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P05027 (AT1B1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sodium/potassium-transporting ATPase subunit beta-1
Alternative name(s):
Sodium/potassium-dependent ATPase subunit beta-1
Gene names
Name:ATP1B1
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Composed of three subunits: alpha (catalytic), beta and gamma. Interacts with NKAIN1, NKAIN2 and NKAIN4 By similarity.

Subcellular location

Membrane; Single-pass type II membrane protein.

Sequence similarities

Belongs to the X(+)/potassium ATPases subunit beta family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Sodium/potassium-transporting ATPase subunit beta-1
PRO_0000219099

Regions

Topological domain1 – 3434Cytoplasmic Potential
Transmembrane35 – 6228Helical; Signal-anchor for type II membrane protein; Potential
Topological domain63 – 303241Extracellular Potential

Amino acid modifications

Modified residue1011Phosphotyrosine By similarity
Glycosylation1581N-linked (GlcNAc...) By similarity
Glycosylation1931N-linked (GlcNAc...) By similarity
Glycosylation2651N-linked (GlcNAc...) By similarity
Disulfide bond126 ↔ 149 By similarity
Disulfide bond159 ↔ 175 By similarity
Disulfide bond213 ↔ 276 By similarity

Experimental info

Sequence conflict15 – 162FI → LM in AAA31001. Ref.3
Sequence conflict1511F → S in CAA27575. Ref.1
Sequence conflict1591C → S in AAA31001. Ref.3

Secondary structure

....... 303
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05027 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 4B9650EDF5942350

FASTA30335,158
        10         20         30         40         50         60 
MARGKAKEEG SWKKFIWNSE KKEFLGRTGG SWFKILLFYV IFYGCLAGIF IGTIQVMLLT 

        70         80         90        100        110        120 
ISEFKPTYQD RVAPPGLTQI PQSQKTEISF RPNDPQSYES YVVSIVRFLE KYKDLAQKDD 

       130        140        150        160        170        180 
MIFEDCGNVP SELKERGEYN NERGERKVCR FRLEWLGNCS GLNDETYGYK DGKPCVIIKL 

       190        200        210        220        230        240 
NRVLGFKPKP PKNESLETYP VMKYNPYVLP VHCTGKRDED KEKVGTMEYF GLGGYPGFPL 

       250        260        270        280        290        300 
QYYPYYGKLL QPKYLQPLMA VQFTNLTMDT EIRIECKAYG ENIGYSEKDR FQGRFDVKIE 


VKS 

« Hide

References

[1]"Pig kidney Na+,K+-ATPase. Primary structure and spatial organization."
Ovchinnikov Y.A., Modyanov N.N., Broude N.E., Petrukhin K.E., Grishin A.V., Arzamazova N.M., Aldanova N.A., Monastyrskaya G.S., Sverdlov E.D.
FEBS Lett. 201:237-245(1986) [PubMed: 2423371] [Abstract]
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: 2436627] [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: 3036581] [Abstract]
Cited for: TOPOLOGY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03937 mRNA. Translation: CAA27575.1.
X04635 mRNA. Translation: CAA28301.1.
M38313 mRNA. Translation: AAA31001.1.
PIRA24862.
I46571.
I47125.
RefSeqNP_001001542.1. NM_001001542.1.
UniGeneSsc.246.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3B8EX-ray3.50B/D28-73[»]
3KDPX-ray3.50B/D18-303[»]
3N23X-ray4.60B/D27-303[»]
3N2FX-ray4.10B/D27-303[»]
ProteinModelPortalP05027.
SMRP05027. Positions 28-73.
ModBaseSearch...

Protein-protein interaction databases

STRINGP05027.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000006901; ENSSSCP00000006713; ENSSSCG00000006296.
GeneID396898.
KEGGssc:396898.

Organism-specific databases

CTD481.

Phylogenomic databases

HOVERGENHBG050603.

Family and domain databases

InterProIPR000402. ATPase_P-typ_cation-exchng_bsu.
IPR015565. ATPase_P-typ_Na/K-dep_b1su.
[Graphical view]
KOK01540.
PANTHERPTHR11523. ATPase_H_Na/K_b. 1 hit.
PTHR11523:SF10. Na/K_ATPaseBeta1. 1 hit.
PfamPF00287. Na_K-ATPase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01107. Na_K_ATPase_bet. 1 hit.
PROSITEPS00390. ATPASE_NA_K_BETA_1. 1 hit.
PS00391. ATPASE_NA_K_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAT1B1_PIG
AccessionPrimary (citable) accession number: P05027
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: October 1, 1996
Last modified: November 16, 2011
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families