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Phospholemman (FXYD domain-containing ion transport regulator 1) (Sodium/potassium-transporting ATPase subunit FXYD1)

 PLM_RAT                 Reviewed;          92 AA.
O08589;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
30-AUG-2002, sequence version 2.
22-NOV-2017, entry version 137.
RecName: Full=Phospholemman {ECO:0000250|UniProtKB:P56513};
AltName: Full=FXYD domain-containing ion transport regulator 1 {ECO:0000312|RGD:69306};
AltName: Full=Sodium/potassium-transporting ATPase subunit FXYD1 {ECO:0000305};
Flags: Precursor;
Name=Fxyd1 {ECO:0000312|RGD:69306};
Synonyms=Plm {ECO:0000303|PubMed:9169143};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
PubMed=9169143; DOI=10.1006/geno.1997.4665;
Chen L.-S.K., Lo C.F., Numann R., Cuddy M.;
"Characterization of the human and rat phospholemman (PLM) cDNAs and
localization of the human PLM gene to chromosome 19q13.1.";
Genomics 41:435-443(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10950925; DOI=10.1006/geno.2000.6274;
Sweadner K.J., Rael E.;
"The FXYD gene family of small ion transport regulators or channels:
cDNA sequence, protein signature sequence, and expression.";
Genomics 68:41-56(2000).
[3]
PROTEIN SEQUENCE OF 70-81, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
[4]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12657675;
Feschenko M.S., Donnet C., Wetzel R.K., Asinovski N.K., Jones L.R.,
Sweadner K.J.;
"Phospholemman, a single-span membrane protein, is an accessory
protein of Na,K-ATPase in cerebellum and choroid plexus.";
J. Neurosci. 23:2161-2169(2003).
[5]
FUNCTION, INTERACTION WITH ATP1A1, DOMAIN, AND ROLE OF PHOSPHORYLATION
AT SER-88.
PubMed=17283221; DOI=10.1096/fj.06-7269com;
Pavlovic D., Fuller W., Shattock M.J.;
"The intracellular region of FXYD1 is sufficient to regulate cardiac
Na/K ATPase.";
FASEB J. 21:1539-1546(2007).
[6]
INTERACTION WITH ATP1A1, AND PHOSPHORYLATION AT SER-83; SER-88 AND
THR-89.
PubMed=19339511; DOI=10.1152/ajpcell.00523.2008;
Fuller W., Howie J., McLatchie L.M., Weber R.J., Hastie C.J.,
Burness K., Pavlovic D., Shattock M.J.;
"FXYD1 phosphorylation in vitro and in adult rat cardiac myocytes:
threonine 69 is a novel substrate for protein kinase C.";
Am. J. Physiol. 296:C1346-C1355(2009).
[7]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=19187398; DOI=10.1111/j.1365-2826.2008.01812.x;
Garcia-Rudaz C., Deng V., Matagne V., Ronnekleiv O.K., Bosch M.,
Han V., Percy A.K., Ojeda S.R.;
"FXYD1, a modulator of Na,K-ATPase activity, facilitates female sexual
development by maintaining gonadotrophin-releasing hormone neuronal
excitability.";
J. Neuroendocrinol. 21:108-122(2009).
[8]
INTERACTION WITH ATP1A1; ATP1A2; ATP1A3 AND ATP1B1, SUBCELLULAR
LOCATION, AND PHOSPHORYLATION AT SER-83 AND SER-88.
PubMed=23532852; DOI=10.1074/jbc.M113.460956;
Wypijewski K.J., Howie J., Reilly L., Tulloch L.B., Aughton K.L.,
McLatchie L.M., Shattock M.J., Calaghan S.C., Fuller W.;
"A separate pool of cardiac phospholemman that does not regulate or
associate with the sodium pump: multimers of phospholemman in
ventricular muscle.";
J. Biol. Chem. 288:13808-13820(2013).
-!- FUNCTION: Associates with and regulates the activity of the
sodium/potassium-transporting ATPase (NKA) which transports Na(+)
out of the cell and K(+) into the cell (By similarity). Inhibits
NKA activity in its unphosphorylated state and stimulates activity
when phosphorylated (PubMed:17283221). Reduces glutathionylation
of the NKA beta-1 subunit ATP1B1, thus reversing
glutathionylation-mediated inhibition of ATP1B1 (By similarity).
Contributes to female sexual development by maintaining the
excitability of neurons which secrete gonadotropin-releasing
hormone (By similarity). {ECO:0000250|UniProtKB:P56513,
ECO:0000250|UniProtKB:Q9Z239, ECO:0000269|PubMed:17283221}.
-!- SUBUNIT: Homotetramer (By similarity). Monomer (By similarity).
Regulatory subunit of the sodium/potassium-transporting ATPase
(NKA) which is composed of a catalytic alpha subunit, a non-
catalytic beta subunit and an additional regulatory subunit (By
similarity). The monomeric form associates with NKA while the
oligomeric form does not (By similarity). Interacts with the
catalytic alpha-1 subunit ATP1A1 (PubMed:17283221,
PubMed:19339511, PubMed:23532852). Also interacts with the
catalytic alpha-2 and alpha-3 subunits ATP1A2 and ATP1A3
(PubMed:23532852). Very little interaction with ATP1A1, ATP1A2 or
ATP1A3 when phosphorylated at Ser-83 (PubMed:23532852). Interacts
with the non-catalytic beta-1 subunit ATP1B1 (PubMed:23532852).
Oxidative stress decreases interaction with ATP1A1 but increases
interaction with ATP1B1 (By similarity).
{ECO:0000250|UniProtKB:O00168, ECO:0000250|UniProtKB:P56513,
ECO:0000250|UniProtKB:Q3SZX0, ECO:0000250|UniProtKB:Q9Z239,
ECO:0000269|PubMed:17283221, ECO:0000269|PubMed:19339511,
ECO:0000269|PubMed:23532852}.
-!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
{ECO:0000269|PubMed:23532852}; Single-pass type I membrane protein
{ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:12657675};
Single-pass type I membrane protein {ECO:0000255}. Membrane,
caveola {ECO:0000269|PubMed:23532852}. Note=Detected in the apical
cell membrane in brain (PubMed:12657675). In myocytes, localizes
to sarcolemma, t-tubules and intercalated disks (PubMed:23532852).
{ECO:0000269|PubMed:12657675, ECO:0000269|PubMed:23532852}.
-!- TISSUE SPECIFICITY: In adult brain, highest levels are found in
the cerebellum and in the lateral, third and fourth ventricles of
the choroid plexus (at protein level) (PubMed:12657675). Also
detected in cells of a portion of the ependymal lining of the
lateral ventricle on its rostral surface posterior to the caudate
putamen (at protein level) (PubMed:12657675). Expressed in a
subset of neurons which secrete gonadotropin-releasing hormone
(PubMed:19187398). {ECO:0000269|PubMed:12657675,
ECO:0000269|PubMed:19187398}.
-!- DEVELOPMENTAL STAGE: In the medial basal hypothalamus, levels are
low at birth and increase during neonatal and infantile
development to reach a maximum during the mid-to-late juvenile
period at postnatal days 24-30. {ECO:0000269|PubMed:19187398}.
-!- DOMAIN: The cytoplasmic domain is sufficient to regulate
sodium/potassium-transporting ATPase activity.
{ECO:0000269|PubMed:17283221}.
-!- PTM: Major plasma membrane substrate for cAMP-dependent protein
kinase (PKA) and protein kinase C (PKC) in several different
tissues (By similarity). Phosphorylated in response to insulin and
adrenergic stimulation (By similarity). Phosphorylation at Ser-88
stimulates sodium/potassium-transporting ATPase activity while the
unphosphorylated form inhibits sodium/potassium-transporting
ATPase activity (PubMed:17283221). Phosphorylation increases
tetramerization, decreases binding to ATP1A1 and reduces
inhibition of ATP1A1 activity (By similarity). Phosphorylation at
Ser-83 leads to greatly reduced interaction with ATP1A1, ATP1A2
and ATP1A3 (PubMed:23532852). May be phosphorylated by DMPK (By
similarity). {ECO:0000250|UniProtKB:O00168,
ECO:0000250|UniProtKB:P56513, ECO:0000269|PubMed:17283221,
ECO:0000269|PubMed:23532852}.
-!- PTM: Palmitoylation increases half-life and stability and is
enhanced upon phosphorylation at Ser-88 by PKA.
{ECO:0000250|UniProtKB:O00168}.
-!- SIMILARITY: Belongs to the FXYD family. {ECO:0000305}.
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EMBL; U72246; AAC53169.1; -; mRNA.
RefSeq; XP_006228901.1; XM_006228839.3.
RefSeq; XP_008757406.1; XM_008759184.2.
RefSeq; XP_017445120.1; XM_017589631.1.
UniGene; Rn.3828; -.
ProteinModelPortal; O08589; -.
SMR; O08589; -.
STRING; 10116.ENSRNOP00000028624; -.
iPTMnet; O08589; -.
PhosphoSitePlus; O08589; -.
SwissPalm; O08589; -.
PaxDb; O08589; -.
PRIDE; O08589; -.
GeneID; 58971; -.
UCSC; RGD:69306; rat.
CTD; 5348; -.
RGD; 69306; Fxyd1.
eggNOG; ENOG410J08K; Eukaryota.
eggNOG; ENOG410YYN6; LUCA.
HOGENOM; HOG000234467; -.
HOVERGEN; HBG008212; -.
InParanoid; O08589; -.
OrthoDB; EOG091G17BP; -.
PhylomeDB; O08589; -.
TreeFam; TF333443; -.
PRO; PR:O08589; -.
Proteomes; UP000002494; Unplaced.
Genevisible; O08589; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0005901; C:caveola; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0042383; C:sarcolemma; IDA:RGD.
GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; ISS:UniProtKB.
GO; GO:0030315; C:T-tubule; IDA:UniProtKB.
GO; GO:0051117; F:ATPase binding; IDA:RGD.
GO; GO:0005216; F:ion channel activity; IEA:InterPro.
GO; GO:0017022; F:myosin binding; IDA:RGD.
GO; GO:0017080; F:sodium channel regulator activity; ISO:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0010734; P:negative regulation of protein glutathionylation; ISS:UniProtKB.
GO; GO:1903797; P:positive regulation of inorganic anion transmembrane transport; IMP:RGD.
GO; GO:0032892; P:positive regulation of organic acid transport; IMP:RGD.
GO; GO:1903278; P:positive regulation of sodium ion export from cell; ISS:UniProtKB.
GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IMP:RGD.
GO; GO:0086036; P:regulation of cardiac muscle cell membrane potential; ISO:RGD.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IMP:RGD.
GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; ISO:RGD.
GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
InterPro; IPR000272; Ion-transport_regulator_FXYD.
Pfam; PF02038; ATP1G1_PLM_MAT8; 1.
ProDom; PD005989; PD005989; 1.
PROSITE; PS01310; FXYD; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Direct protein sequencing;
Glutathionylation; Ion transport; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Potassium; Potassium transport; Reference proteome;
Signal; Sodium; Sodium transport; Sodium/potassium transport;
Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 20 {ECO:0000250|UniProtKB:P56513}.
CHAIN 21 92 Phospholemman.
/FTId=PRO_0000010361.
TOPO_DOM 21 35 Extracellular. {ECO:0000255}.
TRANSMEM 36 56 Helical. {ECO:0000255}.
TOPO_DOM 57 92 Cytoplasmic. {ECO:0000255}.
MOD_RES 62 62 S-glutathionyl cysteine.
{ECO:0000250|UniProtKB:P56513}.
MOD_RES 79 79 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Z239}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z239}.
MOD_RES 83 83 Phosphoserine; by PKA and PKC.
{ECO:0000269|PubMed:19339511,
ECO:0000269|PubMed:23532852}.
MOD_RES 88 88 Phosphoserine; by PKA.
{ECO:0000269|PubMed:19339511,
ECO:0000269|PubMed:23532852}.
MOD_RES 89 89 Phosphothreonine; by PKC.
{ECO:0000269|PubMed:19339511}.
LIPID 60 60 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:O00168}.
LIPID 62 62 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:O00168}.
CONFLICT 3 5 SPG -> PLH (in Ref. 1; AAC53169).
{ECO:0000305}.
CONFLICT 43 46 IAGI -> AGIL (in Ref. 1; AAC53169).
{ECO:0000305}.
SEQUENCE 92 AA; 10365 MW; 29530D084B3CB7C2 CRC64;
MASPGHILIV CVCLLSMASA EAPQEPDPFT YDYHTLRIGG LTIAGILFIL GILIILSKRC
RCKFNQQQRT GEPDEEEGTF RSSIRRLSTR RR


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