVVIRGGQRI DAPAEALVVG
DIIDVKFGDR VPADIRVIKA SSFKVDNSAL TGESEPQTRT AEYTNENPLE TKNLAFFSTN
AVEGTCRGVV VATGDRTVMG RIANLASGLE MGATPIAREI AHFIHIITGV AVFLGVTFFI
IAFILGYYWL DAVIFLIGII VANVPEGLLA TVTVCLTLTA KRMASKNCLV KNLEAVETLG
STSTICSDKT GTLTQNRMTV AHMWFDNKIF EADTSDDQST ANYSRASSTW MALSRIAMLC
NRAEFKPGEE TNPVLKRECN GDASESALLK CVGLSIGGVT GYRTDKPKVA EIPFNSTNKY
QVSVHQTDDG DERYLVVMKG APERILDRCS TVLMEGQELH MDDQWRESFN NAYLELGGIG
ERVLGFCDLR LPADKFPRGF KFDIDEPNFP IEGMPFVGLM SMIDPPRAAV PDAVSKCRSA
GIKVVMVTGD HPITAKAIAK GVGIISDGNK TVEDIAAERG VPVSQVNPRE ASACVVHGSD
LRDMTPAQID EILENHSEIV FARTSPQQKL IIVEGIQRMG AIVAVTGDGV NDSPALKKAD
IGVAMGITGS DVSKQAADMI LLDDNFASIV TGVEEGRIIF DNLKKSIAYT LTSNIPEITP
FLIFILADVP LPLGTITILC IDLGTDMVPA ISLAYEEAED IMKRMPRDPF RDKLVNERLI
SMAYGQIGMI QASGGFFVYF VIMAENGFWP SRLLGLRKQW DSPAINDVAD SYGQEWTYTQ
RKRLEYTCHT AFFASIVIVQ WTDLLICKTR KNSIYQQGMW NHHLTFGLFF ETTLAIFLSY
CPGLEHGLRM MPLRWTWWLP VLPFSVSIFI FDEVRKKFLR TLPPGNWVER ETNY
