AT1A1_RHIMB
ID AT1A1_RHIMB Reviewed; 1023 AA.
AC P30714;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 135.
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 Rhinella marina (Cane toad) (Bufo marinus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae; Rhinella.
OX NCBI_TaxID=8386;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Urinary bladder urothelium;
RX PubMed=1380956; DOI=10.1016/s0021-9258(18)41869-8;
RA Jaisser F., Canessa C.M., Horisberger J.-D., Rossier B.C.;
RT "Primary sequence and functional expression of a novel ouabain-resistant
RT Na,K-ATPase. The beta subunit modulates potassium activation of the Na,K-
RT pump.";
RL J. Biol. Chem. 267:16895-16903(1992).
RN [2]
RP SEQUENCE REVISION TO 835-836.
RA Jaisser F.;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION AT THR-15 AND SER-16 BY PROTEIN KINASE C, AND
RP PHOSPHORYLATION AT SER-943 BY CAMP-DEPENDENT KINASE.
RX PubMed=7929106; DOI=10.1016/s0021-9258(19)51103-6;
RA Beguin P., Beggah A.T., Chibalin A.V., Burgener-Kairuz P., Jaisser F.,
RA Mathews P.M., Rossier B.C., Cotecchia S., Geering K.;
RT "Phosphorylation of the Na,K-ATPase alpha-subunit by protein kinase A and C
RT in vitro and in intact cells. Identification of a novel motif for PKC-
RT mediated phosphorylation.";
RL J. Biol. Chem. 269:24437-24445(1994).
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 -!- ACTIVITY REGULATION: This alpha subunit is resistant to ouabain.
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 -!- TISSUE SPECIFICITY: Mainly expressed in kidney. Found in bladder,
CC colon, eye, and testis. Found in low levels in brain, heart, spleen and
CC liver.
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; Z11798; CAA77842.2; -; mRNA.
DR PIR; A43451; S24650.
DR AlphaFoldDB; P30714; -.
DR SMR; P30714; -.
DR iPTMnet; P30714; -.
DR PRIDE; P30714; -.
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 1: Evidence at protein 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_0000002501"
FT CHAIN 6..1023
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 1"
FT /id="PRO_0000002502"
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..34
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 215..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..34
FT /note="Basic and acidic residues"
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 15
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000269|PubMed:7929106"
FT MOD_RES 16
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:7929106"
FT MOD_RES 943
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:7929106"
SQ SEQUENCE 1023 AA; 112617 MW; D66E8C4028F41BF1 CRC64;
MGYGAGRDKY EPAATSEHGG KKGKGKGKDR DMEELKKEVT MEDHKMTLEE LHRKYGTDLT
RGLTTARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SMLLWIGAIL CFLAYGIRKA
SDLEPDNDNL YLGVVLSAVV IITGCFSYYQ EAKSSRIMES FKNMVPQQAL VIRNGEKLSI
NAENVVQGDL VEVKGGDRIP ADLRIISAHG CKVDNSSLTG ESEPQTRSPD FTNENPLETR
NIAFFSTNCV EGTARGIVIN TGDRTVMGRI ATLASGLEGG QTPIAVEIGH FIHIITGVAV
FLGVSFFILS LILHYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGAS FDKSSPTWTA
LARIAGLCNR AVFPAGQENT PILKRDVVGD ASESALLKCI ELCCGSVKDM REKNQKVAEI
PFNSTNKYQL SVHKNANPSE SRYLLVMKGA PERILDRCSS ILLQGKEQPL DEELKDAFQN
AYLELGGLGE RVLGFCHLLL DDEQFPDGFS FDTEDVNFPT EGLCFVGLIS MIDPPRAAVP
DRVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVNQVNPRDA
KACVIHGTDL KDMNADQIDD ILRHHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN
DSPALKKADI GIAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL
TSNIPEITPF LIFIIADIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK
KDKLVNERLI SMAYGQIGMI QALGGFFAYF VILAENGFLP STLLGIRVAW EDRYVNDVED
SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLIICKTR RNSVFQQGMK NKILIFGLFE
ETALAAFLSY CPGMDVALRM YPLKPTWWFC AFPYSLLIFI YDEVRKLILR RSPGGWVEKE
TYY
