ID FXYD3_HUMAN Reviewed; 87 AA. AC Q14802; A6NDE0; C9JDU2; F5H174; F8WB34; Q13211; Q6IB59; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 02-SEP-2026, entry version 202. DE RecName: Full=FXYD domain-containing ion transport regulator 3; DE AltName: Full=Chloride conductance inducer protein Mat-8; DE AltName: Full=Mammary tumor 8 kDa protein; DE AltName: Full=Phospholemman-like; DE AltName: Full=Sodium/potassium-transporting ATPase subunit FXYD3 {ECO:0000305}; DE Flags: Precursor; GN Name=FXYD3; Synonyms=MAT8, PLML; 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), AND FUNCTION. RC TISSUE=Mammary gland; RX PubMed=7836447; DOI=10.1074/jbc.270.5.2176; RA Morrison B.W., Moorman J.R., Kowdley G.C., Kobayashi Y.M., Jones L.R., RA Leder P.; RT "Mat-8, a novel phospholemman-like protein expressed in human breast RT tumors, induces a chloride conductance in Xenopus oocytes."; RL J. Biol. Chem. 270:2176-2182(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Lung carcinoma; RA Lei W., Wu M.; RT "Two novel cDNAs express specifically in RA-treated human lung RT adenocarcinoma cell line GLC-82."; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Melanoma, and Urinary bladder; 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 [7] RP PROTEIN SEQUENCE OF 21-27, FUNCTION, IDENTIFICATION IN RP SODIUM/POTASSIUM-TRANSPORTING ATPASE COMPLEX, TISSUE SPECIFICITY, AND RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2). RX PubMed=17077088; DOI=10.1074/jbc.m605221200; RA Bibert S., Roy S., Schaer D., Felley-Bosco E., Geering K.; RT "Structural and functional properties of two human FXYD3 (Mat-8) RT isoforms."; RL J. Biol. Chem. 281:39142-39151(2006). RN [8] RP FUNCTION, INTERACTION WITH ATP1A1, GLUTATHIONYLATION, AND MUTAGENESIS OF RP CYS-44; CYS-49; CYS-61 AND CYS-63. RX PubMed=21454534; DOI=10.1074/jbc.m110.184101; RA Bibert S., Liu C.C., Figtree G.A., Garcia A., Hamilton E.J., Marassi F.M., RA Sweadner K.J., Cornelius F., Geering K., Rasmussen H.H.; RT "FXYD proteins reverse inhibition of the Na+-K+ pump mediated by RT glutathionylation of its beta1 subunit."; RL J. Biol. Chem. 286:18562-18572(2011). CC -!- FUNCTION: Associates with and regulates the activity of the CC sodium/potassium-transporting ATPase (NKA) which transports Na(+) out CC of the cell and K(+) into the cell (PubMed:17077088). Reduces CC glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing CC glutathionylation-mediated inhibition of ATP1B1 (PubMed:21454534). CC Induces a hyperpolarization-activated chloride current when expressed CC in Xenopus oocytes (PubMed:7836447). {ECO:0000269|PubMed:17077088, CC ECO:0000269|PubMed:21454534, ECO:0000269|PubMed:7836447}. CC -!- FUNCTION: [Isoform 1]: Decreases the apparent K+ and Na+ affinity of CC the sodium/potassium-transporting ATPase over a large range of membrane CC potentials. {ECO:0000269|PubMed:17077088}. CC -!- FUNCTION: [Isoform 2]: Decreases the apparent K+ affinity of the CC sodium/potassium-transporting ATPase only at slightly negative and CC positive membrane potentials and increases the apparent Na+ affinity CC over a large range of membrane potentials. CC {ECO:0000269|PubMed:17077088}. CC -!- SUBUNIT: Regulatory subunit of the sodium/potassium-transporting ATPase CC which is composed of a catalytic alpha subunit, a non-catalytic beta CC subunit and an additional regulatory subunit (PubMed:17077088). CC Interacts with catalytic alpha subunit ATP1A1 (PubMed:21454534). Also CC interacts with non-catalytic beta subunit ATP1B1 (By similarity). CC Interacts with the ATP1A1-ATP1B1, ATP1A2-ATP1B1 and ATP1A3-ATP1B1 NKA CC isozymes (PubMed:17077088). {ECO:0000250|UniProtKB:Q61835, CC ECO:0000269|PubMed:17077088, ECO:0000269|PubMed:21454534}. CC -!- INTERACTION: CC Q14802-3; Q8TD06: AGR3; NbExp=3; IntAct=EBI-12175685, EBI-3925742; CC Q14802-3; P16157-17: ANK1; NbExp=3; IntAct=EBI-12175685, EBI-941819; CC Q14802-3; Q13520: AQP6; NbExp=3; IntAct=EBI-12175685, EBI-13059134; CC Q14802-3; O43315: AQP9; NbExp=3; IntAct=EBI-12175685, EBI-17444777; CC Q14802-3; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-12175685, EBI-747430; CC Q14802-3; Q8NFU1: BEST2; NbExp=3; IntAct=EBI-12175685, EBI-19947314; CC Q14802-3; P11912: CD79A; NbExp=3; IntAct=EBI-12175685, EBI-7797864; CC Q14802-3; P34972: CNR2; NbExp=3; IntAct=EBI-12175685, EBI-2835940; CC Q14802-3; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12175685, EBI-6942903; CC Q14802-3; P00387: CYB5R3; NbExp=3; IntAct=EBI-12175685, EBI-1046040; CC Q14802-3; Q15125: EBP; NbExp=3; IntAct=EBI-12175685, EBI-3915253; CC Q14802-3; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-12175685, EBI-711490; CC Q14802-3; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12175685, EBI-781551; CC Q14802-3; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-12175685, EBI-18304435; CC Q14802-3; P12318-2: FCGR2A; NbExp=3; IntAct=EBI-12175685, EBI-17187481; CC Q14802-3; O15552: FFAR2; NbExp=3; IntAct=EBI-12175685, EBI-2833872; CC Q14802-3; Q9H3K2: GHITM; NbExp=3; IntAct=EBI-12175685, EBI-2868909; CC Q14802-3; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12175685, EBI-13345167; CC Q14802-3; O60883: GPR37L1; NbExp=3; IntAct=EBI-12175685, EBI-2927498; CC Q14802-3; O15529: GPR42; NbExp=3; IntAct=EBI-12175685, EBI-18076404; CC Q14802-3; Q9NZD1: GPRC5D; NbExp=3; IntAct=EBI-12175685, EBI-13067820; CC Q14802-3; P21815: IBSP; NbExp=3; IntAct=EBI-12175685, EBI-18400392; CC Q14802-3; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-12175685, EBI-749265; CC Q14802-3; O15554: KCNN4; NbExp=3; IntAct=EBI-12175685, EBI-2924473; CC Q14802-3; Q16873: LTC4S; NbExp=3; IntAct=EBI-12175685, EBI-12241118; CC Q14802-3; O43934: MFSD11; NbExp=3; IntAct=EBI-12175685, EBI-17633886; CC Q14802-3; Q6N075: MFSD5; NbExp=3; IntAct=EBI-12175685, EBI-3920969; CC Q14802-3; P10620: MGST1; NbExp=3; IntAct=EBI-12175685, EBI-2691601; CC Q14802-3; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-12175685, EBI-3923617; CC Q14802-3; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-12175685, EBI-11721828; CC Q14802-3; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-12175685, EBI-17247926; CC Q14802-3; O95470: SGPL1; NbExp=3; IntAct=EBI-12175685, EBI-1046170; CC Q14802-3; Q14973: SLC10A1; NbExp=3; IntAct=EBI-12175685, EBI-3923031; CC Q14802-3; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-12175685, EBI-18159983; CC Q14802-3; Q6ZSM3: SLC16A12; NbExp=3; IntAct=EBI-12175685, EBI-17460560; CC Q14802-3; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-12175685, EBI-17595455; CC Q14802-3; P43005: SLC1A1; NbExp=3; IntAct=EBI-12175685, EBI-745376; CC Q14802-3; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-12175685, EBI-8644112; CC Q14802-3; P78382: SLC35A1; NbExp=3; IntAct=EBI-12175685, EBI-12870360; CC Q14802-3; P78383: SLC35B1; NbExp=3; IntAct=EBI-12175685, EBI-12147661; CC Q14802-3; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-12175685, EBI-17295964; CC Q14802-3; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-12175685, EBI-12898013; CC Q14802-3; Q6ZMD2-2: SPNS3; NbExp=3; IntAct=EBI-12175685, EBI-17848320; CC Q14802-3; P0DN84: STRIT1; NbExp=3; IntAct=EBI-12175685, EBI-12200293; CC Q14802-3; Q13277: STX3; NbExp=3; IntAct=EBI-12175685, EBI-1394295; CC Q14802-3; O14925: TIMM23; NbExp=3; IntAct=EBI-12175685, EBI-1047996; CC Q14802-3; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-12175685, EBI-6268651; CC Q14802-3; Q96CP7: TLCD1; NbExp=3; IntAct=EBI-12175685, EBI-11337932; CC Q14802-3; P55061: TMBIM6; NbExp=3; IntAct=EBI-12175685, EBI-1045825; CC Q14802-3; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-12175685, EBI-11724423; CC Q14802-3; P56557: TMEM50B; NbExp=3; IntAct=EBI-12175685, EBI-12366453; CC Q14802-3; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-12175685, EBI-18178701; CC Q14802-3; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-12175685, EBI-11742770; CC Q14802-3; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-12175685, EBI-12015604; CC Q14802-3; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-12175685, EBI-12111910; CC Q14802-3; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-12175685, EBI-12195249; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=FXYD3-sf {ECO:0000303|PubMed:17077088}; CC IsoId=Q14802-1; Sequence=Displayed; CC Name=2; Synonyms=FXYD3-lf {ECO:0000303|PubMed:17077088}; CC IsoId=Q14802-2; Sequence=VSP_034598; CC Name=3; CC IsoId=Q14802-3; Sequence=VSP_045716; CC Name=4; CC IsoId=Q14802-4; Sequence=VSP_034598, VSP_047287; CC Name=5; CC IsoId=Q14802-5; Sequence=VSP_047286; CC -!- TISSUE SPECIFICITY: Isoform 1: Expressed mainly in differentiated cells CC (at protein level). Isoform 2: Expressed mainly in undifferentiated CC cells (at protein level). {ECO:0000269|PubMed:17077088}. CC -!- PTM: Glutathionylated. {ECO:0000269|PubMed:21454534}. CC -!- MISCELLANEOUS: Marker of a cell type preferentially transformed by neu CC or ras oncoprotein. CC -!- SIMILARITY: Belongs to the FXYD family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/43704/FXYD3"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X93036; CAA63604.1; -; mRNA. DR EMBL; U28249; AAA73922.1; -; mRNA. DR EMBL; BT006712; AAP35358.1; -; mRNA. DR EMBL; CR456945; CAG33226.1; -; mRNA. DR EMBL; CR542197; CAG46994.1; -; mRNA. DR EMBL; AC020907; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC005238; AAH05238.1; -; mRNA. DR EMBL; BC090044; AAH90044.1; -; mRNA. DR EMBL; BU157560; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS12442.1; -. [Q14802-1] DR CCDS; CCDS12443.1; -. [Q14802-2] DR CCDS; CCDS46048.1; -. [Q14802-3] DR CCDS; CCDS46049.1; -. [Q14802-4] DR CCDS; CCDS46050.1; -. [Q14802-5] DR PIR; A55571; A55571. DR RefSeq; NP_001129479.1; NM_001136007.2. [Q14802-3] DR RefSeq; NP_001129480.1; NM_001136008.2. [Q14802-4] DR RefSeq; NP_001129481.1; NM_001136009.2. [Q14802-5] DR RefSeq; NP_001129482.1; NM_001136010.2. [Q14802-5] DR RefSeq; NP_001129483.1; NM_001136011.2. [Q14802-1] DR RefSeq; NP_001129484.1; NM_001136012.2. [Q14802-2] DR RefSeq; NP_001374278.1; NM_001387349.1. [Q14802-1] DR RefSeq; NP_001374279.1; NM_001387350.1. [Q14802-1] DR RefSeq; NP_001374281.1; NM_001387352.1. [Q14802-1] DR RefSeq; NP_001374282.1; NM_001387353.1. [Q14802-1] DR RefSeq; NP_005962.1; NM_005971.4. [Q14802-1] DR RefSeq; NP_068710.1; NM_021910.3. [Q14802-2] DR AlphaFoldDB; Q14802; -. DR SMR; Q14802; -. DR BioGRID; 111364; 95. DR ComplexPortal; CPX-8141; Sodium:potassium-exchanging ATPase complex, FXYD3 variant. DR FunCoup; Q14802; 61. DR IntAct; Q14802; 90. DR MINT; Q14802; -. DR STRING; 9606.ENSP00000473929; -. DR TCDB; 1.A.27.1.5; the phospholemman (plm) family. DR iPTMnet; Q14802; -. DR PhosphoSitePlus; Q14802; -. DR SwissPalm; Q14802; -. DR BioMuta; FXYD3; -. DR jPOST; Q14802; -. DR MassIVE; Q14802; -. DR PaxDb; 9606-ENSP00000473929; -. DR PeptideAtlas; Q14802; -. DR ProteomicsDB; 25564; -. DR ProteomicsDB; 30673; -. DR ProteomicsDB; 60187; -. [Q14802-1] DR ProteomicsDB; 60188; -. [Q14802-2] DR Pumba; Q14802; -. DR Antibodypedia; 2266; 182 antibodies from 21 providers. DR DNASU; 5349; -. DR Ensembl; ENST00000344013.10; ENSP00000339499.7; ENSG00000089356.20. [Q14802-2] DR Ensembl; ENST00000346446.9; ENSP00000328259.5; ENSG00000089356.20. [Q14802-2] DR Ensembl; ENST00000435734.6; ENSP00000389770.2; ENSG00000089356.20. [Q14802-2] DR Ensembl; ENST00000603181.5; ENSP00000474851.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000603449.5; ENSP00000474055.1; ENSG00000089356.20. [Q14802-5] DR Ensembl; ENST00000604255.5; ENSP00000473929.1; ENSG00000089356.20. [Q14802-3] DR Ensembl; ENST00000604404.6; ENSP00000474438.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000604621.5; ENSP00000474526.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000605552.5; ENSP00000474855.1; ENSG00000089356.20. [Q14802-5] DR Ensembl; ENST00000605677.1; ENSP00000474622.1; ENSG00000089356.20. [Q14802-4] DR Ensembl; ENST00000648240.1; ENSP00000497169.1; ENSG00000285526.1. [Q14802-2] DR Ensembl; ENST00000874694.1; ENSP00000544753.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874695.1; ENSP00000544754.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874696.1; ENSP00000544755.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874697.1; ENSP00000544756.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874698.1; ENSP00000544757.1; ENSG00000089356.20. [Q14802-2] DR Ensembl; ENST00000874699.1; ENSP00000544758.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874700.1; ENSP00000544759.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874701.1; ENSP00000544760.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874702.1; ENSP00000544761.1; ENSG00000089356.20. [Q14802-2] DR Ensembl; ENST00000874703.1; ENSP00000544762.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874705.1; ENSP00000544764.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874706.1; ENSP00000544765.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874707.1; ENSP00000544766.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874708.1; ENSP00000544767.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874709.1; ENSP00000544768.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874710.1; ENSP00000544769.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874711.1; ENSP00000544770.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874712.1; ENSP00000544771.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874713.1; ENSP00000544772.1; ENSG00000089356.20. [Q14802-2] DR Ensembl; ENST00000874714.1; ENSP00000544773.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000874715.1; ENSP00000544774.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000921323.1; ENSP00000591382.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000921324.1; ENSP00000591383.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000956835.1; ENSP00000626894.1; ENSG00000089356.20. [Q14802-2] DR Ensembl; ENST00000956836.1; ENSP00000626895.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000956837.1; ENSP00000626896.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000956838.1; ENSP00000626897.1; ENSG00000089356.20. [Q14802-2] DR Ensembl; ENST00000956839.1; ENSP00000626898.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000956840.1; ENSP00000626899.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000956841.1; ENSP00000626900.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000956842.1; ENSP00000626901.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000956843.1; ENSP00000626902.1; ENSG00000089356.20. [Q14802-2] DR Ensembl; ENST00000956844.1; ENSP00000626903.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000956846.1; ENSP00000626905.1; ENSG00000089356.20. [Q14802-2] DR Ensembl; ENST00000956848.1; ENSP00000626907.1; ENSG00000089356.20. [Q14802-2] DR Ensembl; ENST00000956850.1; ENSP00000626909.1; ENSG00000089356.20. [Q14802-1] DR Ensembl; ENST00000956851.1; ENSP00000626910.1; ENSG00000089356.20. [Q14802-2] DR Ensembl; ENST00000956852.1; ENSP00000626911.1; ENSG00000089356.20. [Q14802-2] DR GeneID; 5349; -. DR KEGG; hsa:5349; -. DR MANE-Select; ENST00000604404.6; ENSP00000474438.1; NM_005971.4; NP_005962.1. DR UCSC; uc002nxv.4; human. [Q14802-1] DR AGR; HGNC:4027; -. DR ClinPGx; PA28443; -. DR CTD; 5349; -. DR DisGeNET; 5349; -. DR GeneCards; FXYD3; -. DR HGNC; HGNC:4027; FXYD3. DR HPA; ENSG00000089356; Tissue enhanced (intestine). DR MIM; 604996; gene. DR OpenTargets; ENSG00000089356; -. DR VEuPathDB; HostDB:ENSG00000089356; -. DR eggNOG; ENOG502S9Z9; Eukaryota. DR GeneTree; ENSGT00940000153062; -. DR HOGENOM; CLU_1781598_0_0_1; -. DR InParanoid; Q14802; -. DR OMA; IVLMSEC; -. DR OrthoDB; 9888529at2759; -. DR PAN-GO; Q14802; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q14802; -. DR PathwayCommons; Q14802; -. 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; Q14802; -. DR Agora; ENSG00000089356; -. DR BioGRID-ORCS; 5349; 5 hits in 1136 CRISPR screens. DR ChiTaRS; FXYD3; human. DR GeneWiki; FXYD3; -. DR GenomeRNAi; 5349; -. DR Pharos; Q14802; Tbio. DR PRO; PR:Q14802; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q14802; protein. DR Bgee; ENSG00000089356; Expressed in mucosa of transverse colon and 96 other cell types or tissues. DR ExpressionAtlas; Q14802; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; ISS:ComplexPortal. DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl. DR GO; GO:0005254; F:chloride channel activity; TAS:ProtInc. DR GO; GO:0017080; F:sodium channel regulator activity; IBA:GO_Central. DR GO; GO:0006821; P:chloride transport; TAS:ProtInc. DR GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; NAS:ComplexPortal. DR GO; GO:0030007; P:intracellular potassium ion homeostasis; ISS:ComplexPortal. DR GO; GO:0006883; P:intracellular sodium ion homeostasis; ISS:ComplexPortal. DR GO; GO:1903278; P:positive regulation of sodium ion export across plasma membrane; IBA:GO_Central. DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISS:ComplexPortal. DR GO; GO:1902600; P:proton transmembrane transport; NAS:ComplexPortal. DR GO; GO:0036376; P:sodium ion export across plasma membrane; ISS:ComplexPortal. DR CDD; cd20328; FXYD3-like; 1. DR FunFam; 1.20.5.780:FF:000006; FXYD domain-containing ion transport regulator; 1. DR Gene3D; 1.20.5.780; Single helix bin; 1. DR InterPro; IPR047297; FXYD_motif. DR InterPro; IPR000272; Ion-transport_regulator_FXYD. DR PANTHER; PTHR14132:SF11; FXYD DOMAIN-CONTAINING ION TRANSPORT REGULATOR 3; 1. DR PANTHER; PTHR14132; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT GAMMA; 1. DR Pfam; PF02038; ATP1G1_PLM_MAT8; 1. DR PROSITE; PS01310; FXYD; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Direct protein sequencing; KW Glutathionylation; Ion transport; Membrane; Potassium; Potassium transport; KW Proteomics identification; Reference proteome; Signal; Sodium; KW Sodium transport; Sodium/potassium transport; Transmembrane; KW Transmembrane helix; Transport. FT SIGNAL 1..20 FT /evidence="ECO:0000269|PubMed:17077088" FT CHAIN 21..87 FT /note="FXYD domain-containing ion transport regulator 3" FT /id="PRO_0000010362" FT TOPO_DOM 21..38 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 39..59 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 60..87 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 66..87 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1 FT /note="M -> MGRGYSGALQARGGLEEPLERGLRGPSFTQSPLHGAAAAYLSAQRDA FT SLPVPGQRSDM (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045716" FT VAR_SEQ 33..87 FT /note="DWHSLQVGGLICAGVLCAMGIIIVMSAKCKCKFGQKSGHHPGETPPLITPGS FT AQS -> GESPCPLSPPHNPTYCLVPRVPIQGWGLT (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_047286" FT VAR_SEQ 58 FT /note="S -> SEWRSSGEQAGRGWGSPPLTTQLSPTG (in isoform 2 and FT isoform 4)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_034598" FT VAR_SEQ 71..87 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_047287" FT VARIANT 40 FT /note="G -> S (in dbSNP:rs35578165)" FT /id="VAR_049109" FT MUTAGEN 44 FT /note="C->S: Abolishes glutathionylation but does not FT affect interaction with ATP1B1; when associated with S-49; FT S-61 and S-63." FT /evidence="ECO:0000269|PubMed:21454534" FT MUTAGEN 49 FT /note="C->S: Abolishes glutathionylation but does not FT affect interaction with ATP1B1; when associated with S-43; FT S-61 and S-63." FT /evidence="ECO:0000269|PubMed:21454534" FT MUTAGEN 61 FT /note="C->S: Abolishes glutathionylation but does not FT affect interaction with ATP1B1; when associated with S-43; FT S-49 and S-63." FT /evidence="ECO:0000269|PubMed:21454534" FT MUTAGEN 63 FT /note="C->S: Abolishes glutathionylation but does not FT affect interaction with ATP1B1; when associated with S-43; FT S-49 and S-61." FT /evidence="ECO:0000269|PubMed:21454534" FT CONFLICT 36..37 FT /note="Missing (in Ref. 2; AAA73922)" FT /evidence="ECO:0000305" SQ SEQUENCE 87 AA; 9263 MW; 6D674D668EB32493 CRC64; MQKVTLGLLV FLAGFPVLDA NDLEDKNSPF YYDWHSLQVG GLICAGVLCA MGIIIVMSAK CKCKFGQKSG HHPGETPPLI TPGSAQS //