AT1B2_MOUSE
ID AT1B2_MOUSE Reviewed; 290 AA.
AC P14231;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta-2;
DE AltName: Full=Adhesion molecule in glia;
DE Short=AMOG;
DE AltName: Full=Sodium/potassium-dependent ATPase subunit beta-2;
GN Name=Atp1b2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION IN ADHESION.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=1688561; DOI=10.1083/jcb.110.1.165;
RA Gloor S.M., Antonicek H., Sweadner K., Pagliusi S., Frank R., Moos M.,
RA Schachner M.;
RT "The adhesion molecule on glia (AMOG) is a homologue of the beta subunit of
RT the Na,K-ATPase.";
RL J. Cell Biol. 110:165-174(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=1701244; DOI=10.1093/nar/18.22.6695;
RA Magyar J.P., Schachner M.;
RT "Genomic structure of the adhesion molecule on glia (AMOG, Na/K-ATPase beta
RT 2 subunit).";
RL Nucleic Acids Res. 18:6695-6696(1990).
RN [3]
RP SEQUENCE REVISION.
RA Magyar J.P.;
RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1663071; DOI=10.1016/0888-7543(91)90152-5;
RA Shyjan A.W., Canfield V.A., Levenson R.;
RT "Evolution of the Na,K- and H,K-ATPase beta subunit gene family: structure
RT of the murine Na,K-ATPase beta 2 subunit gene.";
RL Genomics 11:435-442(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 9-25; 155-181 AND 248-274, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP FUNCTION IN ADHESION.
RX PubMed=7504672; DOI=10.1016/s0021-9258(19)74309-9;
RA Muller-Husmann G., Gloor S., Schachner M.;
RT "Functional characterization of beta isoforms of murine Na,K-ATPase. The
RT adhesion molecule on glia (AMOG/beta 2), but not beta 1, promotes neurite
RT outgrowth.";
RL J. Biol. Chem. 268:26260-26267(1993).
RN [8]
RP INTERACTION WITH BSG.
RX PubMed=12558975; DOI=10.1046/j.1471-4159.2003.01537.x;
RA Heller M., von der Ohe M., Kleene R., Mohajeri M.H., Schachner M.;
RT "The immunoglobulin-superfamily molecule basigin is a binding protein for
RT oligomannosidic carbohydrates: an anti-idiotypic approach.";
RL J. Neurochem. 84:557-565(2003).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-118 AND ASN-238.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: This is the non-catalytic component of the active enzyme,
CC which catalyzes the hydrolysis of ATP coupled with the exchange of
CC Na(+) and K(+) ions across the plasma membrane. The exact function of
CC the beta-2 subunit is not known.
CC -!- FUNCTION: Mediates cell adhesion of neurons and astrocytes, and
CC promotes neurite outgrowth.
CC -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC additional regulatory subunit. Interacts with isoform 2 of BSG
CC (PubMed:12558975). {ECO:0000269|PubMed:12558975, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein.
CC -!- DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain
CC and mediates cell adhesion properties. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X16645; CAA34638.1; -; mRNA.
DR EMBL; X56007; CAA39482.1; -; Genomic_DNA.
DR EMBL; M60897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042467; AAH42467.1; -; mRNA.
DR EMBL; BC058763; AAH58763.1; -; mRNA.
DR CCDS; CCDS24898.1; -.
DR PIR; A34057; A34057.
DR PIR; S14235; S14235.
DR RefSeq; NP_038201.1; NM_013415.5.
DR AlphaFoldDB; P14231; -.
DR SMR; P14231; -.
DR BioGRID; 198245; 8.
DR IntAct; P14231; 2.
DR MINT; P14231; -.
DR STRING; 10090.ENSMUSP00000047353; -.
DR GlyConnect; 2728; 33 N-Linked glycans (8 sites).
DR GlyGen; P14231; 8 sites, 32 N-linked glycans (8 sites).
DR iPTMnet; P14231; -.
DR PhosphoSitePlus; P14231; -.
DR SwissPalm; P14231; -.
DR PaxDb; P14231; -.
DR PeptideAtlas; P14231; -.
DR PRIDE; P14231; -.
DR ProteomicsDB; 277265; -.
DR Antibodypedia; 2415; 253 antibodies from 31 providers.
DR DNASU; 11932; -.
DR Ensembl; ENSMUST00000047889; ENSMUSP00000047353; ENSMUSG00000041329.
DR GeneID; 11932; -.
DR KEGG; mmu:11932; -.
DR UCSC; uc007jqo.1; mouse.
DR CTD; 482; -.
DR MGI; MGI:88109; Atp1b2.
DR VEuPathDB; HostDB:ENSMUSG00000041329; -.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR HOGENOM; CLU_057702_1_1_1; -.
DR InParanoid; P14231; -.
DR OMA; VCRPGHY; -.
DR OrthoDB; 998086at2759; -.
DR PhylomeDB; P14231; -.
DR TreeFam; TF314618; -.
DR Reactome; R-MMU-210991; Basigin interactions.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 11932; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Atp1b2; mouse.
DR PRO; PR:P14231; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P14231; protein.
DR Bgee; ENSMUSG00000041329; Expressed in retinal neural layer and 195 other tissues.
DR ExpressionAtlas; P14231; baseline and differential.
DR Genevisible; P14231; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0097450; C:astrocyte end-foot; IDA:ARUK-UCL.
DR GO; GO:0097449; C:astrocyte projection; IDA:ARUK-UCL.
DR GO; GO:0044298; C:cell body membrane; IDA:ARUK-UCL.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0031253; C:cell projection membrane; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0098984; C:neuron to neuron synapse; IDA:ARUK-UCL.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; ISO:MGI.
DR GO; GO:0001671; F:ATPase activator activity; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0031589; P:cell-substrate adhesion; IDA:ARUK-UCL.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; ISO:MGI.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; ISO:MGI.
DR GO; GO:0021670; P:lateral ventricle development; IMP:ARUK-UCL.
DR GO; GO:0086009; P:membrane repolarization; ISO:MGI.
DR GO; GO:0061744; P:motor behavior; IMP:ARUK-UCL.
DR GO; GO:1903976; P:negative regulation of glial cell migration; IDA:ARUK-UCL.
DR GO; GO:0021944; P:neuronal-glial interaction involved in hindbrain glial-mediated radial cell migration; IMP:ARUK-UCL.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:ARUK-UCL.
DR GO; GO:0120036; P:plasma membrane bounded cell projection organization; IMP:ARUK-UCL.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:ARUK-UCL.
DR GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; ISO:MGI.
DR GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:1903278; P:positive regulation of sodium ion export across plasma membrane; ISO:MGI.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0001895; P:retina homeostasis; IMP:ARUK-UCL.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; ISO:MGI.
DR GO; GO:0021678; P:third ventricle development; IMP:ARUK-UCL.
DR Gene3D; 2.60.40.1660; -; 1.
DR InterPro; IPR000402; Na/K_ATPase_sub_beta.
DR InterPro; IPR038702; Na/K_ATPase_sub_beta_sf.
DR PANTHER; PTHR11523; PTHR11523; 1.
DR Pfam; PF00287; Na_K-ATPase; 1.
DR TIGRFAMs; TIGR01107; Na_K_ATPase_bet; 1.
DR PROSITE; PS00390; ATPASE_NA_K_BETA_1; 1.
DR PROSITE; PS00391; ATPASE_NA_K_BETA_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Ion transport; Membrane; Potassium; Potassium transport;
KW Reference proteome; Signal-anchor; Sodium; Sodium transport;
KW Sodium/potassium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..290
FT /note="Sodium/potassium-transporting ATPase subunit beta-2"
FT /id="PRO_0000219105"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..67
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 193..290
FT /note="immunoglobulin-like"
FT /evidence="ECO:0000250"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 129..150
FT /evidence="ECO:0000250"
FT DISULFID 160..177
FT /evidence="ECO:0000250"
FT DISULFID 200..261
FT /evidence="ECO:0000250"
SQ SEQUENCE 290 AA; 33344 MW; 731836AFB23198D4 CRC64;
MVIQKEKKSC GQVVEEWKEF VWNPRTHQFM GRTGTSWAFI LLFYLVFYGF LTAMFSLTMW
VMLQTVSDHT PKYQDRLATP GLMIRPKTEN LDVIVNISDT ESWGQHVQKL NKFLEPYNDS
IQAQKNDVCR PGRYYEQPDN GVLNYPKRAC QFNRTQLGDC SGIGDPTHYG YSTGQPCVFI
KMNRVINFYA GANQSMNVTC VGKRDEDAEN LGHFVMFPAN GSIDLMYFPY YGKKFHVNYT
QPLVAVKFLN VTPNVEVNVE CRINAANIAT DDERDKFAGR VAFKLRINKT
