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Sodium/potassium-transporting ATPase subunit beta-3 (Sodium/potassium-dependent ATPase subunit beta-3) (ATPB-3) (CD antigen CD298)

 AT1B3_HUMAN             Reviewed;         279 AA.
P54709; B7Z1N7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 158.
RecName: Full=Sodium/potassium-transporting ATPase subunit beta-3;
AltName: Full=Sodium/potassium-dependent ATPase subunit beta-3;
Short=ATPB-3;
AltName: CD_antigen=CD298;
Name=ATP1B3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=8798450; DOI=10.1074/jbc.271.37.22754;
Malik N., Canfield V.A., Beckers M.C., Gros P., Levenson R.;
"Identification of the mammalian Na,K-ATPase 3 subunit.";
J. Biol. Chem. 271:22754-22758(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9457675; DOI=10.1007/s003359900704;
Malik N., Canfield V., Sanchez-Watts G., Watts A.G., Scherer S.,
Beatty B.G., Gros P., Levenson R.;
"Structural organization and chromosomal localization of the human
Na,K- ATPase beta 3 subunit gene and pseudogene.";
Mamm. Genome 9:136-143(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
GLYCOSYLATION AT ASN-240.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: This is the non-catalytic component of the active
enzyme, which catalyzes the hydrolysis of ATP coupled with the
exchange of Na(+) and K(+) ions across the plasma membrane. The
exact function of the beta-3 subunit is not known.
-!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
catalytic alpha subunit, an auxiliary non-catalytic beta subunit
and an additional regulatory subunit. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17081065};
Single-pass type II membrane protein
{ECO:0000269|PubMed:17081065}. Melanosome
{ECO:0000269|PubMed:17081065}. Note=Identified by mass
spectrometry in melanosome fractions from stage I to stage IV.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P54709-1; Sequence=Displayed;
Name=2;
IsoId=P54709-2; Sequence=VSP_056686, VSP_056687;
Note=No experimental confirmation available.;
-!- DOMAIN: The C-terminal lobe folds into an immunoglobulin-like
domain and may mediate cell adhesion properties. {ECO:0000250}.
-!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U51478; AAC50665.1; -; mRNA.
EMBL; AF005896; AAB61713.1; -; Genomic_DNA.
EMBL; AF005890; AAB61713.1; JOINED; Genomic_DNA.
EMBL; AF005891; AAB61713.1; JOINED; Genomic_DNA.
EMBL; AF005892; AAB61713.1; JOINED; Genomic_DNA.
EMBL; AF005893; AAB61713.1; JOINED; Genomic_DNA.
EMBL; AF005894; AAB61713.1; JOINED; Genomic_DNA.
EMBL; AF005895; AAB61713.1; JOINED; Genomic_DNA.
EMBL; AK293697; BAH11573.1; -; mRNA.
EMBL; AC112504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC011835; AAH11835.1; -; mRNA.
CCDS; CCDS3121.1; -. [P54709-1]
PIR; G02485; G02485.
RefSeq; NP_001670.1; NM_001679.3. [P54709-1]
UniGene; Hs.477789; -.
ProteinModelPortal; P54709; -.
BioGrid; 106973; 106.
DIP; DIP-50717N; -.
IntAct; P54709; 11.
MINT; MINT-5001083; -.
STRING; 9606.ENSP00000286371; -.
ChEMBL; CHEMBL2095186; -.
DrugBank; DB09479; Rubidium chloride Rb-82.
TCDB; 3.A.3.1.1; the p-type atpase (p-atpase) superfamily.
iPTMnet; P54709; -.
PhosphoSitePlus; P54709; -.
SwissPalm; P54709; -.
BioMuta; ATP1B3; -.
DMDM; 1703470; -.
EPD; P54709; -.
MaxQB; P54709; -.
PaxDb; P54709; -.
PeptideAtlas; P54709; -.
PRIDE; P54709; -.
TopDownProteomics; P54709-1; -. [P54709-1]
Ensembl; ENST00000286371; ENSP00000286371; ENSG00000069849. [P54709-1]
GeneID; 483; -.
KEGG; hsa:483; -.
UCSC; uc003eug.2; human. [P54709-1]
CTD; 483; -.
EuPathDB; HostDB:ENSG00000069849.10; -.
GeneCards; ATP1B3; -.
HGNC; HGNC:806; ATP1B3.
HPA; CAB020697; -.
HPA; HPA048963; -.
MIM; 601867; gene.
neXtProt; NX_P54709; -.
OpenTargets; ENSG00000069849; -.
PharmGKB; PA68; -.
eggNOG; KOG3927; Eukaryota.
eggNOG; ENOG411150A; LUCA.
GeneTree; ENSGT00550000074530; -.
HOGENOM; HOG000039248; -.
HOVERGEN; HBG050603; -.
InParanoid; P54709; -.
KO; K01540; -.
OMA; SITINCE; -.
OrthoDB; EOG091G0DJ4; -.
PhylomeDB; P54709; -.
TreeFam; TF314618; -.
Reactome; R-HSA-210991; Basigin interactions.
Reactome; R-HSA-5578775; Ion homeostasis.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
GeneWiki; ATP1B3; -.
GenomeRNAi; 483; -.
PRO; PR:P54709; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000069849; -.
CleanEx; HS_ATP1B3; -.
ExpressionAtlas; P54709; baseline and differential.
Genevisible; P54709; HS.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:BHF-UCL.
GO; GO:0001671; F:ATPase activator activity; IDA:BHF-UCL.
GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
GO; GO:0005391; F:sodium:potassium-exchanging ATPase activity; IDA:BHF-UCL.
GO; GO:0030007; P:cellular potassium ion homeostasis; IDA:BHF-UCL.
GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:BHF-UCL.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0086009; P:membrane repolarization; IDA:BHF-UCL.
GO; GO:0032781; P:positive regulation of ATPase activity; IDA:BHF-UCL.
GO; GO:1903288; P:positive regulation of potassium ion import; IDA:BHF-UCL.
GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:1903278; P:positive regulation of sodium ion export from cell; IDA:BHF-UCL.
GO; GO:0010107; P:potassium ion import; IDA:BHF-UCL.
GO; GO:0072659; P:protein localization to plasma membrane; IDA:BHF-UCL.
GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0036376; P:sodium ion export from cell; IDA:BHF-UCL.
GO; GO:0006810; P:transport; TAS:ProtInc.
InterPro; IPR000402; Na/K_ATPase_sub_beta.
PANTHER; PTHR11523; PTHR11523; 1.
Pfam; PF00287; Na_K-ATPase; 1.
TIGRFAMs; TIGR01107; Na_K_ATPase_bet; 1.
PROSITE; PS00390; ATPASE_NA_K_BETA_1; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Ion transport; Membrane; Potassium;
Potassium transport; Reference proteome; Signal-anchor; Sodium;
Sodium transport; Sodium/potassium transport; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 279 Sodium/potassium-transporting ATPase
subunit beta-3.
/FTId=PRO_0000219108.
TOPO_DOM 1 35 Cytoplasmic. {ECO:0000255}.
TRANSMEM 36 56 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 57 279 Extracellular. {ECO:0000255}.
REGION 186 279 immunoglobulin-like. {ECO:0000250}.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519}.
DISULFID 128 144 {ECO:0000250}.
DISULFID 154 170 {ECO:0000250}.
DISULFID 191 250 {ECO:0000250}.
VAR_SEQ 1 36 MTKNEKKSLNQSLAEWKLFIYNPTTGEFLGRTAKSW -> M
LSEGDILFSSLLSSPSLFWPP (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056686.
VAR_SEQ 195 279 NEDIPNVAVYPHNGMIDLKYFPYYGKKLHVGYLQPLVAVQV
SFAPNNTGKEVTVECKIDGSANLKSQDDRDKFLGRVMFKIT
ARA -> TNNVKDGMKIYQM (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056687.
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


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