AT1A3_CHICK
ID AT1A3_CHICK Reviewed; 1010 AA.
AC P24798;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-3;
DE Short=Na(+)/K(+) ATPase alpha-3 subunit;
DE EC=7.2.2.13;
DE AltName: Full=Na(+)/K(+) ATPase alpha(III) subunit;
DE AltName: Full=Sodium pump subunit alpha-3;
GN Name=ATP1A3;
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].
RX PubMed=2171348; DOI=10.1152/ajpcell.1990.259.4.c619;
RA Takeyasu K., Lemas V., Fambrough D.M.;
RT "Stability of Na(+)-K(+)-ATPase alpha-subunit isoforms in evolution.";
RL Am. J. Physiol. 259:C619-C630(1990).
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 -!- 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 {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M59960; AAA48982.1; -; mRNA.
DR PIR; B37227; B37227.
DR RefSeq; NP_990806.1; NM_205475.1.
DR AlphaFoldDB; P24798; -.
DR SMR; P24798; -.
DR PRIDE; P24798; -.
DR GeneID; 396467; -.
DR CTD; 478; -.
DR VEuPathDB; HostDB:geneid_396530; -.
DR InParanoid; P24798; -.
DR OrthoDB; 388324at2759; -.
DR PhylomeDB; P24798; -.
DR PRO; PR:P24798; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; ISS:UniProtKB.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IBA:GO_Central.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
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 CHAIN 1..1010
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 3"
FT /id="PRO_0000046301"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..307
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..759
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 760..779
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 780..789
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 790..810
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 811..830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 831..853
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 854..905
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 906..925
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 926..938
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 939..957
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 958..972
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 973..993
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 994..1010
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..71
FT /note="Interaction with phosphoinositide-3 kinase"
FT /evidence="ECO:0000250"
FT ACT_SITE 363
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 704
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 708
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 930
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1010 AA; 111284 MW; 71526BC25633BFA6 CRC64;
MGDKGEKESP KKGKGKRDLD DLKKEVAMTE HKMSIEEVCR KYNTDCVQGL THSKAQEILA
RDGPNALTPP PTTPEWVKFC RQLFGGFSIL LWIGAILCFL AYGIQAGTED EPSNDNLYLG
IVLAAVVIIT GCFSYYQEAK SSKIMESFKN MVPQQALVIR EGEKMQLNAE EVVVGDLVEV
KGGDRVPADL RIISAHGCKV DNSSLTGESE PQTRSPDCTH DNPLETRNIT FFSTNCVEGT
ARGVVIATGD RTVMGRIATL ASGLEVGKTP IAVEIEHFIQ LITGVAVFLG ISFFVLSLIL
GYTWLEAVIF LIGIIVANVP EGLLATVTVC LTLTAKRMAR KNCLVKNLEA VETLGSTSTI
CSDKTGTLTQ NRMTVAHMWF DNQIHEADTT EDQSGTSFDK SSATWVALSH IAGLCNRAVF
KGGQENVPIL KRDVAGDASE SALLKCIELS SGSVKVMRER NKKVAEIPFN STNKYQLSIH
ETEDPNDNRY LLVMKGAPER ILDRCSTILL QGKEQPLDEE MKEAFQNAYL ELGGLGERVL
GFCHFYLPEE QYPKGFAFDC DDVNFATDNL CFVGLMSMID PPRAAVPDAV GKCRSAGIKV
IMVTGDHPIT AKAIAKGVGI ISEGNETVED IAARLNIPVS QVNPRDAKAC VIHGTDLKDM
SSEQIDEILQ NHTEIVFART SPQQKLIIVE GCQRQGAIVA VTGDGVNDSP ALKKADIGVA
MGIRGSDVSK QAADMILLDD NFASIVTGVE EGRLIFDNLK KSIAYTLTSN IPEITPFLLF
IMANIPLPLG TITILCIDLG TDMVPAISLA YEAAESDIMK RQPRNPRSDK LVNERLISMA
YGQIGMIQAL GGFFSYFVIL AENGFLPSCL VGIRLSWDDR TINDLEDSYG QQWTYEQRKV
VEFTCHTAFF VSIVVVQWAD LIICKTRRNS VFQQGMKNKI LIFGLFEETA LAAFLSYCPG
MDVALRMYPL KPSWWFCAFP YSFLIFVYDE IRKLILRRNP GGWVEKETYY