AT1B3_HUMAN
ID AT1B3_HUMAN Reviewed; 279 AA.
AC P54709; B7Z1N7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=8798450; DOI=10.1074/jbc.271.37.22754;
RA Malik N., Canfield V.A., Beckers M.C., Gros P., Levenson R.;
RT "Identification of the mammalian Na,K-ATPase 3 subunit.";
RL J. Biol. Chem. 271:22754-22758(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9457675; DOI=10.1007/s003359900704;
RA Malik N., Canfield V., Sanchez-Watts G., Watts A.G., Scherer S.,
RA Beatty B.G., Gros P., Levenson R.;
RT "Structural organization and chromosomal localization of the human
RT Na,K- ATPase beta 3 subunit gene and pseudogene.";
RL Mamm. Genome 9:136-143(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP GLYCOSYLATION AT ASN-240.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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.
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 -!- INTERACTION:
CC P54709; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-1054481, EBI-12019274;
CC P54709; Q0VAQ4: SMAGP; NbExp=3; IntAct=EBI-1054481, EBI-10226799;
CC P54709; P27105: STOM; NbExp=3; IntAct=EBI-1054481, EBI-1211440;
CC P54709; Q9Y2Y6: TMEM98; NbExp=3; IntAct=EBI-1054481, EBI-7333781;
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:0000269|PubMed:17081065}.
CC Note=Identified by mass spectrometry in melanosome fractions from stage
CC I to stage IV.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P54709-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P54709-2; Sequence=VSP_056686, VSP_056687;
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; U51478; AAC50665.1; -; mRNA.
DR EMBL; AF005896; AAB61713.1; -; Genomic_DNA.
DR EMBL; AF005890; AAB61713.1; JOINED; Genomic_DNA.
DR EMBL; AF005891; AAB61713.1; JOINED; Genomic_DNA.
DR EMBL; AF005892; AAB61713.1; JOINED; Genomic_DNA.
DR EMBL; AF005893; AAB61713.1; JOINED; Genomic_DNA.
DR EMBL; AF005894; AAB61713.1; JOINED; Genomic_DNA.
DR EMBL; AF005895; AAB61713.1; JOINED; Genomic_DNA.
DR EMBL; AK293697; BAH11573.1; -; mRNA.
DR EMBL; AC112504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011835; AAH11835.1; -; mRNA.
DR CCDS; CCDS3121.1; -. [P54709-1]
DR PIR; G02485; G02485.
DR RefSeq; NP_001670.1; NM_001679.3. [P54709-1]
DR AlphaFoldDB; P54709; -.
DR SMR; P54709; -.
DR BioGRID; 106973; 199.
DR DIP; DIP-50717N; -.
DR IntAct; P54709; 60.
DR MINT; P54709; -.
DR STRING; 9606.ENSP00000286371; -.
DR BindingDB; P54709; -.
DR ChEMBL; CHEMBL2095186; -.
DR DrugBank; DB09020; Bisacodyl.
DR DrugBank; DB09479; Rubidium Rb-82.
DR DrugBank; DB16690; Tegoprazan.
DR DrugCentral; P54709; -.
DR TCDB; 3.A.3.1.1; the p-type atpase (p-atpase) superfamily.
DR GlyConnect; 1759; 8 N-Linked glycans (2 sites).
DR GlyGen; P54709; 4 sites, 7 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P54709; -.
DR PhosphoSitePlus; P54709; -.
DR SwissPalm; P54709; -.
DR BioMuta; ATP1B3; -.
DR DMDM; 1703470; -.
DR CPTAC; CPTAC-2206; -.
DR EPD; P54709; -.
DR jPOST; P54709; -.
DR MassIVE; P54709; -.
DR MaxQB; P54709; -.
DR PaxDb; P54709; -.
DR PeptideAtlas; P54709; -.
DR PRIDE; P54709; -.
DR ProteomicsDB; 56697; -. [P54709-1]
DR ProteomicsDB; 6354; -.
DR TopDownProteomics; P54709-1; -. [P54709-1]
DR Antibodypedia; 33485; 402 antibodies from 32 providers.
DR DNASU; 483; -.
DR Ensembl; ENST00000286371.8; ENSP00000286371.3; ENSG00000069849.11. [P54709-1]
DR GeneID; 483; -.
DR KEGG; hsa:483; -.
DR MANE-Select; ENST00000286371.8; ENSP00000286371.3; NM_001679.4; NP_001670.1.
DR UCSC; uc003eug.2; human. [P54709-1]
DR CTD; 483; -.
DR DisGeNET; 483; -.
DR GeneCards; ATP1B3; -.
DR HGNC; HGNC:806; ATP1B3.
DR HPA; ENSG00000069849; Low tissue specificity.
DR MIM; 601867; gene.
DR neXtProt; NX_P54709; -.
DR OpenTargets; ENSG00000069849; -.
DR PharmGKB; PA68; -.
DR VEuPathDB; HostDB:ENSG00000069849; -.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR HOGENOM; CLU_057702_1_1_1; -.
DR InParanoid; P54709; -.
DR OMA; PKLGKWE; -.
DR OrthoDB; 998086at2759; -.
DR PhylomeDB; P54709; -.
DR TreeFam; TF314618; -.
DR PathwayCommons; P54709; -.
DR Reactome; R-HSA-210991; Basigin interactions.
DR Reactome; R-HSA-5578775; Ion homeostasis.
DR Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; P54709; -.
DR BioGRID-ORCS; 483; 150 hits in 1048 CRISPR screens.
DR ChiTaRS; ATP1B3; human.
DR GeneWiki; ATP1B3; -.
DR GenomeRNAi; 483; -.
DR Pharos; P54709; Tclin.
DR PRO; PR:P54709; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P54709; protein.
DR Bgee; ENSG00000069849; Expressed in sperm and 204 other tissues.
DR ExpressionAtlas; P54709; baseline and differential.
DR Genevisible; P54709; HS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:BHF-UCL.
DR GO; GO:0036126; C:sperm flagellum; IDA:ARUK-UCL.
DR GO; GO:0001671; F:ATPase activator activity; IDA:BHF-UCL.
DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:BHF-UCL.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0086009; P:membrane repolarization; IDA:BHF-UCL.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:BHF-UCL.
DR GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; IDA:BHF-UCL.
DR GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:1903278; P:positive regulation of sodium ion export across plasma membrane; IDA:BHF-UCL.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:BHF-UCL.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IGI:ARUK-UCL.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IDA:BHF-UCL.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IGI:ARUK-UCL.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion transport; Membrane; Potassium; Potassium transport;
KW Reference proteome; Signal-anchor; Sodium; Sodium transport;
KW Sodium/potassium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..279
FT /note="Sodium/potassium-transporting ATPase subunit beta-3"
FT /id="PRO_0000219108"
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 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519"
FT DISULFID 128..144
FT /evidence="ECO:0000250"
FT DISULFID 154..170
FT /evidence="ECO:0000250"
FT DISULFID 191..250
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..36
FT /note="MTKNEKKSLNQSLAEWKLFIYNPTTGEFLGRTAKSW -> MLSEGDILFSSL
FT LSSPSLFWPP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056686"
FT VAR_SEQ 195..279
FT /note="NEDIPNVAVYPHNGMIDLKYFPYYGKKLHVGYLQPLVAVQVSFAPNNTGKEV
FT TVECKIDGSANLKSQDDRDKFLGRVMFKITARA -> TNNVKDGMKIYQM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056687"
SQ SEQUENCE 279 AA; 31513 MW; D92ECB4F0F6EBFE5 CRC64;
MTKNEKKSLN QSLAEWKLFI YNPTTGEFLG RTAKSWGLIL LFYLVFYGFL AALFSFTMWV
MLQTLNDEVP KYRDQIPSPG LMVFPKPVTA LEYTFSRSDP TSYAGYIEDL KKFLKPYTLE
EQKNLTVCPD GALFEQKGPV YVACQFPISL LQACSGMNDP DFGYSQGNPC ILVKMNRIIG
LKPEGVPRID CVSKNEDIPN VAVYPHNGMI DLKYFPYYGK KLHVGYLQPL VAVQVSFAPN
NTGKEVTVEC KIDGSANLKS QDDRDKFLGR VMFKITARA
