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P13638 (AT1B2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Sodium/potassium-transporting ATPase subunit beta-2
Alternative name(s):
Sodium/potassium-dependent ATPase subunit beta-2
Gene names
Name:Atp1b2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 exact function of the beta-2 subunit is not known.

Subunit structure

Composed of three subunits: alpha (catalytic), beta and gamma.

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 – 290290Sodium/potassium-transporting ATPase subunit beta-2
PRO_0000219106

Regions

Topological domain1 – 3939Cytoplasmic Potential
Transmembrane40 – 6728Helical; Signal-anchor for type II membrane protein; Potential
Topological domain68 – 290223Extracellular Potential

Amino acid modifications

Glycosylation961N-linked (GlcNAc...) Potential
Glycosylation1181N-linked (GlcNAc...) Potential
Glycosylation1531N-linked (GlcNAc...) Potential
Glycosylation1591N-linked (GlcNAc...) Potential
Glycosylation1931N-linked (GlcNAc...) Potential
Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation2381N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Potential
Disulfide bond129 ↔ 150 By similarity
Disulfide bond160 ↔ 177 By similarity
Disulfide bond200 ↔ 261 By similarity

Sequences

Sequence LengthMass (Da)Tools
P13638 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 480ACDCD27A9E086

FASTA29033,412
        10         20         30         40         50         60 
MVIQKEKKSC GQVVEEWKEF VWNPRTHQFM GRTGTSWAFI LLFYLVFYGF LTAMFTLTMW 

        70         80         90        100        110        120 
VMLQTVSDHT PKYQDRLATP GLMIRPKTEN LDVIVNISDT ESWDQHVQKL NKFLEPYNDS 

       130        140        150        160        170        180 
IQAQKNDVCR PGRYYEQPDN GVLNYPKRAC QFNRTQLGNC SGIGDPTHYG YSTGQPCVFI 

       190        200        210        220        230        240 
KMNRVINFYA GANQSMNVTC VGKKDEDAEN LGHFIMFPAN GNIDLMYFPY YGKKFHVNYT 

       250        260        270        280        290 
QPLVAVKFLN VTPNVEVNVE CRINAANIAT DDERDKFAAR VAFKLRINKA 

« Hide

References

[1]"Identification of a putative isoform of the Na,K-ATPase beta subunit. Primary structure and tissue-specific expression."
Martin-Vasallo P., Dackowski W., Emanuel J.R., Levenson R.
J. Biol. Chem. 264:4613-4618(1989) [PubMed: 2538450] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Expression and synthesis of the Na,K-ATPase beta 2 subunit in human retinal pigment epithelium."
Ruiz A.C., Bhat S.P., Bok D.
Gene 176:237-242(1996) [PubMed: 8918259] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retinal pigment epithelium.
[3]"Regulation of Na+,K(+)-ATPase. II. Cloning and analysis of the 5'-flanking region of the rat NKAB2 gene encoding the beta 2 subunit."
Kawakami K., Okamoto H., Yagawa Y., Nagano K.
Gene 91:271-274(1990) [PubMed: 2170236] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04629 mRNA. Translation: AAA40782.1.
U45946 mRNA. Translation: AAC52918.1.
D90048 Genomic DNA. Translation: BAA14101.1.
IPIIPI00203440.
PIRA32459.
UniGeneRn.10624.

3D structure databases

ProteinModelPortalP13638.
SMRP13638. Positions 33-78.
ModBaseSearch...

PTM databases

PhosphoSiteP13638.

Proteomic databases

PRIDEP13638.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD2171. Atp1b2.

Phylogenomic databases

eggNOGmaNOG16450.
HOVERGENHBG050603.

Gene expression databases

GenevestigatorP13638.

Family and domain databases

InterProIPR000402. ATPase_P-typ_cation-exchng_bsu.
[Graphical view]
PANTHERPTHR11523. ATPase_H_Na/K_b. 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 nameAT1B2_RAT
AccessionPrimary (citable) accession number: P13638
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: September 21, 2011
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families