AT1A1_CATCO
ID AT1A1_CATCO Reviewed; 1027 AA.
AC P25489;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 130.
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 Catostomus commersonii (White sucker) (Cyprinus commersonnii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Catostomoidei; Catostomidae; Catostomus.
OX NCBI_TaxID=7971;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hypothalamus;
RX PubMed=1711856; DOI=10.1515/bchm3.1991.372.1.279;
RA Schoenrock C., Morley S.D., Okawara Y., Lederis K., Richter D.;
RT "Sodium and potassium ATPase of the teleost fish Catostomus commersoni.
RT Sequence, protein structure and evolutionary conservation of the alpha-
RT subunit.";
RL Biol. Chem. Hoppe-Seyler 372:279-286(1991).
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; X58629; CAA41483.1; -; mRNA.
DR PIR; S14740; PWCCNM.
DR AlphaFoldDB; P25489; -.
DR SMR; P25489; -.
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_0000002497"
FT CHAIN 6..1027
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 1"
FT /id="PRO_0000002498"
FT TOPO_DOM 6..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..134
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..323
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..776
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 777..796
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 797..806
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 807..827
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 828..847
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 848..870
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 871..922
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 923..942
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 943..955
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 956..974
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 975..989
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 990..1010
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1011..1027
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..87
FT /note="Interaction with phosphoinositide-3 kinase"
FT /evidence="ECO:0000250"
FT REGION 217..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 379
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 721
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 725
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 947
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1027 AA; 113314 MW; BA821A12F85DF8EB CRC64;
MGVGDGRDQY ELAAMSEQSG KKKSKNKKEK KEKDMDELKK EVDLDDHKLS LEELHHKYGT
DLSKGLSNSR AEEILARDGP NALTPPPTTP EWVKFCKQMF GGFSMLLWTG AVLCFLAYGI
LAAMEDEPAN DNLYLGVVLS AVVIITGCFS YYQDAKSSKI MDSFKNLVPQ QALVVRDGEK
KQINAEEVVI GDLVEVKGGD RIPADLRIIS SHGCKVDNSS LTGESEPQTR SPDFSNDNPL
ETKNIAFFST NCVEGTARGI VISTGDRTVM GRIATLASGL EVGRTPISIE IEHFIHIITG
VAVFLGVSFL LLSLVLGYSW LEAVIFLIGI IVANVPEGLL ATVTVCLTLT AKRMAKKNCL
VKNLEAVETL GSTSTICSDK TGTLTQNRMT VAHMWFDNQI HEADTTENQS GTSFDRSSDT
WASLARIAGL CNRAVFLAEQ IDVPILKRDV AGDASESALL KCIELCCGSV KEMREKFTKV
AEIPFNSTNK YQLSVHKIPS GGKESQHLLV MKGAPERILD RCATIMIQGK EQLLDDEIKE
SFQNAYLELG GLGERVLGFC HFYLPDEQFP EGFQFDADDV NFPTENLCFV GLMSMIDPPR
AAVPDAVGKC RSAGIKVIMV TGDHPITAKA IAKGVGIISE GNETVEDIAA RLNIPVNEVN
PRDAKACVVH GGDLKDLSCE QLDDILKYHT EIVFARTSPQ QKLIIVEGCQ RTGAIVAVTG
DGVNDSPALK KADIGVAMGI AGSDVSKQAA DMILLDDNFA SIVTGVEEGR LIFDNLKKSI
AYTLTSNIPE ITPFLFFIIA NIPLPLGTVT ILCIDLGTDM LPAISLAYEA AESDIMKRQP
RNPKTDKLVN ERLISIAYGQ IGMIQALAGF FTYFVILAEN GFLPPRLLGI RMNWDDKYIN
DLEDSYGQQW TYEQRKIVEF TCHTAFFTSI VIVQWADLII CKTRRNSVFQ QGMKNKILIF
GLFEETALAA FLSYCPGMDV ALRMYPLKPN WWFCAFPYSL LIFIYDEIRK LILRRNPGGW
MERETYY
