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Protein

Sodium/potassium-transporting ATPase subunit beta-2

Gene

Atp1b2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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 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

GO - Biological processi

Keywordsi

Biological processCell adhesion, Ion transport, Potassium transport, Sodium transport, Sodium/potassium transport, Transport
LigandPotassium, Sodium

Enzyme and pathway databases

SABIO-RKiP13638

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2171 Atp1b2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 39CytoplasmicSequence analysisAdd BLAST39
Transmembranei40 – 67Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST28
Topological domaini68 – 290ExtracellularSequence analysisAdd BLAST223

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002191061 – 290Sodium/potassium-transporting ATPase subunit beta-2Add BLAST290

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi96N-linked (GlcNAc...) asparagine; alternateSequence analysis1
Glycosylationi96N-linked (HexNAc...) asparagine; alternateCombined sources1
Glycosylationi118N-linked (GlcNAc...) asparagine; alternateSequence analysis1
Glycosylationi118N-linked (HexNAc...) asparagine; alternateCombined sources1
Disulfide bondi129 ↔ 150By similarity
Glycosylationi153N-linked (GlcNAc...) asparagine; alternateSequence analysis1
Glycosylationi153N-linked (HexNAc...) asparagine; alternateCombined sources1
Glycosylationi159N-linked (GlcNAc...) asparagine; alternateSequence analysis1
Glycosylationi159N-linked (HexNAc...) asparagine; alternateCombined sources1
Disulfide bondi160 ↔ 177By similarity
Glycosylationi193N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi197N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi200 ↔ 261By similarity
Glycosylationi238N-linked (GlcNAc...) asparagine; alternateSequence analysis1
Glycosylationi238N-linked (HexNAc...) asparagine; alternateCombined sources1
Glycosylationi250N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP13638
PRIDEiP13638

PTM databases

iPTMnetiP13638
PhosphoSitePlusiP13638
SwissPalmiP13638
UniCarbKBiP13638

Interactioni

Subunit structurei

The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit.Curated

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015076

Structurei

3D structure databases

ProteinModelPortaliP13638
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni193 – 290immunoglobulin-likeBy similarityAdd BLAST98

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

Gene3Di2.60.40.1660, 1 hit
InterProiView protein in InterPro
IPR000402 Na/K_ATPase_sub_beta
IPR038702 Na/K_ATPase_sub_beta_sf
PANTHERiPTHR11523 PTHR11523, 1 hit
PfamiView protein in Pfam
PF00287 Na_K-ATPase, 1 hit
TIGRFAMsiTIGR01107 Na_K_ATPase_bet, 1 hit
PROSITEiView protein in PROSITE
PS00390 ATPASE_NA_K_BETA_1, 1 hit
PS00391 ATPASE_NA_K_BETA_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiAT1B2_RAT
AccessioniPrimary (citable) accession number: P13638
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 25, 2018
This is version 112 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health