FXYD3_HUMAN
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 03-AUG-2022, entry version 184.
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="http://atlasgeneticsoncology.org/Genes/FXYD3ID43704ch19q13.html";
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_001136007.1. [Q14802-3]
DR RefSeq; NP_001129480.1; NM_001136008.1. [Q14802-4]
DR RefSeq; NP_001129481.1; NM_001136009.1. [Q14802-5]
DR RefSeq; NP_001129482.1; NM_001136010.1. [Q14802-5]
DR RefSeq; NP_001129483.1; NM_001136011.1. [Q14802-1]
DR RefSeq; NP_001129484.1; NM_001136012.1. [Q14802-2]
DR RefSeq; NP_005962.1; NM_005971.3. [Q14802-1]
DR RefSeq; NP_068710.1; NM_021910.2. [Q14802-2]
DR RefSeq; XP_005259053.1; XM_005258996.4. [Q14802-2]
DR RefSeq; XP_016882366.1; XM_017026877.1. [Q14802-1]
DR RefSeq; XP_016882367.1; XM_017026878.1. [Q14802-1]
DR AlphaFoldDB; Q14802; -.
DR SMR; Q14802; -.
DR BioGRID; 111364; 94.
DR IntAct; Q14802; 62.
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 BioMuta; FXYD3; -.
DR EPD; Q14802; -.
DR jPOST; Q14802; -.
DR MassIVE; Q14802; -.
DR MaxQB; Q14802; -.
DR PaxDb; Q14802; -.
DR PeptideAtlas; Q14802; -.
DR PRIDE; Q14802; -.
DR ProteomicsDB; 25564; -.
DR ProteomicsDB; 30673; -.
DR ProteomicsDB; 60187; -. [Q14802-1]
DR ProteomicsDB; 60188; -. [Q14802-2]
DR Antibodypedia; 2266; 173 antibodies from 18 providers.
DR DNASU; 5349; -.
DR Ensembl; ENST00000344013.10; ENSP00000339499.7; ENSG00000089356.19. [Q14802-2]
DR Ensembl; ENST00000346446.9; ENSP00000328259.5; ENSG00000089356.19. [Q14802-2]
DR Ensembl; ENST00000435734.6; ENSP00000389770.2; ENSG00000089356.19. [Q14802-2]
DR Ensembl; ENST00000603181.5; ENSP00000474851.1; ENSG00000089356.19. [Q14802-1]
DR Ensembl; ENST00000603449.5; ENSP00000474055.1; ENSG00000089356.19. [Q14802-5]
DR Ensembl; ENST00000604255.5; ENSP00000473929.1; ENSG00000089356.19. [Q14802-3]
DR Ensembl; ENST00000604404.6; ENSP00000474438.1; ENSG00000089356.19. [Q14802-1]
DR Ensembl; ENST00000604621.5; ENSP00000474526.1; ENSG00000089356.19. [Q14802-1]
DR Ensembl; ENST00000605552.5; ENSP00000474855.1; ENSG00000089356.19. [Q14802-5]
DR Ensembl; ENST00000605677.1; ENSP00000474622.1; ENSG00000089356.19. [Q14802-4]
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 CTD; 5349; -.
DR DisGeNET; 5349; -.
DR GeneCards; FXYD3; -.
DR HGNC; HGNC:4027; FXYD3.
DR HPA; ENSG00000089356; Tissue enhanced (intestine).
DR MIM; 604996; gene.
DR neXtProt; NX_Q14802; -.
DR OpenTargets; ENSG00000089356; -.
DR PharmGKB; PA28443; -.
DR VEuPathDB; HostDB:ENSG00000089356; -.
DR eggNOG; ENOG502S9Z9; Eukaryota.
DR GeneTree; ENSGT00940000153062; -.
DR HOGENOM; CLU_1781598_0_0_1; -.
DR InParanoid; Q14802; -.
DR OMA; IVLMSEW; -.
DR OrthoDB; 1606794at2759; -.
DR PhylomeDB; Q14802; -.
DR TreeFam; TF333443; -.
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 BioGRID-ORCS; 5349; 4 hits in 1056 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 94 other tissues.
DR ExpressionAtlas; Q14802; baseline and differential.
DR Genevisible; Q14802; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0005254; F:chloride channel activity; TAS:ProtInc.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:InterPro.
DR GO; GO:0006821; P:chloride transport; TAS:ProtInc.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:Ensembl.
DR GO; GO:0043269; P:regulation of ion transport; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR000272; Ion-transport_regulator_FXYD.
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 Reference proteome; Signal; Sodium; Sodium transport;
KW Sodium/potassium transport; Transmembrane; 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
