AT1B1_PIG
ID AT1B1_PIG Reviewed; 303 AA.
AC P05027;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
DE AltName: Full=Sodium/potassium-dependent ATPase subunit beta-1;
GN Name=ATP1B1;
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].
RX PubMed=2423371; DOI=10.1016/0014-5793(86)80616-0;
RA Ovchinnikov Y.A., Modyanov N.N., Broude N.E., Petrukhin K.E., Grishin A.V.,
RA Arzamazova N.M., Aldanova N.A., Monastyrskaya G.S., Sverdlov E.D.;
RT "Pig kidney Na+,K+-ATPase. Primary structure and spatial organization.";
RL FEBS Lett. 201:237-245(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Ovchinnikov Y.A., Broude N.E., Petrukhin K.E., Grishin A.V., Kiyatkin N.I.,
RA Arzamazova N.M., Gevondyan N.M., Chertova E.N., Melkov A.M., Smirnov Y.V.,
RA Malyshev I.V., Monastyrskaya G.S., Modyanov N.N.;
RT "Nucleotide sequence of cDNA and primary structure of the beta-subunit of
RT Na+,K+-ATPase from pig kidneys.";
RL Dokl. Biochem. 287:149-152(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2436627;
RA Broude N.E., Monastyrskaya G.S., Petrukhin K.E., Grishin A.V.,
RA Kiyatkin N.I., Melkov A.M., Smirnov Y.V., Sverdiov V.E., Malyshev I.V.,
RA Modyanov N.N.;
RT "Primary structure of the beta-subunit of Na+,K+-ATPase from the swine
RT kidney. II. Reverse transcription, cloning of mRNA, complete nucleotide
RT sequence corresponding to the structural region of the gene.";
RL Bioorg. Khim. 13:14-19(1987).
RN [4]
RP TOPOLOGY.
RX PubMed=3036581; DOI=10.1016/0014-5793(87)80676-2;
RA Ovchinnikov Y.A., Arzamazova N.M., Arystarkhova E.A., Gevondyan N.M.,
RA Aldanova N.A., Modyanov N.N.;
RT "Detailed structural analysis of exposed domains of membrane-bound Na+,K+-
RT ATPase. A model of transmembrane arrangement.";
RL FEBS Lett. 217:269-274(1987).
CC -!- FUNCTION: This is the non-catalytic component of the active enzyme,
CC which catalyzes the hydrolysis of ATP coupled with the exchange of
CC Na(+) and K(+) ions across the plasma membrane. The beta subunit
CC regulates, through assembly of alpha/beta heterodimers, the number of
CC sodium pumps transported to the plasma membrane. Plays a role in innate
CC immunity by enhancing virus-triggered induction of interferons (IFNs)
CC and interferon stimulated genes (ISGs). Mechanistically, enhances the
CC ubiquitination of TRAF3 and TRAF6 as well as the phosphorylation of
CC TAK1 and TBK1. {ECO:0000250|UniProtKB:P05026}.
CC -!- FUNCTION: Involved in cell adhesion and establishing epithelial cell
CC polarity. {ECO:0000250|UniProtKB:P05026}.
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 catalytic subunit ATP12A
CC (By similarity). Interacts with regulatory subunit FXYD1 (By
CC similarity). Interacts with regulatory subunit FXYD3 (By similarity).
CC Interacts with NKAIN1, NKAIN2 and NKAIN4 (By similarity). Interacts
CC with MLC1. Part of a complex containing MLC1, TRPV4, AQP4 and HEPACAM.
CC Interacts with KIRREL3 (By similarity). Interacts with OBSCN (via
CC protein kinase domain 1) (By similarity). Interacts with TRAF3 and
CC TRAF6 (By similarity). {ECO:0000250|UniProtKB:P05026,
CC ECO:0000250|UniProtKB:P07340, ECO:0000250|UniProtKB:P14094}.
CC -!- INTERACTION:
CC P05027; P05024: ATP1A1; NbExp=3; IntAct=EBI-9014008, EBI-9014019;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000250|UniProtKB:P07340}; Single-pass type II membrane protein
CC {ECO:0000255}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P14094}. Note=Colocalizes with OBSCN at the
CC intercalated disk and sarcolemma in cardiomyocytes. Localizes in long
CC striations at the level of Z and M lines.
CC {ECO:0000250|UniProtKB:P14094}.
CC -!- DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain
CC and mediates cell adhesion properties. {ECO:0000250}.
CC -!- PTM: Glutathionylated (By similarity). N-glycosylated (By similarity).
CC {ECO:0000250|UniProtKB:P07340, ECO:0000250|UniProtKB:P14094}.
CC -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC {ECO:0000305}.
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DR EMBL; X03937; CAA27575.1; -; mRNA.
DR EMBL; X04635; CAA28301.1; -; mRNA.
DR EMBL; M38313; AAA31001.1; -; mRNA.
DR PIR; A24862; A24862.
DR PIR; I46571; I46571.
DR PIR; I47125; I47125.
DR RefSeq; NP_001001542.1; NM_001001542.1.
DR RefSeq; XP_013852243.1; XM_013996789.1.
DR PDB; 3B8E; X-ray; 3.50 A; B/D=28-73.
DR PDB; 3KDP; X-ray; 3.50 A; B/D=18-303.
DR PDB; 3N23; X-ray; 4.60 A; B/D=27-303.
DR PDB; 3WGU; X-ray; 2.80 A; B/D=1-303.
DR PDB; 3WGV; X-ray; 2.80 A; B/D=1-303.
DR PDB; 4HQJ; X-ray; 4.30 A; B/D=1-303.
DR PDB; 4HYT; X-ray; 3.40 A; B/D=1-303.
DR PDB; 4RES; X-ray; 3.41 A; B/D=1-303.
DR PDB; 4RET; X-ray; 4.00 A; B/D=1-303.
DR PDB; 7D91; X-ray; 3.35 A; B=1-303.
DR PDB; 7D92; X-ray; 3.90 A; B=1-303.
DR PDB; 7D93; X-ray; 3.65 A; B/D=1-303.
DR PDB; 7D94; X-ray; 3.50 A; B/D=1-303.
DR PDB; 7DDF; X-ray; 4.62 A; B/D=1-303.
DR PDB; 7DDH; X-ray; 3.46 A; B/D=1-303.
DR PDB; 7DDI; X-ray; 3.72 A; B/D=1-303.
DR PDB; 7DDK; X-ray; 3.50 A; B/D=1-303.
DR PDB; 7DDL; X-ray; 3.20 A; B/D=1-303.
DR PDB; 7WYS; X-ray; 3.71 A; B/D=1-303.
DR PDB; 7WYT; X-ray; 2.90 A; B/D=1-303.
DR PDBsum; 3B8E; -.
DR PDBsum; 3KDP; -.
DR PDBsum; 3N23; -.
DR PDBsum; 3WGU; -.
DR PDBsum; 3WGV; -.
DR PDBsum; 4HQJ; -.
DR PDBsum; 4HYT; -.
DR PDBsum; 4RES; -.
DR PDBsum; 4RET; -.
DR PDBsum; 7D91; -.
DR PDBsum; 7D92; -.
DR PDBsum; 7D93; -.
DR PDBsum; 7D94; -.
DR PDBsum; 7DDF; -.
DR PDBsum; 7DDH; -.
DR PDBsum; 7DDI; -.
DR PDBsum; 7DDK; -.
DR PDBsum; 7DDL; -.
DR PDBsum; 7WYS; -.
DR PDBsum; 7WYT; -.
DR AlphaFoldDB; P05027; -.
DR SMR; P05027; -.
DR ComplexPortal; CPX-57; Sodium:potassium-exchanging ATPase complex.
DR CORUM; P05027; -.
DR DIP; DIP-60366N; -.
DR IntAct; P05027; 1.
DR STRING; 9823.ENSSSCP00000006713; -.
DR ChEMBL; CHEMBL4524015; -.
DR PaxDb; P05027; -.
DR PeptideAtlas; P05027; -.
DR PRIDE; P05027; -.
DR Ensembl; ENSSSCT00000006901; ENSSSCP00000006713; ENSSSCG00000006296.
DR Ensembl; ENSSSCT00025071802; ENSSSCP00025031098; ENSSSCG00025052482.
DR Ensembl; ENSSSCT00035086630; ENSSSCP00035036104; ENSSSCG00035064350.
DR Ensembl; ENSSSCT00045067159; ENSSSCP00045047697; ENSSSCG00045038671.
DR Ensembl; ENSSSCT00055021364; ENSSSCP00055016922; ENSSSCG00055010846.
DR Ensembl; ENSSSCT00070042092; ENSSSCP00070035369; ENSSSCG00070021088.
DR Ensembl; ENSSSCT00070042253; ENSSSCP00070035513; ENSSSCG00070021088.
DR Ensembl; ENSSSCT00070042300; ENSSSCP00070035557; ENSSSCG00070021088.
DR GeneID; 396898; -.
DR KEGG; ssc:396898; -.
DR CTD; 481; -.
DR VGNC; VGNC:85642; ATP1B1.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR HOGENOM; CLU_057702_2_0_1; -.
DR InParanoid; P05027; -.
DR OMA; ECKAYGQ; -.
DR OrthoDB; 998086at2759; -.
DR BRENDA; 7.2.2.13; 6170.
DR EvolutionaryTrace; P05027; -.
DR Proteomes; UP000008227; Chromosome 4.
DR Proteomes; UP000314985; Chromosome 4.
DR Bgee; ENSSSCG00000006296; Expressed in Ammon's horn and 43 other tissues.
DR ExpressionAtlas; P05027; baseline and differential.
DR Genevisible; P05027; SS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0031090; C:organelle membrane; IEA:Ensembl.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:BHF-UCL.
DR GO; GO:0036126; C:sperm flagellum; IEA:Ensembl.
DR GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR GO; GO:0001671; F:ATPase activator activity; IDA:BHF-UCL.
DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:BHF-UCL.
DR GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
DR GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; IC:BHF-UCL.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0086009; P:membrane repolarization; IDA:BHF-UCL.
DR GO; GO:1903281; P:positive regulation of calcium:sodium antiporter activity; IEA:Ensembl.
DR GO; GO:1903408; P:positive regulation of P-type sodium:potassium-exchanging transporter activity; IDA:BHF-UCL.
DR GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; IDA:BHF-UCL.
DR GO; GO:1903278; P:positive regulation of sodium ion export across plasma membrane; IDA:BHF-UCL.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:BHF-UCL.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:1902600; P:proton transmembrane transport; IC:ComplexPortal.
DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0055119; P:relaxation of cardiac muscle; IEA:Ensembl.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IDA:BHF-UCL.
DR GO; GO:0055085; P:transmembrane transport; IDA:BHF-UCL.
DR Gene3D; 2.60.40.1660; -; 1.
DR InterPro; IPR000402; Na/K_ATPase_sub_beta.
DR InterPro; IPR015565; Na/K_ATPase_sub_beta_chordates.
DR InterPro; IPR038702; Na/K_ATPase_sub_beta_sf.
DR PANTHER; PTHR11523; PTHR11523; 1.
DR PANTHER; PTHR11523:SF10; PTHR11523:SF10; 1.
DR Pfam; PF00287; Na_K-ATPase; 1.
DR TIGRFAMs; TIGR01107; Na_K_ATPase_bet; 1.
DR PROSITE; PS00390; ATPASE_NA_K_BETA_1; 1.
DR PROSITE; PS00391; ATPASE_NA_K_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane; Disulfide bond;
KW Glutathionylation; Glycoprotein; Immunity; Innate immunity; Ion transport;
KW Membrane; Phosphoprotein; Potassium; Potassium transport;
KW Reference proteome; Signal-anchor; Sodium; Sodium transport;
KW Sodium/potassium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..303
FT /note="Sodium/potassium-transporting ATPase subunit beta-1"
FT /id="PRO_0000219099"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..62
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 191..303
FT /note="immunoglobulin-like"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07340"
FT MOD_RES 101
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14094"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 126..149
FT /evidence="ECO:0000250"
FT DISULFID 159..175
FT /evidence="ECO:0000250"
FT DISULFID 213..276
FT /evidence="ECO:0000250"
FT CONFLICT 15..16
FT /note="FI -> LM (in Ref. 3; AAA31001)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="F -> S (in Ref. 1; CAA27575)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="C -> S (in Ref. 3; AAA31001)"
FT /evidence="ECO:0000305"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:4HYT"
FT HELIX 31..58
FT /evidence="ECO:0007829|PDB:3WGU"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:3B8E"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:7DDL"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:7WYT"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:3WGU"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3WGU"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:3WGU"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:4HYT"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:3KDP"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:7WYT"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:3WGU"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:3WGU"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:3WGU"
SQ SEQUENCE 303 AA; 35158 MW; 4B9650EDF5942350 CRC64;
MARGKAKEEG SWKKFIWNSE KKEFLGRTGG SWFKILLFYV IFYGCLAGIF IGTIQVMLLT
ISEFKPTYQD RVAPPGLTQI PQSQKTEISF RPNDPQSYES YVVSIVRFLE KYKDLAQKDD
MIFEDCGNVP SELKERGEYN NERGERKVCR FRLEWLGNCS GLNDETYGYK DGKPCVIIKL
NRVLGFKPKP PKNESLETYP VMKYNPYVLP VHCTGKRDED KEKVGTMEYF GLGGYPGFPL
QYYPYYGKLL QPKYLQPLMA VQFTNLTMDT EIRIECKAYG ENIGYSEKDR FQGRFDVKIE
VKS
