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Protein

Sodium/potassium-transporting ATPase subunit beta-1

Gene

ATP1B1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na+ and K+ ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane.
Involved in cell adhesion and establishing epithelial cell polarity.By similarity

GO - Molecular functioni

  • ATPase binding Source: BHF-UCL
  • sodium:potassium-exchanging ATPase activity Source: BHF-UCL

GO - Biological processi

  • ATP hydrolysis coupled transmembrane transport Source: BHF-UCL
  • cell adhesion Source: UniProtKB-KW
  • cellular potassium ion homeostasis Source: BHF-UCL
  • cellular sodium ion homeostasis Source: BHF-UCL
  • establishment or maintenance of transmembrane electrochemical gradient Source: BHF-UCL
  • membrane repolarization Source: BHF-UCL
  • potassium ion import Source: BHF-UCL
  • potassium ion import across plasma membrane Source: BHF-UCL
  • sodium ion export from cell Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Ion transport, Potassium transport, Sodium transport, Sodium/potassium transport, Transport

Keywords - Ligandi

Potassium, Sodium

Enzyme and pathway databases

ReactomeiR-SSC-210991. Basigin interactions.
R-SSC-5578775. Ion homeostasis.
R-SSC-936837. Ion transport by P-type ATPases.

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium/potassium-transporting ATPase subunit beta-1
Alternative name(s):
Sodium/potassium-dependent ATPase subunit beta-1
Gene namesi
Name:ATP1B1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3434CytoplasmicSequence analysisAdd
BLAST
Transmembranei35 – 6228Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini63 – 303241ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • sodium:potassium-exchanging ATPase complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303Sodium/potassium-transporting ATPase subunit beta-1PRO_0000219099Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111PhosphoserineBy similarity
Modified residuei101 – 1011PhosphotyrosineBy similarity
Disulfide bondi126 ↔ 149By similarity
Glycosylationi158 – 1581N-linked (GlcNAc...)By similarity
Disulfide bondi159 ↔ 175By similarity
Glycosylationi193 – 1931N-linked (GlcNAc...)By similarity
Disulfide bondi213 ↔ 276By similarity
Glycosylationi265 – 2651N-linked (GlcNAc...)By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP05027.

Expressioni

Gene expression databases

GenevisibleiP05027. SS.

Interactioni

Subunit structurei

Composed of three subunits: alpha (catalytic), beta and gamma. Interacts with NKAIN1, NKAIN2 and NKAIN4 (By similarity). Interacts with MLC1. Part of a complex containing MLC1, TRPV4, AQP4 and HEPACAM. Interacts with KIRREL3 (By similarity).By similarity

GO - Molecular functioni

  • ATPase binding Source: BHF-UCL

Protein-protein interaction databases

DIPiDIP-60366N.
IntActiP05027. 1 interaction.
STRINGi9823.ENSSSCP00000006713.

Structurei

Secondary structure

1
303
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 154Combined sources
Beta strandi19 – 213Combined sources
Beta strandi24 – 274Combined sources
Helixi31 – 5828Combined sources
Turni59 – 613Combined sources
Beta strandi63 – 653Combined sources
Helixi70 – 723Combined sources
Beta strandi77 – 815Combined sources
Beta strandi84 – 896Combined sources
Helixi96 – 983Combined sources
Helixi99 – 10911Combined sources
Turni114 – 1163Combined sources
Turni120 – 1223Combined sources
Beta strandi139 – 1435Combined sources
Turni153 – 1553Combined sources
Beta strandi156 – 1605Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi175 – 1806Combined sources
Beta strandi193 – 1953Combined sources
Beta strandi200 – 2023Combined sources
Turni205 – 2073Combined sources
Beta strandi208 – 2136Combined sources
Beta strandi215 – 2206Combined sources
Beta strandi227 – 2304Combined sources
Helixi232 – 2343Combined sources
Beta strandi236 – 2394Combined sources
Helixi240 – 2423Combined sources
Helixi247 – 2504Combined sources
Beta strandi258 – 2625Combined sources
Beta strandi269 – 2746Combined sources
Beta strandi276 – 2783Combined sources
Beta strandi280 – 2823Combined sources
Beta strandi292 – 2943Combined sources
Beta strandi297 – 3004Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3B8EX-ray3.50B/D28-73[»]
3KDPX-ray3.50B/D18-303[»]
3N23X-ray4.60B/D27-303[»]
3WGUX-ray2.80B/D1-303[»]
3WGVX-ray2.80B/D1-303[»]
4HQJX-ray4.30B/D1-303[»]
4HYTX-ray3.40B/D1-303[»]
4RESX-ray3.41B/D1-303[»]
4RETX-ray4.00B/D1-303[»]
ProteinModelPortaliP05027.
SMRiP05027. Positions 28-73.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05027.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 303113immunoglobulin-likeBy similarityAdd
BLAST

Domaini

The C-terminal lobe folds into an immunoglobulin-like domain and mediates cell adhesion properties.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3927. Eukaryota.
ENOG411150A. LUCA.
HOGENOMiHOG000039248.
HOVERGENiHBG050603.
InParanoidiP05027.
KOiK01540.

Family and domain databases

InterProiIPR000402. Na/K_ATPase_sub_beta.
IPR015565. Na/K_ATPase_sub_beta_chordates.
[Graphical view]
PANTHERiPTHR11523. PTHR11523. 1 hit.
PTHR11523:SF10. PTHR11523:SF10. 1 hit.
PfamiPF00287. Na_K-ATPase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01107. Na_K_ATPase_bet. 1 hit.
PROSITEiPS00390. ATPASE_NA_K_BETA_1. 1 hit.
PS00391. ATPASE_NA_K_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05027-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARGKAKEEG SWKKFIWNSE KKEFLGRTGG SWFKILLFYV IFYGCLAGIF
60 70 80 90 100
IGTIQVMLLT ISEFKPTYQD RVAPPGLTQI PQSQKTEISF RPNDPQSYES
110 120 130 140 150
YVVSIVRFLE KYKDLAQKDD MIFEDCGNVP SELKERGEYN NERGERKVCR
160 170 180 190 200
FRLEWLGNCS GLNDETYGYK DGKPCVIIKL NRVLGFKPKP PKNESLETYP
210 220 230 240 250
VMKYNPYVLP VHCTGKRDED KEKVGTMEYF GLGGYPGFPL QYYPYYGKLL
260 270 280 290 300
QPKYLQPLMA VQFTNLTMDT EIRIECKAYG ENIGYSEKDR FQGRFDVKIE

VKS
Length:303
Mass (Da):35,158
Last modified:October 1, 1996 - v2
Checksum:i4B9650EDF5942350
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 162FI → LM in AAA31001 (PubMed:2436627).Curated
Sequence conflicti151 – 1511F → S in CAA27575 (PubMed:2423371).Curated
Sequence conflicti159 – 1591C → S in AAA31001 (PubMed:2436627).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03937 mRNA. Translation: CAA27575.1.
X04635 mRNA. Translation: CAA28301.1.
M38313 mRNA. Translation: AAA31001.1.
PIRiA24862.
I46571.
I47125.
RefSeqiNP_001001542.1. NM_001001542.1.
XP_013852243.1. XM_013996789.1.
UniGeneiSsc.246.

Genome annotation databases

GeneIDi106510095.
396898.
KEGGissc:396898.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03937 mRNA. Translation: CAA27575.1.
X04635 mRNA. Translation: CAA28301.1.
M38313 mRNA. Translation: AAA31001.1.
PIRiA24862.
I46571.
I47125.
RefSeqiNP_001001542.1. NM_001001542.1.
XP_013852243.1. XM_013996789.1.
UniGeneiSsc.246.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3B8EX-ray3.50B/D28-73[»]
3KDPX-ray3.50B/D18-303[»]
3N23X-ray4.60B/D27-303[»]
3WGUX-ray2.80B/D1-303[»]
3WGVX-ray2.80B/D1-303[»]
4HQJX-ray4.30B/D1-303[»]
4HYTX-ray3.40B/D1-303[»]
4RESX-ray3.41B/D1-303[»]
4RETX-ray4.00B/D1-303[»]
ProteinModelPortaliP05027.
SMRiP05027. Positions 28-73.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60366N.
IntActiP05027. 1 interaction.
STRINGi9823.ENSSSCP00000006713.

Proteomic databases

PaxDbiP05027.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi106510095.
396898.
KEGGissc:396898.

Organism-specific databases

CTDi481.

Phylogenomic databases

eggNOGiKOG3927. Eukaryota.
ENOG411150A. LUCA.
HOGENOMiHOG000039248.
HOVERGENiHBG050603.
InParanoidiP05027.
KOiK01540.

Enzyme and pathway databases

ReactomeiR-SSC-210991. Basigin interactions.
R-SSC-5578775. Ion homeostasis.
R-SSC-936837. Ion transport by P-type ATPases.

Miscellaneous databases

EvolutionaryTraceiP05027.

Gene expression databases

GenevisibleiP05027. SS.

Family and domain databases

InterProiIPR000402. Na/K_ATPase_sub_beta.
IPR015565. Na/K_ATPase_sub_beta_chordates.
[Graphical view]
PANTHERiPTHR11523. PTHR11523. 1 hit.
PTHR11523:SF10. PTHR11523:SF10. 1 hit.
PfamiPF00287. Na_K-ATPase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01107. Na_K_ATPase_bet. 1 hit.
PROSITEiPS00390. ATPASE_NA_K_BETA_1. 1 hit.
PS00391. ATPASE_NA_K_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Nucleotide sequence of cDNA and primary structure of the beta-subunit of Na+,K+-ATPase from pig kidneys."
    Ovchinnikov Y.A., Broude N.E., Petrukhin K.E., Grishin A.V., Kiyatkin N.I., Arzamazova N.M., Gevondyan N.M., Chertova E.N., Melkov A.M., Smirnov Y.V., Malyshev I.V., Monastyrskaya G.S., Modyanov N.N.
    Dokl. Biochem. 287:149-152(1986)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  3. "Primary structure of the beta-subunit of Na+,K+-ATPase from the swine kidney. II. Reverse transcription, cloning of mRNA, complete nucleotide sequence corresponding to the structural region of the gene."
    Broude N.E., Monastyrskaya G.S., Petrukhin K.E., Grishin A.V., Kiyatkin N.I., Melkov A.M., Smirnov Y.V., Sverdiov V.E., Malyshev I.V., Modyanov N.N.
    Bioorg. Khim. 13:14-19(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Detailed structural analysis of exposed domains of membrane-bound Na+,K+-ATPase. A model of transmembrane arrangement."
    Ovchinnikov Y.A., Arzamazova N.M., Arystarkhova E.A., Gevondyan N.M., Aldanova N.A., Modyanov N.N.
    FEBS Lett. 217:269-274(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.

Entry informationi

Entry nameiAT1B1_PIG
AccessioniPrimary (citable) accession number: P05027
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: October 1, 1996
Last modified: March 16, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.