ID   AT1B2_OCHCU             Reviewed;         290 AA.
AC   Q5J583;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit beta-2;
DE   AltName: Full=Sodium/potassium-dependent ATPase subunit beta-2;
GN   Name=ATP1B2; Synonyms=NKA1B2;
OS   Ochotona curzoniae (Black-lipped pika).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Ochotonidae; Ochotona.
OX   NCBI_TaxID=130825;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Zhang C., Shang A., Hou B., Ge R.;
RT   "Na+-K+-ATPase beta 2 subunit is highly conserved in Ochotona curzoniae
RT   (pika).";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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 BSG (By similarity).
CC       {ECO:0000250|UniProtKB:P14231, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
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; AY505494; AAS84453.1; -; mRNA.
DR   AlphaFoldDB; Q5J583; -.
DR   SMR; Q5J583; -.
DR   GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; Ion transport;
KW   Membrane; Potassium; Potassium transport; Signal-anchor; Sodium;
KW   Sodium transport; Sodium/potassium transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..290
FT                   /note="Sodium/potassium-transporting ATPase subunit beta-2"
FT                   /id="PRO_0000265959"
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:0000255"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        159
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        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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;  33377 MW;  CC5BF966D1C344F1 CRC64;
     MVIQKEKKSC GQVVEEWKEF VWNPRTHQFM GRTGTSWAFI LLFYLVFYGF LTAMFTLTMW
     VMLQTVSDHT PKYQDRLATP GLMIRPKTEN LDVIVNVSDT ESWDQHVQKL NKFLEPYNDS
     IQAQKNDVCR PGRYYEQPDN GVLNYPKRAC QFNRTQLGNC SGIGDPTHYG YSTGQPCVFI
     KMNRVINFYA GANQSMNVTC AGKRDEDAEN LGNFVMFPAN GNIDLMYFPY YGKKFHVNYT
     QPLVAVKFLN VTPNVEVNVE CRINAANIAT DDERDKFAGR VAFKLRINKT