PLM_PIG
ID PLM_PIG Reviewed; 87 AA.
AC I3LMB3;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, sequence version 2.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Phospholemman {ECO:0000250|UniProtKB:P56513};
DE AltName: Full=FXYD domain-containing ion transport regulator 1 {ECO:0000250|UniProtKB:O00168};
DE AltName: Full=Sodium/potassium-transporting ATPase subunit FXYD1 {ECO:0000305};
DE Flags: Precursor;
GN Name=FXYD1 {ECO:0000250|UniProtKB:O00168};
GN Synonyms=PLM {ECO:0000250|UniProtKB:O00168};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000312|Proteomes:UP000008227};
RN [1] {ECO:0000312|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc;
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP IDENTIFICATION IN SODIUM/POTASSIUM-TRANSPORTING ATPASE COMPLEX, AND
RP INTERACTION WITH ATP1A1.
RX PubMed=15563542; DOI=10.1152/ajpheart.00142.2004;
RA Jia L.G., Donnet C., Bogaev R.C., Blatt R.J., McKinney C.E., Day K.H.,
RA Berr S.S., Jones L.R., Moorman J.R., Sweadner K.J., Tucker A.L.;
RT "Hypertrophy, increased ejection fraction, and reduced Na-K-ATPase activity
RT in phospholemman-deficient mice.";
RL Am. J. Physiol. 288:H1982-H1988(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. Inhibits NKA activity in its
CC unphosphorylated state and stimulates activity when phosphorylated.
CC Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus
CC reversing glutathionylation-mediated inhibition of ATP1B1. Contributes
CC to female sexual development by maintaining the excitability of neurons
CC which secrete gonadotropin-releasing hormone.
CC {ECO:0000250|UniProtKB:O08589, ECO:0000250|UniProtKB:P56513,
CC ECO:0000250|UniProtKB:Q9Z239}.
CC -!- SUBUNIT: Homotetramer (By similarity). Monomer (By similarity).
CC Regulatory subunit of the sodium/potassium-transporting ATPase (NKA)
CC which is composed of a catalytic alpha subunit, a non-catalytic beta
CC subunit and an additional regulatory subunit (PubMed:15563542). The
CC monomeric form associates with NKA while the oligomeric form does not
CC (By similarity). Interacts with the catalytic alpha-1 subunit ATP1A1
CC (PubMed:15563542). Also interacts with the catalytic alpha-2 and alpha-
CC 3 subunits ATP1A2 and ATP1A3 (By similarity). Very little interaction
CC with ATP1A1, ATP1A2 or ATP1A3 when phosphorylated at Ser-83 (By
CC similarity). Interacts with the non-catalytic beta-1 subunit ATP1B1 (By
CC similarity). Oxidative stress decreases interaction with ATP1A1 but
CC increases interaction with ATP1B1 (By similarity).
CC {ECO:0000250|UniProtKB:O00168, ECO:0000250|UniProtKB:O08589,
CC ECO:0000250|UniProtKB:P56513, ECO:0000250|UniProtKB:Q3SZX0,
CC ECO:0000250|UniProtKB:Q9Z239, ECO:0000269|PubMed:15563542}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P56513}; Single-pass type I membrane protein
CC {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O08589};
CC Single-pass type I membrane protein {ECO:0000255}. Membrane, caveola
CC {ECO:0000250|UniProtKB:O08589}. Cell membrane, sarcolemma, T-tubule
CC {ECO:0000250|UniProtKB:O08589}. Note=Detected in the apical cell
CC membrane in brain. In myocytes, localizes to sarcolemma, t-tubules and
CC intercalated disks. {ECO:0000250|UniProtKB:O08589}.
CC -!- DOMAIN: The cytoplasmic domain is sufficient to regulate
CC sodium/potassium-transporting ATPase activity.
CC {ECO:0000250|UniProtKB:O08589}.
CC -!- PTM: Major plasma membrane substrate for cAMP-dependent protein kinase
CC (PKA) and protein kinase C (PKC) in several different tissues.
CC Phosphorylated in response to insulin and adrenergic stimulation.
CC Phosphorylation at Ser-83 stimulates sodium/potassium-transporting
CC ATPase activity while the unphosphorylated form inhibits
CC sodium/potassium-transporting ATPase activity. Phosphorylation
CC increases tetramerization, decreases binding to ATP1A1 and reduces
CC inhibition of ATP1A1 activity. Phosphorylation at Ser-75 leads to
CC greatly reduced interaction with ATP1A1, ATP1A2 and ATP1A3. May be
CC phosphorylated by DMPK. {ECO:0000250|UniProtKB:O00168,
CC ECO:0000250|UniProtKB:O08589, ECO:0000250|UniProtKB:P56513}.
CC -!- PTM: Palmitoylation increases half-life and stability and is enhanced
CC upon phosphorylation at Ser-83 by PKA. {ECO:0000250|UniProtKB:O00168}.
CC -!- SIMILARITY: Belongs to the FXYD family. {ECO:0000305}.
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DR EMBL; FP565327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3LMB3; -.
DR SMR; I3LMB3; -.
DR STRING; 9823.ENSSSCP00000025234; -.
DR PaxDb; I3LMB3; -.
DR PeptideAtlas; I3LMB3; -.
DR Ensembl; ENSSSCT00000076450; ENSSSCP00000072479; ENSSSCG00000021374.
DR Ensembl; ENSSSCT00005050641; ENSSSCP00005031305; ENSSSCG00005031622.
DR Ensembl; ENSSSCT00015038812; ENSSSCP00015015419; ENSSSCG00015028298.
DR Ensembl; ENSSSCT00025041671; ENSSSCP00025017735; ENSSSCG00025030566.
DR Ensembl; ENSSSCT00030028686; ENSSSCP00030012808; ENSSSCG00030020741.
DR Ensembl; ENSSSCT00035028330; ENSSSCP00035010911; ENSSSCG00035021670.
DR Ensembl; ENSSSCT00040094677; ENSSSCP00040041835; ENSSSCG00040068829.
DR Ensembl; ENSSSCT00045059949; ENSSSCP00045042083; ENSSSCG00045034732.
DR Ensembl; ENSSSCT00050008215; ENSSSCP00050003502; ENSSSCG00050006033.
DR Ensembl; ENSSSCT00055059231; ENSSSCP00055047435; ENSSSCG00055029735.
DR Ensembl; ENSSSCT00060074058; ENSSSCP00060031938; ENSSSCG00060054384.
DR Ensembl; ENSSSCT00065071044; ENSSSCP00065030965; ENSSSCG00065051846.
DR Ensembl; ENSSSCT00070020418; ENSSSCP00070016965; ENSSSCG00070010455.
DR eggNOG; ENOG502S5XM; Eukaryota.
DR GeneTree; ENSGT00940000153062; -.
DR HOGENOM; CLU_171208_0_1_1; -.
DR InParanoid; I3LMB3; -.
DR TreeFam; TF333443; -.
DR Proteomes; UP000008227; Chromosome 6.
DR Proteomes; UP000314985; Chromosome 6.
DR Bgee; ENSSSCG00000021374; Expressed in longissimus lumborum muscle and 45 other tissues.
DR ExpressionAtlas; I3LMB3; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IMP:BHF-UCL.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:BHF-UCL.
DR GO; GO:0030315; C:T-tubule; ISS:UniProtKB.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:InterPro.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0010734; P:negative regulation of protein glutathionylation; ISS:UniProtKB.
DR GO; GO:1903278; P:positive regulation of sodium ion export across plasma membrane; ISS:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
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; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; 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:0000250|UniProtKB:P56513"
FT CHAIN 21..87
FT /note="Phospholemman"
FT /id="PRO_5003675504"
FT TOPO_DOM 21..35
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 62
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56513"
FT MOD_RES 75
FT /note="Phosphoserine; by PKA and PKC"
FT /evidence="ECO:0000250|UniProtKB:Q9Z239"
FT MOD_RES 83
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P56513"
FT LIPID 60
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O00168"
FT LIPID 62
FT /note="S-palmitoyl cysteine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O00168"
SQ SEQUENCE 87 AA; 9672 MW; D2223FE0B231349B CRC64;
MASLSHILVL WVGILTVVNA EAPQEHDPFT YDYQSLRIGG LIIAGILFIL GILIVLSRRC
RCKFNQQQSL GKMRSPHLAA QFSSESC
