AT1A1_CHICK
ID AT1A1_CHICK Reviewed; 1021 AA.
AC P09572;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 165.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=2831227; DOI=10.1016/s0021-9258(18)68932-x;
RA Takeyasu K., Tamkun M.M., Renaud K.J., Fambrough D.M.;
RT "Ouabain-sensitive (Na+ + K+)-ATPase activity expressed in mouse L cells by
RT transfection with DNA encoding the alpha-subunit of an avian sodium pump.";
RL J. Biol. Chem. 263:4347-4354(1988).
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 -!- PTM: Phosphorylation on Tyr-10 modulates pumping activity.
CC {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; J03230; AAA48607.1; -; mRNA.
DR PIR; A28199; A28199.
DR RefSeq; NP_990852.1; NM_205521.1.
DR AlphaFoldDB; P09572; -.
DR BMRB; P09572; -.
DR SMR; P09572; -.
DR BioGRID; 676774; 1.
DR DIP; DIP-27N; -.
DR IntAct; P09572; 1.
DR STRING; 9031.ENSGALP00000024150; -.
DR PaxDb; P09572; -.
DR PRIDE; P09572; -.
DR GeneID; 396530; -.
DR KEGG; gga:396530; -.
DR CTD; 476; -.
DR VEuPathDB; HostDB:geneid_396530; -.
DR eggNOG; KOG0203; Eukaryota.
DR InParanoid; P09572; -.
DR OrthoDB; 100699at2759; -.
DR PhylomeDB; P09572; -.
DR PRO; PR:P09572; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:1990794; C:basolateral part of cell; IDA:AgBase.
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; Reference proteome; Sodium; Sodium transport;
KW Sodium/potassium transport; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT PROPEP 1..5
FT /id="PRO_0000002493"
FT CHAIN 6..1021
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 1"
FT /id="PRO_0000002494"
FT TOPO_DOM 6..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..129
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..318
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..770
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 771..790
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 791..800
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 801..821
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 822..841
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 842..864
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 865..916
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 917..936
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 937..949
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 950..968
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 969..983
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 984..1004
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1005..1021
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..82
FT /note="Phosphoinositide-3 kinase binding"
FT /evidence="ECO:0000250"
FT REGION 214..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 374
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 715
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 719
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 16
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 941
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1021 AA; 112231 MW; 921E86B6FD843EEB CRC64;
MGKGAGRDKY EPTATSEHGT KKKKAKERDM DELKKEISMD DHKLSLDELH RKYGTDLSRG
LTTARAAEIL ARDGPNTLTP PPTTPEWVKF CRQLFGGFSL LLWIGSLLCF LAYGITSVME
GEPNSDNLYL GVVLAAVVII TGCFSYYQEA KSSKIMESFK NMVPQQALVV RNGEKMSINA
EGVVVGDLVE VKGGDRIPAD LRIISAHGCK VDNSSLTGES EPQTRSPDFS NENPLETRNI
AFFSTNCVEG TAVGIVISTG DRTVMGRIAS LASGLEGGKT PIAMEIEHFI HLITGVAVFL
GVSFFILSLI LEYTWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE
AVGTLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT TENQSGASFD KSSATWLALS
RIAGLCNRAV FQANQENVPI LKRAVAGDAS ESALLKCIEL CCGSVKEMRE RYPKVVEIPF
NSTNKYQLSI HKNANAGESR HLLVMKGAPE RILDRCDSIL IHGKVQPLDE EIKDAFQNAY
LELGGLGERV LGFCHLALPD DQFPEGFQFD TDEVNFPVEK LCFVGLMSMI DPPRAAVPDA
VGKCRSAGIK VIMVTGDHPI TAKAIAKGVG IISDGNETVE DIAARLNIPV SQVNPRDAKA
CVVHGSDLKD MTSEQLDDIL LHHTEIVFAR TSPQQKLIIV EGCQRQGAIV AVTGDGVNDS
PALKKADIGV AMGIAGSDVS KQAADMILLD DNFASIVTGV EEGRLIFDNL KKSIAYTLTS
NIPEITPFLI FIIANIPLPL GTCTILCIDL GTDMVPAISL AYEQAESDIM KRQPRNPKTD
KLVNERLISM AYGQIGMIQA LGGFFTYFVI MAENGFLPSG LVGIRLQWDD RWINDVEDSY
GQQWTFEQRK IVEFTCHTAF FVSIVVVQWA DLIICKTRRN SVFQQGMKNK ILIFGLFEET
ALAAFLSYCP GMDVALRMYP LKPTWWFCAF PYSLLIFLYD EIRKLIIRRN PGGWVERETY
Y
