AT1B4_CHICK
ID AT1B4_CHICK Reviewed; 321 AA.
AC Q2HZ96;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Protein ATP1B4;
DE AltName: Full=X,K-ATPase subunit beta-m;
DE AltName: Full=X/potassium-transporting ATPase subunit beta-m;
GN Name=ATP1B4;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, GLYCOSYLATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=17592128; DOI=10.1073/pnas.0704809104;
RA Pestov N.B., Ahmad N., Korneenko T.V., Zhao H., Radkov R., Schaer D.,
RA Roy S., Bibert S., Geering K., Modyanov N.N.;
RT "Evolution of Na,K-ATPase betam-subunit into a coregulator of transcription
RT in placental mammals.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:11215-11220(2007).
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:0000269|PubMed:17592128}.
CC -!- SUBUNIT: Composed of two subunits: alpha (catalytic) and beta
CC (accessory). {ECO:0000269|PubMed:17592128}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, intestine, heart,
CC brain, retina, inner ear and skin. {ECO:0000269|PubMed:17592128}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo in skeletal muscle, heart,
CC brain, retina, inner ear and skin at 19 dpc.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:17592128}.
CC -!- MISCELLANEOUS: Its function as a Na,K-ATPase beta-subunit will be lost
CC in placental mammals.
CC -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC {ECO:0000305}.
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DR EMBL; DQ358914; ABC94911.1; -; mRNA.
DR RefSeq; NP_001038116.1; NM_001044651.1.
DR AlphaFoldDB; Q2HZ96; -.
DR SMR; Q2HZ96; -.
DR STRING; 9031.ENSGALP00000038293; -.
DR PaxDb; Q2HZ96; -.
DR Ensembl; ENSGALT00000039082; ENSGALP00000038293; ENSGALG00000008593.
DR GeneID; 422365; -.
DR KEGG; gga:422365; -.
DR CTD; 23439; -.
DR VEuPathDB; HostDB:geneid_422365; -.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR HOGENOM; CLU_057702_1_1_1; -.
DR InParanoid; Q2HZ96; -.
DR OMA; GVQYDTH; -.
DR OrthoDB; 998086at2759; -.
DR PhylomeDB; Q2HZ96; -.
DR Reactome; R-GGA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR PRO; PR:Q2HZ96; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000008593; Expressed in muscle tissue and 11 other tissues.
DR GO; GO:0005637; C:nuclear inner membrane; IBA:GO_Central.
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:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..321
FT /note="Protein ATP1B4"
FT /id="PRO_0000393964"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
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 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 165..184
FT /evidence="ECO:0000250"
FT DISULFID 194..210
FT /evidence="ECO:0000250"
FT DISULFID 233..293
FT /evidence="ECO:0000250"
SQ SEQUENCE 321 AA; 36363 MW; DE0AFFC005561318 CRC64;
MEPGMEMNTA SEGGTRRGPE NKHEEKVQDP NRGEAETKAE MGNKTWADLA GEMKTFLWNP
EERTCMGRTA KSWGLILLFY FIFYTCLAGM FAFCMYVMLL TLSPYTPTYR DRVSPPGVMI
RPYLNGFTIA FNVSKPSTWQ PYVDSMHQFL AAYDDKVQEE KNIECISGQY FIQGGNDSEE
KKACQFKRSL LQNCSGIEDP TFGFSKGQPC ILLKMNRIIG YRPGAGVPVN VDCKVQKGNE
SDLRSVDFYP GNGTFDLMYY PYYGKLTHVN YTSPLVAMHF TDVKRNSLVH IQCKLNGKGI
INDVNSDRFL GRIIFTLSIG K
