AT1A2_PIG
ID AT1A2_PIG Reviewed; 1020 AA.
AC D2WKD8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-2;
DE Short=Na(+)/K(+) ATPase alpha-2 subunit;
DE EC=7.2.2.13;
DE AltName: Full=Sodium pump subunit alpha-2;
DE Flags: Precursor;
GN Name=ATP1A2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Henriksen C., Bendixen C., Andersen J.P., Vilsen B., Larsen K.;
RT "Cloning of Porcine ATP1A2 mRNA.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 384-590.
RX PubMed=14499619; DOI=10.1016/j.jmb.2003.07.012;
RA Hakansson K.O.;
RT "The crystallographic structure of Na,K-ATPase N-domain at 2.6A
RT resolution.";
RL J. Mol. Biol. 332:1175-1182(2003).
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, providing the energy
CC for active transport of various nutrients (By similarity).
CC {ECO:0000250}.
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 {ECO:0000250|UniProtKB:A2VDL6}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. 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}.
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DR EMBL; GQ340776; ADB19854.1; -; mRNA.
DR EMBL; CU138477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001165012.1; NM_001171541.1.
DR RefSeq; XP_013852329.1; XM_013996875.1.
DR PDB; 1Q3I; X-ray; 2.60 A; A=384-590.
DR PDBsum; 1Q3I; -.
DR AlphaFoldDB; D2WKD8; -.
DR SMR; D2WKD8; -.
DR STRING; 9823.ENSSSCP00000006814; -.
DR ChEMBL; CHEMBL4524015; -.
DR DrugCentral; D2WKD8; -.
DR PaxDb; D2WKD8; -.
DR PeptideAtlas; D2WKD8; -.
DR PRIDE; D2WKD8; -.
DR Ensembl; ENSSSCT00015109895; ENSSSCP00015046828; ENSSSCG00015079042.
DR Ensembl; ENSSSCT00045028856; ENSSSCP00045019976; ENSSSCG00045016895.
DR Ensembl; ENSSSCT00045029077; ENSSSCP00045020133; ENSSSCG00045016895.
DR Ensembl; ENSSSCT00070054049; ENSSSCP00070045817; ENSSSCG00070026761.
DR GeneID; 396828; -.
DR KEGG; ssc:396828; -.
DR CTD; 477; -.
DR eggNOG; KOG0203; Eukaryota.
DR HOGENOM; CLU_002360_4_3_1; -.
DR InParanoid; D2WKD8; -.
DR OrthoDB; 388324at2759; -.
DR TreeFam; TF312838; -.
DR Reactome; R-SSC-5578775; Ion homeostasis.
DR Reactome; R-SSC-936837; Ion transport by P-type ATPases.
DR EvolutionaryTrace; D2WKD8; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 4.
DR Genevisible; D2WKD8; SS.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IBA:GO_Central.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Ion transport; Magnesium;
KW Membrane; 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 /evidence="ECO:0000250"
FT /id="PRO_0000411080"
FT CHAIN 6..1020
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 2"
FT /id="PRO_0000411081"
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..769
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 770..789
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 790..799
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 800..820
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 821..840
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 841..863
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 864..915
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 916..935
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 936..948
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 949..967
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 968..982
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 983..1003
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1004..1020
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="Interaction with phosphoinositide-3 kinase"
FT /evidence="ECO:0000250"
FT REGION 212..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 374
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 714
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 718
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIE5"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06686"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIE5"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIE5"
FT MOD_RES 570
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P50993"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50993"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIE5"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09626"
FT MOD_RES 940
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
FT STRAND 385..391
FT /evidence="ECO:0007829|PDB:1Q3I"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:1Q3I"
FT HELIX 414..425
FT /evidence="ECO:0007829|PDB:1Q3I"
FT HELIX 449..462
FT /evidence="ECO:0007829|PDB:1Q3I"
FT HELIX 465..470
FT /evidence="ECO:0007829|PDB:1Q3I"
FT STRAND 474..478
FT /evidence="ECO:0007829|PDB:1Q3I"
FT STRAND 487..492
FT /evidence="ECO:0007829|PDB:1Q3I"
FT STRAND 499..506
FT /evidence="ECO:0007829|PDB:1Q3I"
FT HELIX 508..513
FT /evidence="ECO:0007829|PDB:1Q3I"
FT STRAND 515..520
FT /evidence="ECO:0007829|PDB:1Q3I"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:1Q3I"
FT HELIX 529..544
FT /evidence="ECO:0007829|PDB:1Q3I"
FT STRAND 548..557
FT /evidence="ECO:0007829|PDB:1Q3I"
FT TURN 559..561
FT /evidence="ECO:0007829|PDB:1Q3I"
FT TURN 570..573
FT /evidence="ECO:0007829|PDB:1Q3I"
FT STRAND 578..590
FT /evidence="ECO:0007829|PDB:1Q3I"
SQ SEQUENCE 1020 AA; 112208 MW; 0DFB46632BBA2E2D CRC64;
MGRGAGREYS PAATTAENGG GKKKQKEKEL DELKKEVAMD DHKLSLDELG RKYQVDLSKG
LTNQRAQDIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSI LLWIGAILCF LAYGIQAAME
DEPSNDNLYL GVVLAAVVIV TGCFSYYQEA KSSKIMDSFK NMVPQQALVV REGEKMQINA
EEVVVGDLVE VKGGDRVPAD LRIISSHGCK VDNSSLTGES EPQTRSPEFT HENPLETRNI
CFFSTNCVEG TARGIVIATG DRTVMGRIAT LASGLEVGRT PIAMEIEHFI QLITGVAVFL
GVSFFVLSLI LGYSWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE
AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT TEDQSGATFD KRSPTWTALS
RIAGLCNRAV FKAGQENISV SKRDTAGDAS ESALLKCIEL SCGSVRKMRD RNPKVAEIPF
NSTNKYQLSI HEREDNPQSH VLVMKGAPER ILDRCSSILV QGKEIPLDKE MQDAFQNAYL
ELGGLGERVL GFCQLNLPSG KFPRGFKFDT DELNFPTEKL CFVGLMSMID PPRAAVPDAV
GKCRSAGIKV IMVTGDHPIT AKAIAKGVGI ISEGNETVED IAARLNIPVS QVNPREAKAC
VVHGSDLKDM TSEQLDEILK NHTEIVFART SPQQKLIIVE GCQRQGAIVA VTGDGVNDSP
ALKKADIGIA MGIAGSDVSK QAADMILLDD NFASIVTGVE EGRLIFDNLK KSIAYTLTSN
IPEITPFLLF IIANIPLPLG TVTILCIDLG TDMVPAISLA YEAAESDIMK RQPRNPQTDK
LVNERLISMA YGQIGMIQAL GGFFTYFVIL AENGFLPSRL LGIRLDWDDR SMNDLEDSYG
QEWTYEQRKV VEFTCHTAFF ASIVVVQWAD LIICKTRRNS VFQQGMKNKI LIFGLLEETA
LAAFLSYCPG MGVALRMYPL KVTWWFCAFP YSLLIFIYDE VRKLILRRYP GGWVEKETYY
