AT1B3_CAVPO
ID AT1B3_CAVPO Reviewed; 279 AA.
AC Q60489;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta-3;
DE AltName: Full=Sodium/potassium-dependent ATPase subunit beta-3;
DE Short=ATPB-3;
DE AltName: CD_antigen=CD298;
GN Name=ATP1B3;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hartley; TISSUE=Distal colon;
RA Watanabe T., Sato M., Yoshida T., Suzuki Y.;
RT "Isolation of cDNA encoding the guinea pig Na+,K+-ATPase beta-3 subunit.";
RL Submitted (MAY-1996) 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-3 subunit is not known (By similarity). {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 catalytic alpha subunit
CC ATP12A. {ECO:0000250|UniProtKB:Q63377}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q63377}; Single-pass type II membrane protein
CC {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q63377}; Single-pass type II membrane protein
CC {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:P54709}.
CC Note=Identified by mass spectrometry in melanosome fractions from stage
CC I to stage IV. {ECO:0000250|UniProtKB:P54709}.
CC -!- DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain
CC and may mediate 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; D84448; BAA12665.1; -; mRNA.
DR RefSeq; NP_001166389.1; NM_001172918.2.
DR AlphaFoldDB; Q60489; -.
DR SMR; Q60489; -.
DR STRING; 10141.ENSCPOP00000003376; -.
DR Ensembl; ENSCPOT00000003783; ENSCPOP00000003376; ENSCPOG00000003739.
DR GeneID; 100135484; -.
DR KEGG; cpoc:100135484; -.
DR CTD; 483; -.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR HOGENOM; CLU_057702_1_1_1; -.
DR InParanoid; Q60489; -.
DR OMA; PKLGKWE; -.
DR OrthoDB; 998086at2759; -.
DR TreeFam; TF314618; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000003739; Expressed in zone of skin and 13 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IEA:InterPro.
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.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Membrane;
KW Potassium; Potassium transport; Reference proteome; Signal-anchor; Sodium;
KW Sodium transport; Sodium/potassium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..279
FT /note="Sodium/potassium-transporting ATPase subunit beta-3"
FT /id="PRO_0000219107"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 186..279
FT /note="immunoglobulin-like"
FT /evidence="ECO:0000250"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 128..144
FT /evidence="ECO:0000250"
FT DISULFID 154..170
FT /evidence="ECO:0000250"
FT DISULFID 191..250
FT /evidence="ECO:0000250"
SQ SEQUENCE 279 AA; 31570 MW; EB87CB770D82DF7A CRC64;
MTKSEKKSLN ESLAQWKLFL YNPTTREFLG RTAKSWGLIL LFYLVFYGFL AALFTFTMWA
MLQTLNDEIP KYRDQIPSPG LMVFPKPVTA LEYTFSVSDP SSYEGYIKDL KKFLKSYSLD
EQKNLNKCTD GVLFEQTGPV YAACQFPDSL LEACSGTDDP DFGYSQGQPC VLVKMNRIIG
LKPEGSPRID CISKDENTAM VSTYPNQGVI DLKYFPYYGK KLHVGYLQPL VAVQVSFGSN
STKKEVTVEC KIEGSKNLRN EDDRDKFLGR VAFKITARA