ID   AT1B2_BOVIN             Reviewed;         290 AA.
AC   Q28030;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit beta-2;
DE   AltName: Full=Sodium/potassium-dependent ATPase subunit beta-2;
GN   Name=ATP1B2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-94.
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).
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 BSG (By similarity).
CC       {ECO:0000250|UniProtKB:P14231, 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; U45944; AAC48681.1; -; mRNA.
DR   PIR; JC5108; JC5108.
DR   RefSeq; NP_777102.1; NM_174677.2.
DR   AlphaFoldDB; Q28030; -.
DR   SMR; Q28030; -.
DR   BioGRID; 159782; 1.
DR   IntAct; Q28030; 1.
DR   STRING; 9913.ENSBTAP00000018181; -.
DR   PaxDb; Q28030; -.
DR   PRIDE; Q28030; -.
DR   GeneID; 282562; -.
DR   KEGG; bta:282562; -.
DR   CTD; 482; -.
DR   eggNOG; KOG3927; Eukaryota.
DR   InParanoid; Q28030; -.
DR   OrthoDB; 998086at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IBA:GO_Central.
DR   GO; GO:0001671; F:ATPase activator activity; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0030007; P:cellular potassium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0006883; P:cellular sodium ion homeostasis; IBA:GO_Central.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
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; 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_0000219103"
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..289
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        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;  33401 MW;  5B21764A0DFB0B86 CRC64;
     MVIQKEKKSC GQVVEEWKEF VWNPRTHQFM GRTGTSWAFI LLFYLVFYGF LTAMFTLTMW
     VMLQTVSDHT PKYQDRLATP GLMIRPKTEN LDVIVNVSDT ESWDQHVQKL NKFLEPYNDS
     IQAQKNDVCR PGRYYEQPDN GVLNYPKRAC QFNRTQLGDC SGIGDPTHYG YSTGQPCVFI
     KMNRVISFYA GANQSMNVTC VGKRDEDAEN LGNFVMFPAN GNIDLIYFPY YGKKFHVNYT
     QPLVAVKFLN VTPNVEVNVE CRINAANIAT DDERDKFAPR VAFKLRINKT