AT1A3_OREMO
ID AT1A3_OREMO Reviewed; 1010 AA.
AC P58312;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-3;
DE Short=Na(+)/K(+) ATPase alpha-3 subunit;
DE EC=7.2.2.13;
DE AltName: Full=Na(+)/K(+) ATPase alpha(III) subunit;
DE AltName: Full=Sodium pump subunit alpha-3;
GN Name=atp1a3;
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].
RA Feng H.H., Leu J.H., Huang C.J., Hwang P.P.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
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:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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; AF109409; AAF75108.1; -; mRNA.
DR AlphaFoldDB; P58312; -.
DR SMR; P58312; -.
DR PRIDE; P58312; -.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
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; ISS:UniProtKB.
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..1010
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 3"
FT /id="PRO_0000046302"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..307
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..759
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 760..779
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 780..789
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 790..810
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 811..830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 831..853
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 854..905
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 906..925
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 926..938
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 939..957
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 958..972
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 973..993
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 994..1010
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..71
FT /note="Interaction with phosphoinositide-3 kinase"
FT /evidence="ECO:0000250"
FT REGION 201..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 363
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 704
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 708
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 930
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1010 AA; 111507 MW; 9FEDB07C7547F0D1 CRC64;
MGDKDDRFPK KKKGGTKDMD ALKKEVPITE HKMSVEEVCR KFQTDVVQGL TNAKAAEFLL
RDGPNALTPP PTTPEWVKFC RQLFGGFSIL LWTGAILCFL AYAIQAATED EPAGDNLYLG
IVLTAVVVIT GCFSYFQEAK SSKIMESFKN MVPQQALVIR EGEKVQVNAE EVMAGDLIEV
KGGDRIPADI RVTSAHGCKV DNSSLTGESE PQSRSPDCTH DNPLETRNIA FFSTNCVEGT
ARGIVICTGD RTVMGRIATL TSGLETGKTP IAVEIEHFIH IITGVAVFLG VTFFILAIIL
GYTWLKAVIF LIGIIVANVP EGLLATVTVC LTLTAKRMAK KNCLVKNLEA VETLGSTSTI
CSDKTGTLTQ NRMTVAHMWF DNQIHEADTT EDQSGAAFDK SSVTWLSLSR VAPLCNRAQF
KPRQDSVSIL KRDVAGDASE SALLKCIELS CGSVRMMRDK NKKVAEIPFN PTNKYQLSIH
ETEDPNDNRY LLVMKGALER ILDRCSTIML QGKEQPMDEE MKEAFQNAYM ELGGLGERVL
GFRHLLLPED QYPKGFAFDT DDVNFQTDNL CFVGLMSMID PPRAAVPDAV GKCRSAGIKV
IMVTGDHPIT AKAIAKGVGI ISEGNETVED IAARLNIPVS QVNPRDAKAC VIHGSDLKDL
SQDQMDDILR NHTEIVFART SPQQKLIIVE GCQRLGAIVA VTGDGVNDSP ALKKADIGVA
MGISGSDVSK QAADMILLDD NFASIVTGVE EGRLIFDNLK KSIAYTLTSN IPEITPFLFF
IIVNIPLALG TITILCIDLG TDMGSAISLA YETAESDIMK RQPRNPCRDK LVNERLISIA
YGQIGMIQAL GGFFSYFVIL AENGFLPSQL VGIRLNWDDR SLNDLEDSYG QQWTYEQRKI
VEFTCHTAFF VSIVVVQWAD LIICKTRRNS VFQQGMKNKI LIFGLFEETA LAAFLSYCPG
MDVALRMYPL KPTWWFWAFP YSFLIFVYDE ARKLILCRNP GGWVEKETYY
