AT1B1_MACFA
ID AT1B1_MACFA Reviewed; 303 AA.
AC Q4R4V5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
DE AltName: Full=Sodium/potassium-dependent ATPase subunit beta-1;
GN Name=ATP1B1; ORFNames=QtrA-13828;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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 beta subunit
CC regulates, through assembly of alpha/beta heterodimers, the number of
CC sodium pumps transported to the plasma membrane. Plays a role in innate
CC immunity by enhancing virus-triggered induction of interferons (IFNs)
CC and interferon stimulated genes (ISGs). Mechanistically, enhances the
CC ubiquitination of TRAF3 and TRAF6 as well as the phosphorylation of
CC TAK1 and TBK1. {ECO:0000250|UniProtKB:P05026}.
CC -!- FUNCTION: Involved in cell adhesion and establishing epithelial cell
CC polarity. {ECO:0000250|UniProtKB:P05026}.
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 catalytic subunit ATP12A
CC (By similarity). Interacts with regulatory subunit FXYD1 (By
CC similarity). Interacts with regulatory subunit FXYD3 (By similarity).
CC Interacts with NKAIN1, NKAIN2 and NKAIN4 (By similarity). Interacts
CC with MLC1. Part of a complex containing MLC1, TRPV4, AQP4 and HEPACAM.
CC Interacts with KIRREL3 (By similarity). Interacts with OBSCN (via
CC protein kinase domain 1) (By similarity). Interacts with TRAF3 and
CC TRAF6 (By similarity). {ECO:0000250|UniProtKB:P05026,
CC ECO:0000250|UniProtKB:P07340, ECO:0000250|UniProtKB:P14094}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000250|UniProtKB:P07340}; Single-pass type II membrane protein
CC {ECO:0000255}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P14094}. Note=Colocalizes with OBSCN at the
CC intercalated disk and sarcolemma in cardiomyocytes. Localizes in long
CC striations at the level of Z and M lines.
CC {ECO:0000250|UniProtKB:P14094}.
CC -!- DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain
CC and mediates cell adhesion properties. {ECO:0000250}.
CC -!- PTM: Glutathionylated (By similarity). N-glycosylated (By similarity).
CC {ECO:0000250|UniProtKB:P07340, ECO:0000250|UniProtKB:P14094}.
CC -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC {ECO:0000305}.
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DR EMBL; AB169789; BAE01870.1; -; mRNA.
DR RefSeq; NP_001272243.1; NM_001285314.1.
DR AlphaFoldDB; Q4R4V5; -.
DR SMR; Q4R4V5; -.
DR STRING; 9541.XP_005539982.1; -.
DR GeneID; 101866484; -.
DR CTD; 481; -.
DR VEuPathDB; HostDB:ENSMFAG00000039661; -.
DR eggNOG; KOG3927; Eukaryota.
DR OMA; ECKAYGQ; -.
DR OrthoDB; 998086at2759; -.
DR Proteomes; UP000233100; Chromosome 1.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
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:0045087; P:innate immune response; 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; IPR015565; Na/K_ATPase_sub_beta_chordates.
DR InterPro; IPR038702; Na/K_ATPase_sub_beta_sf.
DR PANTHER; PTHR11523; PTHR11523; 1.
DR PANTHER; PTHR11523:SF10; PTHR11523:SF10; 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; Glutathionylation;
KW Glycoprotein; Immunity; Innate immunity; Ion transport; Membrane;
KW Phosphoprotein; Potassium; Potassium transport; Reference proteome;
KW Signal-anchor; Sodium; Sodium transport; Sodium/potassium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..303
FT /note="Sodium/potassium-transporting ATPase subunit beta-1"
FT /id="PRO_0000265956"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..62
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 191..303
FT /note="immunoglobulin-like"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07340"
FT MOD_RES 101
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14094"
FT CARBOHYD 158
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 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 126..149
FT /evidence="ECO:0000250"
FT DISULFID 159..175
FT /evidence="ECO:0000250"
FT DISULFID 213..276
FT /evidence="ECO:0000250"
SQ SEQUENCE 303 AA; 35001 MW; 30704D9F83420248 CRC64;
MARGKAKEEG SWKKFIWNSE KKEFLGRTGG SWFKILLFYV IFYGCLAGIF IGTIQVMLLT
ISELKPTYQD RVAPPGLTQI PQIQKTEISF RPNDPKSYEA YVLNIVRFLE KYKDSAQRDD
MIFEDCGDVP SEPKERGEFN HERGERKVCR FKLEWLGNCS GLNDETYGYK EGKPCIIIKL
NRVLGFKPKP PKNESLETYP GMKYNANVLP VQCTGKRDED KEKIGNVEYF GLGNSPGFPL
QYYPYYGKLL QPKYLQPLLA VQFTNLTMDT EIRIECKAYG ENIGYSEKDR FQGRFDVKIE
VKS
