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AT1B2_RABIT
ID   AT1B2_RABIT             Reviewed;         290 AA.
AC   Q8WMG3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit beta-2;
DE   AltName: Full=Sodium/potassium-dependent ATPase subunit beta-2;
GN   Name=ATP1B2;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Renal medulla;
RA   Gumz M.L., Cain B.D.;
RT   "Identification of the rabbit Na+K+ ATPase beta 2 subunit.";
RL   Submitted (DEC-2001) 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; AY069937; AAL55426.1; -; mRNA.
DR   RefSeq; NP_001076249.1; NM_001082780.1.
DR   AlphaFoldDB; Q8WMG3; -.
DR   SMR; Q8WMG3; -.
DR   STRING; 9986.ENSOCUP00000002598; -.
DR   Ensembl; ENSOCUT00000002988; ENSOCUP00000002598; ENSOCUG00000002988.
DR   GeneID; 100009577; -.
DR   KEGG; ocu:100009577; -.
DR   CTD; 482; -.
DR   eggNOG; KOG3927; Eukaryota.
DR   GeneTree; ENSGT01030000234579; -.
DR   HOGENOM; CLU_057702_1_1_1; -.
DR   InParanoid; Q8WMG3; -.
DR   OMA; VCRPGHY; -.
DR   OrthoDB; 998086at2759; -.
DR   TreeFam; TF314618; -.
DR   Proteomes; UP000001811; Chromosome 19.
DR   Bgee; ENSOCUG00000002988; Expressed in frontal cortex and 17 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0097450; C:astrocyte end-foot; IEA:Ensembl.
DR   GO; GO:0044298; C:cell body membrane; IEA:Ensembl.
DR   GO; GO:0031253; C:cell projection membrane; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0098984; C:neuron to neuron synapse; IEA:Ensembl.
DR   GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR   GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IEA:Ensembl.
DR   GO; GO:0001671; F:ATPase activator activity; IEA:Ensembl.
DR   GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR   GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl.
DR   GO; GO:0030007; P:cellular potassium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0006883; P:cellular sodium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0021670; P:lateral ventricle development; IEA:Ensembl.
DR   GO; GO:0086009; P:membrane repolarization; IEA:Ensembl.
DR   GO; GO:0061744; P:motor behavior; IEA:Ensembl.
DR   GO; GO:1903976; P:negative regulation of glial cell migration; IEA:Ensembl.
DR   GO; GO:0021944; P:neuronal-glial interaction involved in hindbrain glial-mediated radial cell migration; IEA:Ensembl.
DR   GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR   GO; GO:0120036; P:plasma membrane bounded cell projection organization; IEA:Ensembl.
DR   GO; GO:0032781; P:positive regulation of ATP-dependent activity; IEA:Ensembl.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; IEA:Ensembl.
DR   GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:1903278; P:positive regulation of sodium ion export across plasma membrane; IEA:Ensembl.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR   GO; GO:0036376; P:sodium ion export across plasma membrane; IEA:Ensembl.
DR   GO; GO:0021678; P:third ventricle development; IEA:Ensembl.
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_0000265960"
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;  33391 MW;  2D1F477D307D5F51 CRC64;
     MVIQKEKKSC GQVVEEWKEF VWNPRTHQFM GRTGTSWAFI LLFYLVFYGF LTAMFTLTMW
     VMLQTVSEHT PKYQDRLATP GLMIRPKTEN LDVIVNVSDT ESWDQHVQKL NKFLEPYNDS
     IQAQKNDVCR PGRYYEQPDN GVLNYPKRAC QFNRTQLGNC SGIGDPTHYG YSTGQPCVFI
     KMNRVINFYA GANQSMNVTC AGKRDEDAEN LGNFVMFPAN GNIDLMYFPY YGKKFHVNYT
     QPLVAVKFLN VTPNVEVNVE CRINAANIAT DDERDKFAGR VAFKLRINKT
 
 
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