AT1A_HYDVU
ID AT1A_HYDVU Reviewed; 1031 AA.
AC P35317;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 120.
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;
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1320398;
RA Canfield V.A., Xu K.Y., D'Aquila T., Shyjan A.W., Levenson R.;
RT "Molecular cloning and characterization of Na,K-ATPase from Hydra vulgaris:
RT implications for enzyme evolution and ouabain sensitivity.";
RL New Biol. 4:339-348(1992).
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 -!- ACTIVITY REGULATION: This alpha subunit is resistant to ouabain.
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; M75140; AAA29207.1; -; mRNA.
DR RefSeq; NP_001296716.1; NM_001309787.1.
DR AlphaFoldDB; P35317; -.
DR SMR; P35317; -.
DR PRIDE; P35317; -.
DR GeneID; 105846521; -.
DR KEGG; hmg:105846521; -.
DR OrthoDB; 388324at2759; -.
DR Proteomes; UP000694840; Unplaced.
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; Reference proteome; Sodium; Sodium transport;
KW Sodium/potassium transport; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1031
FT /note="Sodium/potassium-transporting ATPase subunit alpha"
FT /id="PRO_0000046308"
FT TRANSMEM 102..123
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 136..155
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 297..319
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 326..354
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 795..818
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 857..882
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 924..944
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 961..986
FT /note="Helical"
FT /evidence="ECO:0000250"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 382
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305"
FT BINDING 512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 725
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 729
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1031 AA; 114161 MW; D2F4A07B811B356F CRC64;
MADPGDLESR GKADSYSVAE KKSAPKKISK KNANKAKLED LKKELEMTEH SMKLESLLSM
YETSLEKGLS ENIVARNLER DGLNALTPPK QTPEWVKFCK QMFGGFSMLL WIGAILCFFA
FGIRAVRDTN PNMDELYLGI VLSVVVIITG CFSYYQESKS SKIMESFKKM IPQEALVLRD
GKKITINAEQ CVVGDVVFVK FGDRIPADIR IVECKGLKVD NSSLTGESEP QSRAVDFTHE
NPIETKNLAF FSTNAVEGTA TGIVVRIGDN TVMGRIANLA SGLGSGKTPI ALEIEHFIHI
VTGVAVFLGV SFLIISLAMG YHWLEAIIFL IGIIVANVPE GLLATVTVCL TLTAKKMAKK
NCLVKHLEAV ETLGSTSVIC SDKTGTLTQN RMTVAHMWFD KMIVEADTTE DQSGIAHDKG
SLTWKSLAKV AALCSRAEFK PNQNDVAVLR KECTGDASET AILKFVELSV GNVMDIRAKN
KKVTEIPFNS TNKYQVSVHE QENSSGYLLV MKGAPEKVLE RCSTILINGE EQPLKDDVIE
IYNKAYDELG GLGERVLGFC HYYLPVDQYP KGFLFKTEEE QNFPLEGLCF LGLLSMIDPP
RAAVPDAVSK CRSAGIKVIM VTGDHPITAK AIAKGVGIIS EGNECEEDIA LRLNIPLEDL
SEDQKKSAKA CVIHGAKLKD IKNEELDKIL CDHTEIVFAR TSPQQKLIIV EGCQRQGAIV
AVTGDGVNDS PALKKADIGV AMGIAGSDVS KQAADMILLD DNFASIVTGV EEGRLIFDNL
KKSIVYTLTS NIPEISPFLM FILFGIPLPL GTITILCIDL GTDMVPAISL AYEKAESDIM
KRHPRNPIRD KLVNERLISL AYGQIGMMQA TAGFFTYFII LAENGFLPSY LFGLRSQWDD
MSNNNLLDSF GSEWTYFQRK EIELTCQTAF FTTIVVVQWA DLIISKTRRL SLFQQGMTNW
FLNFGLFFET ALAAFLQYTP GVNTGLRLRP MNFTWWLPGL PFSLLIFVYD EIRRYLLRKN
PGGWVEKETY Y
