AT1B2_RAT
ID AT1B2_RAT Reviewed; 290 AA.
AC P13638;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta-2;
DE AltName: Full=Sodium/potassium-dependent ATPase subunit beta-2;
GN Name=Atp1b2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2538450; DOI=10.1016/s0021-9258(18)83787-5;
RA Martin-Vasallo P., Dackowski W., Emanuel J.R., Levenson R.;
RT "Identification of a putative isoform of the Na,K-ATPase beta subunit.
RT Primary structure and tissue-specific expression.";
RL J. Biol. Chem. 264:4613-4618(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retinal pigment epithelium;
RX PubMed=8918259; DOI=10.1016/0378-1119(96)00258-2;
RA Ruiz A.C., Bhat S.P., Bok D.;
RT "Expression and synthesis of the Na,K-ATPase beta 2 subunit in human
RT retinal pigment epithelium.";
RL Gene 176:237-242(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
RX PubMed=2170236; DOI=10.1016/0378-1119(90)90099-d;
RA Kawakami K., Okamoto H., Yagawa Y., Nagano K.;
RT "Regulation of Na+,K(+)-ATPase. II. Cloning and analysis of the 5'-flanking
RT region of the rat NKAB2 gene encoding the beta 2 subunit.";
RL Gene 91:271-274(1990).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=14749213; DOI=10.1152/ajpcell.00393.2003;
RA Pestov N.B., Korneenko T.V., Radkov R., Zhao H., Shakhparonov M.I.,
RA Modyanov N.N.;
RT "Identification of the beta-subunit for nongastric H-K-ATPase in rat
RT anterior prostate.";
RL Am. J. Physiol. 286:C1229-C1237(2004).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-96; ASN-118; ASN-153; ASN-159
RP AND ASN-238, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
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. {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250|UniProtKB:P14231, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain (at protein level).
CC {ECO:0000269|PubMed:14749213}.
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}.
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DR EMBL; J04629; AAA40782.1; -; mRNA.
DR EMBL; U45946; AAC52918.1; -; mRNA.
DR EMBL; D90048; BAA14101.1; -; Genomic_DNA.
DR PIR; A32459; A32459.
DR AlphaFoldDB; P13638; -.
DR SMR; P13638; -.
DR IntAct; P13638; 1.
DR MINT; P13638; -.
DR STRING; 10116.ENSRNOP00000015076; -.
DR GlyGen; P13638; 7 sites, 29 N-linked glycans (4 sites).
DR iPTMnet; P13638; -.
DR PhosphoSitePlus; P13638; -.
DR SwissPalm; P13638; -.
DR PaxDb; P13638; -.
DR PRIDE; P13638; -.
DR UCSC; RGD:2171; rat.
DR RGD; 2171; Atp1b2.
DR eggNOG; KOG3927; Eukaryota.
DR InParanoid; P13638; -.
DR PhylomeDB; P13638; -.
DR Reactome; R-RNO-210991; Basigin interactions.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR Reactome; R-RNO-936837; Ion transport by P-type ATPases.
DR SABIO-RK; P13638; -.
DR PRO; PR:P13638; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0097450; C:astrocyte end-foot; ISO:RGD.
DR GO; GO:0097449; C:astrocyte projection; ISO:RGD.
DR GO; GO:0044298; C:cell body membrane; ISO:RGD.
DR GO; GO:0071944; C:cell periphery; IDA:ARUK-UCL.
DR GO; GO:0031253; C:cell projection membrane; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:ARUK-UCL.
DR GO; GO:0098984; C:neuron to neuron synapse; ISO:RGD.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:ARUK-UCL.
DR GO; GO:0001671; F:ATPase activator activity; ISO:RGD.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IDA:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ARUK-UCL.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
DR GO; GO:0031589; P:cell-substrate adhesion; ISO:RGD.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; ISO:RGD.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; ISO:RGD.
DR GO; GO:0021670; P:lateral ventricle development; ISO:RGD.
DR GO; GO:0086009; P:membrane repolarization; ISO:RGD.
DR GO; GO:0061744; P:motor behavior; ISO:RGD.
DR GO; GO:1903976; P:negative regulation of glial cell migration; ISO:RGD.
DR GO; GO:0021944; P:neuronal-glial interaction involved in hindbrain glial-mediated radial cell migration; ISO:RGD.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISO:RGD.
DR GO; GO:0120036; P:plasma membrane bounded cell projection organization; ISO:RGD.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:RGD.
DR GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; ISO:RGD.
DR GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:1903278; P:positive regulation of sodium ion export across plasma membrane; ISO:RGD.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0001895; P:retina homeostasis; ISO:RGD.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; ISO:RGD.
DR GO; GO:0021678; P:third ventricle development; ISO:RGD.
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; Disulfide bond; Glycoprotein; Ion transport;
KW Membrane; Potassium; Potassium transport; Reference proteome;
KW Signal-anchor; Sodium; Sodium transport; Sodium/potassium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..290
FT /note="Sodium/potassium-transporting ATPase subunit beta-2"
FT /id="PRO_0000219106"
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:0007744|PubMed:24090084"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
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 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
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; 33412 MW; 480ACDCD27A9E086 CRC64;
MVIQKEKKSC GQVVEEWKEF VWNPRTHQFM GRTGTSWAFI LLFYLVFYGF LTAMFTLTMW
VMLQTVSDHT PKYQDRLATP GLMIRPKTEN LDVIVNISDT ESWDQHVQKL NKFLEPYNDS
IQAQKNDVCR PGRYYEQPDN GVLNYPKRAC QFNRTQLGNC SGIGDPTHYG YSTGQPCVFI
KMNRVINFYA GANQSMNVTC VGKKDEDAEN LGHFIMFPAN GNIDLMYFPY YGKKFHVNYT
QPLVAVKFLN VTPNVEVNVE CRINAANIAT DDERDKFAAR VAFKLRINKA
