ID A0A2K5MSJ1_CERAT Unreviewed; 348 AA.
AC A0A2K5MSJ1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta {ECO:0000256|RuleBase:RU362099};
GN Name=ATP1B4 {ECO:0000313|Ensembl:ENSCATP00000028169.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000028169.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000028169.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: May act as a transcriptional coregulator during muscle
CC development through its interaction with SNW1. Has lost its ancestral
CC function as a Na,K-ATPase beta-subunit.
CC {ECO:0000256|ARBA:ARBA00037398}.
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.
CC {ECO:0000256|RuleBase:RU362099}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Nucleus
CC inner membrane {ECO:0000256|ARBA:ARBA00037816}; Single-pass type II
CC membrane protein {ECO:0000256|ARBA:ARBA00037816}.
CC -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC {ECO:0000256|ARBA:ARBA00005876, ECO:0000256|RuleBase:RU362099}.
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DR AlphaFoldDB; A0A2K5MSJ1; -.
DR Ensembl; ENSCATT00000052420.1; ENSCATP00000028169.1; ENSCATG00000037392.1.
DR GeneTree; ENSGT01030000234579; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000037392; Expressed in skeletal muscle tissue.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.60.40.1660; Na, k-atpase alpha subunit; 2.
DR InterPro; IPR000402; Na/K_ATPase_sub_beta.
DR InterPro; IPR038702; Na/K_ATPase_sub_beta_sf.
DR NCBIfam; TIGR01107; Na_K_ATPase_bet; 1.
DR PANTHER; PTHR11523:SF12; PROTEIN ATP1B4; 1.
DR PANTHER; PTHR11523; SODIUM/POTASSIUM-DEPENDENT ATPASE BETA SUBUNIT; 1.
DR Pfam; PF00287; Na_K-ATPase; 1.
DR PROSITE; PS00390; ATPASE_NA_K_BETA_1; 1.
DR PROSITE; PS00391; ATPASE_NA_K_BETA_2; 1.
PE 3: Inferred from homology;
KW Ion transport {ECO:0000256|RuleBase:RU362099};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362099};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362099};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362099}; Transport {ECO:0000256|RuleBase:RU362099}.
FT TRANSMEM 108..135
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362099"
FT REGION 26..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..72
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 40794 MW; 30D618FB94D51BE7 CRC64;
MRRQLRSRRA PSFPYSYRYR LDDPDEVNQN YLADEEEEAE EEARVTVVPK SEEEEEEEEK
EEEEEEEKEE EEGQGQPTGN AWWQKLQIMN EYLWDPERRM FLARTGQSWS LILLVYFFFY
ASLAAVITLC MYTLFLTISP YIPTFTERVK PPGVMIRPFA HSLNFNFNVS EPDTWQHYVI
SLNGFLQGYN DSLQEEMNVD CPPGQYFIQD GNEDEDKKAC QFKRSFLKNC SGLEDPTFGY
STGQPCILLK MNRHPTYTCF CLQRGDENDI RSISYYPESA SFDLRYYPYY GKLTHVNYTS
PLVAMHFTDV VKNQAVPVQC QLKGKGIIND VINDRFVGRV IFTLNIET
//