FXYD3_MOUSE
ID FXYD3_MOUSE Reviewed; 88 AA.
AC Q61835;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=7970700;
RA Morrison B.W., Leder P.;
RT "neu and ras initiate murine mammary tumors that share genetic markers
RT generally absent in c-myc and int-2-initiated tumors.";
RL Oncogene 9:3417-3426(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [3]
RP TISSUE SPECIFICITY.
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 [4]
RP FUNCTION, IDENTIFICATION IN SODIUM/POTASSIUM-TRANSPORTING ATPASE COMPLEX,
RP INTERACTION WITH ATP1A1 AND ATP1B1, TISSUE SPECIFICITY, NON-CLEAVABLE
RP SIGNAL SEQUENCE, AND MUTAGENESIS OF VAL-5.
RX PubMed=15743908; DOI=10.1091/mbc.e04-10-0878;
RA Crambert G., Li C., Claeys D., Geering K.;
RT "FXYD3 (Mat-8), a new regulator of Na,K-ATPase.";
RL Mol. Biol. Cell 16:2363-2371(2005).
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:15743908). Reduces
CC glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing
CC glutathionylation-mediated inhibition of ATP1B1 (By similarity).
CC Induces a hyperpolarization-activated chloride current when expressed
CC in Xenopus oocytes (By similarity). {ECO:0000250|UniProtKB:Q14802,
CC ECO:0000269|PubMed:15743908}.
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:15743908).
CC Interacts with catalytic alpha subunit ATP1A1 (PubMed:15743908). Also
CC interacts with non-catalytic beta subunit ATP1B1 (PubMed:15743908).
CC Interacts with the ATP1A1-ATP1B1, ATP1A2-ATP1B1 and ATP1A3-ATP1B1 NKA
CC isozymes (By similarity). {ECO:0000250|UniProtKB:Q14802,
CC ECO:0000269|PubMed:15743908}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in heart, skeletal muscle
CC and liver with low levels of expression in breast, brain, lung, stomach
CC and colon (PubMed:7836447). In the gastric gland, mainly expressed in
CC the mucus cells forming the upper part of the gland and is absent from
CC the parietal cells (PubMed:15743908). {ECO:0000269|PubMed:15743908,
CC ECO:0000269|PubMed:7836447}.
CC -!- PTM: Glutathionylated. {ECO:0000250|UniProtKB:Q14802}.
CC -!- MISCELLANEOUS: Marker of a cell type preferentially transformed by neu
CC or ras oncoprotein.
CC -!- SIMILARITY: Belongs to the FXYD family. {ECO:0000305}.
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DR EMBL; X93038; CAA63606.1; -; mRNA.
DR EMBL; BC002039; AAH02039.1; -; mRNA.
DR EMBL; BC056223; AAH56223.1; -; mRNA.
DR CCDS; CCDS21125.1; -.
DR PIR; S61552; S61552.
DR RefSeq; NP_032583.1; NM_008557.2.
DR AlphaFoldDB; Q61835; -.
DR SMR; Q61835; -.
DR BioGRID; 201318; 2.
DR STRING; 10090.ENSMUSP00000130245; -.
DR TCDB; 1.A.27.1.2; the phospholemman (plm) family.
DR PhosphoSitePlus; Q61835; -.
DR PaxDb; Q61835; -.
DR PRIDE; Q61835; -.
DR ProteomicsDB; 273395; -.
DR DNASU; 17178; -.
DR Ensembl; ENSMUST00000167369; ENSMUSP00000130245; ENSMUSG00000057092.
DR GeneID; 17178; -.
DR KEGG; mmu:17178; -.
DR UCSC; uc009gia.2; mouse.
DR CTD; 5349; -.
DR MGI; MGI:107497; Fxyd3.
DR VEuPathDB; HostDB:ENSMUSG00000057092; -.
DR eggNOG; ENOG502S9Z9; Eukaryota.
DR GeneTree; ENSGT00940000153062; -.
DR InParanoid; Q61835; -.
DR OMA; IVLMSEW; -.
DR OrthoDB; 1606794at2759; -.
DR PhylomeDB; Q61835; -.
DR TreeFam; TF333443; -.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 17178; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Fxyd3; mouse.
DR PRO; PR:Q61835; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q61835; protein.
DR Bgee; ENSMUSG00000057092; Expressed in epithelium of stomach and 149 other tissues.
DR ExpressionAtlas; Q61835; baseline and differential.
DR Genevisible; Q61835; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051117; F:ATPase binding; IPI:MGI.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0050790; P:regulation of catalytic activity; IDA:MGI.
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 Cell membrane; Glutathionylation; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Signal; Sodium; Sodium transport;
KW Sodium/potassium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..88
FT /note="FXYD domain-containing ion transport regulator 3"
FT /id="PRO_0000010363"
FT SIGNAL 1..20
FT /note="Not cleaved"
FT /evidence="ECO:0000269|PubMed:15743908"
FT TOPO_DOM 1..38
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 67..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 5
FT /note="V->N: Does not lead to glycosylation, suggesting
FT that the non-cleavable signal sequence remains partly or
FT entirely embedded in the membrane."
FT /evidence="ECO:0000269|PubMed:15743908"
SQ SEQUENCE 88 AA; 9526 MW; 9CD61684B856E35D CRC64;
MQEVVLSLLV LLAGLPTLDA NDPENKNDPF YYDWYSLRVG GLICAGILCA LGIIVLMSGK
CKCKFRQKPS HRPGEGPPLI TPGSAHNC
