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Protein

Sodium/potassium-transporting ATPase subunit beta-2

Gene

Atp1b2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 exact function of the beta-2 subunit is not known.
Mediates cell adhesion of neurons and astrocytes, and promotes neurite outgrowth.By similarity

GO - Molecular functioni

  • sodium:potassium-exchanging ATPase activity Source: RGD

GO - Biological processi

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

SABIO-RKP13638.

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium/potassium-transporting ATPase subunit beta-2
Alternative name(s):
Sodium/potassium-dependent ATPase subunit beta-2
Gene namesi
Name:Atp1b2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2171. Atp1b2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3939CytoplasmicSequence analysisAdd
BLAST
Transmembranei40 – 6728Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini68 – 290223ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: RGD
  • sodium:potassium-exchanging ATPase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290Sodium/potassium-transporting ATPase subunit beta-2PRO_0000219106Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi96 – 961N-linked (GlcNAc...)Sequence analysis
Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence analysis
Disulfide bondi129 ↔ 150By similarity
Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence analysis
Glycosylationi159 – 1591N-linked (GlcNAc...)Sequence analysis
Disulfide bondi160 ↔ 177By similarity
Glycosylationi193 – 1931N-linked (GlcNAc...)Sequence analysis
Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence analysis
Disulfide bondi200 ↔ 261By similarity
Glycosylationi238 – 2381N-linked (GlcNAc...)Sequence analysis
Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP13638.
PRIDEiP13638.

PTM databases

iPTMnetiP13638.
PhosphoSiteiP13638.
SwissPalmiP13638.
UniCarbKBiP13638.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015076.

Structurei

3D structure databases

ProteinModelPortaliP13638.
SMRiP13638. Positions 33-78.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni193 – 29098immunoglobulin-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.
HOVERGENiHBG050603.
InParanoidiP13638.
PhylomeDBiP13638.

Family and domain databases

InterProiIPR000402. Na/K_ATPase_sub_beta.
[Graphical view]
PANTHERiPTHR11523. PTHR11523. 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.

P13638-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVIQKEKKSC GQVVEEWKEF VWNPRTHQFM GRTGTSWAFI LLFYLVFYGF
60 70 80 90 100
LTAMFTLTMW VMLQTVSDHT PKYQDRLATP GLMIRPKTEN LDVIVNISDT
110 120 130 140 150
ESWDQHVQKL NKFLEPYNDS IQAQKNDVCR PGRYYEQPDN GVLNYPKRAC
160 170 180 190 200
QFNRTQLGNC SGIGDPTHYG YSTGQPCVFI KMNRVINFYA GANQSMNVTC
210 220 230 240 250
VGKKDEDAEN LGHFIMFPAN GNIDLMYFPY YGKKFHVNYT QPLVAVKFLN
260 270 280 290
VTPNVEVNVE CRINAANIAT DDERDKFAAR VAFKLRINKA
Length:290
Mass (Da):33,412
Last modified:January 1, 1990 - v1
Checksum:i480ACDCD27A9E086
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04629 mRNA. Translation: AAA40782.1.
U45946 mRNA. Translation: AAC52918.1.
D90048 Genomic DNA. Translation: BAA14101.1.
PIRiA32459.
UniGeneiRn.10624.

Genome annotation databases

UCSCiRGD:2171. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04629 mRNA. Translation: AAA40782.1.
U45946 mRNA. Translation: AAC52918.1.
D90048 Genomic DNA. Translation: BAA14101.1.
PIRiA32459.
UniGeneiRn.10624.

3D structure databases

ProteinModelPortaliP13638.
SMRiP13638. Positions 33-78.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015076.

PTM databases

iPTMnetiP13638.
PhosphoSiteiP13638.
SwissPalmiP13638.
UniCarbKBiP13638.

Proteomic databases

PaxDbiP13638.
PRIDEiP13638.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2171. rat.

Organism-specific databases

RGDi2171. Atp1b2.

Phylogenomic databases

eggNOGiKOG3927. Eukaryota.
ENOG411150A. LUCA.
HOVERGENiHBG050603.
InParanoidiP13638.
PhylomeDBiP13638.

Enzyme and pathway databases

SABIO-RKP13638.

Miscellaneous databases

PROiP13638.

Family and domain databases

InterProiIPR000402. Na/K_ATPase_sub_beta.
[Graphical view]
PANTHERiPTHR11523. PTHR11523. 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. "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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.

Entry informationi

Entry nameiAT1B2_RAT
AccessioniPrimary (citable) accession number: P13638
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: July 6, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.