AT1A1_ANGAN
ID AT1A1_ANGAN Reviewed; 1022 AA.
AC Q92030;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
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 Anguilla anguilla (European freshwater eel) (Muraena anguilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC Anguilla.
OX NCBI_TaxID=7936;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Gill;
RX PubMed=8574922; DOI=10.1016/0305-0491(95)00037-9;
RA Cutler C., Sanders I.L., Hazon N., Cramb G.;
RT "Primary sequence, tissue specificity and expression of the Na+,K(+)-ATPase
RT alpha 1 subunit in the European eel (Anguilla anguilla).";
RL Comp. Biochem. Physiol. 111B:567-573(1995).
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}.
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DR EMBL; X76108; CAA53714.1; -; mRNA.
DR PIR; S49127; S49127.
DR AlphaFoldDB; Q92030; -.
DR SMR; Q92030; -.
DR PRIDE; Q92030; -.
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_0000002495"
FT CHAIN 6..1022
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 1"
FT /id="PRO_0000002496"
FT TOPO_DOM 6..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..319
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..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="Extracellular"
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="Extracellular"
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="Extracellular"
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 81..83
FT /note="Interaction with phosphoinositide-3 kinase"
FT /evidence="ECO:0000250"
FT REGION 213..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 375
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 486
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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; 112716 MW; 5186DBFBC70C3C5C CRC64;
MGRGTGHDQY ELAATSEGGR KKKRDKKKKD MDDLKKEVDL DDHKLTLDEL HRKYGTDLTR
GLTSSRAAEI LARDGPNALT PPPTTPEWVK FCRQLFGGFS MLLWIGAILC FLAYGIQAAS
EDEPANDNLY LGVVLSAVVI ITGCFSYYQE AKSSRIMDSF KNLVPQQALV IRDGEKKCIN
AEEVVAGDLV EVKGGDRIPA DLRVASAQGC KVDNSSLTGE SEPQTRSPDF SNENPLETRN
IAFFSTNCVE GTARGVVINT GDRTVMGRIA TLASSLEVGR TPISIEIEHF IHIITGVAVF
LGVSFFILSL ILGYAWLEAV IFLIGIIVAN VPEGLLATVT VCLTLTAKRM AKKNCLVKNL
EAVETLGSTS TICSDKTGTL TQNRMTVAHM WFDNQIHEAD TTENQSGTSF DRSSATWAAL
ARIAGLCNRA VFLAEQSNVP ILKRDVAGDA SESALLKCIE LCCGSVNDMR DKHVKIAEIP
FNSTNKYQLS IHKNANSEES KHLLVMKGAP ERILDRCSTI MIHGKEQPLD DEMKDAFQNA
YVELGGLGER VLGFCHYFLP DDQFAEGFQF DTEEVNFPTE NLCFIGLMSM IDPPRAAVLD
AVGKCRSPGI KVIMVTGDHP ITAKAIAKGV GIISEGNETV EDIAARLNIP INEVNPRDAK
ACVVHGGELK DLTPEQLDDI LKHHTEIVFA RTSPQQKLII VEGCQRQGAI VAVTGDGVND
SPALKKADIG VAMGIAGSDV SKQAADMILL DDNFASIVTG VEEGRLIFDN LKKSIAYTLT
SNIPEITPFL LFIIANIPLP LGTVTILCID LGTDMVPAIS LAYEAAESDI MKRQPRNPRT
DKLVNERLIS IAYGQIGMMQ ATAGFFTYFV ILAENGFLPS TLLGIRVKWD DKYVNDLEDS
YGQQWTYEQR KIVEYTCHTS FFASIVIVQW ADLIICKTRR NSIIQQGMKN KILIFGLFEE
TALAAFLSYC PGMDVALRMY PLKPSWWFCA FPYSLLIFLY DEARRFILRR NPDGWVERET
YY
