AT1A1_OREMO
ID AT1A1_OREMO Reviewed; 1023 AA.
AC Q9YH26;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-1;
DE Short=Na(+)/K(+) ATPase alpha-1 subunit;
DE EC=7.2.2.13;
DE AltName: Full=Sodium pump subunit alpha-1;
DE Flags: Precursor;
GN Name=atp1a1;
OS Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8127;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14961249; DOI=10.1007/s10126-002-0006-0;
RA Feng S.H., Leu J.H., Yang C.H., Fang M.J., Huang C.J., Hwang P.P.;
RT "Gene expression of Na+-K+-ATPase alpha 1 and alpha 3 subunits in gills of
RT the teleost Oreochromis mossambicus, adapted to different environmental
RT salinities.";
RL Mar. Biotechnol. 4:379-391(2002).
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:0000250|UniProtKB:P05023}.
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, sarcolemma
CC {ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U82549; AAD11455.2; -; mRNA.
DR AlphaFoldDB; Q9YH26; -.
DR SMR; Q9YH26; -.
DR PRIDE; Q9YH26; -.
DR BRENDA; 7.2.2.13; 4428.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; 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 PROPEP 1..5
FT /evidence="ECO:0000250"
FT /id="PRO_0000002499"
FT CHAIN 6..1023
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 1"
FT /id="PRO_0000002500"
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="Extracellular"
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="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..792
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 793..802
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..823
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 824..843
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 844..866
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 867..918
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 919..938
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 939..951
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 952..970
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 971..985
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 986..1006
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1007..1023
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..33
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 216..237
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 487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 717
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 721
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 943
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1023 AA; 112669 MW; 19B5221173BC4454 CRC64;
MGLGKGKDEY KLAATSEDGG KKDKKAKAKK DMDDLKKEVD LDDHKLTLDE LHRKYGTDLT
RGLSSSRAKE ILARDGPNAL TPPPTTPEWV KFCKQLFGGF SMLLWIGAIL CFLAYGIQAA
SEDEPANDNL YLGIVLSAVV IITGCFSYYQ EAKSSKIMES FKNLVPRQAL GIRDGEKKNI
NAEEVVLGDL VEVKGGDRIP ADLRIISAHG CKVDNSSLTG ESEPQTRSPD FSNENPLETR
NISFFSTNCI EGTARGIVIN TEDRTVMGRI ATLASSLEGG KTPIAIEIEH FIHIITGVAV
FLGVSFFILS LILGYNWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MAKKNCLVKN
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGTS FDRSSATWAN
LSRIAGLCNR AVFLADQSNI PILKRDVAGD ASEAALLKCI ELCCGSVNEM REKYPKIAEI
PFNSTNKYQL SIHKNTTPGE TKHLLVMKGA PERILDRCNS IVLQGKVQAL DDEMKDAFQN
AYVELGGLGE RVLGFCHYHL PDDEFPEGFA FDTDEVNFPT ENLCFVGLMA MIDPPRAAVP
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNV PVSEVNPRDA
KACVVHGSEL KDMTSEELDD LLKHHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN
DSPALKKADI GVAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL
TSNIPEISPF LLFIIANIPL PLGTVTILCI DLGTDMVPAI SLAYEKAESD IMKRQPRNPK
TDKLVNERLI SIAYGQIGMM QATAGFFTYF VILAENGFLP MDLIGVRVLW DDKYVNDLED
SYGQQWTYER RKIVEYSCHT AFFASIVIVQ WADLIICKTR RNSIVQQGMT NRILIFGLFE
ETALAAFLSY CPGMDVALRM YPMKPLWWFC AFPYSLLIFL YDEARRYILR RNPGGWVEKE
TYY
