AT1A1_RABIT
ID AT1A1_RABIT Reviewed; 1023 AA.
AC Q9N0Z6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 122.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11738066; DOI=10.1016/s0008-6363(01)00412-6;
RA Fransen P., Hendrickx J., Brutsaert D.L., Sys S.U.;
RT "Distribution and role of Na(+)/K(+) ATPase in endocardial endothelium.";
RL Cardiovasc. Res. 52:487-499(2001).
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 (By similarity). May
CC contribute to blood-heart barrier properties of endocardial endothelium
CC and may control cardiac performance via endothelial Na(+)/H(+) exchange
CC (PubMed:11738066). {ECO:0000250|UniProtKB:P05023,
CC ECO:0000269|PubMed:11738066}.
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. Interacts with regulatory subunit FXYD1.
CC Interacts with regulatory subunit FXYD3. Interacts with SIK1. Interacts
CC with SLC35G1 and STIM1. Interacts with CLN3; this interaction regulates
CC the sodium/potassium-transporting ATPase complex localization at the
CC plasma membrane (By similarity). {ECO:0000250|UniProtKB:P05023,
CC ECO:0000250|UniProtKB:P06685}.
CC -!- INTERACTION:
CC Q9N0Z6; Q9TT37: ATP1B1; NbExp=2; IntAct=EBI-9685690, EBI-9685670;
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000250|UniProtKB:P06685}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein
CC {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:P06685}.
CC Melanosome {ECO:0000250|UniProtKB:P05023}.
CC -!- TISSUE SPECIFICITY: Expressed in endocardial endothelial cells.
CC {ECO:0000269|PubMed:11738066}.
CC -!- PTM: Phosphorylation on Tyr-10 modulates pumping activity.
CC Phosphorylation of Ser-943 by PKA modulates the response of ATP1A1 to
CC PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following
CC increases in intracellular sodium, leading to increase catalytic
CC activity (By similarity). {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; AF235024; AAF60310.2; -; mRNA.
DR RefSeq; NP_001156546.1; NM_001163074.1.
DR AlphaFoldDB; Q9N0Z6; -.
DR SMR; Q9N0Z6; -.
DR IntAct; Q9N0Z6; 2.
DR STRING; 9986.ENSOCUP00000024821; -.
DR PRIDE; Q9N0Z6; -.
DR GeneID; 100302415; -.
DR KEGG; ocu:100302415; -.
DR CTD; 476; -.
DR eggNOG; KOG0203; Eukaryota.
DR InParanoid; Q9N0Z6; -.
DR OrthoDB; 100699at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
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:0051117; F:ATPase binding; IPI:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:BHF-UCL.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0002028; P:regulation of sodium ion transport; 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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell membrane; Cell projection; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Potassium; Potassium transport; Reference proteome; Sodium;
KW Sodium transport; Sodium/potassium transport; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT PROPEP 1..5
FT /evidence="ECO:0000250"
FT /id="PRO_0000305979"
FT CHAIN 6..1023
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000305980"
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..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..84
FT /note="Phosphoinositide-3 kinase binding"
FT /evidence="ECO:0000250"
FT REGION 216..235
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 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 10
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 16
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 260
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06685"
FT MOD_RES 542
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05023"
FT MOD_RES 661
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDN2"
FT MOD_RES 943
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P06685"
SQ SEQUENCE 1023 AA; 112994 MW; F6BA59C8979F574D CRC64;
MGKGVGRDKY EPAAVSEHGD KKGKKAKKER DMDELKKEVS MDDHKLSLDE LHRKYGTDLS
RGLTTARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SMLLWIGAIL CFLAYGILAA
TEEDFDNDNL YLGVVLAAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIRNGEKMSI
NAEDVVVGDL VEVKGGDRIP ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR
NIAFFSTNCV EGTARGIVIY TGDRTVMGRI ATLASGLEGG QTPIAAEIEH FIHIITGVAV
FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGVS FDKTSATWLA
LSRIAGLCNR AVFQANQENL PILKRAVAGD ASESALLKCI ELCCGSVKEM RERYTKIVEI
PFNSTNKYQL SIHKNLNANE PRHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN
AYLELGGLGE RVLGFCHLLL PDEQFPEGFQ FDTDEVNFPV DNLCFIGLIS MIDPPRAAVP
DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA
KACVVHGSDL KDMTSEQLDD ILKYHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN
DSPALKKADI GVAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL
TSNIPEITPF LIFIIANIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK
TDKLVNERLI SMAYGQIGMI QALGGFFTYF VILAENGFLP FHLLGIRVDW DDRWINDVED
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK NKILIFGLFE
ETALAAFLSY CPGMGVALRM YPLKPTWWFC AFPYSLLIFV YDEIRKLIIR RRPGGWVEKE
TYY
